|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
237-1601 |
1.39e-119 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 418.26 E-value: 1.39e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 237 FIYYVSVNVT----QERQYITSLMTMMGLRESAFWLSWGLMYAGFILIMATLMALIVKSAQIVVLTGFVMVFTLFLLYGL 312
Cdd:TIGR01257 663 WIYSVSMTVKsivlEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFIMHGRILHYSDPFILFLFLLAFST 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 313 SLITLAFLMSVLIKKPFLTGL---VVFLLIVFWGILGFpALYTRLPAFLEWTLCLLSPFAFTVGMAQLIH-------LDY 382
Cdd:TIGR01257 743 ATIMQCFLLSTFFSKASLAAAcsgVIYFTLYLPHILCF-AWQDRMTADLKTAVSLLSPVAFGFGTEYLVRfeeqglgLQW 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 383 DVNSNAHLDSSQNPYLIiaTLFMLVFDTLLYLVLTLYFDKILPAEYGHRCSPLFFLKSCFWF-------QHGRANHVV-- 453
Cdd:TIGR01257 822 SNIGNSPLEGDEFSFLL--SMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLggegcstREERALEKTep 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 454 LENETDSDPTP---NDCF-EPVSPEFCgkEAIRIKNLKKEYAgKCERvEALKGVVFDIYEGQITALLGHSGAGKTTLLNI 529
Cdd:TIGR01257 900 LTEEMEDPEHPegiNDSFfERELPGLV--PGVCVKNLVKIFE-PSGR-PAVDRLNITFYENQITAFLGHNGAGKTTTLSI 975
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 530 LSGLSVPTSGSVTVYNHTLSRMADIenISKFTGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMEN 609
Cdd:TIGR01257 976 LTGLLPPTSGTVLVGGKDIETNLDA--VRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHH 1053
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 610 IQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVILFSTQFIDEADILADRKVFI 689
Cdd:TIGR01257 1054 KRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAII 1133
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 690 SNGKLKCAGSSLFLKKKWGIGYHLSL-----------------------HLNERC---------------DPESITSLVK 731
Cdd:TIGR01257 1134 SQGRLYCSGTPLFLKNCFGTGFYLTLvrkmkniqsqrggcegtcsctskGFSTRCparvdeitpeqvldgDVNELMDLVY 1213
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 732 QHISDAKLTAQSEEKLVYILPLE--RTNKFPELYRDLDRC-SNQGIEDYGVSITTLNEVFLKLegkstIDESDIgiwGQL 808
Cdd:TIGR01257 1214 HHVPEAKLVECIGQELIFLLPNKnfKQRAYASLFRELEETlADLGLSSFGISDTPLEEIFLKV-----TEDADS---GSL 1285
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 809 QTDGAKDIGSLVELEQVLSSFHETRKTI--------------------------------SGVALWRQQVCAIAKVRFLK 856
Cdd:TIGR01257 1286 FAGGAQQKRENANLRHPCSGPTEKAGQTpqashtcspgqpaahpegqpppepedpgvplnTGARLILQHVQALLVKRFQH 1365
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 857 LKKERKSLWT--------ILLLFGISFI-------PQLLEHLFYESYQKSYPWELSPNTYFLS---------PG------ 906
Cdd:TIGR01257 1366 TIRSHKDFLAqivlpatfVFLALMLSIIippfgeyPALTLHPWMYGQQYTFFSMDEPNSEHLEvladvllnkPGfgnrcl 1445
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 907 ---QQPQDP---------------LTHLLviNKTGSTIDN-------------------------------------FLH 931
Cdd:TIGR01257 1446 keeWLPEYPcgnstpwktpsvspnITHLF--QKQKWTAAHpspscrcstrekltmlpecpegagglpppqrtqrsteILQ 1523
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 932 SLRRQNI---------AIEVDAFGTRNGTDDPSYNG--------AIIVSGD----------------------------- 965
Cdd:TIGR01257 1524 DLTDRNIsdflvktypALIRSSLKSKFWVNEQRYGGisiggklpAIPITGEalvgflsdlgqmmnvsggpvtreaskemp 1603
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 966 ------EKDHRFSIACNTKRLNCFPVLLDVISNGLL-------------GIFNSSEHI-----QTDRSTFFEEHMDYEYG 1021
Cdd:TIGR01257 1604 dflkhlETEDNIKVWFNNKGWHALVSFLNVAHNAILraslpkdrdpeeyGITVISQPLnltkeQLSEITVLTTSVDAVVA 1683
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1022 YrSNTFFWIPMAASFTPYIAMSSIgdyKKKAHSQLrISGLYPSAYWFGQALVDVSLYFL-------ILLLMQIMDYIfSP 1094
Cdd:TIGR01257 1684 I-CVIFAMSFVPASFVLYLIQERV---NKAKHLQF-ISGVSPTTYWLTNFLWDIMNYAVsaglvvgIFIGFQKKAYT-SP 1757
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1095 EEIIFIIQNLLIqilcsigYVSSLVFLTYVISFIFRNGRKNSGIWSFFFLIVVIFSIVAT---DLNEYGFLGLFFGTML- 1170
Cdd:TIGR01257 1758 ENLPALVALLML-------YGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINSSAITfvlELFENNRTLLRFNAMLr 1830
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1171 -----IPPFTLIGSL--FIFSEISPDSMDYLGASESEIVY---------LALLIP-YLHFLIFLFILRCLEMNCRKKLMR 1233
Cdd:TIGR01257 1831 kllivFPHFCLGRGLidLALSQAVTDVYAQFGEEHSANPFqwdligknlVAMAVEgVVYFLLTLLIQHHFFLSRWIAEPA 1910
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1234 KDPVFrisprsnaifpnpeepeGEEEDIQMERMRTVNAMavrdfDETPVIIASCLRKEYAGKKKNcfskrkkkiATRNVS 1313
Cdd:TIGR01257 1911 KEPIF-----------------DEDDDVAEERQRIISGG-----NKTDILRLNELTKVYSGTSSP---------AVDRLC 1959
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1314 FCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG----SGGGEPLGFLGYCPQENALWPNLTVRQHLEVYAAV 1389
Cdd:TIGR01257 1960 VGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGksilTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARL 2039
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1390 KGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRATFRN 1469
Cdd:TIGR01257 2040 RGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE 2119
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1470 tERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLLEMKLKN-----LAQMEPLHAEILRLFPQAAQ 1544
Cdd:TIGR01257 2120 -GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSpkddlLPDLNPVEQFFQGNFPGSVQ 2198
|
1610 1620 1630 1640 1650
....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 1545 QERFSSLMVYKLPVEDvrpLSQAFFKLEIVKQSFDLEEYSLSQSTLEQVFLELSKEQ 1601
Cdd:TIGR01257 2199 RERHYNMLQFQVSSSS---LARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQ 2252
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1288-1509 |
1.94e-83 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 272.84 E-value: 1.94e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1288 LRKEYagkkkncfsKRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG----SGGGEPLGF 1363
Cdd:cd03263 6 LTKTY---------KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1364 LGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVL 1443
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 1444 LDEPSTGMDPEGQQQMWQVIRATFRNteRGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLK 1509
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKG--RSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
481-704 |
5.18e-81 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 265.91 E-value: 5.18e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYaGKCERVeALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHtlSRMADIENISKF 560
Cdd:cd03263 1 LQIRNLTKTY-KKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY--SIRTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLL 640
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477115 641 LDEPTAGLDPLSRHRIWNLLKEGKSDRVILFSTQFIDEADILADRKVFISNGKLKCAGSSLFLK 704
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1301-1512 |
1.20e-73 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 245.36 E-value: 1.20e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1301 SKR-KKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG----SGGGEPLGFLGYCPQENALWP 1375
Cdd:COG1131 7 TKRyGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvaRDPAEVRRRIGYVPQEPALYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1376 NLTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEG 1455
Cdd:COG1131 87 DLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 1456 QQQMWQVIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKF 1512
Cdd:COG1131 167 RRELWELLRE-LAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
481-699 |
1.74e-69 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 233.42 E-value: 1.74e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRmaDIENISKF 560
Cdd:COG1131 1 IEVRGLTKRYGDK----TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR--DPAEVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLL 640
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 641 LDEPTAGLDPLSRHRIWNLLKE-GKSDRVILFSTQFIDEADILADRKVFISNGKLKCAGS 699
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGT 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
481-699 |
3.58e-57 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 198.16 E-value: 3.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYaGKcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADI--ENIs 558
Cdd:COG4555 2 IEVENLSKKY-GK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREarRQI- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 559 kftGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQV 638
Cdd:COG4555 77 ---GVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477115 639 LLLDEPTAGLDPLSRHRIWNLLKE-GKSDRVILFSTQFIDEADILADRKVFISNGKLKCAGS 699
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGS 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1304-1515 |
4.56e-57 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 198.16 E-value: 4.56e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1304 KKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG-SGGGEPLGF---LGYCPQENALWPNLTV 1379
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGeDVRKEPREArrqIGVLPDERGLYDRLTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1380 RQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1459
Cdd:COG4555 92 RENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 1460 WQVIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKD 1515
Cdd:COG4555 172 REILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1301-1499 |
1.97e-56 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 193.38 E-value: 1.97e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1301 SKR-KKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG----SGGGEPLGFLGYCPQENALWP 1375
Cdd:cd03230 7 SKRyGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGkdikKEPEEVKRRIGYLPEEPSLYE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1376 NLTVRQHLEvyaavkglrkgdamiaitrlvdalklqdqlkapvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEG 1455
Cdd:cd03230 87 NLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPES 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27477115 1456 QQQMWQVIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:cd03230 131 RREFWELLR-ELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1301-1602 |
3.72e-55 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 194.56 E-value: 3.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1301 SKR-KKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGsgggEPLGF-----LGYCPQENALW 1374
Cdd:COG4152 8 TKRfGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG----EPLDPedrrrIGYLPEERGLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1375 PNLTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1454
Cdd:COG4152 84 PKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1455 GQQQMWQVIRATfrnTERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKD-YLLEMKlknlaqmepL 1531
Cdd:COG4152 164 NVELLKDVIREL---AAKGTtvIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNtLRLEAD---------G 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27477115 1532 HAEILRLFPQAAQQERFSSLMVYKLPVEDVrplSQAFfkLEIVKQSFDLEEYSLSQSTLEQVFLELSKEQE 1602
Cdd:COG4152 232 DAGWLRALPGVTVVEEDGDGAELKLEDGAD---AQEL--LRALLARGPVREFEEVRPSLNEIFIEVVGEKA 297
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1308-1597 |
5.43e-55 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 194.15 E-value: 5.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSG-GGEPLGF---LGYCPQENALWPNLTVRQHL 1383
Cdd:TIGR01188 8 AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDvVREPRKVrrsIGIVPQYASVDEDLTGRENL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1384 EVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVI 1463
Cdd:TIGR01188 88 EMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1464 RAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYlLEMKLKNLAQMEPLHAEILRLFPQAA 1543
Cdd:TIGR01188 168 RA-LKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDT-LESRPRDIQSLKVEVSMLIAELGETG 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1544 qqerFSSLMVY------KLPVEDVRPLSQAFFKlEIVKQSFDLEEYSLSQSTLEQVFLEL 1597
Cdd:TIGR01188 246 ----LGLLAVTvdsdriKILVPDGDETVPEIVE-AAIRNGIRIRSISTERPSLDDVFLKL 300
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
481-694 |
1.15e-53 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 185.29 E-value: 1.15e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRmaDIENISKF 560
Cdd:cd03230 1 IEVRNLSKRYGKK----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK--EPEEVKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQFGFLTVKENLRLfakikgilphevekevqrvvqelemeniqdilaqnlSGGQNRKLTFGIAILGDPQVLL 640
Cdd:cd03230 75 IGYLPEEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 641 LDEPTAGLDPLSRHRIWNLLKE-GKSDRVILFSTQFIDEADILADRKVFISNGKL 694
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1308-1509 |
5.70e-52 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 182.57 E-value: 5.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG-SGGGEPLGF---LGYCPQENALWPNLTVRQHL 1383
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhDVVREPREVrrrIGIVFQDLSVDDELTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1384 EVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVI 1463
Cdd:cd03265 95 YIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27477115 1464 RATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLK 1509
Cdd:cd03265 175 EKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
481-695 |
3.11e-49 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 174.30 E-value: 3.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKCerveALKGVVFDIYEGqITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADieNISKF 560
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ--KLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQsnvQFGF---LTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQ 637
Cdd:cd03264 74 IGYLPQ---EFGVypnFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 638 VLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVILFSTQFIDEADILADRKVFISNGKLK 695
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1296-1500 |
8.76e-48 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 170.09 E-value: 8.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1296 KKNCFSKR-KKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGGG---EPLGFLGYCPQEN 1371
Cdd:cd03268 2 KTNDLTKTyGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQkniEALRRIGALIEAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1372 ALWPNLTVRQHLEVYAAVKGLRKGDamiaITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGM 1451
Cdd:cd03268 82 GFYPNLTARENLRLLARLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27477115 1452 DPEGQQQMWQVIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLR 1500
Cdd:cd03268 158 DPDGIKELRELILS-LRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
481-694 |
1.79e-47 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 169.59 E-value: 1.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIENIS-- 558
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 559 -KFTGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQ 637
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 638 VLLLDEPTAGLDPLSRHRIWNLLKE--GKSDRVILFSTQFIDEADiLADRKVFISNGKL 694
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1300-1503 |
2.84e-47 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 168.61 E-value: 2.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1300 FSKR-KKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSG-GGEPLGFLGYCPQENALWPNL 1377
Cdd:cd03269 6 VTKRfGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPlDIAARNRIGYLPEERGLYPKM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1378 TVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1457
Cdd:cd03269 86 KVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27477115 1458 QMWQVIRATFRNtERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1503
Cdd:cd03269 166 LLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1282-1562 |
1.37e-46 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 170.65 E-value: 1.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1282 VIIASCLRKEY---------AGKKKNCFSKRKKKI-ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVI 1351
Cdd:COG4586 1 IIEVENLSKTYrvyekepglKGALKGLFRREYREVeAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1352 lkgsgggeplgFLGYCP----------------QENALWPNLTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLK 1415
Cdd:COG4586 81 -----------VLGYVPfkrrkefarrigvvfgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1416 APVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRAtfRNTERGA--LLTTHYMAEAEAVCDRVAI 1493
Cdd:COG4586 150 TPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKE--YNRERGTtiLLTSHDMDDIEALCDRVIV 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 1494 MVSGRLRCIGSIQHLKSKFGKDYLLEMKLKNLAQMEPL--HAEILR--------LFPQAAQQERFSSLMVYKLPVEDVR 1562
Cdd:COG4586 228 IDHGRIIYDGSLEELKERFGPYKTIVLELAEPVPPLELprGGEVIEregnrvrlEVDPRESLAEVLARLLARYPVRDLT 306
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
498-793 |
2.03e-46 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 169.49 E-value: 2.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 498 EALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADieNISKFTGFCPQSNVQFGFLTVK 577
Cdd:TIGR01188 7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPR--KVRRSIGIVPQYASVDEDLTGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 578 ENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIW 657
Cdd:TIGR01188 85 ENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 658 NLLKEGKSDRV-ILFSTQFIDEADILADRKVFISNGKLKCAGSSLFLKKKWGiGYHLSLhlnERCDPESITSLVKQ---- 732
Cdd:TIGR01188 165 DYIRALKEEGVtILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLG-KDTLES---RPRDIQSLKVEVSMliae 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 733 ----HISDAKLTAQSEEKLVYILPLERTnkFPELYRDLDRcsnQGIEDYGVSIT--TLNEVFLKLEG 793
Cdd:TIGR01188 241 lgetGLGLLAVTVDSDRIKILVPDGDET--VPEIVEAAIR---NGIRIRSISTErpSLDDVFLKLTG 302
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
481-704 |
3.36e-45 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 162.92 E-value: 3.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGkcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADieNISKF 560
Cdd:cd03265 1 IEVENLVKKYGD----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR--EVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLL 640
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 641 LDEPTAGLDPLSRHRIWNLLKEGKS--DRVILFSTQFIDEADILADRKVFISNGKLKCAGSSLFLK 704
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
481-699 |
6.27e-44 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 159.81 E-value: 6.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRmADIENISKF 560
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK-KNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQ-SNVQFGFLTVKENLrLFA-KIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLtfgiAILG---- 634
Cdd:COG1122 77 VGLVFQnPDDQLFAPTVEEDV-AFGpENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRV----AIAGvlam 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 635 DPQVLLLDEPTAGLDPLSRHRIWNLLKE-GKSDRVILFSTQFIDEADILADRKVFISNGKLKCAGS 699
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1301-1500 |
8.38e-44 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 158.51 E-value: 8.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1301 SKR-KKKIATRNVSFCVKKGeVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG-SGGGEPLGF---LGYCPQENALWP 1375
Cdd:cd03264 7 TKRyGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqDVLKQPQKLrrrIGYLPQEFGVYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1376 NLTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEg 1455
Cdd:cd03264 86 NFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27477115 1456 qqqmwQVIRatFRN------TERGALLTTHYMAEAEAVCDRVAIMVSGRLR 1500
Cdd:cd03264 165 -----ERIR--FRNllselgEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
478-694 |
1.70e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 155.59 E-value: 1.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 478 KEAIRIKNLKKEYAGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIE-- 555
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREla 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 556 -----NIskftGFCPQS-NVqFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQN------ 623
Cdd:COG1136 82 rlrrrHI----GFVFQFfNL-LPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQqrvaia 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 624 RkltfgiAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--GKSDRVILFSTQfidEADIL--ADRKVFISNGKL 694
Cdd:COG1136 157 R------ALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTH---DPELAarADRVIRLRDGRI 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
482-693 |
3.11e-41 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 151.47 E-value: 3.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 482 RIKNLKKEYAGKCErvEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVyNHTLSRMADIENISKFT 561
Cdd:cd03225 1 ELKNLSFSYPDGAR--PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLV-DGKDLTKLSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 562 GFCPQ-SNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLL 640
Cdd:cd03225 78 GLVFQnPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 641 LDEPTAGLDPLSRHRIWNLLK----EGKSdrvILFSTQFIDEADILADRKVFISNGK 693
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKklkaEGKT---IIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
481-698 |
3.33e-41 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 151.37 E-value: 3.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRmADIENISKF 560
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 tGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLL 640
Cdd:cd03266 81 -GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 641 LDEPTAGLDPLSRHRIWNLLKEGKSD-RVILFSTQFIDEADILADRKVFISNGKLKCAG 698
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1300-1503 |
2.52e-40 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 149.06 E-value: 2.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1300 FSKRKKKI-ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG----SGGGEPLGFLGYCPQENALW 1374
Cdd:cd03266 11 FRDVKKTVqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvKEPAEARRRLGFVSDSTGLY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1375 PNLTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1454
Cdd:cd03266 91 DRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27477115 1455 GQQQMWQVIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1503
Cdd:cd03266 171 ATRALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1306-1598 |
3.02e-40 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 151.88 E-value: 3.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1306 KIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPL--------GFLGYCPQENALWPNL 1377
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISL----CGEPVpsrarharQRVGVVPQFDNLDPDF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1378 TVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1457
Cdd:PRK13537 96 TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARH 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1458 QMWQVIRATFrntERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL-KSKFGKDyLLEMKLKNLAQMEPLhae 1534
Cdd:PRK13537 176 LMWERLRSLL---ARGKtiLLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALiESEIGCD-VIEIYGPDPVALRDE--- 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 1535 ilrLFPQAAQQE-RFSSLMVYklpVEDVRPLSQAffkleiVKQSFDLeEYSLSQSTLEQVFLELS 1598
Cdd:PRK13537 249 ---LAPLAERTEiSGETLFCY---VRDPEPLHAR------LKGRAGL-RYLHRPANLEDVFLRLT 300
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
481-694 |
1.23e-39 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 146.59 E-value: 1.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTV----YNHTLSRMADIEN 556
Cdd:cd03268 1 LKTNDLTKTYGKK----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFdgksYQKNIEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 557 ISKFTGFcpqsnvqFGFLTVKENLRLFAKIKGILphevEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDP 636
Cdd:cd03268 77 LIEAPGF-------YPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477115 637 QVLLLDEPTAGLDPLS----RHRIWNLLKEGKSdrvILFSTQFIDEADILADRKVFISNGKL 694
Cdd:cd03268 146 DLLILDEPTNGLDPDGikelRELILSLRDQGIT---VLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
481-691 |
1.30e-39 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 146.85 E-value: 1.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNhtlsrmADIENISKF 560
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG------EPVTGPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLL 640
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 641 LDEPTAGLDPLSRHRIWNLL-----KEGKSdrvILFSTQFIDEADILADRKVFISN 691
Cdd:cd03293 155 LDEPFSALDALTREQLQEELldiwrETGKT---VLLVTHDIDEAVFLADRVVVLSA 207
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
480-692 |
2.26e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 144.85 E-value: 2.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRM-ADIenis 558
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPgPDR---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 559 kftGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLtfGIA--ILGDP 636
Cdd:COG1116 83 ---GVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRV--AIAraLANDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27477115 637 QVLLLDEPTAGLDPLSRHRIWNLL-----KEGKSdrvILFSTQFIDEADILADRKVFISNG 692
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELlrlwqETGKT---VLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1311-1606 |
4.34e-38 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 157.10 E-value: 4.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1311 NVSFcvKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGGGEPLGF----LGYCPQENALWPNLTVRQHLEVY 1386
Cdd:TIGR01257 950 NITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAvrqsLGMCPQHNILFHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1387 AAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIrAT 1466
Cdd:TIGR01257 1028 AQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL-LK 1106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1467 FRnTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLLEM--KLKNLAQME--------------- 1529
Cdd:TIGR01257 1107 YR-SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLvrKMKNIQSQRggcegtcsctskgfs 1185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1530 ---PLHAE------------------ILRLFPQAAQQERFSSLMVYKLPVEDV--RPLSQAFFKLEIVKQSFDLEEYSLS 1586
Cdd:TIGR01257 1186 trcPARVDeitpeqvldgdvnelmdlVYHHVPEAKLVECIGQELIFLLPNKNFkqRAYASLFRELEETLADLGLSSFGIS 1265
|
330 340
....*....|....*....|
gi 27477115 1587 QSTLEQVFLELSKEQELGDL 1606
Cdd:TIGR01257 1266 DTPLEEIFLKVTEDADSGSL 1285
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
481-693 |
7.97e-38 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 141.80 E-value: 7.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYaGKcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIENISKF 560
Cdd:cd03224 1 LEVENLNAGY-GK---SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQFGFLTVKENLRLFAKIKGilPHEVEKEVQRVvqeLEM----ENIQDILAQNLSGGQNRKLTFGIAILGDP 636
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENLLLGAYARR--RAKRKARLERV---YELfprlKERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 637 QVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRV-ILFSTQFIDEADILADRKVFISNGK 693
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVtILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
481-694 |
9.18e-38 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 142.26 E-value: 9.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKCerveALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIE--NIS 558
Cdd:cd03261 1 IELRGLTKSFGGRT----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 559 KFTGFCPQSNVQFGFLTVKENLRLFAKIKGILPhevEKEVQRVVQE-LEM---ENIQDILAQNLSGGQNRKLTFGIAILG 634
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLREHTRLS---EEEIREIVLEkLEAvglRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27477115 635 DPQVLLLDEPTAGLDPLSRHRIWNL---LKEGKSDRVILFSTQfIDEADILADRKVFISNGKL 694
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLirsLKKELGLTSIMVTHD-LDTAFAIADRIAVLYDGKI 215
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
481-693 |
1.35e-37 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 140.69 E-value: 1.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGkcERVeaLKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRmaDIENISKF 560
Cdd:COG4133 3 LEAENLSCRRGE--RLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD--AREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEkeVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLL 640
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27477115 641 LDEPTAGLDPLSRHRIWNLLKE-GKSDRVILFSTqfIDEADILADRKVFISNGK 693
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAhLARGGAVLLTT--HQPLELAAARVLDLGDFK 206
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
481-698 |
1.99e-37 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 140.49 E-value: 1.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAgkceRVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLsrmaDIENISKF 560
Cdd:cd03269 1 LEVENVTKRFG----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 tGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLL 640
Cdd:cd03269 73 -GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 641 LDEPTAGLDPLSRHRIWNLLKEGKSD-RVILFSTQFIDEADILADRKVFISNGKLKCAG 698
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1302-1499 |
2.28e-37 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 140.93 E-value: 2.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1302 KRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgggeplgfLGYCP------------- 1368
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV-----------AGLVPwkrrkkflrrigv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1369 ---QENALWPNLTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLD 1445
Cdd:cd03267 99 vfgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27477115 1446 EPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1310-1479 |
3.11e-37 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 139.54 E-value: 3.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGGGEPL----GFLGYCPQENALWPNLTVRQHLEV 1385
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARedyrRRLAYLGHADGLKPELTVRENLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1386 YAAVKGLRKGDAmiAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRA 1465
Cdd:COG4133 99 WAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
170
....*....|....
gi 27477115 1466 tFRNTERGALLTTH 1479
Cdd:COG4133 177 -HLARGGAVLLTTH 189
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
500-646 |
1.82e-36 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 135.47 E-value: 1.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 500 LKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMaDIENISKFTGFCPQSNVQFGFLTVKEN 579
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD-ERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27477115 580 LRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQN----LSGGQNRKLTFGIAILGDPQVLLLDEPTA 646
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
480-795 |
2.63e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 140.24 E-value: 2.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRmADIENIsk 559
Cdd:COG4152 1 MLELKGLTKRFGDK----TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-EDRRRI-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 ftgfcpqsnvqfGFL----------TVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFG 629
Cdd:COG4152 74 ------------GYLpeerglypkmKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 630 IAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGK-SDRVILFSTQFIDEADILADRKVFISNGKLKCAGSSLFLKKKWG 708
Cdd:COG4152 142 AALLHDPELLILDEPFSGLDPVNVELLKDVIRELAaKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 709 iGYHLSLHLNErcDPESITSLvkqhisdAKLTAQSEEKLVYILPLERTNKFPELYRDLdrCSNQGIEDYGVSITTLNEVF 788
Cdd:COG4152 222 -RNTLRLEADG--DAGWLRAL-------PGVTVVEEDGDGAELKLEDGADAQELLRAL--LARGPVREFEEVRPSLNEIF 289
|
....*..
gi 27477115 789 LKLEGKS 795
Cdd:COG4152 290 IEVVGEK 296
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
481-694 |
3.26e-36 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 137.31 E-value: 3.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGL-----SVPTSGSVTVYNHTL-SRMADI 554
Cdd:cd03260 1 IELRDLNVYYGDK----HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIyDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 555 ENISKFTGFCPQSNVQFGfLTVKENLRLFAKIKGILPHEVEKEvqRVVQELEM----ENIQDIL-AQNLSGGQNRKLTFG 629
Cdd:cd03260 77 LELRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDE--RVEEALRKaalwDEVKDRLhALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 630 IAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVILFSTQFIDEADILADRKVFISNGKL 694
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1308-1498 |
5.52e-36 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 136.41 E-value: 5.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGS--GGGEP-----LGfLGYCPQENALWPNLTVR 1380
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRdiTGLPPherarAG-IGYVPEGRRIFPELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1381 QHLEVYAAVKGLRKGDAMIAitRLVDAL-KLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1459
Cdd:cd03224 94 ENLLLGAYARRRAKRKARLE--RVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEI 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 27477115 1460 WQVIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1498
Cdd:cd03224 172 FEAIR-ELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1270-1498 |
6.90e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 140.35 E-value: 6.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1270 NAMAVRDFDETPVIIA-SCLRKEYAGKkkncfskrkkkIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAG 1348
Cdd:PRK13536 28 EAKASIPGSMSTVAIDlAGVSKSYGDK-----------AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1349 QVILKGsgggEPL--------GFLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKT 1420
Cdd:PRK13536 97 KITVLG----VPVpararlarARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1421 LSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRATFrntERGA--LLTTHYMAEAEAVCDRVAIMVSGR 1498
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLL---ARGKtiLLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
481-796 |
1.01e-35 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 149.39 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKCErvEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLsrMADIENISKF 560
Cdd:TIGR01257 1938 LRLNELTKVYSGTSS--PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTNISDVHQN 2013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLL 640
Cdd:TIGR01257 2014 MGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 641 LDEPTAGLDPLSRHRIWN----LLKEGksdRVILFSTQFIDEADILADRKVFISNGKLKCAGSSLFLKKKWGIGYHLSLH 716
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNtivsIIREG---RAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMK 2170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 717 LNERCD-----------------PESITSlvKQHISDAKLTAQSEEkLVYILPLERTNKFPELyrdldrcsnqgIEDYGV 779
Cdd:TIGR01257 2171 IKSPKDdllpdlnpveqffqgnfPGSVQR--ERHYNMLQFQVSSSS-LARIFQLLISHKDSLL-----------IEEYSV 2236
|
330
....*....|....*..
gi 27477115 780 SITTLNEVFLKLEGKST 796
Cdd:TIGR01257 2237 TQTTLDQVFVNFAKQQT 2253
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
478-694 |
1.45e-35 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 135.92 E-value: 1.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 478 KEAIRIKNLKKEYAGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVynhtlsrmADIENI 557
Cdd:cd03267 15 KEPGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV--------AGLVPW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 558 SKFTGFCPQSNVQFGF-------LTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGI 630
Cdd:cd03267 87 KRRKKFLRRIGVVFGQktqlwwdLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 631 AILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDR--VILFSTQFIDEADILADRKVFISNGKL 694
Cdd:cd03267 167 ALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
480-693 |
1.52e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 138.01 E-value: 1.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGKCerveALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIENISk 559
Cdd:PRK13537 7 PIDFRNVEKRYGDKL----VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 fTGFCPQ-SNVQFGFlTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQV 638
Cdd:PRK13537 82 -VGVVPQfDNLDPDF-TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 639 LLLDEPTAGLDPLSRHRIW----NLLKEGKSdrvILFSTQFIDEADILADRKVFISNGK 693
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWerlrSLLARGKT---ILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
481-720 |
1.78e-34 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 133.71 E-value: 1.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGkcERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIENISKF 560
Cdd:TIGR04520 1 IEVENVSFSYPE--SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQS--NvQFGFLTVK-------ENLrlfakikGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKltfgIA 631
Cdd:TIGR04520 79 VGMVFQNpdN-QFVGATVEddvafglENL-------GVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQR----VA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 632 ILG----DPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDR--VILFSTQFIDEAdILADRKVFISNGKLKCAGS--SLFL 703
Cdd:TIGR04520 147 IAGvlamRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEA-VLADRVIVMNKGKIVAEGTprEIFS 225
|
250 260
....*....|....*....|....*
gi 27477115 704 K----KKWGIG----YHLSLHLNER 720
Cdd:TIGR04520 226 QvellKEIGLDvpfiTELAKALKKR 250
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
482-693 |
5.48e-34 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 128.52 E-value: 5.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 482 RIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRmadieniskft 561
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 562 gfcpqsnvqfgfltvkenlrlfakikgILPHEVEKEVQRVVQelemeniqdilaqnLSGGQNRKLTFGIAILGDPQVLLL 641
Cdd:cd00267 66 ---------------------------LPLEELRRRIGYVPQ--------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27477115 642 DEPTAGLDPLSRHRIWNLLKE-GKSDRVILFSTQFIDEADILADRKVFISNGK 693
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
480-733 |
8.06e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 134.19 E-value: 8.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGKCerveALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIENISk 559
Cdd:PRK13536 41 AIDLAGVSKSYGDKA----VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARAR- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 fTGFCPQ-SNVQFGFlTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQV 638
Cdd:PRK13536 116 -IGVVPQfDNLDLEF-TVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 639 LLLDEPTAGLDPLSRHRIW----NLLKEGKSdrvILFSTQFIDEADILADRKVFISNGKLKCAGSSLFLkkkwgIGYHLS 714
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWerlrSLLARGKT---ILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL-----IDEHIG 265
|
250 260
....*....|....*....|.
gi 27477115 715 LHLNE--RCDPESITSLVKQH 733
Cdd:PRK13536 266 CQVIEiyGGDPHELSSLVKPY 286
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
480-731 |
8.37e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 133.67 E-value: 8.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEY------AG-----------KCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVT 542
Cdd:COG4586 1 IIEVENLSKTYrvyekePGlkgalkglfrrEYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 543 VYNHTLSRmADIENISKFTgfcpqsnVQFG-------FLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILA 615
Cdd:COG4586 81 VLGYVPFK-RRKEFARRIG-------VVFGqrsqlwwDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 616 QNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDR---VILFSTqfiDEADI--LADRKVFIS 690
Cdd:COG4586 153 RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgttILLTSH---DMDDIeaLCDRVIVID 229
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 27477115 691 NGKLKCAGSSLFLKKKWGIGYHLSLHLNERCDPESITSLVK 731
Cdd:COG4586 230 HGRIIYDGSLEELKERFGPYKTIVLELAEPVPPLELPRGGE 270
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
480-699 |
8.38e-34 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 131.32 E-value: 8.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIEnISK 559
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE-LAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 FTGFCPQSNVQFGFLTVKENLRLfakikGILPH---------EVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGI 630
Cdd:COG1120 76 RIAYVPQEPPAPFGLTVRELVAL-----GRYPHlglfgrpsaEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27477115 631 AILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--GKSDRVILFSTQFIDEADILADRKVFISNGKLKCAGS 699
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1300-1503 |
2.01e-33 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 128.79 E-value: 2.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1300 FSKR-KKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGFL-------GYCPQEN 1371
Cdd:cd03259 6 LSKTyGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI----DGRDVTGVpperrniGMVFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1372 ALWPNLTVRQHLeVYA-AVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1450
Cdd:cd03259 82 ALFPHLTVAENI-AFGlKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27477115 1451 MDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1503
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
496-700 |
3.44e-33 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 128.95 E-value: 3.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 496 RVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIENISKFTGFCPQS-NVqFGFL 574
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYVPEGrRI-FPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 575 TVKENLRLFAKIKGIlPHEVEKEVQRVVqEL-----EMeniQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLD 649
Cdd:COG0410 94 TVEENLLLGAYARRD-RAEVRADLERVY-ELfprlkER---RRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27477115 650 PLSRHRIWNLLKEGKSDRV-ILFSTQFIDEADILADRKVFISNGKLKCAGSS 700
Cdd:COG0410 169 PLIVEEIFEIIRRLNREGVtILLVEQNARFALEIADRAYVLERGRIVLEGTA 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
480-699 |
3.62e-33 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 128.94 E-value: 3.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRM--ADIENI 557
Cdd:COG1127 5 MIEVRNLTKSFGDR----VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLseKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 558 SKFTGFCPQSNVQFGFLTVKENLRLFAKIKGILPhevEKEVQRVVQE-LEM---ENIQDILAQNLSGGQNRKLtfGIA-- 631
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLREHTDLS---EAEIRELVLEkLELvglPGAADKMPSELSGGMRKRV--ALAra 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27477115 632 ILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDrviLFSTQFI-----DEADILADRKVFISNGKLKCAGS 699
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDE---LGLTSVVvthdlDSAFAIADRVAVLADGKIIAEGT 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1308-1499 |
4.31e-33 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 128.71 E-value: 4.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG-SGGGEP------LGfLGYCPQENALWPNLTVR 1380
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeDITGLPpheiarLG-IGRTFQIPRLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1381 QHLEVyAAVKGLRKGDAMI-----------AITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPST 1449
Cdd:cd03219 94 ENVMV-AAQARTGSGLLLArarreereareRAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27477115 1450 GMDPEGQQQMWQVIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:cd03219 173 GLNPEETEELAELIRE-LRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
481-694 |
2.32e-32 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 125.71 E-value: 2.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGkcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIE-NIsk 559
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERrNI-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 ftGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVL 639
Cdd:cd03259 75 --GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 640 LLDEPTAGLDPLSRHRIWNLLKE--GKSDRVILFSTQFIDEADILADRKVFISNGKL 694
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
481-694 |
2.58e-32 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 126.54 E-value: 2.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIE--NIS 558
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 559 KFTGFCPQsnvQFGFL---TVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGD 635
Cdd:cd03258 82 RRIGMIFQ---HFNLLssrTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27477115 636 PQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDR--VILFSTQFIDEADILADRKVFISNGKL 694
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
480-694 |
3.12e-32 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 126.84 E-value: 3.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIEnisk 559
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 ftgFCPQsnVQFGF----------LTVKENLRLFAKIKGILphEVEKEVQRVVQELEM-ENIQDILAQNLSGGQNRKLTF 628
Cdd:COG1124 77 ---FRRR--VQMVFqdpyaslhprHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 629 GIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDR--VILFSTQFIDEADILADRKVFISNGKL 694
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1308-1499 |
3.97e-32 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 126.69 E-value: 3.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGS--GGGEP-----LG----FlgycpQENALWPN 1376
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRdiTGLPPhriarLGiartF-----QNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1377 LTVRQHLEVyAAVKGLRKG----------------DAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPS 1440
Cdd:COG0411 94 LTVLENVLV-AAHARLGRGllaallrlprarreerEARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27477115 1441 VVLLDEPSTGMDPEGQQQMWQVIRATfrNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:COG0411 173 LLLLDEPAAGLNPEETEELAELIRRL--RDERGItiLLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
481-694 |
4.66e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 125.16 E-value: 4.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADiENISKF 560
Cdd:COG2884 2 IRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKR-REIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 ---TGFCPQSnvqFGFL---TVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLtfGI--AI 632
Cdd:COG2884 78 rrrIGVVFQD---FRLLpdrTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRV--AIarAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 633 LGDPQVLLLDEPTAGLDPLSRHRIWNLLKE----GKSdrvILFST---QFIDEadiLADRKVFISNGKL 694
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEIMELLEEinrrGTT---VLIAThdlELVDR---MPKRVLELEDGRL 215
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
481-700 |
6.29e-32 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 125.35 E-value: 6.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKCerveALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIENISKF 560
Cdd:cd03218 1 LRAENLSKRYGKRK----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLL 640
Cdd:cd03218 77 IGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27477115 641 LDEPTAGLDPLSRHRIWNLLKEGKSDRV-ILFSTQFIDEADILADRKVFISNGKLKCAGSS 700
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRGIgVLITDHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
481-699 |
6.91e-32 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 125.24 E-value: 6.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGkcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVtVYNHTlsrmaDIeniskf 560
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSV-LFDGE-----DI------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQFGF------------LTVKENLRL---FAKIKGILP-------HEVEKEVQRVVQELEMENIQDILAQNL 618
Cdd:cd03219 65 TGLPPHEIARLGIgrtfqiprlfpeLTVLENVMVaaqARTGSGLLLararreeREARERAEELLERVGLADLADRPAGEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 619 SGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-GKSDRVILfstqFIdEADI-----LADRKVFISNG 692
Cdd:cd03219 145 SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRElRERGITVL----LV-EHDMdvvmsLADRVTVLDQG 219
|
....*..
gi 27477115 693 KLKCAGS 699
Cdd:cd03219 220 RVIAEGT 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1310-1449 |
7.26e-32 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 121.99 E-value: 7.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG-----SGGGEPLGFLGYCPQENALWPNLTVRQHLE 1384
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdDERKSLRKEIGYVFQDPQLFPRLTVRENLR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 1385 VYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPV----KTLSEGIKRKLCFVLSILGNPSVVLLDEPST 1449
Cdd:pfam00005 82 LGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
500-694 |
9.75e-32 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 123.43 E-value: 9.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 500 LKGVVFDIYEGQITALLGHSGAGKTTLLNILSGL--SVPTSGSVTVYNHTLSRmadiENISKFTGFCPQSNVQFGFLTVK 577
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDK----RSFRKIIGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 578 ENLRLFAKIKGIlphevekevqrvvqelemeniqdilaqnlSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIW 657
Cdd:cd03213 101 ETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 27477115 658 NLLKE-GKSDRVILFST-QFIDEADILADRKVFISNGKL 694
Cdd:cd03213 152 SLLRRlADTGRTIICSIhQPSSEIFELFDKLLLLSQGRV 190
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1299-1519 |
1.09e-31 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 124.37 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1299 CFSKRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLG---------FLGYCPQ 1369
Cdd:COG1122 7 SFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLV----DGKDITkknlrelrrKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1370 --ENALWpNLTVRQhlEV-YAAV-KGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCF--VLSIlgNPSVVL 1443
Cdd:COG1122 83 npDDQLF-APTVEE--DVaFGPEnLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIagVLAM--EPEVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 1444 LDEPSTGMDPEGQQQMWQVIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLkskFGKDYLLE 1519
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKR-LNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV---FSDYELLE 229
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
481-693 |
1.61e-31 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 122.11 E-value: 1.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKceRVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLsRMADIENISKF 560
Cdd:cd03228 1 IEFKNVSFSYPGR--PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDL-RDLDLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQFGFlTVKENLrlfakikgilphevekevqrvvqelemeniqdilaqnLSGGQNRKLTFGIAILGDPQVLL 640
Cdd:cd03228 78 IAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27477115 641 LDEPTAGLDPLSRHRIWNLLKEGKSDRVILFSTQFIDEADiLADRKVFISNGK 693
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
481-694 |
1.80e-31 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 123.77 E-value: 1.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHtlsrmaDIENISKF 560
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGK------DLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQFGF----------LTVKENLRLFAKIKGILPHEVEKEvQRVVQELEM----ENIQDILAQNLSGGQNRKL 626
Cdd:cd03257 76 LRKIRRKEIQMVFqdpmsslnprMTIGEQIAEPLRIHGKLSKKEARK-EAVLLLLVGvglpEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 627 TFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDR--VILFSTQFIDEADILADRKVFISNGKL 694
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
481-693 |
2.50e-31 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 121.53 E-value: 2.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIENISKF 560
Cdd:cd03229 1 LELKNVSKRYGQK----TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 -TGFCPQSNVQFGFLTVKENLRLfakikgilphevekevqrvvqelemeniqdilaqNLSGGQNRKLTFGIAILGDPQVL 639
Cdd:cd03229 77 rIGMVFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 640 LLDEPTAGLDPLSRHRIWNLLKE--GKSDRVILFSTQFIDEADILADRKVFISNGK 693
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSlqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1301-1504 |
3.04e-31 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 123.42 E-value: 3.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1301 SKR-KKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSG-GGEP------LGfLGYCPQENA 1372
Cdd:cd03218 7 SKRyGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDiTKLPmhkrarLG-IGYLPQEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1373 LWPNLTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1452
Cdd:cd03218 86 IFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27477115 1453 PEGQQQMWQVIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1504
Cdd:cd03218 166 PIAVQDIQKIIK-ILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGT 216
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1302-1498 |
5.41e-31 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 121.81 E-value: 5.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1302 KRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG-----SGGGEPLGFLGYCPQEnalwP- 1375
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltkLSLKELRRKVGLVFQN----Pd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1376 ----NLTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCfVLSIL-GNPSVVLLDEPSTG 1450
Cdd:cd03225 86 dqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVA-IAGVLaMDPDILLLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27477115 1451 MDPEGQQQMWQVIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1498
Cdd:cd03225 165 LDPAGRRELLELLK-KLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
482-662 |
5.74e-31 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 123.23 E-value: 5.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 482 RIKNLKKEYAGkcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIEnISK-- 559
Cdd:COG0411 6 EVRGLTKRFGG----LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHR-IARlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 ----FtgfcpQsNVQ-FGFLTVKENLRL---------FAKIKGILP------HEVEKEVQRVVQELEMENIQDILAQNLS 619
Cdd:COG0411 81 iartF-----Q-NPRlFPELTVLENVLVaaharlgrgLLAALLRLPrarreeREARERAEELLERVGLADRADEPAGNLS 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27477115 620 GGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE 662
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRR 197
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
477-700 |
6.62e-31 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 129.25 E-value: 6.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 477 GKEAIRIKNLKKEYAGKC-ERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADiE 555
Cdd:COG1123 257 AEPLLEVRNLSKRYPVRGkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSR-R 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 556 NISKFtgfcpQSNVQFGF----------LTVKENLRLFAKIKGILPHEVEKEvqRVVQELEM----ENIQDILAQNLSGG 621
Cdd:COG1123 336 SLREL-----RRRVQMVFqdpysslnprMTVGDIIAEPLRLHGLLSRAERRE--RVAELLERvglpPDLADRYPHELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 622 QNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-----GKSdrvILFSTQFIDEADILADRKVFISNGKLKC 696
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDlqrelGLT---YLFISHDLAVVRYIADRVAVMYDGRIVE 485
|
....
gi 27477115 697 AGSS 700
Cdd:COG1123 486 DGPT 489
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
480-694 |
9.29e-31 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 122.47 E-value: 9.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGKcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRM--ADIENI 557
Cdd:COG3638 2 MLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALrgRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 558 SKFTGFCPQsnvQFGF---LTVKEN--------LRLFAKIKGILPHEvekEVQRVVQELEMENIQDILAQ---NLSGGQN 623
Cdd:COG3638 79 RRRIGMIFQ---QFNLvprLSVLTNvlagrlgrTSTWRSLLGLFPPE---DRERALEALERVGLADKAYQradQLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 624 RKLtfGIA--ILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-GKSDRV-ILFSTQFIDEADILADRKVFISNGKL 694
Cdd:COG3638 153 QRV--AIAraLVQEPKLILADEPVASLDPKTARQVMDLLRRiAREDGItVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
482-695 |
1.13e-30 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 120.82 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 482 RIKNLKKEYAGKcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIENIskft 561
Cdd:cd03226 1 RIENISFSYKKG---TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSI---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 562 GFCPQ-SNVQFGFLTVKENLRLFAKikgiLPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLL 640
Cdd:cd03226 74 GYVMQdVDYQLFTDSVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 641 LDEPTAGLDPLSRHRIWNLLKE-GKSDRVILFSTQFIDEADILADRKVFISNGKLK 695
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
480-699 |
1.57e-30 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 128.72 E-value: 1.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGkceRVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMaDIENISK 559
Cdd:COG4988 336 SIELEDVSFSYPG---GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDL-DPASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 FTGFCPQSNVQFGfLTVKENLRLFAkikgilPHEVEKEVQRVVQELemeNIQDILAQ--------------NLSGGQNRK 625
Cdd:COG4988 412 QIAWVPQNPYLFA-GTIRENLRLGR------PDASDEELEAALEAA---GLDEFVAAlpdgldtplgeggrGLSGGQAQR 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 626 LTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVILFSTQfiDEADI-LADRKVFISNGKLKCAGS 699
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITH--RLALLaQADRILVLDDGRIVEQGT 554
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
480-713 |
2.65e-30 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 128.35 E-value: 2.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGkcERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADiENISK 559
Cdd:COG4987 333 SLELEDVSFRYPG--AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDE-DDLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 FTGFCPQSNVQF-GflTVKENLRLfAKikgilPHEVEKEVQRVvqeLEMENIQDILAQ--------------NLSGGQNR 624
Cdd:COG4987 410 RIAVVPQRPHLFdT--TLRENLRL-AR-----PDATDEELWAA---LERVGLGDWLAAlpdgldtwlgeggrRLSGGERR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 625 KLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVILFSTQFIDEADiLADRKVFISNGKLKCAGSSLFLK 704
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE-RMDRILVLEDGRIVEQGTHEELL 557
|
....*....
gi 27477115 705 KKWGIGYHL 713
Cdd:COG4987 558 AQNGRYRQL 566
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1302-1498 |
2.66e-30 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 118.12 E-value: 2.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1302 KRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGsgggeplgflgycpQENALWPNLTVRQ 1381
Cdd:cd00267 8 RYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG--------------KDIAKLPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1382 HLevyaavkglrkgdamiaitrlvdALKLQdqlkapvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ 1461
Cdd:cd00267 74 RI-----------------------GYVPQ---------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLE 121
|
170 180 190
....*....|....*....|....*....|....*..
gi 27477115 1462 VIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1498
Cdd:cd00267 122 LLRE-LAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1301-1505 |
4.16e-30 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 120.57 E-value: 4.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1301 SKRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGGGePLGFLGycpqenALWPNLTVR 1380
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSA-LLELGA------GFHPELTGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1381 QHLEVYAAVKGLRKGDamiaITRLVDALK----LQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP-STGmDPEG 1455
Cdd:COG1134 107 ENIYLNGRLLGLSRKE----IDEKFDEIVefaeLGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVlAVG-DAAF 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27477115 1456 QQQMWQVIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSI 1505
Cdd:COG1134 182 QKKCLARIRE-LRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1302-1503 |
6.54e-30 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 119.17 E-value: 6.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1302 KRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGGGePLGFLGycpqenALWPNLTVRQ 1381
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS-LLGLGG------GFNPELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1382 HLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP-STGmDPEGQQQMW 1460
Cdd:cd03220 104 NIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVlAVG-DAAFQEKCQ 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27477115 1461 QVIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1503
Cdd:cd03220 183 RRLR-ELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1310-1498 |
7.82e-30 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 119.32 E-value: 7.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGS--GGGEP-----LGfLGYCPQENALWPNLTVRQH 1382
Cdd:COG0410 20 HGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEdiTGLPPhriarLG-IGYVPEGRRIFPSLTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1383 LEVYAAVKGLRKGDAMIAitRLVDAL--KLQDQLKAPVKTLSEG------IKRKLcfvlsiLGNPSVVLLDEPSTGMDPE 1454
Cdd:COG0410 99 LLLGAYARRDRAEVRADL--ERVYELfpRLKERRRQRAGTLSGGeqqmlaIGRAL------MSRPKLLLLDEPSLGLAPL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27477115 1455 GQQQMWQVIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1498
Cdd:COG0410 171 IVEEIFEIIR-RLNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
480-699 |
8.84e-30 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 119.37 E-value: 8.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYagkcERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIE-NIs 558
Cdd:cd03296 2 SIEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQErNV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 559 kftGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQEL----EMENIQDILAQNLSGGQNRKLTFGIAILG 634
Cdd:cd03296 77 ---GFVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELlklvQLDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 635 DPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVI--LFSTQFIDEADILADRKVFISNGKLKCAGS 699
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVttVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1281-1504 |
1.26e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 118.98 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1281 PVIIASCLRKEYagkkkncfskrKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEP 1360
Cdd:COG1137 2 MTLEAENLVKSY-----------GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFL----DGED 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1361 -----------LGfLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKL 1429
Cdd:COG1137 67 ithlpmhkrarLG-IGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 1430 CFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRatfRNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1504
Cdd:COG1137 146 EIARALATNPKFILLDEPFAGVDPIAVADIQKIIR---HLKERGIgvLITDHNVRETLGICDRAYIISEGKVLAEGT 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
481-694 |
2.10e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 117.22 E-value: 2.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMaDIENISKF 560
Cdd:COG4619 1 LELEGLSFRVGGK----PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM-PPPEWRRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQFGfLTVKENLRLFAKIKGILPHEveKEVQRVVQELEMEniQDIL---AQNLSGGQNRKLTFGIAILGDPQ 637
Cdd:COG4619 76 VAYVPQEPALWG-GTVRDNLPFPFQLRERKFDR--ERALELLERLGLP--PDILdkpVERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 638 VLLLDEPTAGLDPLSRHRIWNLLKE--GKSDRVILFSTQFIDEADILADRKVFISNGKL 694
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1305-1507 |
2.63e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 118.27 E-value: 2.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1305 KKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGGGEPLGFLGYCPQENALWPN--LTVRqh 1382
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQRAEVDWDfpITVR-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1383 lEV-----YAAV---KGLRKGDAMiAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1454
Cdd:COG1121 96 -DVvlmgrYGRRglfRRPSRADRE-AVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27477115 1455 GQQQMWQVIRAtFRNTERGALLTTHYMAEAEAVCDRVaIMVSGRLRCIGSIQH 1507
Cdd:COG1121 174 TEEALYELLRE-LRREGKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGPPEE 224
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
482-699 |
2.77e-29 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 117.63 E-value: 2.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 482 RIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIENISKFT 561
Cdd:TIGR03410 2 EVSNLNVYYGQS----HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 562 GFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVqrvvqeLEM----ENIQDILAQNLSGGQNRKLTFGIAILGDPQ 637
Cdd:TIGR03410 78 AYVPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEI------YELfpvlKEMLGRRGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 638 VLLLDEPTAGLDP---LSRHRIWNLLKEGKsDRVILFSTQFIDEADILADRKVFISNGKLKCAGS 699
Cdd:TIGR03410 152 LLLLDEPTEGIQPsiiKDIGRVIRRLRAEG-GMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
480-694 |
2.97e-29 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 120.97 E-value: 2.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGkcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMA----DIe 555
Cdd:COG3842 5 ALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPpekrNV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 556 niskftGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQN------Rkltfg 629
Cdd:COG3842 80 ------GMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQqrvalaR----- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477115 630 iAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-----GKSdrvILFST--QfiDEADILADRKVFISNGKL 694
Cdd:COG3842 149 -ALAPEPRVLLLDEPLSALDAKLREEMREELRRlqrelGIT---FIYVThdQ--EEALALADRIAVMNDGRI 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
480-699 |
3.26e-29 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 124.25 E-value: 3.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGkcERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPT---SGSVTVYNHTLSRMaDIEN 556
Cdd:COG1123 4 LLEVRDLSVRYPG--GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLEL-SEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 557 ISKFTGFCPQS-NVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGD 635
Cdd:COG1123 81 RGRRIGMVFQDpMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 636 PQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDR--VILFSTQFIDEADILADRKVFISNGKLKCAGS 699
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
482-698 |
4.84e-29 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 116.48 E-value: 4.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 482 RIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNhtlsrmADIENISKFT 561
Cdd:cd03235 1 EVEDLTVSYGGH----PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG------KPLEKERKRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 562 GFCPQS-NVQFGF-LTVKE--NLRLFAKIK--GILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGD 635
Cdd:cd03235 71 GYVPQRrSIDRDFpISVRDvvLMGLYGHKGlfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477115 636 PQVLLLDEPTAGLDPLSRHRIWNLLKEGKSD-RVILFSTQFIDEADILADRKVFIsNGKLKCAG 698
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
480-699 |
5.72e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.11 E-value: 5.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMadieniSK 559
Cdd:COG1121 6 AIELENLTVSYGGR----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA------RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 FTGFCPQ-SNVQFGF-LTVKE--------NLRLFakikGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFG 629
Cdd:COG1121 76 RIGYVPQrAEVDWDFpITVRDvvlmgrygRRGLF----RRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27477115 630 IAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-GKSDRVILFSTQFIDEADILADRKVFIsNGKLKCAGS 699
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGP 221
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
481-715 |
5.72e-29 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 117.94 E-value: 5.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKC--ERVeALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTL--SRMADIEN 556
Cdd:TIGR04521 1 IKLKNVSYIYQPGTpfEKK-ALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItaKKKKKLKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 557 ISKFTGFcpqsnV-QFgfltvKENlRLFAKikgilphEVEKEV---------------QRVVQELEMENI-QDILAQN-- 617
Cdd:TIGR04521 80 LRKKVGL-----VfQF-----PEH-QLFEE-------TVYKDIafgpknlglseeeaeERVKEALELVGLdEEYLERSpf 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 618 -LSGGQNRKltfgIAILG----DPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDR---VILFSTQfIDEADILADRKVFI 689
Cdd:TIGR04521 142 eLSGGQMRR----VAIAGvlamEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKgltVILVTHS-MEDVAEYADRVIVM 216
|
250 260
....*....|....*....|....*...
gi 27477115 690 SNGKLKCAGSS--LFLKKKWGIGYHLSL 715
Cdd:TIGR04521 217 HKGKIVLDGTPreVFSDVDELEKIGLDV 244
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1309-1503 |
7.33e-29 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 115.86 E-value: 7.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1309 TRNVSFCVKkGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGS--GGGEPLGFL-------GYCPQENALWPNLTV 1379
Cdd:cd03297 14 TLKIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlFDSRKKINLppqqrkiGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1380 RQHLEVyaAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1459
Cdd:cd03297 93 RENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27477115 1460 WQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1503
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
482-698 |
8.36e-29 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 114.45 E-value: 8.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 482 RIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMadieniskft 561
Cdd:cd03214 1 EVENLSVGYGGR----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASL---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 562 gfcpqsnvqfgfltvkeNLRLFAKIKGILPhevekevqrvvQELEMENIQDILAQN---LSGGQNRKLTFGIAILGDPQV 638
Cdd:cd03214 67 -----------------SPKELARKIAYVP-----------QALELLGLAHLADRPfneLSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477115 639 LLLDEPTAGLDPLSRHRIWNLLKE--GKSDRVILFSTQFIDEADILADRKVFISNGKLKCAG 698
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
480-699 |
8.48e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 117.40 E-value: 8.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGkcERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRmADIENISK 559
Cdd:PRK13632 7 MIKVENVSFSYPN--SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK-ENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 FTGFCPQS-NVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQV 638
Cdd:PRK13632 84 KIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27477115 639 LLLDEPTAGLDPLSRHRIWNLLKE--GKSDRVILFSTQFIDEAdILADRKVFISNGKLKCAGS 699
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGK 225
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1310-1504 |
9.85e-29 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 116.68 E-value: 9.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLG---------FLGYCPQENALWPNLTVR 1380
Cdd:COG1120 18 DDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLL----DGRDLAslsrrelarRIAYVPQEPPAPFGLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1381 Q--------HL--------EVYAAVKglrkgDAMiaitRLVDALKLQDQlkaPVKTLSEGIKRKLCFVLSILGNPSVVLL 1444
Cdd:COG1120 94 ElvalgrypHLglfgrpsaEDREAVE-----EAL----ERTGLEHLADR---PVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1445 DEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1504
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
481-694 |
1.84e-28 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 115.47 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRM--ADIENIS 558
Cdd:TIGR02315 2 LEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrgKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 559 KFTGFCPQSNVQFGFLTVKENL---RLFAK--IKGILPHEVEKEVQRVVQELEMENIQD---ILAQNLSGGQNRKLTFGI 630
Cdd:TIGR02315 79 RRIGMIFQHYNLIERLTVLENVlhgRLGYKptWRSLLGRFSEEDKERALSALERVGLADkayQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 631 AILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-----GKSdrvILFSTQFIDEADILADRKVFISNGKL 694
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRinkedGIT---VIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
481-695 |
1.93e-28 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 114.80 E-value: 1.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRmADIENIskf 560
Cdd:TIGR03740 1 LETKNLSKRFGKQ----TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR-KDLHKI--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 tGFCPQSNVQFGFLTVKENLRLFAKIKGiLPhevEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLL 640
Cdd:TIGR03740 73 -GSLIESPPLYENLTARENLKVHTTLLG-LP---DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLI 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 641 LDEPTAGLDPLSRHRIWNLLKEGKSDRV-ILFSTQFIDEADILADRKVFISNGKLK 695
Cdd:TIGR03740 148 LDEPTNGLDPIGIQELRELIRSFPEQGItVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
481-694 |
3.06e-28 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 117.94 E-value: 3.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGkcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSV-----TVYNHTLSRMADIe 555
Cdd:COG1118 3 IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIvlngrDLFTNLPPRERRV- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 556 niskftGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQN------RKLtfg 629
Cdd:COG1118 78 ------GFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRqrvalaRAL--- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 630 iAIlgDPQVLLLDEPTAGLDPLSRH--RIW--NLLKEgkSDRVILFSTQFIDEADILADRKVFISNGKL 694
Cdd:COG1118 149 -AV--EPEVLLLDEPFGALDAKVRKelRRWlrRLHDE--LGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
453-713 |
5.50e-28 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 122.25 E-value: 5.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 453 VLENETDSDPTPNDcfePVSPEFCGkeAIRIKNLKKEYAGkcERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSG 532
Cdd:COG2274 451 ILDLPPEREEGRSK---LSLPRLKG--DIELENVSFRYPG--DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 533 LSVPTSGSVTVYNHTLSRMaDIENISKFTGFCPQSNVQF-GflTVKENLRLFAkikgilPHEVEKEVQRVVQELEMEniQ 611
Cdd:COG2274 524 LYEPTSGRILIDGIDLRQI-DPASLRRQIGVVLQDVFLFsG--TIRENITLGD------PDATDEEIIEAARLAGLH--D 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 612 DILA-------------QNLSGGQNRKLtfGIA--ILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVILFSTQ-- 674
Cdd:COG2274 593 FIEAlpmgydtvvgeggSNLSGGQRQRL--AIAraLLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHrl 670
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 27477115 675 -FIDeadiLADRKVFISNGKLKCAGSSLFLKKKWGIGYHL 713
Cdd:COG2274 671 sTIR----LADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1300-1498 |
6.12e-28 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 111.90 E-value: 6.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1300 FSKR-KKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGFL-----------GYC 1367
Cdd:cd03229 6 VSKRyGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILI----DGEDLTDLedelpplrrriGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1368 PQENALWPNLTVRQHLeVYAavkglrkgdamiaitrlvdalklqdqlkapvktLSEGIKRKLCFVLSILGNPSVVLLDEP 1447
Cdd:cd03229 82 FQDFALFPHLTVLENI-ALG---------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27477115 1448 STGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1498
Cdd:cd03229 128 TSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1283-1498 |
8.24e-28 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 112.95 E-value: 8.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1283 IIASCLRKEYAGKkkncfskRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGGGEPLG 1362
Cdd:cd03293 1 LEVRNVSKTYGGG-------GGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1363 FLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVV 1442
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 1443 LLDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMvSGR 1498
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL-SAR 208
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
481-694 |
9.12e-28 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 112.73 E-value: 9.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHtlsRMADIENISKF 560
Cdd:cd03301 1 VELENVTKRFGNV----TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR---DVTDLPPKDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLL 640
Cdd:cd03301 74 IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 641 LDEPTAGLDPLSRHRIWNLLKE--GKSDRVILFSTQFIDEADILADRKVFISNGKL 694
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1301-1504 |
1.32e-27 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 116.35 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1301 SKR-KKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGFL-------GYCPQENA 1372
Cdd:COG3842 12 SKRyGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILL----DGRDVTGLppekrnvGMVFQDYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1373 LWPNLTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEG------IKRKLCFvlsilgNPSVVLLDE 1446
Cdd:COG3842 88 LFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGqqqrvaLARALAP------EPRVLLLDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 1447 PSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1504
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGT 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
481-662 |
1.47e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 112.82 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVynhtlsrmaDIENISKF 560
Cdd:COG1137 4 LEAENLVKSYGKR----TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFL---------DGEDITHL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 T---------GFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIA 631
Cdd:COG1137 71 PmhkrarlgiGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARA 150
|
170 180 190
....*....|....*....|....*....|....
gi 27477115 632 ILGDPQVLLLDEPTAGLDPLSRHRIWNL---LKE 662
Cdd:COG1137 151 LATNPKFILLDEPFAGVDPIAVADIQKIirhLKE 184
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1306-1503 |
1.63e-27 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 111.86 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1306 KIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGGGEPLGFLGYCPQ-ENALW--PnLTVRQ- 1381
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQrRSIDRdfP-ISVRDv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1382 -------HLEVYAAVKGLRKGDAMIAITRlVDALKLQDQlkaPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1454
Cdd:cd03235 91 vlmglygHKGLFRRLSKADKAKVDEALER-VGLSELADR---QIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27477115 1455 GQQQMWQVIRaTFRNTERGALLTTHYMAEAEAVCDRVaIMVSGRLRCIG 1503
Cdd:cd03235 167 TQEDIYELLR-ELRREGMTILVVTHDLGLVLEYFDRV-LLLNRTVVASG 213
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
486-694 |
1.74e-27 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 112.36 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 486 LKKEYAGKCERVeaLKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLsVP----TSGSVTVYNHTLSRmadiENISKFT 561
Cdd:cd03234 11 LKAKNWNKYARI--LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR-VEgggtTSGQILFNGQPRKP----DQFQKCV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 562 GFCPQSNVQFGFLTVKENLRLFAKIKgiLPHEVEKEVQRVVQELEMEN------IQDILAQNLSGGQNRKLTFGIAILGD 635
Cdd:cd03234 84 AYVRQDDILLPGLTVRETLTYTAILR--LPRKSSDAIRKKRVEDVLLRdlaltrIGGNLVKGISGGERRRVSIAVQLLWD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477115 636 PQVLLLDEPTAGLDPLSRHRIWNLLKE-GKSDRVILFStqfIDE--ADI--LADRKVFISNGKL 694
Cdd:cd03234 162 PKVLILDEPTSGLDSFTALNLVSTLSQlARRNRIVILT---IHQprSDLfrLFDRILLLSSGEI 222
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
479-690 |
2.70e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 112.65 E-value: 2.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 479 EAIRIKNLKKEYAGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLsrmadienis 558
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 559 kfTG--------FcpQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLtfGI 630
Cdd:COG4525 72 --TGpgadrgvvF--QKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRV--GI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477115 631 A--ILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--GKSDRVILFSTQFIDEADILADRKVFIS 690
Cdd:COG4525 146 AraLAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITHSVEEALFLATRLVVMS 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
481-693 |
2.90e-27 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 112.28 E-value: 2.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRM--ADIENIS 558
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 559 KFTGFCPQS-----------NVQFGFLTVKENLRLFAkikGILPhevEKEVQRVVQELEMENIQD---ILAQNLSGGQNR 624
Cdd:cd03256 78 RQIGMIFQQfnlierlsvleNVLSGRLGRRSTWRSLF---GLFP---KEEKQRALAALERVGLLDkayQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27477115 625 KLtfGIA--ILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--GKSDRVILFSTQFIDEADILADRKVFISNGK 693
Cdd:cd03256 152 RV--AIAraLMQQPKLILADEPVASLDPASSRQVMDLLKRinREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
481-694 |
3.01e-27 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 112.01 E-value: 3.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGkceRVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIE---NI 557
Cdd:cd03295 1 IEFENVTKRYGG---GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrrKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 558 skftGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQ--ELEMENIQDILAQNLSGGQNRKLTFGIAILGD 635
Cdd:cd03295 78 ----GYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLAlvGLDPAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27477115 636 PQVLLLDEPTAGLDPLSRHRIWNLLKEGKSD--RVILFSTQFIDEADILADRKVFISNGKL 694
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
481-662 |
3.48e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 114.40 E-value: 3.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIE--NIS 558
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElrAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 559 KFTGFCPQsnvQFGFL---TVKENLRLFAKIKGILPHEVEKevqRVVQELEMENIQDILAQ---NLSGGQNRKLtfGIA- 631
Cdd:COG1135 82 RKIGMIFQ---HFNLLssrTVAENVALPLEIAGVPKAEIRK---RVAELLELVGLSDKADAypsQLSGGQKQRV--GIAr 153
|
170 180 190
....*....|....*....|....*....|..
gi 27477115 632 -ILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE 662
Cdd:COG1135 154 aLANNPKVLLCDEATSALDPETTRSILDLLKD 185
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
481-699 |
5.03e-27 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 111.17 E-value: 5.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHtlsrmaDIENISKF 560
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK------DITNLPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 -----TGFcpQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGD 635
Cdd:cd03300 71 krpvnTVF--QNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 636 PQVLLLDEPTAGLDPLSRHRIWNLLKEgKSDRV---ILFSTQFIDEADILADRKVFISNGKLKCAGS 699
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKR-LQKELgitFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
480-694 |
8.70e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 113.63 E-value: 8.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGkcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHtlsRMADIE---- 555
Cdd:COG3839 3 SLELENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGR---DVTDLPpkdr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 556 NIskftGFCPQSNVQFGFLTVKENLrLFA-KIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILG 634
Cdd:COG3839 76 NI----AMVFQSYALYPHMTVYENI-AFPlKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 635 DPQVLLLDEPTAGLDPLSRHR----IWNLLKEGKSdrVILFST--QfiDEADILADRKVFISNGKL 694
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKLRVEmraeIKRLHRRLGT--TTIYVThdQ--VEAMTLADRIAVMNDGRI 212
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
481-694 |
1.52e-26 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 109.16 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLS-RMADIENISK 559
Cdd:cd03262 1 IEIKNLHKSFGDF----HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTdDKKNINELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 FTGFCPQSNVQFGFLTVKENLRL-FAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQV 638
Cdd:cd03262 77 KVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 639 LLLDEPTAGLDPLSRHRIWNLLKE-GKSDRVILFSTQFIDEADILADRKVFISNGKL 694
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
481-694 |
1.86e-26 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 109.03 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMAD--IENIS 558
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 559 KFTGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQV 638
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 639 LLLDEPTAGLDPLSRHRIWNLLKE-GKSDRVILFSTQFIDEADILADRKVFISNGKL 694
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKiNKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
481-694 |
2.02e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 110.55 E-value: 2.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAgkcERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLS-RMADIENISK 559
Cdd:PRK13639 2 LETRDLKYSYP---DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 FTGFCPQ-SNVQFGFLTVKENLRlFAKIKGILPH-EVEKEVQRVVQELEMENIQDILAQNLSGGQNRKltfgIAILG--- 634
Cdd:PRK13639 79 TVGIVFQnPDDQLFAPTVEEDVA-FGPLNLGLSKeEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKR----VAIAGila 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477115 635 -DPQVLLLDEPTAGLDPLSRHRIWNLLKE-GKSDRVILFSTQFIDEADILADRKVFISNGKL 694
Cdd:PRK13639 154 mKPEIIVLDEPTSGLDPMGASQIMKLLYDlNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
510-698 |
2.33e-26 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 108.73 E-value: 2.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 510 GQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVY--NHTLSRMADIENISKFtgfcpQSNVQFGFLTVKENLRLfAKIK 587
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgvDVTAAPPADRPVSMLF-----QENNLFAHLTVEQNVGL-GLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 588 GILPHEVEKE-VQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSD 666
Cdd:cd03298 98 GLKLTAEDRQaIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAE 177
|
170 180 190
....*....|....*....|....*....|....
gi 27477115 667 R--VILFSTQFIDEADILADRKVFISNGKLKCAG 698
Cdd:cd03298 178 TkmTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
481-694 |
2.72e-26 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 108.77 E-value: 2.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEY------------------AGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVT 542
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 543 VynhtLSRMADIENISkfTGFCPQsnvqfgfLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQ 622
Cdd:cd03220 81 V----RGRVSSLLGLG--GGFNPE-------LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGM 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 623 NRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSD-RVILFSTQfiDEADI--LADRKVFISNGKL 694
Cdd:cd03220 148 KARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQgKTVILVSH--DPSSIkrLCDRALVLEKGKI 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
495-694 |
3.06e-26 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 108.45 E-value: 3.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 495 ERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVtVYNHTLSRMADIENISKFTGFCPQSNVQFgFL 574
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV-LLDGTDIRQLDPADLRRNIGYVPQDVTLF-YG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 575 TVKENLRLFAkikgilpheVEKEVQRVVQELEMENIQDILA--------------QNLSGGQNRKLTFGIAILGDPQVLL 640
Cdd:cd03245 93 TLRDNITLGA---------PLADDERILRAAELAGVTDFVNkhpngldlqigergRGLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 641 LDEPTAGLDPLSRHRIWNLLKEGKSDRVILFSTQ---FIDeadiLADRKVFISNGKL 694
Cdd:cd03245 164 LDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHrpsLLD----LVDRIIVMDSGRI 216
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
500-692 |
5.12e-26 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 108.32 E-value: 5.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 500 LKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLS-----RMADIENISKFTgfcpqsnvqfgFL 574
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITepgpdRMVVFQNYSLLP-----------WL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 575 TVKENLRLfaKIKGILPHEVEKEVQRVVQE-LEMENI---QDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDP 650
Cdd:TIGR01184 70 TVRENIAL--AVDRVLPDLSKSERRAIVEEhIALVGLteaADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27477115 651 LSRH-------RIWNllkegKSDRVILFSTQFIDEADILADRKVFISNG 692
Cdd:TIGR01184 148 LTRGnlqeelmQIWE-----EHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1310-1499 |
5.94e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 113.96 E-value: 5.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKgsggGEPLGFLGycP------------QENALWPNL 1377
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLD----GEPVRFRS--PrdaqaagiaiihQELNLVPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1378 TVRQ--HLEVYAAVKGLRKGDAMIAITR-LVDALKLQDQLKAPVKTLSEGiKRKLcfVL---SILGNPSVVLLDEPSTGM 1451
Cdd:COG1129 95 SVAEniFLGREPRRGGLIDWRAMRRRAReLLARLGLDIDPDTPVGDLSVA-QQQL--VEiarALSRDARVLILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27477115 1452 DPEGQQQMWQVIRaTFRntERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:COG1129 172 TEREVERLFRIIR-RLK--AQGVaiIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1308-1499 |
7.17e-26 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 105.59 E-value: 7.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGFLGycPQEnalwpnltvrqhlevya 1387
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV----DGKEVSFAS--PRD----------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1388 avkGLRKGDAMIAitrlvdalklQdqlkapvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRAtF 1467
Cdd:cd03216 72 ---ARRAGIAMVY----------Q---------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRR-L 128
|
170 180 190
....*....|....*....|....*....|..
gi 27477115 1468 RNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:cd03216 129 RAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
495-679 |
1.19e-25 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 105.97 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 495 ERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTL--SRMADIENISKFTGFCPQSNVQFG 572
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdySRKGLLERRQRVGLVFQDPDDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 573 FLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLS 652
Cdd:TIGR01166 83 AADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAG 162
|
170 180 190
....*....|....*....|....*....|.
gi 27477115 653 RHRIWNLLK----EGKSdrvILFSTQFIDEA 679
Cdd:TIGR01166 163 REQMLAILRrlraEGMT---VVISTHDVDLA 190
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1288-1499 |
1.21e-25 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 106.81 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1288 LRKEYAGKKKncfskrkKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLG----- 1362
Cdd:cd03255 6 LSKTYGGGGE-------KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRV----DGTDISklsek 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1363 --------FLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLS 1434
Cdd:cd03255 75 elaafrrrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 1435 ILGNPSVVLLDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAvCDRVAIMVSGRL 1499
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1278-1508 |
3.00e-25 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 111.92 E-value: 3.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1278 DETPVIIASCLRKEYAGKKKncfskrKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG--- 1354
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVRGK------GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdl 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1355 --SGGGEPLGF---LGYCPQ--ENALWPNLTVRQHL-EVYAAVKGLRKGDAMIAITRLVDALKLQ-DQLKAPVKTLSEGI 1425
Cdd:COG1123 330 tkLSRRSLRELrrrVQMVFQdpYSSLNPRMTVGDIIaEPLRLHGLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1426 KRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSI 1505
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPT 489
|
...
gi 27477115 1506 QHL 1508
Cdd:COG1123 490 EEV 492
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1280-1508 |
3.40e-25 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 111.92 E-value: 3.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1280 TPVIIASCLRKEYAGKKKNcfskrkkkiATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTA---GQVILKG-- 1354
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVP---------AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGrd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1355 ---SGGGEPLGFLGYCPQE--NALWPnLTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKL 1429
Cdd:COG1123 73 lleLSEALRGRRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 1430 CFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1508
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1300-1499 |
5.44e-25 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 105.28 E-value: 5.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1300 FSKRKKKI-ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG---SGGGEPL-----GFLGYCPQE 1370
Cdd:cd03257 11 FPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdlLKLSRRLrkirrKEIQMVFQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1371 --NALWPNLTVRQHL-EVYAAVKGLRKGDAM-IAITRLVDALKLQDQL--KAPVKtLSEGIKRKLCFVLSILGNPSVVLL 1444
Cdd:cd03257 91 pmSSLNPRMTIGEQIaEPLRIHGKLSKKEARkEAVLLLLVGVGLPEEVlnRYPHE-LSGGQRQRVAIARALALNPKLLIA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 1445 DEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:cd03257 170 DEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
481-694 |
7.96e-25 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 102.51 E-value: 7.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGkcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSrmadieniskf 560
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 tgfcpqsnvqfgFLTVKENLRLfakikGIlphevekevQRVVQelemeniqdilaqnLSGGQNRKLTFGIAILGDPQVLL 640
Cdd:cd03216 66 ------------FASPRDARRA-----GI---------AMVYQ--------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 641 LDEPTAGLDPLSRHRIWNLLKEGKSDRV-ILFSTQFIDEADILADRKVFISNGKL 694
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGVaVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
477-699 |
9.17e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 105.94 E-value: 9.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 477 GKEAIRIKNLKKEYAGKCERVE--ALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADI 554
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 555 ENISKFTGFCPQS------------NVQFGfltvKENLrlfakikGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQ 622
Cdd:PRK13633 81 WDIRNKAGMVFQNpdnqivativeeDVAFG----PENL-------GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 623 NRKltfgIAILG----DPQVLLLDEPTAGLDPLSRHRIWNLLKE--GKSDRVILFSTQFIDEAdILADRKVFISNGKLKC 696
Cdd:PRK13633 150 KQR----VAIAGilamRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEA-VEADRIIVMDSGKVVM 224
|
...
gi 27477115 697 AGS 699
Cdd:PRK13633 225 EGT 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1308-1517 |
1.05e-24 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 112.53 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKgsggGEPLGF--------LGYCPQENALWPNLTV 1379
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLF----GQPVDAgdiatrrrVGYMSQAFSLYGELTV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1380 RQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1459
Cdd:NF033858 357 RQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMF 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 1460 WQVIRATFRNTERGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSKFGKDYL 1517
Cdd:NF033858 437 WRLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVAARGAATL 493
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
478-694 |
1.49e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 104.47 E-value: 1.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 478 KEAIRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLS-----VPTSGSVTVYNHTL-SRM 551
Cdd:PRK14239 3 EPILQVSDLSVYYNKK----KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlnpeVTITGSIVYNGHNIySPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 552 ADIENISKFTGFCPQSNVQFGFlTVKENLRLFAKIKGI-----LPHEVEKEVQrvvQELEMENIQDIL---AQNLSGGQN 623
Cdd:PRK14239 79 TDTVDLRKEIGMVFQQPNPFPM-SIYENVVYGLRLKGIkdkqvLDEAVEKSLK---GASIWDEVKDRLhdsALGLSGGQQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27477115 624 RKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVILFSTQFIDEADILADRKVFISNGKL 694
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
510-695 |
1.58e-24 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 103.40 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 510 GQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIEnisKFTGFCPQSNVQFGFLTVKENLRLFAKIKGI 589
Cdd:TIGR01277 24 GEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ---RPVSMLFQENNLFAHLTVRQNIGLGLHPGLK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 590 LPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--GKSDR 667
Cdd:TIGR01277 101 LNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQlcSERQR 180
|
170 180
....*....|....*....|....*...
gi 27477115 668 VILFSTQFIDEADILADRKVFISNGKLK 695
Cdd:TIGR01277 181 TLLMVTHHLSDARAIASQIAVVSQGKIK 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
505-698 |
2.96e-24 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 102.37 E-value: 2.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 505 FDIyEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVtVYNHTL----SRMADIENISKFTGFCPQSNVQFGFLTVKENL 580
Cdd:cd03297 19 FDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTI-VLNGTVlfdsRKKINLPPQQRKIGLVFQQYALFPHLNVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 581 rLFAkIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLL 660
Cdd:cd03297 97 -AFG-LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27477115 661 KEGKSDRVI--LFSTQFIDEADILADRKVFISNGKLKCAG 698
Cdd:cd03297 175 KQIKKNLNIpvIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1300-1503 |
3.44e-24 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 101.36 E-value: 3.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1300 FSKRKKKIAtRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLG---------FLGYCPQe 1370
Cdd:cd03214 7 VGYGGRTVL-DDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL----DGKDLAslspkelarKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1371 nalwpnltvrqhlevyaavkglrkgdAMiaitRLVDALKLQDQlkaPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1450
Cdd:cd03214 81 --------------------------AL----ELLGLAHLADR---PFNELSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27477115 1451 MDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1503
Cdd:cd03214 128 LDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
481-698 |
4.07e-24 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 102.80 E-value: 4.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYagkceRVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVtvynhtLSRMADIENIS-- 558
Cdd:cd03299 1 LKVENLSKDW-----KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKI------LLNGKDITNLPpe 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 559 -KFTGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQ 637
Cdd:cd03299 70 kRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27477115 638 VLLLDEPTAGLDPLSRHRIWNLLKE--GKSDRVILFSTQFIDEADILADRKVFISNGKLKCAG 698
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKirKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVG 212
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1310-1498 |
6.50e-24 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 102.47 E-value: 6.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQV--ILkgsggGEPLGF---------LGYCPQENALW--PN 1376
Cdd:COG1119 20 DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrLF-----GERRGGedvwelrkrIGLVSPALQLRfpRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1377 LTVRqhlEV-----YAAVkGLRK--GDAMIAITR-LVDALKLQDQLKAPVKTLSEGIKRKlcfVL---SILGNPSVVLLD 1445
Cdd:COG1119 95 ETVL---DVvlsgfFDSI-GLYRepTDEQRERAReLLELLGLAHLADRPFGTLSQGEQRR---VLiarALVKDPELLILD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27477115 1446 EPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1498
Cdd:COG1119 168 EPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
479-694 |
7.39e-24 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 103.11 E-value: 7.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 479 EAIRIKNLKKEYAGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIENI- 557
Cdd:cd03294 19 KLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 558 --SKFTGFCPQSnvqFGFL---TVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAI 632
Cdd:cd03294 99 lrRKKISMVFQS---FALLphrTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARAL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477115 633 LGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--GKSDRVILFSTQFIDEADILADRKVFISNGKL 694
Cdd:cd03294 176 AVDPDILLMDEAFSALDPLIRREMQDELLRlqAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
480-694 |
7.91e-24 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 102.42 E-value: 7.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLS--VP---TSGSVTVYNH-TLSRMAD 553
Cdd:COG1117 11 KIEVRNLNVYYGDK----QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPgarVEGEILLDGEdIYDPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 554 IENISKFTG--------FcPQS---NVQFGfltvkenlrlfAKIKGILPHEVEKEvqRVVQELEM----ENIQDIL---A 615
Cdd:COG1117 87 VVELRRRVGmvfqkpnpF-PKSiydNVAYG-----------LRLHGIKSKSELDE--IVEESLRKaalwDEVKDRLkksA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 616 QNLSGGQNRKLTfgIA--ILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVILFSTQFIDEADILADRKVFISNGK 693
Cdd:COG1117 153 LGLSGGQQQRLC--IAraLAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGE 230
|
.
gi 27477115 694 L 694
Cdd:COG1117 231 L 231
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
480-699 |
9.99e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 102.90 E-value: 9.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEY-AGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTL---SRMADIE 555
Cdd:PRK13649 2 GINLQNVSYTYqAGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 556 NISKFTGFC---PQSnvQFGFLTVKENLRLFAKIKGILPHEVEKevqRVVQELEMENI-QDILAQN---LSGGQNRKltf 628
Cdd:PRK13649 82 QIRKKVGLVfqfPES--QLFEETVLKDVAFGPQNFGVSQEEAEA---LAREKLALVGIsESLFEKNpfeLSGGQMRR--- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 629 gIAILG----DPQVLLLDEPTAGLDPLSRHRIWNLLKE-GKSDRVILFSTQFIDEADILADRKVFISNGKLKCAGS 699
Cdd:PRK13649 154 -VAIAGilamEPKILVLDEPTAGLDPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
480-699 |
1.00e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 104.78 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAgkceRVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIEnisK 559
Cdd:PRK10851 2 SIEIANIKKSFG----RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 FTGFCPQSNVQFGFLTVKEN----LRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGD 635
Cdd:PRK10851 75 KVGFVFQHYALFRHMTVFDNiafgLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 636 PQVLLLDEPTAGLDPLSRH--RIW--NLLKEGKSDRVilFSTQFIDEADILADRKVFISNGKLKCAGS 699
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKelRRWlrQLHEELKFTSV--FVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
481-726 |
1.15e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 103.18 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKC--ERvEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLS---RMADIE 555
Cdd:PRK13634 3 ITFQKVEHRYQYKTpfER-RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 556 NISKFTGfcpqsnVQFGF-------LTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMEniQDILAQN---LSGGQNRK 625
Cdd:PRK13634 82 PLRKKVG------IVFQFpehqlfeETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLP--EELLARSpfeLSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 626 ltfgIAILG----DPQVLLLDEPTAGLDPLSRHRI----WNLLKEGksDRVILFSTQFIDEADILADRKVFISNGKLKCA 697
Cdd:PRK13634 154 ----VAIAGvlamEPEVLVLDEPTAGLDPKGRKEMmemfYKLHKEK--GLTTVLVTHSMEDAARYADQIVVMHKGTVFLQ 227
|
250 260 270
....*....|....*....|....*....|.
gi 27477115 698 GS--SLFLKKKWGIGYHLSLhlnercdPESI 726
Cdd:PRK13634 228 GTprEIFADPDELEAIGLDL-------PETV 251
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
484-661 |
1.26e-23 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 100.01 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 484 KNLKKEYAGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSvpTSGSVTvYNHTLSRMADIENISKFTGF 563
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRK--TAGVIT-GEILINGRPLDKNFQRSTGY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 564 CPQSNVQFGFLTVKENLRLFAKIKGilphevekevqrvvqelemeniqdilaqnLSGGQNRKLTFGIAILGDPQVLLLDE 643
Cdd:cd03232 84 VEQQDVHSPNLTVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDE 134
|
170
....*....|....*...
gi 27477115 644 PTAGLDPLSRHRIWNLLK 661
Cdd:cd03232 135 PTSGLDSQAAYNIVRFLK 152
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
480-694 |
1.28e-23 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 108.41 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGkcERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLsRMADIENISK 559
Cdd:TIGR03375 463 EIEFRNVSFAYPG--QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDI-RQIDPADLRR 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 FTGFCPQSNVQFgFLTVKENLRLFAkikgilPHEVEKEVQRVVQELEMENIQDILAQ-----------NLSGGQNRKLTF 628
Cdd:TIGR03375 540 NIGYVPQDPRLF-YGTLRDNIALGA------PYADDEEILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVAL 612
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 629 GIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVILFST---QFIDeadiLADRKVFISNGKL 694
Cdd:TIGR03375 613 ARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVThrtSLLD----LVDRIIVMDNGRI 677
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
480-687 |
1.31e-23 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 106.99 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGkceRVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRmADIENISK 559
Cdd:TIGR02857 321 SLEFSGVSVAYPG---RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAD-ADADSWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 FTGFCPQSNVQF-GflTVKENLRLFAkiKGILPHEVEKEVQRV-----VQELEmENIQDILAQN---LSGGQNRKLTFGI 630
Cdd:TIGR02857 397 QIAWVPQHPFLFaG--TIAENIRLAR--PDASDAEIREALERAgldefVAALP-QGLDTPIGEGgagLSGGQAQRLALAR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 631 AILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVILFSTQfiDEADI-LADRKV 687
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH--RLALAaLADRIV 527
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
481-650 |
1.64e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 101.70 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKE-YAGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADiENISK 559
Cdd:COG1101 2 LELKNLSKTfNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 F---------TGFCPQsnvqfgfLTVKENLRLfAKIKGI-------LPHEVEKEVQRVVQELEM--ENIQDILAQNLSGG 621
Cdd:COG1101 81 YigrvfqdpmMGTAPS-------MTIEENLAL-AYRRGKrrglrrgLTKKRRELFRELLATLGLglENRLDTKVGLLSGG 152
|
170 180
....*....|....*....|....*....
gi 27477115 622 QNRKLTFGIAILGDPQVLLLDEPTAGLDP 650
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDP 181
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1303-1479 |
1.92e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 99.95 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1303 RKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGGGEPLGFLG--YCPQENALWPNLTVR 1380
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAchYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1381 QHLEVYAAVKGLRKGDAMIAItrlvDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1460
Cdd:PRK13539 92 ENLEFWAAFLGGEELDIAAAL----EAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFA 167
|
170 180
....*....|....*....|.
gi 27477115 1461 QVIRAtfrNTERG--ALLTTH 1479
Cdd:PRK13539 168 ELIRA---HLAQGgiVIAATH 185
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
479-699 |
2.22e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 100.93 E-value: 2.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 479 EAIRIKNLKKEY------------------AGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGS 540
Cdd:COG1134 3 SMIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 541 VTVYnhtlSRMADIENISkfTGFCPQsnvqfgfLTVKENLRLFAKIKGILPHEVEKEVQRVVQ--ELEmeniqDILAQ-- 616
Cdd:COG1134 83 VEVN----GRVSALLELG--AGFHPE-------LTGRENIYLNGRLLGLSRKEIDEKFDEIVEfaELG-----DFIDQpv 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 617 -NLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPL----SRHRIWNLLKEGKSdrvILF---STQFIDEadiLADRKVF 688
Cdd:COG1134 145 kTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELRESGRT---VIFvshSMGAVRR---LCDRAIW 218
|
250
....*....|.
gi 27477115 689 ISNGKLKCAGS 699
Cdd:COG1134 219 LEKGRLVMDGD 229
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
481-650 |
2.51e-23 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 100.45 E-value: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGkcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLS-RMADIENISK 559
Cdd:COG1126 2 IEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdSKKDINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 FTGFCPQS-NVqFGFLTVKENLRLfA--KIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQ-NRkltfgIAI--- 632
Cdd:COG1126 78 KVGMVFQQfNL-FPHLTVLENVTL-ApiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQqQR-----VAIara 150
|
170
....*....|....*....
gi 27477115 633 LG-DPQVLLLDEPTAGLDP 650
Cdd:COG1126 151 LAmEPKVMLFDEPTSALDP 169
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
480-694 |
2.87e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 100.47 E-value: 2.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGkcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHT--LSRMADIENI 557
Cdd:COG4161 2 SIQLKNINCFYGS----HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdFSQKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 558 SKFtgfcpQSNVQFGF--------LTVKENLrLFAKIK--GILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLT 627
Cdd:COG4161 78 RLL-----RQKVGMVFqqynlwphLTVMENL-IEAPCKvlGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 628 FGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKS---DRVILfsTQFIDEADILADRKVFISNGKL 694
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtgiTQVIV--THEVEFARKVASQVVYMEKGRI 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
479-698 |
2.96e-23 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 100.54 E-value: 2.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 479 EAIRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSG-SVTVYNHTLSRmADIENI 557
Cdd:COG1119 2 PLLELRNVTVRRGGK----TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGG-EDVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 558 SKFTGFCpqSNVQFGFLTVKENLR------LFAKIkGILPHEVEKEVQRVVQ---ELEMENIQDILAQNLSGGQNRKLTF 628
Cdd:COG1119 77 RKRIGLV--SPALQLRFPRDETVLdvvlsgFFDSI-GLYREPTDEQRERARElleLLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477115 629 GIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--GKSDRVILFSTQFIDEadILA--DRKVFISNGKLKCAG 698
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEE--IPPgiTHVLLLKDGRVVAAG 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
479-699 |
3.40e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 100.62 E-value: 3.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 479 EAIRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIEnIS 558
Cdd:PRK13548 1 AMLEARNLSVRLGGR----TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAE-LA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 559 KFTGFCPQ-SNVQFGFlTVKENLRLfakikGILPH-EVEKEVQRVVQE-LEMENIQDiLA----QNLSGGQN------RK 625
Cdd:PRK13548 76 RRRAVLPQhSSLSFPF-TVEEVVAM-----GRAPHgLSRAEDDALVAAaLAQVDLAH-LAgrdyPQLSGGEQqrvqlaRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 626 LTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDR-----VIL----FSTQFideadilADRKVFISNGKLKC 696
Cdd:PRK13548 149 LAQLWEPDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglaviVVLhdlnLAARY-------ADRIVLLHQGRLVA 221
|
...
gi 27477115 697 AGS 699
Cdd:PRK13548 222 DGT 224
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
480-694 |
3.57e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 100.09 E-value: 3.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHT--LSRMADIENI 557
Cdd:PRK11124 2 SIQLNGINCFYGAH----QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 558 SKFtgfcpQSNVQFGF--------LTVKENL-RLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTF 628
Cdd:PRK11124 78 REL-----RRNVGMVFqqynlwphLTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 629 GIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSD---RVILfsTQFIDEADILADRKVFISNGKL 694
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETgitQVIV--THEVEVARKTASRVVYMENGHI 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
505-699 |
3.77e-23 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 103.26 E-value: 3.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 505 FDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSrmaDIENiSKFT-------GFCPQSNVQFGFLTVK 577
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQ---DSAR-GIFLpphrrriGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 578 ENLRlFAkIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIW 657
Cdd:COG4148 96 GNLL-YG-RKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27477115 658 NLLkEGKSDRV---ILFSTQFIDEADILADRKVFISNGKLKCAGS 699
Cdd:COG4148 174 PYL-ERLRDELdipILYVSHSLDEVARLADHVVLLEQGRVVASGP 217
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
481-694 |
8.79e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 99.22 E-value: 8.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAgkceRVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGL-----SVPTSGSVTVYNHTLSRMADIE 555
Cdd:PRK14247 4 IEIRDLKVSFG----QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 556 niskftgfcPQSNVQFGF--------LTVKENLRLFAKIKGILPHEVEKEvQRVVQELEM----ENIQDIL---AQNLSG 620
Cdd:PRK14247 80 ---------LRRRVQMVFqipnpipnLSIFENVALGLKLNRLVKSKKELQ-ERVRWALEKaqlwDEVKDRLdapAGKLSG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477115 621 GQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVILFSTQFIDEADILADRKVFISNGKL 694
Cdd:PRK14247 150 GQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1288-1508 |
9.73e-23 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 98.81 E-value: 9.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1288 LRKEYAGKKKncfskrkKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGS-----GGGEPLG 1362
Cdd:cd03258 7 VSKVFGDTGG-------KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltllSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1363 F---LGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNP 1439
Cdd:cd03258 80 ArrrIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27477115 1440 SVVLLDEPSTGMDPEGQQQMWQVIRATfrNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1508
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDI--NRELGltIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
481-719 |
1.26e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 99.92 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAgkcERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMAD-IENISK 559
Cdd:PRK13636 6 LKVEELNYNYS---DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKgLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 FTGFCPQS-NVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQV 638
Cdd:PRK13636 83 SVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 639 LLLDEPTAGLDPLSRHRIWNLLKEGKS--DRVILFSTQFIDEADILADRKVFISNGKLKCAG--SSLFLKKKWGIGYHLS 714
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGnpKEVFAEKEMLRKVNLR 242
|
....*....
gi 27477115 715 L----HLNE 719
Cdd:PRK13636 243 LprigHLME 251
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1310-1505 |
1.60e-22 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 97.92 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGGGEPLGFLGYCPQENALWPNLTVRQH--LEVYA 1387
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENiaLAVDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1388 AVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP-------EGQQQMW 1460
Cdd:TIGR01184 82 VLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrgnlqEELMQIW 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27477115 1461 QVIRATfrntergALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSI 1505
Cdd:TIGR01184 162 EEHRVT-------VLMVTHDVDEALLLSDRVVMLTNGPAANIGQI 199
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1301-1503 |
1.80e-22 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 97.33 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1301 SKR-KKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGFLGycP---------QE 1370
Cdd:cd03301 7 TKRfGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYI----GGRDVTDLP--PkdrdiamvfQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1371 NALWPNLTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1450
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27477115 1451 MDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1503
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
480-698 |
2.00e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.04 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAgkcERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRmADIENISK 559
Cdd:PRK13647 4 IIEVEDLHFRYK---DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA-ENEKWVRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 FTGFCPQS-NVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKltfgIAILG---- 634
Cdd:PRK13647 80 KVGLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKR----VAIAGvlam 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 635 DPQVLLLDEPTAGLDPLSRHRI----WNLLKEGKSdrvILFSTQFIDEADILADRKVFISNGKLKCAG 698
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLmeilDRLHNQGKT---VIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
484-699 |
2.01e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 98.04 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 484 KNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIENISKFTGF 563
Cdd:PRK10895 7 KNLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 564 CPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKE-VQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLD 642
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 643 EPTAGLDPLSRHRIWNLLKEGKSDRV-ILFSTQFIDEADILADRKVFISNGKLKCAGS 699
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDSGLgVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1301-1517 |
3.05e-22 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 97.41 E-value: 3.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1301 SKRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSG----GGEPLGFlGYCPQENALWPN 1376
Cdd:cd03299 7 SKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDitnlPPEKRDI-SYVPQNYALFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1377 LTVRQHLEVyaavkGLRKGDAM-IAITRLVD----ALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGM 1451
Cdd:cd03299 86 MTVYKNIAY-----GLKKRKVDkKEIERKVLeiaeMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1452 DPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQ----HLKSKFGKDYL 1517
Cdd:cd03299 161 DVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEevfkKPKNEFVAEFL 230
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
481-698 |
3.37e-22 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 95.46 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKCERVeaLKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADieNISKF 560
Cdd:cd03247 1 LSINNVSFSYPEQEQQV--LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK--ALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQFGfLTVKENLrlfakikgilphevekevqrvvqelemeniqdilAQNLSGGQNRKLTFGIAILGDPQVLL 640
Cdd:cd03247 77 ISVLNQRPYLFD-TTLRNNL----------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 641 LDEPTAGLDPLSRHRIWNLLKEGKSDRVILFSTQFIDEADiLADRKVFISNGKLKCAG 698
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIE-HMDKILFLENGKIIMQG 178
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1305-1522 |
5.40e-22 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 97.50 E-value: 5.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1305 KKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGsgggeplgfLGYCPQENaLWpnlTVRQHLE 1384
Cdd:TIGR04520 14 EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG---------LDTLDEEN-LW---EIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1385 ----------VYAAV----------KGLrKGDAMiaITRLVDALK---LQDQLKAPVKTLSEGIKRKLCfVLSILG-NPS 1440
Cdd:TIGR04520 81 mvfqnpdnqfVGATVeddvafglenLGV-PREEM--RKRVDEALKlvgMEDFRDREPHLLSGGQKQRVA-IAGVLAmRPD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1441 VVLLDEPsTGM-DPEGQQQMWQVIRATfrNTERGA--LLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQHLKSKfgKDYL 1517
Cdd:TIGR04520 157 IIILDEA-TSMlDPKGRKEVLETIRKL--NKEEGItvISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQ--VELL 230
|
....*
gi 27477115 1518 LEMKL 1522
Cdd:TIGR04520 231 KEIGL 235
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
503-699 |
5.72e-22 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 99.42 E-value: 5.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 503 VVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTL--SRMADIENISK-FTGFCPQSNVQFGFLTVKEN 579
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdSRKGIFLPPEKrRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 580 LRLfaKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNL 659
Cdd:TIGR02142 96 LRY--GMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27477115 660 LkEGKSDRV---ILFSTQFIDEADILADRKVFISNGKLKCAGS 699
Cdd:TIGR02142 174 L-ERLHAEFgipILYVSHSLQEVLRLADRVVVLEDGRVAAAGP 215
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
478-698 |
6.75e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 97.39 E-value: 6.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 478 KEAIRIKNLKKEYAGKCERveALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSrmadIENI 557
Cdd:PRK13635 3 EEIIRVEHISFRYPDAATY--ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS----EETV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 558 ---------------SKFTGFCPQSNVQFGFltvkENlrlfakiKGIlPHevEKEVQRVVQELEMENIQDILAQ---NLS 619
Cdd:PRK13635 77 wdvrrqvgmvfqnpdNQFVGATVQDDVAFGL----EN-------IGV-PR--EEMVERVDQALRQVGMEDFLNRephRLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 620 GGQNRKltfgIAILG----DPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVI--LFSTQFIDEAdILADRKVFISNGK 693
Cdd:PRK13635 143 GGQKQR----VAIAGvlalQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGItvLSITHDLDEA-AQADRVIVMNKGE 217
|
....*
gi 27477115 694 LKCAG 698
Cdd:PRK13635 218 ILEEG 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
496-702 |
7.54e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 96.49 E-value: 7.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 496 RVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIENISKFTGFCPQSNVQFGFLT 575
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSRMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 576 VKENLRL---FA----------KIKGILPHEVEKEVQRvvqelemeniqdilAQNLSGGQNRKLTFGIAILGDPQVLLLD 642
Cdd:PRK11614 97 VEENLAMggfFAerdqfqerikWVYELFPRLHERRIQR--------------AGTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27477115 643 EPTAGLDPLSRHRIWNLLKEGKSDRVILFST-QFIDEADILADRKVFISNGK--LKCAGSSLF 702
Cdd:PRK11614 163 EPSLGLAPIIIQQIFDTIEQLREQGMTIFLVeQNANQALKLADRGYVLENGHvvLEDTGDALL 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
481-694 |
7.59e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 98.72 E-value: 7.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIE----- 555
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 556 -NIskftGFCPQsnvQFGFL---TVKENLRLFAKIKGILPHEVEKevqRVVQELEMENIQDiLAQ----NLSGGQnrKLT 627
Cdd:PRK11153 82 rQI----GMIFQ---HFNLLssrTVFDNVALPLELAGTPKAEIKA---RVTELLELVGLSD-KADrypaQLSGGQ--KQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477115 628 FGIA--ILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-----GKSdrvILFSTQFIDEADILADRKVFISNGKL 694
Cdd:PRK11153 149 VAIAraLASNPKVLLCDEATSALDPATTRSILELLKDinrelGLT---IVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1282-1504 |
9.17e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 96.12 E-value: 9.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1282 VIIASCLRKEYAGKKkncfskrkkkiATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKgsggGEPL 1361
Cdd:PRK10895 3 TLTAKNLAKAYKGRR-----------VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIID----DEDI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1362 GFL----------GYCPQENALWPNLTVRQH----LEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKapvKTLSEGIKR 1427
Cdd:PRK10895 68 SLLplhararrgiGYLPQEASIFRRLSVYDNlmavLQIRDDLSAEQREDRANELMEEFHIEHLRDSMG---QSLSGGERR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 1428 KLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1504
Cdd:PRK10895 145 RVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEH-LRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
477-662 |
9.67e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 102.05 E-value: 9.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 477 GKEAIRIKNLKKEYAGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLS---VPTSGSVTVYNHTLsrmaD 553
Cdd:TIGR00955 18 GSWKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSpkgVKGSGSVLLNGMPI----D 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 554 IENISKFTGFCPQSNVQFGFLTVKENLRLFAKIKgiLPHEVEKE-----VQRVVQELEMENIQDILAQ------NLSGGQ 622
Cdd:TIGR00955 94 AKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLR--MPRRVTKKekrerVDEVLQALGLRKCANTRIGvpgrvkGLSGGE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27477115 623 NRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE 662
Cdd:TIGR00955 172 RKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKG 211
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
503-679 |
1.07e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 102.51 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 503 VVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLsrmaDIENIS--KFTGFCPQSNVQFGFLTVKENL 580
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV----DAGDIAtrRRVGYMSQAFSLYGELTVRQNL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 581 RLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLL 660
Cdd:NF033858 361 ELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLL 440
|
170 180
....*....|....*....|.
gi 27477115 661 KE-GKSDRVILF-STQFIDEA 679
Cdd:NF033858 441 IElSREDGVTIFiSTHFMNEA 461
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
480-699 |
1.20e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 96.79 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYagKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGS---VTVYNHTLSRmADIEN 556
Cdd:PRK13640 5 IVEFKHVSFTY--PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTA-KTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 557 ISKFTGFCPQS-NVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKltfgIAILG- 634
Cdd:PRK13640 82 IREKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQR----VAIAGi 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 635 ---DPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDR-VILFS-TQFIDEADiLADRKVFISNGKLKCAGS 699
Cdd:PRK13640 158 lavEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnLTVISiTHDIDEAN-MADQVLVLDDGKLLAQGS 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
481-693 |
1.40e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 95.21 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGkcervEALKgvvFD--IYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMAdienIS 558
Cdd:COG3840 2 LRLDDLTYRYGD-----FPLR---FDltIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP----PA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 559 K------FtgfcpQSNVQFGFLTVKENLRLfakikGILPH----EVEKevQRVVQELEMENIQDILA---QNLSGGQNRK 625
Cdd:COG3840 70 ErpvsmlF-----QENNLFPHLTVAQNIGL-----GLRPGlkltAEQR--AQVEQALERVGLAGLLDrlpGQLSGGQRQR 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 626 LTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDR--VILFSTQFIDEADILADRKVFISNGK 693
Cdd:COG3840 138 VALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1288-1504 |
1.53e-21 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 95.38 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1288 LRKEYAGKkkncfskrkkkIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGFL--- 1364
Cdd:cd03300 6 VSKFYGGF-----------VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL----DGKDITNLpph 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1365 ----GYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPS 1440
Cdd:cd03300 71 krpvNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477115 1441 VVLLDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1504
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
481-699 |
1.73e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 96.66 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKC--ERVeALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTL-SRMADIENI 557
Cdd:PRK13637 3 IKIENLTHIYMEGTpfEKK-ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItDKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 558 SKFTGFCPQ-SNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQ--ELEMENIQDILAQNLSGGQNRKltfgIAILG 634
Cdd:PRK13637 82 RKKVGLVFQyPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNivGLDYEDYKDKSPFELSGGQKRR----VAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477115 635 ----DPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDR---VILFSTQFIDEADIlADRKVFISNGKLKCAGS 699
Cdd:PRK13637 158 vvamEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmtIILVSHSMEDVAKL-ADRIIVMNKGKCELQGT 228
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
459-680 |
1.91e-21 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 100.62 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 459 DSDPTPNDCFEPVSPEFcGKEAIRIKNLKKEYAGKcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTS 538
Cdd:COG1132 319 DEPPEIPDPPGAVPLPP-VRGEIEFENVSFSYPGD---RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTS 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 539 GSVTVYNHTLSRMaDIENISKFTGFCPQSNVQFGfLTVKENLRLFAkikgilPHEVEKEVQRVvqeLEMENIQDILAQ-- 616
Cdd:COG1132 395 GRILIDGVDIRDL-TLESLRRQIGVVPQDTFLFS-GTIRENIRYGR------PDATDEEVEEA---AKAAQAHEFIEAlp 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 617 ------------NLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDR-VIL----FSTqfIDEA 679
Cdd:COG1132 464 dgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRtTIViahrLST--IRNA 541
|
.
gi 27477115 680 D 680
Cdd:COG1132 542 D 542
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
481-746 |
3.01e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 95.64 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRmADIENISKF 560
Cdd:PRK13652 4 IETRDLCYSYSGS---KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK-ENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQ-SNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVL 639
Cdd:PRK13652 80 VGLVFQnPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 640 LLDEPTAGLDPLSRHRIWNLLKE--GKSDRVILFSTQFIDEADILADRKVFISNGKLKCAGS--SLFLKKKWGIGYHLSL 715
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDlpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTveEIFLQPDLLARVHLDL 239
|
250 260 270
....*....|....*....|....*....|..
gi 27477115 716 HLNercdPESITSLVKQHIS-DAKLTAQSEEK 746
Cdd:PRK13652 240 PSL----PKLIRSLQAQGIAiDMAYTYQEAED 267
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1299-1497 |
3.43e-21 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 93.48 E-value: 3.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1299 CFSKRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGS--GGGEPLGFLGYCPQEnalwpn 1376
Cdd:cd03226 6 SFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpiKAKERRKSIGYVMQD------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1377 ltVRQHL-------EVYAAVKGLRKGDAMIA-ITRLVDALKLQDQLKApvkTLSEGIKRKLCFVLSILGNPSVVLLDEPS 1448
Cdd:cd03226 80 --VDYQLftdsvreELLLGLKELDAGNEQAEtVLKDLDLYALKERHPL---SLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27477115 1449 TGMDPEGQQQMWQVIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSG 1497
Cdd:cd03226 155 SGLDYKNMERVGELIR-ELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
477-694 |
3.89e-21 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 92.50 E-value: 3.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 477 GKEAIRIKNLKKEYAgkcerveaLKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIEN 556
Cdd:cd03215 1 GEPVLEVRGLSVKGA--------VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 557 ISKFTGFCPQSNVQFGF---LTVKENLrlfakikgilphevekevqrvvqelemeniqdILAQNLSGGQNRKLTFGIAIL 633
Cdd:cd03215 73 IRAGIAYVPEDRKREGLvldLSVAENI--------------------------------ALSSLLSGGNQQKVVLARWLA 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 634 GDPQVLLLDEPTAGLDPLSRHRIWNLL----KEGKSdrVILFSTQFiDEADILADRKVFISNGKL 694
Cdd:cd03215 121 RDPRVLILDEPTRGVDVGAKAEIYRLIrelaDAGKA--VLLISSEL-DELLGLCDRILVMYEGRI 182
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
498-673 |
5.22e-21 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 98.97 E-value: 5.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 498 EALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRmADIENISKFTGFCPQSNVQFGfLTVK 577
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSS-LDQDEVRRRVSVCAQDAHLFD-TTVR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 578 ENLRLFAKikGILPHEVEKEVQRV-----VQELEmENIQDIL---AQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLD 649
Cdd:TIGR02868 427 ENLRLARP--DATDEELWAALERVgladwLRALP-DGLDTVLgegGARLSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
170 180
....*....|....*....|....
gi 27477115 650 PLSRHRIWNLLKEGKSDRVILFST 673
Cdd:TIGR02868 504 AETADELLEDLLAALSGRTVVLIT 527
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
498-715 |
9.01e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 94.46 E-value: 9.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 498 EALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTL-SRMAD--IENISKFTGFC---PQSnvQF 571
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDkyIRPVRKRIGMVfqfPES--QL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 572 GFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMEniQDILAQN---LSGGQNRKLTFgIAILG-DPQVLLLDEPTAG 647
Cdd:PRK13646 99 FEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFS--RDVMSQSpfqMSGGQMRKIAI-VSILAmNPDIIVLDEPTAG 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477115 648 LDPLSRHRIWNLLKE--GKSDRVILFSTQFIDEADILADRKVFISNGKL--KCAGSSLFLKKKWGIGYHLSL 715
Cdd:PRK13646 176 LDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARYADEVIVMKEGSIvsQTSPKELFKDKKKLADWHIGL 247
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
480-694 |
1.31e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 92.89 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTL-------SRMA 552
Cdd:PRK11264 3 AIEVKNLVKKFHGQ----TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 553 DIENISKFTGFCPQSNVQFGFLTVKENLRLFAKI-KGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIA 631
Cdd:PRK11264 79 LIRQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477115 632 ILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-GKSDRVILFSTQFIDEADILADRKVFISNGKL 694
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
456-661 |
1.70e-20 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 99.03 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 456 NETDSDPTPNDcfEPVSPEFCGKEAIRIKNLKKEYAGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSG--- 532
Cdd:TIGR00956 737 DLTDESDDVND--EKDMEKESGEDIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAErvt 814
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 533 LSVPTSGSVTVYNHTLSrmadiENISKFTGFCPQSNVQFGFLTVKENLRLFAKIKgiLPHEVEKE-----VQRVVQELEM 607
Cdd:TIGR00956 815 TGVITGGDRLVNGRPLD-----SSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLR--QPKSVSKSekmeyVEEVIKLLEM 887
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 608 ENIQDIL----AQNLSGGQNRKLTFGIAILGDPQVLL-LDEPTAGLDPLSRHRIWNLLK 661
Cdd:TIGR00956 888 ESYADAVvgvpGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMR 946
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1300-1499 |
1.84e-20 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 91.07 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1300 FSKRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTA--GQVILKG--SGGGEPLGFLGYCPQENALWP 1375
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGrpLDKRSFRKIIGYVPQDDILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1376 NLTVRQHLEVYAAVKGLrkgdamiaitrlvdalklqdqlkapvktlSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEG 1455
Cdd:cd03213 96 TLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27477115 1456 QQQMWQVIRAtFRNTERGALLTTHY-MAEAEAVCDRVAIMVSGRL 1499
Cdd:cd03213 147 ALQVMSLLRR-LADTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1307-1499 |
2.24e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 96.63 E-value: 2.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1307 IATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKgsggGEPLGF----------LGYCPQENALWPN 1376
Cdd:COG3845 19 VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILID----GKPVRIrsprdaialgIGMVHQHFMLVPN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1377 LTVRQHLeVYAAVKG----LRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1452
Cdd:COG3845 95 LTVAENI-VLGLEPTkggrLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27477115 1453 PEGQQQMWQVIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:COG3845 174 PQEADELFEILRR-LAAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
512-708 |
2.40e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 94.56 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 512 ITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSrmaDIENiskftGFC-PQSNVQFGFltVKENLRLFA--KIKG 588
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF---DAEK-----GIClPPEKRRIGY--VFQDARLFPhyKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 589 ILPHEVEKEVQ----RVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDpLSRHRiwNLLK--E 662
Cdd:PRK11144 96 NLRYGMAKSMVaqfdKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD-LPRKR--ELLPylE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27477115 663 GKSDRV---ILFSTQFIDEADILADRKVFISNGKLKCAGSslfLKKKWG 708
Cdd:PRK11144 173 RLAREInipILYVSHSLDEILRLADRVVVLEQGKVKAFGP---LEEVWA 218
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
481-705 |
2.83e-20 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 91.52 E-value: 2.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNhtlsrmADIENISKF 560
Cdd:cd03254 3 IEFENVNFSYDEK---KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDG------IDIRDISRK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 T-----GFCPQSNVQF-GflTVKENLRLFAkikgilPHEVEKEVQRVVQELEMENIQDIL-----------AQNLSGGQN 623
Cdd:cd03254 74 SlrsmiGVVLQDTFLFsG--TIMENIRLGR------PNATDEEVIEAAKEAGAHDFIMKLpngydtvlgenGGNLSQGER 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 624 RKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWN---LLKEGKSDRVILFSTQFIDEADILadrkVFISNGKLKCAGS- 699
Cdd:cd03254 146 QLLAIARAMLRDPKILILDEATSNIDTETEKLIQEaleKLMKGRTSIIIAHRLSTIKNADKI----LVLDDGKIIEEGTh 221
|
....*..
gi 27477115 700 -SLFLKK 705
Cdd:cd03254 222 dELLAKK 228
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
481-699 |
2.87e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 94.63 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKCerveALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRM-ADIENISk 559
Cdd:PRK09452 15 VELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpAENRHVN- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 fTGFcpQSNVQFGFLTVKENLRLFAKIKGILPHEVEKevqRVVQELEM---ENIQDILAQNLSGGQNRKLTFGIAILGDP 636
Cdd:PRK09452 90 -TVF--QSYALFPHMTVFENVAFGLRMQKTPAAEITP---RVMEALRMvqlEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 637 QVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVI--LFSTQFIDEADILADRKVFISNGKLKCAGS 699
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKALQRKLGItfVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
481-662 |
4.12e-20 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 93.19 E-value: 4.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGL---SVPTSGSVTVYNHTLSRMADiENI 557
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLKLSE-KEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 558 SKFTGfcpqSNVQFGF----------LTVKENLRLFAKIKGILPHEVEKEvqRVVQELEMENIQD---ILAQ---NLSGG 621
Cdd:COG0444 81 RKIRG----REIQMIFqdpmtslnpvMTVGDQIAEPLRIHGGLSKAEARE--RAIELLERVGLPDperRLDRyphELSGG 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 27477115 622 QNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE 662
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKD 195
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
480-685 |
4.21e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.86 E-value: 4.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGkcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIENISK 559
Cdd:COG1129 4 LLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 FTGFCPQSNVQFGFLTVKENLRL--FAKIKGILPH-EVEKEVQRVVQELEMeNIQ-DILAQNLSGGQnRKLtfgIAI--- 632
Cdd:COG1129 80 GIAIIHQELNLVPNLSVAENIFLgrEPRRGGLIDWrAMRRRARELLARLGL-DIDpDTPVGDLSVAQ-QQL---VEIara 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 633 -LGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRV-ILFSTQFIDEADILADR 685
Cdd:COG1129 155 lSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVaIIYISHRLDEVFEIADR 209
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
481-713 |
4.24e-20 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 91.14 E-value: 4.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKCErvEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLsRMADIENISKF 560
Cdd:cd03251 1 VEFKNVTFRYPGDGP--PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV-RDYTLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQFGFlTVKENLRlFAKikgilPHEVEKEVQRV---------VQELEmENIQDILAQN---LSGGQNRKLTF 628
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIA-YGR-----PGATREEVEEAaraanahefIMELP-EGYDTVIGERgvkLSGGQRQRIAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 629 GIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVIL-----FSTqfIDEadilADRKVFISNGKLKCAGSSLFL 703
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFviahrLST--IEN----ADRIVVLEDGKIVERGTHEEL 223
|
250
....*....|
gi 27477115 704 KKKWGIGYHL 713
Cdd:cd03251 224 LAQGGVYAKL 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
477-694 |
5.65e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 95.64 E-value: 5.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 477 GKEAIRIKNLKKEYAgKCER--VEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTV------YNHTL 548
Cdd:TIGR03269 276 GEPIIKVRNVSKRYI-SVDRgvVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewVDMTK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 549 SRMADIENISKFTGFCPQSNVQFGFLTVKENLrlfAKIKGI-LPHEVEKevQRVVQELEM--------ENIQDILAQNLS 619
Cdd:TIGR03269 355 PGPDGRGRAKRYIGILHQEYDLYPHRTVLDNL---TEAIGLeLPDELAR--MKAVITLKMvgfdeekaEEILDKYPDELS 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 620 GGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSR----HRIWNLLKEGKSDRVILfsTQFIDEADILADRKVFISNGKL 694
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKvdvtHSILKAREEMEQTFIIV--SHDMDFVLDVCDRAALMRDGKI 506
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
485-662 |
5.88e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 90.65 E-value: 5.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 485 NLKKEYAGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRM-----ADIENisK 559
Cdd:PRK11629 10 NLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakAELRN--Q 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 FTGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVL 639
Cdd:PRK11629 88 KLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLV 167
|
170 180
....*....|....*....|...
gi 27477115 640 LLDEPTAGLDPLSRHRIWNLLKE 662
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLGE 190
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1310-1518 |
7.98e-20 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 96.06 E-value: 7.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPL---------GFLGYCPQENALWP----- 1375
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI----DGIDLrqidpaslrRQIGVVLQDVFLFSgtire 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1376 NLTVrqhlevyaavkglrkGDAMIAITRLVDALK----------LQDQLKAPV----KTLSEGIKRKLCFVLSILGNPSV 1441
Cdd:COG2274 568 NITL---------------GDPDATDEEIIEAARlaglhdfieaLPMGYDTVVgeggSNLSGGQRQRLAIARALLRNPRI 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 1442 VLLDEPSTGMDPEGQQQMWQVIRATFRNteRGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLL 1518
Cdd:COG2274 633 LILDEATSALDAETEAIILENLRRLLKG--RTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1310-1509 |
8.54e-20 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 90.25 E-value: 8.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGFL------------GYCPQENALWPNL 1377
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLI----DGEDISGLseaelyrlrrrmGMLFQSGALFDSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1378 TVRQHLEVYaavkgLRKGDAMIA--ITRLVdALKLQ------DQLKAPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPST 1449
Cdd:cd03261 93 TVFENVAFP-----LREHTRLSEeeIREIV-LEKLEavglrgAEDLYPAE-LSGGMKKRVALARALALDPELLLYDEPTA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1450 GMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLK 1509
Cdd:cd03261 166 GLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
499-739 |
1.59e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.95 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 499 ALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYN---HTLSRMADIENISKFTGFC---PQSnvQFG 572
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvSSTSKQKEIKPVRKKVGVVfqfPES--QLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 573 FLTVKENLRLFAKIKGILPHEVEKevqRVVQELEMENIQDILAQN----LSGGQNRKLTFGIAILGDPQVLLLDEPTAGL 648
Cdd:PRK13643 99 EETVLKDVAFGPQNFGIPKEKAEK---IAAEKLEMVGLADEFWEKspfeLSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 649 DPLSRHRIWNLLKE-GKSDRVILFSTQFIDEADILADRKVFISNGKLKCAG--SSLFLK----KKWGIGYHLSLHLNERC 721
Cdd:PRK13643 176 DPKARIEMMQLFESiHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGtpSDVFQEvdflKAHELGVPKATHFADQL 255
|
250
....*....|....*...
gi 27477115 722 DPESITSLVKQHISDAKL 739
Cdd:PRK13643 256 QKTGAVTFEKLPITRAEL 273
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
481-669 |
1.84e-19 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 87.27 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKCERVeaLKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRmADIENISKF 560
Cdd:cd03246 1 LEVENVSFRYPGAEPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQ-WDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQsnvqfgfltvkeNLRLFAkikGILphevekevqrvvqeleMENIqdilaqnLSGGQNRKLTFGIAILGDPQVLL 640
Cdd:cd03246 78 VGYLPQ------------DDELFS---GSI----------------AENI-------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190
....*....|....*....|....*....|..
gi 27477115 641 LDEPTAGLDPLSRHRIWNL---LKEGKSDRVI 669
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAiaaLKAAGATRIV 151
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
480-688 |
2.42e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 89.71 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYagkcERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLS-----VPTSGSVTVYNHTL-SRMAD 553
Cdd:PRK14258 7 AIKVNNLSFYY----DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNeleseVRVEGRVEFFNQNIyERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 554 IENISKFTGFC-PQSNVqfgF-LTVKENLRLFAKIKGILPH-EVEKEVQRVVQELEM-ENIQDIL---AQNLSGGQNRKL 626
Cdd:PRK14258 83 LNRLRRQVSMVhPKPNL---FpMSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLwDEIKHKIhksALDLSGGQQQRL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477115 627 TFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEG--KSDRVILFSTQFIDEADILADRKVF 688
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlRSELTMVIVSHNLHQVSRLSDFTAF 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1310-1499 |
2.95e-19 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 87.97 E-value: 2.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGF-----------LGYCPQENALWPNLT 1378
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIII----DGLKLTDdkkninelrqkVGMVFQQFNLFPHLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1379 VRQHL-EVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEG------IKRKLCFvlsilgNPSVVLLDEPSTGM 1451
Cdd:cd03262 93 VLENItLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGqqqrvaIARALAM------NPKVMLFDEPTSAL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27477115 1452 DPEGQQQMWQVIRatfRNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:cd03262 167 DPELVGEVLDVMK---DLAEEGMtmVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1310-1504 |
3.57e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 90.90 E-value: 3.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGFL-------GYCPQENALWPNLTVRQH 1382
Cdd:COG3839 20 KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI----GGRDVTDLppkdrniAMVFQSYALYPHMTVYEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1383 LEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEG------IKRklcfvlSILGNPSVVLLDEPSTGMDPEGQ 1456
Cdd:COG3839 96 IAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGqrqrvaLGR------ALVREPKVFLLDEPLSNLDAKLR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27477115 1457 QQMWQVIRATFRntERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1504
Cdd:COG3839 170 VEMRAEIKRLHR--RLGTttIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
481-695 |
3.77e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 88.30 E-value: 3.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIENI--- 557
Cdd:PRK10584 7 VEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 558 SKFTGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQ 637
Cdd:PRK10584 87 AKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 638 VLLLDEPTAGLDPLSRHRIWNLLKEGKSDrvilFSTQFI----DEAdiLA---DRKVFISNGKLK 695
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNRE----HGTTLIlvthDLQ--LAarcDRRLRLVNGQLQ 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
480-714 |
4.23e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 89.50 E-value: 4.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYA-GKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMA---DIE 555
Cdd:PRK13641 2 SIKFENVDYIYSpGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnkNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 556 NISKFTGFCPQ-SNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEM-ENIQDILAQNLSGGQNRKLTFGIAIL 633
Cdd:PRK13641 82 KLRKKVSLVFQfPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 634 GDPQVLLLDEPTAGLDPLSRHRIWNLLKE-GKSDRVILFSTQFIDEADILADRKVFISNGKL--KCAGSSLFLKKKWGIG 710
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDyQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLikHASPKEIFSDKEWLKK 241
|
....
gi 27477115 711 YHLS 714
Cdd:PRK13641 242 HYLD 245
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1310-1447 |
4.57e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.82 E-value: 4.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsggGEPLgFLGYCPQENA-LWPNLTVRQHLEvyaa 1388
Cdd:COG0488 332 DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-----GETV-KIGYFDQHQEeLDPDKTVLDELR---- 401
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 1389 vKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1447
Cdd:COG0488 402 -DGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
499-687 |
5.58e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.52 E-value: 5.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 499 ALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVynHTLSRMAdieniskftgFCPQ-SNVQFGF-LTV 576
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRR--AGGARVA----------YVPQrSEVPDSLpLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 577 KE--NLRLFAKIKGILPHEVEKEvQRVVQELEMENIQDILA---QNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPL 651
Cdd:NF040873 75 RDlvAMGRWARRGLWRRLTRDDR-AAVDDALERVGLADLAGrqlGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 27477115 652 SRHRIWNLLKEGKSD-RVILFSTQFIDEAdILADRKV 687
Cdd:NF040873 154 SRERIIALLAEEHARgATVVVVTHDLELV-RRADPCV 189
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1301-1499 |
5.76e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 87.42 E-value: 5.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1301 SKR--KKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLG--------FL----GY 1366
Cdd:COG2884 8 SKRypGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLV----NGQDLSrlkrreipYLrrriGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1367 CPQENALWPNLTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDE 1446
Cdd:COG2884 84 VFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 1447 PSTGMDPEgqqQMWQVIRATFRNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:COG2884 164 PTGNLDPE---TSWEIMELLEEINRRGTtvLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1308-1544 |
5.98e-19 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 90.56 E-value: 5.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAG--KSTTIKMITGdtkPTAGQvilkgsgggEPLGFLGYCPQENALW----------- 1374
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGR---------RPWRF*TWCANRRALRrtig*hrpvr* 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1375 ---PNLTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGM 1451
Cdd:NF000106 96 grrESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1452 DPEGQQQMWQVIRATFRNTERgALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLlemklknlaQMEPL 1531
Cdd:NF000106 176 DPRTRNEVWDEVRSMVRDGAT-VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTL---------QIRPA 245
|
250
....*....|....
gi 27477115 1532 H-AEILRLFPQAAQ 1544
Cdd:NF000106 246 HaAELDRMVGAIAQ 259
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
494-649 |
6.08e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.85 E-value: 6.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 494 CER--VEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTlsrmADIENISKFTGFCPQSNVQF 571
Cdd:PRK13539 10 CVRggRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD----IDDPDVAEACHYLGHRNAMK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 572 GFLTVKENLRLFAKIKGILPHEVEKEVQRVvqelEMENIQDILAQNLSGGQNRKLtfGIAIL---GDPqVLLLDEPTAGL 648
Cdd:PRK13539 86 PALTVAENLEFWAAFLGGEELDIAAALEAV----GLAPLAHLPFGYLSAGQKRRV--ALARLlvsNRP-IWILDEPTAAL 158
|
.
gi 27477115 649 D 649
Cdd:PRK13539 159 D 159
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1310-1498 |
6.29e-19 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 85.90 E-value: 6.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGFL---------GYCPQENALWpNLTVR 1380
Cdd:cd03228 19 KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI----DGVDLRDLdleslrkniAYVPQDPFLF-SGTIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1381 QHLevyaavkglrkgdamiaitrlvdalklqdqlkapvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1460
Cdd:cd03228 94 ENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALIL 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 27477115 1461 QVIRATFRntERGALLTTHYMAEAEAvCDRVAIMVSGR 1498
Cdd:cd03228 137 EALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1294-1499 |
6.31e-19 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 87.33 E-value: 6.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1294 GKKKNcfsKRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITG---DTKPTAGQVILKGSgGGEPLGFL---GYC 1367
Cdd:cd03234 11 LKAKN---WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQ-PRKPDQFQkcvAYV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1368 PQENALWPNLTVRQHLEVYAAVKGLRKGD-----AMIAITRLVDaLKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVV 1442
Cdd:cd03234 87 RQDDILLPGLTVRETLTYTAILRLPRKSSdairkKRVEDVLLRD-LALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 1443 LLDEPSTGMDPEGQQQMWQVIRATFRnTERGALLTTHY-MAEAEAVCDRVAIMVSGRL 1499
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLAR-RNRIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
505-694 |
6.47e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 87.72 E-value: 6.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 505 FDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTV--YNHTLSRMADiENISKFtgFcpQSNVQFGFLTVKENLRL 582
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLngQDHTTTPPSR-RPVSML--F--QENNLFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 583 fakikGILP-----HEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIW 657
Cdd:PRK10771 95 -----GLNPglklnAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEML 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 27477115 658 NLLKEGKSDRVI--LFSTQFIDEADILADRKVFISNGKL 694
Cdd:PRK10771 170 TLVSQVCQERQLtlLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
480-680 |
6.63e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 93.65 E-value: 6.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYaGKcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIENISK 559
Cdd:NF033858 1 VARLEGVSHRY-GK---TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 FTGFCPQsnvqfGF-------LTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAI 632
Cdd:NF033858 77 RIAYMPQ-----GLgknlyptLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCAL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27477115 633 LGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRV---ILFSTQFIDEAD 680
Cdd:NF033858 152 IHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPgmsVLVATAYMEEAE 202
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
472-695 |
7.29e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.05 E-value: 7.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 472 SPEFCGKEAIRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVyNHTLSrm 551
Cdd:COG0488 307 PPERLGKKVLELEGLSKSYGDK----TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK-- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 552 adieniskfTGFCPQSNVQF-GFLTVKENLRLFA------KIKGIL------PHEVEKEVQRvvqelemeniqdilaqnL 618
Cdd:COG0488 380 ---------IGYFDQHQEELdPDKTVLDELRDGApggteqEVRGYLgrflfsGDDAFKPVGV-----------------L 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 619 SGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLK--EGksdrVILFST---QFIDEadiLADRKVFISNGK 693
Cdd:COG0488 434 SGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDdfPG----TVLLVShdrYFLDR---VATRILEFEDGG 506
|
..
gi 27477115 694 LK 695
Cdd:COG0488 507 VR 508
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
478-694 |
8.70e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 87.98 E-value: 8.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 478 KEAIRIKNLKKEYAgkceRVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGL-----SVPTSGSVTVYNHTL-SRM 551
Cdd:PRK14267 2 KFAIETVNLRVYYG----SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIySPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 552 ADIENISKFTGFCPQSNVQFGFLTVKENLRLFAKIKGILP--HEVEKEVQRVVQELEM-ENIQDIL---AQNLSGGQNRK 625
Cdd:PRK14267 78 VDPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKskKELDERVEWALKKAALwDEVKDRLndyPSNLSGGQRQR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 626 LTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVILFSTQFIDEADILADRKVFISNGKL 694
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
481-701 |
1.16e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 91.40 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLS--VPTSGSVtVYNHTL-SRMADIENI 557
Cdd:TIGR03269 1 IEVKNLTKKFDGK----EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRI-IYHVALcEKCGYVERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 558 SKFTGFCP-------QSNVQFGFLTVKENLRLFAKIKGILP-----------------------HEVEKEVQRVVQELEM 607
Cdd:TIGR03269 76 SKVGEPCPvcggtlePEEVDFWNLSDKLRRRIRKRIAIMLQrtfalygddtvldnvlealeeigYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 608 ENIQDI---LAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEG--KSDRVILFSTQFIDEADIL 682
Cdd:TIGR03269 156 VQLSHRithIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDL 235
|
250
....*....|....*....
gi 27477115 683 ADRKVFISNGKLKCAGSSL 701
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPD 254
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
481-699 |
1.18e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 87.38 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKceRVeaLKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIEnISKF 560
Cdd:PRK11231 3 LRTENLTVGYGTK--RI--LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-LARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQFGFLTVKE--------NLRLFakikGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAI 632
Cdd:PRK11231 78 LALLPQHHLTPEGITVRElvaygrspWLSLW----GRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477115 633 LGDPQVLLLDEPTAGLDpLSRH-RIWNLLKE----GKSDRVILFStqfIDEADILADRKVFISNGKLKCAGS 699
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLD-INHQvELMRLMRElntqGKTVVTVLHD---LNQASRYCDHLVVLANGHVMAQGT 221
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1308-1517 |
1.23e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 89.89 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGggeplgfLGYCP----------QENALWPNL 1377
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-------LSHVPpyqrpinmmfQSYALFPHM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1378 TVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1457
Cdd:PRK11607 107 TVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477115 1458 QMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS----IQHLKSKFGKDYL 1517
Cdd:PRK11607 187 RMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEpeeiYEHPTTRYSAEFI 250
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
481-656 |
1.31e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 89.89 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIEnisKF 560
Cdd:PRK11607 20 LEIRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ---RP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLL 640
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170
....*....|....*.
gi 27477115 641 LDEPTAGLDPLSRHRI 656
Cdd:PRK11607 173 LDEPMGALDKKLRDRM 188
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1295-1503 |
1.55e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 91.02 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1295 KKKNCFSKRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILK------------GSGGGEPLG 1362
Cdd:TIGR03269 286 SKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmtkpgPDGRGRAKR 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1363 FLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAMIAITRLV----DALKLQDQLKAPVKTLSEGIKRKLCFVLSILGN 1438
Cdd:TIGR03269 366 YIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARMKAVITLKmvgfDEEKAEEILDKYPDELSEGERHRVALAQVLIKE 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 1439 PSVVLLDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1503
Cdd:TIGR03269 446 PRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1310-1447 |
1.58e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.28 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKgsgGGEPLGFLgycPQENALWPNLTVRQ-----HLE 1384
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---KGLRIGYL---PQEPPLDDDLTVLDtvldgDAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1385 VYAAVKGLRK--------GDAMIAITRL-------------------VDALKL-QDQLKAPVKTLSEGIKRK--LCFVLs 1434
Cdd:COG0488 89 LRALEAELEEleaklaepDEDLERLAELqeefealggweaearaeeiLSGLGFpEEDLDRPVSELSGGWRRRvaLARAL- 167
|
170
....*....|...
gi 27477115 1435 iLGNPSVVLLDEP 1447
Cdd:COG0488 168 -LSEPDLLLLDEP 179
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1308-1511 |
1.59e-18 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 91.36 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGFL---------GYCPQeNALWPNLT 1378
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILI----NGVDLSDLdpaswrrqiAWVPQ-NPYLFAGT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1379 VRQHLEVYAAVKGlrkGDAMIAITRLVDAL----KLQDQLKAPV----KTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1450
Cdd:COG4988 427 IRENLRLGRPDAS---DEELEAALEAAGLDefvaALPDGLDTPLgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAH 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27477115 1451 MDPEGQQQMWQVIRATFRNteRGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSK 1511
Cdd:COG4988 504 LDAETEAEILQALRRLAKG--RTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1296-1503 |
1.93e-18 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 87.31 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1296 KKNCFSKRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGFL----------- 1364
Cdd:cd03294 27 KEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLI----DGQDIAAMsrkelrelrrk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1365 --GYCPQENALWPNLTVRQH----LEVYAAVKGLRKGDAMIAItRLVDalkLQDQLKAPVKTLSEGIKRKLCFVLSILGN 1438
Cdd:cd03294 103 kiSMVFQSFALLPHRTVLENvafgLEVQGVPRAEREERAAEAL-ELVG---LEGWEHKYPDELSGGMQQRVGLARALAVD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 1439 PSVVLLDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1503
Cdd:cd03294 179 PDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVG 243
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
481-654 |
1.94e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 86.68 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMaDIENISKF 560
Cdd:COG4604 2 IEIKNVSKRYGGK----VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATT-PSRELAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNvQFGF-LTVKEnLRLFakikGILPH-------EVEKEVQRVVQELEMENIQDILAQNLSGGQnRKLTFgIA- 631
Cdd:COG4604 77 LAILRQEN-HINSrLTVRE-LVAF----GRFPYskgrltaEDREIIDEAIAYLDLEDLADRYLDELSGGQ-RQRAF-IAm 148
|
170 180
....*....|....*....|....
gi 27477115 632 -ILGDPQVLLLDEPTAGLDPlsRH 654
Cdd:COG4604 149 vLAQDTDYVLLDEPLNNLDM--KH 170
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1306-1499 |
2.84e-18 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 84.41 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1306 KIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGsgggEPLGF----------LGYCP---QENA 1372
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG----KPVTRrsprdairagIAYVPedrKREG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1373 LWPNLTVRQHlevyaavkglrkgdamIAITRLvdalklqdqlkapvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1452
Cdd:cd03215 89 LVLDLSVAEN----------------IALSSL----------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27477115 1453 PEGQQQMWQVIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:cd03215 137 VGAKAEIYRLIRE-LADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1308-1499 |
3.61e-18 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 84.95 E-value: 3.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGFL---------GYCPQENALWpNLT 1378
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLL----DGTDIRQLdpadlrrniGYVPQDVTLF-YGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1379 VRQHL----------EVYAAVKglrkgdaMIAITRLVDALK--LQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDE 1446
Cdd:cd03245 94 LRDNItlgapladdeRILRAAE-------LAGVTDFVNKHPngLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27477115 1447 PSTGMDPEGQQQMWQVIRATFRntERGALLTTHYMAeAEAVCDRVAIMVSGRL 1499
Cdd:cd03245 167 PTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1302-1506 |
3.66e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 85.98 E-value: 3.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1302 KRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLG---------FLGYCPQENA 1372
Cdd:PRK13548 11 RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRL----NGRPLAdwspaelarRRAVLPQHSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1373 LWPNLTVRQHLEVYAAVKGLRKGDAMIAIT---RLVDALKLQDQlkaPVKTLSEGIK------RKLCFVLSILGNPSVVL 1443
Cdd:PRK13548 87 LSFPFTVEEVVAMGRAPHGLSRAEDDALVAaalAQVDLAHLAGR---DYPQLSGGEQqrvqlaRVLAQLWEPDGPPRWLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477115 1444 LDEPSTGMDPEGQQQMWQVIRAtfRNTERGA--------L-LTTHYmaeaeavCDRVAIMVSGRLRCIGSIQ 1506
Cdd:PRK13548 164 LDEPTSALDLAHQHHVLRLARQ--LAHERGLavivvlhdLnLAARY-------ADRIVLLHQGRLVADGTPA 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
494-650 |
4.01e-18 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 84.33 E-value: 4.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 494 CERVE--ALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIeniskftgfcPQSNVQF 571
Cdd:TIGR01189 8 CSRGErmLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE----------PHENILY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 572 --------GFLTVKENLRLFAKIKGILPHEVEKEVQRVvqelEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDE 643
Cdd:TIGR01189 78 lghlpglkPELSALENLHFWAAIHGGAQRTIEDALAAV----GLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
....*..
gi 27477115 644 PTAGLDP 650
Cdd:TIGR01189 154 PTTALDK 160
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
499-690 |
5.00e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 85.99 E-value: 5.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 499 ALKGVVFDIYEGQITALLGHSGAGKTTLL---NILSGL--SVPTSGSVTVYNHTL-SRMADIENISKFTGFCPQSNVQFG 572
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLipGFRVEGKVTFHGKNLyAPDVDPVEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 573 fLTVKENLRLFAKI---KGILPHEVEKEVQRVVQELEmenIQDILAQN---LSGGQNRKLTFGIAILGDPQVLLLDEPTA 646
Cdd:PRK14243 105 -KSIYDNIAYGARIngyKGDMDELVERSLRQAALWDE---VKDKLKQSglsLSGGQQQRLCIARAIAVQPEVILMDEPCS 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27477115 647 GLDPLSRHRIWNLLKEGKSDRVILFSTQFIDEADILADRKVFIS 690
Cdd:PRK14243 181 ALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFN 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
480-692 |
5.03e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.52 E-value: 5.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNhtlsrmADIENISK 559
Cdd:PRK11248 1 MLQISHLYADYGGK----PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG------KPVEGPGA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 FTGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVL 639
Cdd:PRK11248 71 ERGVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 640 LLDEPTAGLDPLSRHRIWNLL-----KEGKSdrvILFSTQFIDEADILADRKVFISNG 692
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLLlklwqETGKQ---VLLITHDIEEAVFMATELVLLSPG 205
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
480-649 |
5.15e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 87.59 E-value: 5.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGKcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSV----TVYNHTLSRMADIE 555
Cdd:PRK11650 3 GLKLQAVRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIwiggRVVNELEPADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 556 NIskFtgfcpQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGD 635
Cdd:PRK11650 80 MV--F-----QNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVRE 152
|
170
....*....|....
gi 27477115 636 PQVLLLDEPTAGLD 649
Cdd:PRK11650 153 PAVFLFDEPLSNLD 166
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
481-698 |
5.16e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.46 E-value: 5.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGkcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIENISKF 560
Cdd:PRK09700 6 ISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQFGFLTVKENL---RLFAK----IKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAIL 633
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLyigRHLTKkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 634 GDPQVLLLDEPTAGLDPLSRHRIW----NLLKEGKSdrvILFSTQFIDEADILADRKVFISNGKLKCAG 698
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFlimnQLRKEGTA---IVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
481-712 |
5.81e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 87.78 E-value: 5.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGkcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNhtlSRMADIENISKF 560
Cdd:PRK11000 4 VTLRNVTKAYGD----VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE---KRMNDVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLL 640
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 641 LDEPTAGLDPL----SRHRIWNLLKegKSDRVILFSTQFIDEADILADRKVFISNGKLKCAGSSLFLkkkwgigYH 712
Cdd:PRK11000 157 LDEPLSNLDAAlrvqMRIEISRLHK--RLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL-------YH 223
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
481-698 |
6.10e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 85.57 E-value: 6.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGkcERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMaDIENISKF 560
Cdd:PRK13648 8 IVFKNVSFQYQS--DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDD-NFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQS-NVQFGFLTVKENLRlFAKIKGILPHE-VEKEVQRVVQELEMENIQDILAQNLSGGQNRKltfgIAILG---- 634
Cdd:PRK13648 85 IGIVFQNpDNQFVGSIVKYDVA-FGLENHAVPYDeMHRRVSEALKQVDMLERADYEPNALSGGQKQR----VAIAGvlal 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 635 DPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDR--VILFSTQFIDEAdILADRKVFISNGKLKCAG 698
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTVYKEG 224
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
515-700 |
7.48e-18 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 86.78 E-value: 7.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 515 LLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADiENISKFTGFcpQSNVQFGFLTVKENLRLFAKIKGiLPHEV 594
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPP-HLRHINMVF--QSYALFPHMTVEENVAFGLKMRK-VPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 595 EKEvqRVVQELEMENIQDILAQ---NLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLK--EGKSDRVI 669
Cdd:TIGR01187 77 IKP--RVLEALRLVQLEEFADRkphQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKtiQEQLGITF 154
|
170 180 190
....*....|....*....|....*....|.
gi 27477115 670 LFSTQFIDEADILADRKVFISNGKLKCAGSS 700
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTP 185
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
481-699 |
9.02e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.57 E-value: 9.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGkcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIENISKF 560
Cdd:PRK15439 12 LCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQFGFLTVKENLrLFAKIKgilPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLL 640
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENI-LFGLPK---RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 641 LDEPTAGLDPLSRHRIWNLLKEGKSDRV-ILFSTQFIDEADILADRKVFISNGKLKCAGS 699
Cdd:PRK15439 164 LDEPTASLTPAETERLFSRIRELLAQGVgIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
481-699 |
1.10e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.04 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAgkcERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIENISKF 560
Cdd:PRK13644 2 IRLENVSYSYP---DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQS-NVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVL 639
Cdd:PRK13644 79 VGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477115 640 LLDEPTAGLDPLS----RHRIWNLLKEGKSdrvILFSTQFIDEADIlADRKVFISNGKLKCAGS 699
Cdd:PRK13644 159 IFDEVTSMLDPDSgiavLERIKKLHEKGKT---IVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
481-694 |
1.25e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 85.52 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKCE-RVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVT-VYN--HTLSRMADIE- 555
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwIFKdeKNKKKTKEKEk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 556 -------------NISKFTGFCPQSNVQFGFL-------TVKENLRLFAKIKGILPHEVEKevqRVVQELEMENI-QDIL 614
Cdd:PRK13651 83 vleklviqktrfkKIKKIKEIRRRVGVVFQFAeyqlfeqTIEKDIIFGPVSMGVSKEEAKK---RAAKYIELVGLdESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 615 AQ---NLSGGQNRKltfgIAILG----DPQVLLLDEPTAGLDPLSRHRIWNLLKE-GKSDRVILFSTQFIDEADILADRK 686
Cdd:PRK13651 160 QRspfELSGGQKRR----VALAGilamEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEWTKRT 235
|
....*...
gi 27477115 687 VFISNGKL 694
Cdd:PRK13651 236 IFFKDGKI 243
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1308-1504 |
1.31e-17 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 83.93 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGFL-------GYCPQENALWPNLTVR 1380
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILF----GGEDATDVpvqernvGFVFQHYALFRHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1381 QHLEVYAAVKGLRKGDAMIAITRLVDAL-------KLQDQLKApvkTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP 1453
Cdd:cd03296 93 DNVAFGLRVKPRSERPPEAEIRAKVHELlklvqldWLADRYPA---QLSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27477115 1454 EGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1504
Cdd:cd03296 170 KVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
482-685 |
2.61e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 87.27 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 482 RIKNLKKEYAGkcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTV------YNHTLSRM-ADI 554
Cdd:PRK11288 6 SFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdgqemrFASTTAALaAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 555 ENISKFTGFCPQsnvqfgfLTVKENLRLfakikGILPH--------EVEKEVQRVVQELEMENIQDILAQNLSGGQNRKL 626
Cdd:PRK11288 82 AIIYQELHLVPE-------MTVAENLYL-----GQLPHkggivnrrLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 627 TFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSD-RVILFSTQFIDEADILADR 685
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEgRVILYVSHRMEEIFALCDA 209
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1310-1479 |
2.95e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.16 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG----SGGGEPLGFLGYCPQENALWPNLTVRQHLEV 1385
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepirRQRDEYHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1386 YAAVKGLRKGDAMIAItrlVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRA 1465
Cdd:PRK13538 98 YQRLHGPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQ 174
|
170
....*....|....*.
gi 27477115 1466 tfrNTERG--ALLTTH 1479
Cdd:PRK13538 175 ---HAEQGgmVILTTH 187
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
483-662 |
3.08e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 87.47 E-value: 3.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 483 IKNLKKEYAGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMaDIENISKFT- 561
Cdd:PRK10535 7 LKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATL-DADALAQLRr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 562 ---GFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQV 638
Cdd:PRK10535 86 ehfGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQV 165
|
170 180
....*....|....*....|....
gi 27477115 639 LLLDEPTAGLDPLSRHRIWNLLKE 662
Cdd:PRK10535 166 ILADEPTGALDSHSGEEVMAILHQ 189
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1300-1504 |
3.17e-17 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 83.12 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1300 FSKRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGGGE--PLGF---LGYCPQENALW 1374
Cdd:cd03295 8 KRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqdPVELrrkIGYVIQQIGLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1375 PNLTVRQHLevyAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVK-----TLSEGIKRKLCFVLSILGNPSVVLLDEPST 1449
Cdd:cd03295 88 PHMTVEENI---ALVPKLLKWPKEKIRERADELLALVGLDPAEFAdryphELSGGQQQRVGVARALAADPPLLLMDEPFG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 1450 GMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1504
Cdd:cd03295 165 ALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
494-656 |
3.34e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 81.77 E-value: 3.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 494 CERVE--ALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIenISKFTGFCPQSNVQF 571
Cdd:cd03231 8 CERDGraLFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS--IARGLLYLGHAPGIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 572 GFLTVKENLRLFAKIKGilphevEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPL 651
Cdd:cd03231 86 TTLSVLENLRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
....*
gi 27477115 652 SRHRI 656
Cdd:cd03231 160 GVARF 164
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
481-699 |
4.28e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 83.63 E-value: 4.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKCERVEaLKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRmADIENISKF 560
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE-ENVWDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQS-NVQFGFLTVKENLRLFAKIKGIlPHEVEKEvqRVVQELE---MENIQDILAQNLSGGQNRKLTFGIAILGDP 636
Cdd:PRK13650 83 IGMVFQNpDNQFVGATVEDDVAFGLENKGI-PHEEMKE--RVNEALElvgMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 637 QVLLLDEPTAGLDPLSRHRIWNLLKEGKSDR--VILFSTQFIDEAdILADRKVFISNGKLKCAGS 699
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEV-ALSDRVLVMKNGQVESTST 223
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
495-649 |
4.42e-17 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 87.98 E-value: 4.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 495 ERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVP--TSGSVTVYNHTLSRmadiENISKFTGFCPQSNVQFG 572
Cdd:PLN03140 891 DRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFPKKQ----ETFARISGYCEQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 573 FLTVKENLRLFAKIKgiLPHEVEKE-----VQRVVQELEMENIQDILA-----QNLSGGQNRKLTFGIAILGDPQVLLLD 642
Cdd:PLN03140 967 QVTVRESLIYSAFLR--LPKEVSKEekmmfVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMD 1044
|
....*..
gi 27477115 643 EPTAGLD 649
Cdd:PLN03140 1045 EPTSGLD 1051
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
481-693 |
4.42e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 79.41 E-value: 4.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYnhtlsrmadieniskf 560
Cdd:cd03221 1 IELENLSKTYGGK----LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 tgfcpqSNVQFGFltvkenlrlfakikgilphevekevqrvvqelemeniqdiLAQnLSGGQNRKLTFGIAILGDPQVLL 640
Cdd:cd03221 61 ------STVKIGY----------------------------------------FEQ-LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 641 LDEPTAGLDPLSRHRIWNLLKEGKSDrVILFS--TQFIDEadiLADRKVFISNGK 693
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEYPGT-VILVShdRYFLDQ---VATKIIELEDGK 144
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1300-1499 |
5.28e-17 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 83.95 E-value: 5.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1300 FSKRKKKI-ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKP---TAGQVILKG----SGGGEPL-----GFLGY 1366
Cdd:COG0444 11 FPTRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGedllKLSEKELrkirgREIQM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1367 CPQE--NALWPNLTVRQHL-EVYAAVKGLRKGDAMiaiTRLVDALKLQdQLKAPVKT-------LSEGIKRKLCFVLSIL 1436
Cdd:COG0444 91 IFQDpmTSLNPVMTVGDQIaEPLRIHGGLSKAEAR---ERAIELLERV-GLPDPERRldrypheLSGGMRQRVMIARALA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 1437 GNPSVVLLDEPSTGMDPEGQQQMWQVIRAtfRNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:COG0444 167 LEPKLLIADEPTTALDVTIQAQILNLLKD--LQRELGLaiLFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1316-1491 |
5.52e-17 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 82.46 E-value: 5.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1316 VKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgggePLGFLGYCPQENALWPNLTVRQHLevYAAVKGlrKG 1395
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-------ELDTVSYKPQYIKADYEGTVRDLL--SSITKD--FY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1396 DAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRATFRNTERGAL 1475
Cdd:cd03237 91 THPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAF 170
|
170
....*....|....*.
gi 27477115 1476 LTTHYMAEAEAVCDRV 1491
Cdd:cd03237 171 VVEHDIIMIDYLADRL 186
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
481-662 |
6.99e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.46 E-value: 6.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRM--ADIENIS 558
Cdd:PRK10908 2 IRFEHVSKAYLGG---RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknREVPFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 559 KFTGFCPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQV 638
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180
....*....|....*....|....
gi 27477115 639 LLLDEPTAGLDPLSRHRIWNLLKE 662
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEE 182
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1306-1505 |
7.12e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.79 E-value: 7.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1306 KIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG---SGGGEPLGFL----GYCPQ--ENALWPN 1376
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvdiTDKKVKLSDIrkkvGLVFQypEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1377 lTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQL---KAPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP 1453
Cdd:PRK13637 100 -TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDykdKSPFE-LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27477115 1454 EGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSI 1505
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
499-650 |
7.21e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 82.35 E-value: 7.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 499 ALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMAD--IENISKFTGFcpqSNVQ-FGFLT 575
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGhqIARMGVVRTF---QHVRlFREMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 576 VKENLrLFAK--------IKGILP----HEVEKE-VQRVVQELEMENIQDIL---AQNLSGGQNRKLTFGIAILGDPQVL 639
Cdd:PRK11300 97 VIENL-LVAQhqqlktglFSGLLKtpafRRAESEaLDRAATWLERVGLLEHAnrqAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170
....*....|.
gi 27477115 640 LLDEPTAGLDP 650
Cdd:PRK11300 176 MLDEPAAGLNP 186
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
477-700 |
7.31e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 82.40 E-value: 7.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 477 GKEAIRIKNLKKEYAGKCERVeALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGL------SVPTSGSVTVYNHTLSR 550
Cdd:PRK14246 4 GKSAEDVFNISRLYLYINDKA-ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 551 MADIEnISKFTGFCPQSNVQFGFLTVKENLRLFAKIKGIlphEVEKEVQRVVQEL--------EMENIQDILAQNLSGGQ 622
Cdd:PRK14246 83 IDAIK-LRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGI---KEKREIKKIVEEClrkvglwkEVYDRLNSPASQLSGGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 623 NRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVILFSTQFIDEADILADRKVFISNGKLKCAGSS 700
Cdd:PRK14246 159 QQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1308-1479 |
7.80e-17 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 80.91 E-value: 7.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGS------GGGEPL--GFLGYCPQENALWPNLTV 1379
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdlrGRAIPYlrRKIGVVFQDFRLLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1380 RQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEgqqQM 1459
Cdd:cd03292 96 YENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD---TT 172
|
170 180
....*....|....*....|..
gi 27477115 1460 WQVIRATFRNTERGA--LLTTH 1479
Cdd:cd03292 173 WEIMNLLKKINKAGTtvVVATH 194
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1316-1499 |
7.87e-17 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 81.00 E-value: 7.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1316 VKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGGG------EPLGFLGycpQENALWPNLTVRQHLEVyAAV 1389
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTaappadRPVSMLF---QENNLFAHLTVEQNVGL-GLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1390 KGLR----KGDAMIAITRLVDalkLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRA 1465
Cdd:cd03298 97 PGLKltaeDRQAIEVALARVG---LAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....
gi 27477115 1466 TFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:cd03298 174 LHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1310-1499 |
8.67e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.46 E-value: 8.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKgsggGEPLGF----------LGYCP---QENALWPN 1376
Cdd:COG1129 269 RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLD----GKPVRIrsprdairagIAYVPedrKGEGLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1377 LTVRQ-----HLEVYAAVKGLRKGDAMIAITRLVDAL--KLQDqLKAPVKTLSEGIKRKLcfVLS--ILGNPSVVLLDEP 1447
Cdd:COG1129 345 LSIREnitlaSLDRLSRGGLLDRRRERALAEEYIKRLriKTPS-PEQPVGNLSGGNQQKV--VLAkwLATDPKVLILDEP 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27477115 1448 STGMDPEGQQQMWQVIRatfRNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:COG1129 422 TRGIDVGAKAEIYRLIR---ELAAEGKavIVISSELPELLGLSDRILVMREGRI 472
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
480-685 |
1.18e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.08 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGkcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVT----------------- 542
Cdd:COG3845 5 ALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILidgkpvrirsprdaial 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 543 ----VYNH-TLsrmadIENiskftgfcpqsnvqfgfLTVKENLRLFAKIKGIL---PHEVEKEVQRVVQELEMEnIQ-DI 613
Cdd:COG3845 81 gigmVHQHfML-----VPN-----------------LTVAENIVLGLEPTKGGrldRKAARARIRELSERYGLD-VDpDA 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 614 LAQNLSGGQNRKLTfgI--AILGDPQVLLLDEPTAGLDP-----LSRHrIWNLLKEGKSdrvILFSTQFIDEADILADR 685
Cdd:COG3845 138 KVEDLSVGEQQRVE--IlkALYRGARILILDEPTAVLTPqeadeLFEI-LRRLAAEGKS---IIFITHKLREVMAIADR 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1310-1499 |
1.25e-16 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 79.18 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPL---------GFLGYCPQENALWPNlTVR 1380
Cdd:cd03246 19 RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL----DGADIsqwdpnelgDHVGYLPQDDELFSG-SIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1381 QHLevyaavkglrkgdamiaitrlvdalklqdqlkapvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1460
Cdd:cd03246 94 ENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALN 136
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 27477115 1461 QVIRATfrnTERGA--LLTTHYMaEAEAVCDRVAIMVSGRL 1499
Cdd:cd03246 137 QAIAAL---KAAGAtrIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
500-694 |
1.42e-16 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 80.59 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 500 LKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSrMADIENISKFTGFCPQSNVQFGfLTVKEN 579
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS-QYEHKYLHSKVSLVGQEPVLFA-RSLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 580 LrlfAKIKGILPHEVEKEVQR------VVQELEMENIQDI--LAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPL 651
Cdd:cd03248 108 I---AYGLQSCSFECVKEAAQkahahsFISELASGYDTEVgeKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27477115 652 SRHRIWNLLKEGKSDRVILFSTQFIDEADiLADRKVFISNGKL 694
Cdd:cd03248 185 SEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
499-699 |
1.55e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.93 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 499 ALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIENIS---KFTGFCPQSNVQFGFLT 575
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 576 VKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHR 655
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27477115 656 IWN-LLK-EGKSDRVILFSTQFIDEADILADRKVFISNGKLKCAGS 699
Cdd:PRK10070 203 MQDeLVKlQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1311-1499 |
1.79e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 80.83 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1311 NVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGF---------------LGYCPQENALWP 1375
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNI----AGHQFDFsqkpsekairllrqkVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1376 NLTVRQHL-EVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1454
Cdd:COG4161 96 HLTVMENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27477115 1455 GQQQMWQVIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:COG4161 176 ITAQVVEIIR-ELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1308-1499 |
2.19e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.19 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGF----------LGYCPQENALWPNL 1377
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILI----DGQEMRFasttaalaagVAIIYQELHLVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1378 TVRQ-----HLEVYAAVkgLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1452
Cdd:PRK11288 95 TVAEnlylgQLPHKGGI--VNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27477115 1453 PEGQQQMWQVIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:PRK11288 173 AREIEQLFRVIRE-LRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
481-699 |
2.41e-16 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 79.85 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGkcERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMaDIENISKF 560
Cdd:cd03244 3 IEFKNVSLRYRP--NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI-GLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQF-GflTVKENLRLF-----AKIKGILpheveKEVQ--RVVQELEMENIQDILA--QNLSGGQNRKLTFGI 630
Cdd:cd03244 80 ISIIPQDPVLFsG--TIRSNLDPFgeysdEELWQAL-----ERVGlkEFVESLPGGLDTVVEEggENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 631 AILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVILFSTQFIDEadIL-ADRKVFISNGKLKCAGS 699
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDT--IIdSDRILVLDKGRVVEFDS 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
481-713 |
2.70e-16 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 80.28 E-value: 2.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKCErVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMAdIENISKF 560
Cdd:cd03249 1 IEFKNVSFRYPSRPD-VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN-LRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQFgFLTVKENLRLfakikGILPHEVEkEVQRVVqelEMENIQDILAQ--------------NLSGGQNRKL 626
Cdd:cd03249 79 IGLVSQEPVLF-DGTIAENIRY-----GKPDATDE-EVEEAA---KKANIHDFIMSlpdgydtlvgergsQLSGGQKQRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 627 TFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVIL-----FSTqfIDEADILAdrkvFISNGKLKCAGSSL 701
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIviahrLST--IRNADLIA----VLQNGQVVEQGTHD 222
|
250
....*....|..
gi 27477115 702 FLKKKWGIGYHL 713
Cdd:cd03249 223 ELMAQKGVYAKL 234
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1311-1497 |
2.78e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.54 E-value: 2.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1311 NVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVIlkgsggGEPLGFLGYCPQENALWPN--LTVRQHLEVYAA 1388
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------RNGKLRIGYVPQKLYLDTTlpLTVNRFLRLRPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1389 VKglrKGDAMIAITRlVDALKLqdqLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRATFR 1468
Cdd:PRK09544 96 TK---KEDILPALKR-VQAGHL---IDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRR 168
|
170 180 190
....*....|....*....|....*....|....
gi 27477115 1469 NTERGALLTTH----YMAEA-EAVCDRVAIMVSG 1497
Cdd:PRK09544 169 ELDCAVLMVSHdlhlVMAKTdEVLCLNHHICCSG 202
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1310-1498 |
3.48e-16 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 79.65 E-value: 3.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGF-----------LGYCPQENALWPNLT 1378
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITV----DGEDLTDskkdinklrrkVGMVFQQFNLFPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1379 VRQHLeVYA--AVKGLRKGDAM-IAItRLVDALKLQDQLKAPVKTLSEG------IKRKLCFvlsilgNPSVVLLDEPST 1449
Cdd:COG1126 94 VLENV-TLApiKVKKMSKAEAEeRAM-ELLERVGLADKADAYPAQLSGGqqqrvaIARALAM------EPKVMLFDEPTS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27477115 1450 GMDPEGQQQMWQVIR--AtfrntERGA--LLTTHYMAEAEAVCDRVAIMVSGR 1498
Cdd:COG1126 166 ALDPELVGEVLDVMRdlA-----KEGMtmVVVTHEMGFAREVADRVVFMDGGR 213
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
498-656 |
4.37e-16 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 79.45 E-value: 4.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 498 EALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSrMADIENISKFTGFCPQSNVQFGfLTVK 577
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA-LADPAWLRRQVGVVLQENVLFN-RSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 578 ENLRLfaKIKGILPHEVEkEVQRV------VQELEmENIQDILAQN---LSGGQNRKLTFGIAILGDPQVLLLDEPTAGL 648
Cdd:cd03252 94 DNIAL--ADPGMSMERVI-EAAKLagahdfISELP-EGYDTIVGEQgagLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
....*...
gi 27477115 649 DPLSRHRI 656
Cdd:cd03252 170 DYESEHAI 177
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1306-1498 |
6.14e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 79.74 E-value: 6.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1306 KIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGE--------------------PLgfLG 1365
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILI----DGKdvtklpeykrakyigrvfqdPM--MG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1366 YCpqenalwPNLTVRQHLEVyAAVKGLRKGDAmIAITR-----LVDALK-----LQDQLKAPVKTLSEGIKRKLCFVLSI 1435
Cdd:COG1101 93 TA-------PSMTIEENLAL-AYRRGKRRGLR-RGLTKkrrelFRELLAtlglgLENRLDTKVGLLSGGQRQALSLLMAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 1436 LGNPSVVLLDEPSTGMDPEGQQqmwQVIRATFRNTERG---ALLTTHYMAEAEAVCDRVAIMVSGR 1498
Cdd:COG1101 164 LTKPKLLLLDEHTAALDPKTAA---LVLELTEKIVEENnltTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1312-1479 |
7.06e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 77.92 E-value: 7.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1312 VSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGGGEPLGFLG----YCPQENALWPNLTVRQHLEVYA 1387
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIArgllYLGHAPGIKTTLSVLENLRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1388 AVkglrKGDAmiAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRAtf 1467
Cdd:cd03231 99 AD----HSDE--QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAG-- 170
|
170
....*....|....
gi 27477115 1468 rNTERG--ALLTTH 1479
Cdd:cd03231 171 -HCARGgmVVLTTH 183
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1304-1499 |
7.08e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 79.75 E-value: 7.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1304 KKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGsgggeplgfLGYCPQENaLWpnlTVRQHL 1383
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG---------LDTSDEEN-LW---DIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1384 ---------EVYAAV--KGLRKGDAMIAI------TRLVDALK---LQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVL 1443
Cdd:PRK13633 88 gmvfqnpdnQIVATIveEDVAFGPENLGIppeeirERVDESLKkvgMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 1444 LDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSGRL 1499
Cdd:PRK13633 168 FDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKV 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1313-1508 |
7.40e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 78.64 E-value: 7.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1313 SFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLgfLGYCP---------QENALWPNLTVRQHL 1383
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILW----NGQDL--TALPPaerpvsmlfQENNLFPHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1384 EVyaavkGLRKGdamiaitrlvdaLKLQDQLKAPVKTLSE-----GIKRKLCFVLS------------ILGNPSVVLLDE 1446
Cdd:COG3840 93 GL-----GLRPG------------LKLTAEQRAQVEQALErvglaGLLDRLPGQLSggqrqrvalarcLVRKRPILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477115 1447 PSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1508
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1303-1499 |
7.96e-16 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 78.38 E-value: 7.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1303 RKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITG-----DTKPTAGQVILKG----SGGGEPLGF---LGYCPQE 1370
Cdd:cd03260 10 YGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGkdiyDLDVDVLELrrrVGMVFQK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1371 NALWPnLTVRQHLEVYAAVKGLRKGDAMIAITRlvDALK-------LQDQLKApvKTLSEGIKRKLCFVLSILGNPSVVL 1443
Cdd:cd03260 90 PNPFP-GSIYDNVAYGLRLHGIKLKEELDERVE--EALRkaalwdeVKDRLHA--LGLSGGQQQRLCLARALANEPEVLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 1444 LDEPSTGMDPEGQQQMWQVIRATfrNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:cd03260 165 LDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
469-694 |
8.73e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.38 E-value: 8.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 469 EPVSPefcGKEAIRIKNLkkeYAGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTL 548
Cdd:COG3845 249 APAEP---GEVVLEVENL---SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 549 SRMadieNISKFT----GFCPQSNVQFGF---LTVKENLRL-------FAKiKGIL-PHEVEKEVQRVVQELemeNIQ-- 611
Cdd:COG3845 323 TGL----SPRERRrlgvAYIPEDRLGRGLvpdMSVAENLILgryrrppFSR-GGFLdRKAIRAFAEELIEEF---DVRtp 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 612 --DILAQNLSGG--QnrKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE----GKSdrVILFSTQfIDEADILA 683
Cdd:COG3845 395 gpDTPARSLSGGnqQ--KVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLElrdaGAA--VLLISED-LDEILALS 469
|
250
....*....|.
gi 27477115 684 DRKVFISNGKL 694
Cdd:COG3845 470 DRIAVMYEGRI 480
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
477-815 |
1.07e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 80.55 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 477 GKEAIRIKNLKKEYAgkceRVEALKGVVFDIYEGQITALLGHSGAG--KTTLLNILSGlsvPTSGSVTVYNHTLSrmADI 554
Cdd:NF000106 10 ARNAVEVRGLVKHFG----EVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWC--ANR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 555 ENISKFTGFC-PQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAIL 633
Cdd:NF000106 81 RALRRTIG*HrPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 634 GDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSD-RVILFSTQFIDEADILADRKVFISNGKLKCAGSSLFLKKKWGiGYH 712
Cdd:NF000106 161 GRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG-GRT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 713 LSLHLNERCDPESITSLVKQHISD--AKLTAQSEEKLVYIlPLERTNKFPELYRDLDRcSNQGIEDYGVSITTLNEVFLK 790
Cdd:NF000106 240 LQIRPAHAAELDRMVGAIAQAGLDgiAGATADHEDGVVNV-PIVSDEQLSAVVGMLGE-RGFTISGHQHPSAQL*EVFLA 317
|
330 340
....*....|....*....|....*
gi 27477115 791 LEGKSTIDESDIGiwgqlQTDGAKD 815
Cdd:NF000106 318 ITGQKTSEAADGG-----PQDGPQD 337
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1295-1551 |
1.09e-15 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 82.25 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1295 KKKNCFSKRKK---KIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGGGEPLGflgycpqeN 1371
Cdd:PRK13545 23 KLKDLFFRSKDgeyHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAIS--------S 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1372 ALWPNLTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGM 1451
Cdd:PRK13545 95 GLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1452 DPEGQQQMWQVIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGkDYLLEMKLKNLAQMEPL 1531
Cdd:PRK13545 175 DQTFTKKCLDKMN-EFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYD-EFLKKYNQMSVEERKDF 252
|
250 260
....*....|....*....|
gi 27477115 1532 HAEILRLFPQAAQQERFSSL 1551
Cdd:PRK13545 253 REEQISQFQHGLLQEDQTGR 272
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1272-1497 |
1.19e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.02 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1272 MAVRDFDETPVIIASCLRKEYAGKKkncfskrkkkiATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVI 1351
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQYSGVE-----------VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1352 LKGS-------GGGEPLGfLGYCPQENALWPNLTVRQHLEVyaavkGL-RKGDAMIAITRLVDALKLQDQLKAPVKTLsE 1423
Cdd:PRK15439 70 IGGNpcarltpAKAHQLG-IYLVPQEPLLFPNLSVKENILF-----GLpKRQASMQKMKQLLAALGCQLDLDSSAGSL-E 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 1424 GIKRKLCFVL-SILGNPSVVLLDEPSTGMDPEGQQQMWQVIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSG 1497
Cdd:PRK15439 143 VADRQIVEILrGLMRDSRILILDEPTASLTPAETERLFSRIRE-LLAQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1308-1499 |
1.21e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 78.97 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKgsggGEPL--------------GFLGYCPQENAL 1373
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIK----GEPIkydkksllevrktvGIVFQNPDDQLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1374 WPnlTVRQHLEVYAAVKGLRKGDAMiaiTRLVDALK---LQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1450
Cdd:PRK13639 93 AP--TVEEDVAFGPLNLGLSKEEVE---KRVKEALKavgMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27477115 1451 MDPEGQQqmwQVIRATFRNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:PRK13639 168 LDPMGAS---QIMKLLYDLNKEGitIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
483-649 |
1.21e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.03 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 483 IKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTlsRMadieniskftG 562
Cdd:COG0488 1 LENLSKSFGGR----PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL--RI----------G 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 563 FCPQSNVQFGFLTVKEN-LRLFAKIKGIL------------PHEVEKEVQRVVQELEMEN-------IQDILAQ------ 616
Cdd:COG0488 65 YLPQEPPLDDDLTVLDTvLDGDAELRALEaeleeleaklaePDEDLERLAELQEEFEALGgweaearAEEILSGlgfpee 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27477115 617 -------NLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLD 649
Cdd:COG0488 145 dldrpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
481-694 |
1.51e-15 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 78.69 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYA-----GKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMaDIE 555
Cdd:TIGR02769 3 LEVRDVTHTYRtgglfGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQL-DRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 556 NISKF------------TGFCPQSNVQFgflTVKENLRLFAKIKgilphevEKEVQRVVQEL--EME---NIQDILAQNL 618
Cdd:TIGR02769 82 QRRAFrrdvqlvfqdspSAVNPRMTVRQ---IIGEPLRHLTSLD-------ESEQKARIAELldMVGlrsEDADKLPRQL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 619 SGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVI--LFSTQFIDEADILADRKVFISNGKL 694
Cdd:TIGR02769 152 SGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
481-694 |
1.86e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 77.83 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAgkceRVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYN-HTLSRMADIENISK 559
Cdd:PRK09493 2 IEFKNVSKHFG----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlKVNDPKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 FTGFCPQSNVQFGFLTVKENLrLFA--KIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQ 637
Cdd:PRK09493 78 EAGMVFQQFYLFPHLTALENV-MFGplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27477115 638 VLLLDEPTAGLDPLSRHRIWNLLK----EGKSDRVILFSTQFideADILADRKVFISNGKL 694
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQdlaeEGMTMVIVTHEIGF---AEKVASRLIFIDKGRI 214
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1297-1502 |
1.92e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 81.37 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1297 KNCFSKRKKKIatRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGS--GGGEPL-------GFLGYC 1367
Cdd:PRK09700 269 RNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdiSPRSPLdavkkgmAYITES 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1368 PQENALWPNLTVRQHLEVYAAVKGLRKGDAMiAITRLVDALKLQDQLKA-----------PVKTLSEGIKRKLCFVLSIL 1436
Cdd:PRK09700 347 RRDNGFFPNFSIAQNMAISRSLKDGGYKGAM-GLFHEVDEQRTAENQREllalkchsvnqNITELSGGNQQKVLISKWLC 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 1437 GNPSVVLLDEPSTGMDPEGQQQMWQVIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCI 1502
Cdd:PRK09700 426 CCPEVIIFDEPTRGIDVGAKAEIYKVMR-QLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
486-674 |
2.15e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.20 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 486 LKKEYAGKCERVEALKG-----VVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTlsrmadIENISkf 560
Cdd:PRK10762 249 LDKAPGEVRLKVDNLSGpgvndVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHE------VVTRS-- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 tgfcPQSNVQFGF---------------LTVKEN-----LRLFAKIKGILPHEveKEVQRVVQELEMENI----QDILAQ 616
Cdd:PRK10762 321 ----PQDGLANGIvyisedrkrdglvlgMSVKENmsltaLRYFSRAGGSLKHA--DEQQAVSDFIRLFNIktpsMEQAIG 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477115 617 NLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLL----KEGKSdrVILFSTQ 674
Cdd:PRK10762 395 LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLInqfkAEGLS--IILVSSE 454
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1311-1522 |
2.34e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 78.23 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1311 NVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKgsggGEPLgflgycpQENALWpnlTVRQHLE------ 1384
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIID----GDLL-------TEENVW---DIRHKIGmvfqnp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1385 ----VYAAVK-----GLR-KG-DAMIAITRLVDALKL---QD-QLKAPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPST 1449
Cdd:PRK13650 91 dnqfVGATVEddvafGLEnKGiPHEEMKERVNEALELvgmQDfKEREPAR-LSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27477115 1450 GMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQHLKSKfGKDyLLEMKL 1522
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSR-GND-LLQLGL 239
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
500-698 |
2.92e-15 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 80.85 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 500 LKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMaDIENISKFTGFCPQsNVQFGFLTVKEN 579
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQW-DRETFGKHIGYLPQ-DVELFPGTVAEN 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 580 LRLF------------AKIKGIlpHEVekevqrvVQELEMENIQDILA--QNLSGGQNRKLTFGIAILGDPQVLLLDEPT 645
Cdd:TIGR01842 412 IARFgenadpekiieaAKLAGV--HEL-------ILRLPDGYDTVIGPggATLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27477115 646 AGLDPLSRHRIWNLLKEGKSDRVI-LFSTQFIdEADILADRKVFISNGKLKCAG 698
Cdd:TIGR01842 483 SNLDEEGEQALANAIKALKARGITvVVITHRP-SLLGCVDKILVLQDGRIARFG 535
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
498-699 |
3.18e-15 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 81.32 E-value: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 498 EALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMaDIENISKFTGFCPQSNVQFGFlTVK 577
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI-DRHTLRQFINYLPQEPYIFSG-SIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 578 ENLRLFAKiKGILPHEVEKEVQRVVQELEMENIQDIL-------AQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDP 650
Cdd:TIGR01193 566 ENLLLGAK-ENVSQDEIWAACEIAEIKDDIENMPLGYqtelseeGSSISGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27477115 651 LSRHRIW-NLLKegKSDRVILFSTQFIDEADiLADRKVFISNGKLKCAGS 699
Cdd:TIGR01193 645 ITEKKIVnNLLN--LQDKTIIFVAHRLSVAK-QSDKIIVLDHGKIIEQGS 691
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1306-1498 |
3.44e-15 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 76.84 E-value: 3.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1306 KIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKgsggGEPLGFL------------GYCPQENAL 1373
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLID----GTDINKLkgkalrqlrrqiGMIFQQFNL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1374 WPNLTVRQH-----LEVYAAVKGLRKGDAMIAITRLVDALK---LQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLD 1445
Cdd:cd03256 90 IERLSVLENvlsgrLGRRSTWRSLFGLFPKEEKQRALAALErvgLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILAD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 1446 EPSTGMDPEGQQQMWQVIRATfrNTERG--ALLTTHYMAEAEAVCDRVAIMVSGR 1498
Cdd:cd03256 170 EPVASLDPASSRQVMDLLKRI--NREEGitVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
481-702 |
4.13e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 77.44 E-value: 4.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKCErVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSrMADIENISKF 560
Cdd:PRK13642 5 LEVENLVFKYEKESD-VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT-AENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQS-NVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVL 639
Cdd:PRK13642 83 IGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 640 LLDEPTAGLDPLSRHRIWNLLKE--GKSDRVILFSTQFIDEAdILADRKVFISNGKL--KCAGSSLF 702
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEikEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIikEAAPSELF 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1308-1511 |
4.89e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 77.58 E-value: 4.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGF-----------LGYCPQ--ENALW 1374
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILF----DGKPIDYsrkglmklresVGMVFQdpDNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1375 pNLTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1454
Cdd:PRK13636 97 -SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 1455 GQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSK 1511
Cdd:PRK13636 176 GVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
477-694 |
5.08e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 79.68 E-value: 5.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 477 GKEAIRIKNLKkeyagkceRVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIEN 556
Cdd:COG1129 253 GEVVLEVEGLS--------VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 557 ISKFTGFCPQSNVQFGF---LTVKEN-----LRLFAKiKGILPHEVEKE-VQRVVQELemeNI----QDILAQNLSGG-- 621
Cdd:COG1129 325 IRAGIAYVPEDRKGEGLvldLSIRENitlasLDRLSR-GGLLDRRRERAlAEEYIKRL---RIktpsPEQPVGNLSGGnq 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 622 QnrKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLL----KEGKSdrVILFSTQfIDEADILADRKVFISNGKL 694
Cdd:COG1129 401 Q--KVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIrelaAEGKA--VIVISSE-LPELLGLSDRILVMREGRI 472
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1304-1499 |
5.38e-15 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 74.66 E-value: 5.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1304 KKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGFLGYC--------PQENALWp 1375
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITL----DGVPVSDLEKAlsslisvlNQRPYLF- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1376 NLTVRQHLevyaavkGLRkgdamiaitrlvdalklqdqlkapvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEG 1455
Cdd:cd03247 88 DTTLRNNL-------GRR---------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPIT 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27477115 1456 QQQMWQVIRATFRNteRGALLTTHYMAEAEAVcDRVAIMVSGRL 1499
Cdd:cd03247 134 ERQLLSLIFEVLKD--KTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1312-1503 |
5.60e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.12 E-value: 5.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1312 VSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGFL---------GYCPQENALWPNLTVRQH 1382
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLV----AGDDVEALsaraasrrvASVPQDTSLSFEFDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1383 LEVYAAVKGLRKGDAMIAITRLVD-------ALKLQDQlkaPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEG 1455
Cdd:PRK09536 98 VEMGRTPHRSRFDTWTETDRAAVEramertgVAQFADR---PVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27477115 1456 QQQMWQVIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1503
Cdd:PRK09536 175 QVRTLELVR-RLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
479-692 |
5.71e-15 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 75.93 E-value: 5.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 479 EAIRIKNLKKEYA-----GKceRVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVtVYNHTLSR--M 551
Cdd:COG4778 3 TLLEVENLSKTFTlhlqgGK--RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSI-LVRHDGGWvdL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 552 A-----DIENISKFT-GFCPQsnvqfgFL----------TVKENLRLfakiKGILPHEVEKEVQRVVQELemeNIQDILA 615
Cdd:COG4778 80 AqasprEILALRRRTiGYVSQ------FLrviprvsaldVVAEPLLE----RGVDREEARARARELLARL---NLPERLW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 616 Q----NLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVILFSTqFIDEA--DILADRKVFI 689
Cdd:COG4778 147 DlppaTFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGI-FHDEEvrEAVADRVVDV 225
|
...
gi 27477115 690 SNG 692
Cdd:COG4778 226 TPF 228
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1288-1499 |
5.73e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 78.30 E-value: 5.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1288 LRKEYAGKKKncfskrkKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGFLGyc 1367
Cdd:PRK11153 7 ISKVFPQGGR-------TIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLV----DGQDLTALS-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1368 pqENALwpNLTVR------QHLE------VYAAV------KGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKL 1429
Cdd:PRK11153 74 --EKEL--RKARRqigmifQHFNllssrtVFDNValplelAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477115 1430 CFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRATfrNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDI--NRELGltIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1310-1506 |
6.00e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 76.69 E-value: 6.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGflGYCPQENALwpNLTV-RQH------ 1382
Cdd:COG4559 18 DDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRL----NGRPLA--AWSPWELAR--RRAVlPQHsslafp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1383 ---LEV-------YAAVKGLRKGDAMIAITRlVDALKLQDQLkapVKTLSEGIK------RKLCFVL-SILGNPSVVLLD 1445
Cdd:COG4559 90 ftvEEVvalgrapHGSSAAQDRQIVREALAL-VGLAHLAGRS---YQTLSGGEQqrvqlaRVLAQLWePVDGGPRWLFLD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1446 EPSTGMDPEGQQQMWQVIRatfRNTERGA--------L-LTTHYmaeaeavCDRVAIMVSGRLRCIGSIQ 1506
Cdd:COG4559 166 EPTSALDLAHQHAVLRLAR---QLARRGGgvvavlhdLnLAAQY-------ADRILLLHQGRLVAQGTPE 225
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
481-692 |
6.31e-15 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 79.76 E-value: 6.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKceRVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLS--RMADIENIS 558
Cdd:TIGR02203 331 VEFRNVTFRYPGR--DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAdyTLASLRRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 559 KFTGfcpQSNVQFGFlTVKENLRlFAKIKGIlpheVEKEVQRVvqeLEMENIQDILAQ--------------NLSGGQNR 624
Cdd:TIGR02203 409 ALVS---QDVVLFND-TIANNIA-YGRTEQA----DRAEIERA---LAAAYAQDFVDKlplgldtpigengvLLSGGQRQ 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27477115 625 KLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLK---EGKSDRVILFSTQFIDEAD--ILADRKVFISNG 692
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESERLVQAALErlmQGRTTLVIAHRLSTIEKADriVVMDDGRIVERG 549
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1305-1517 |
7.14e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 80.55 E-value: 7.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1305 KKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVilkgsgggEPLGflG----------------YCP 1368
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRV--------EVLG--GdmadarhrravcpriaYMP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1369 Q---ENaLWPNLTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRK--LCFVLsiLGNPSVVL 1443
Cdd:NF033858 83 QglgKN-LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKlgLCCAL--IHDPDLLI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 1444 LDEPSTGMDPEGQQQMWQVIrATFRnTERGA---LLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSKFGKDYL 1517
Cdd:NF033858 160 LDEPTTGVDPLSRRQFWELI-DRIR-AERPGmsvLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLARTGADTL 233
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1288-1499 |
9.32e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 77.43 E-value: 9.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1288 LRKEYAGKKKncfskrkKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGFLGyc 1367
Cdd:COG1135 7 LSKTFPTKGG-------PVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLV----DGVDLTALS-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1368 pqENALWP------------NL----TVRQH----LEvyaaVKGLRKGDamiaITRLVDAL----KLQDQLKAPVKTLSE 1423
Cdd:COG1135 74 --ERELRAarrkigmifqhfNLlssrTVAENvalpLE----IAGVPKAE----IRKRVAELlelvGLSDKADAYPSQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1424 G------IKRKLCfvlsilGNPSVVLLDEPSTGMDPEGQQQMWQVIRatfR-NTERGA--LLTTHYMAEAEAVCDRVAIM 1494
Cdd:COG1135 144 GqkqrvgIARALA------NNPKVLLCDEATSALDPETTRSILDLLK---DiNRELGLtiVLITHEMDVVRRICDRVAVL 214
|
....*
gi 27477115 1495 VSGRL 1499
Cdd:COG1135 215 ENGRI 219
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1305-1511 |
1.11e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 76.41 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1305 KKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG-----SGGGEPLGFL----GYCPQ--ENAL 1373
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpETGNKNLKKLrkkvSLVFQfpEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1374 WPNlTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQL--KAPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPSTGM 1451
Cdd:PRK13641 99 FEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLisKSPFE-LSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27477115 1452 DPEGQQQMWQViratFRNTERGA---LLTTHYMAEAEAVCDRVAIMVSGRLrcigsIQHLKSK 1511
Cdd:PRK13641 177 DPEGRKEMMQL----FKDYQKAGhtvILVTHNMDDVAEYADDVLVLEHGKL-----IKHASPK 230
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1307-1498 |
1.17e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 75.80 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1307 IATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKgsggGEPLGflGYCPQENA-------------- 1372
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLR----GQHIE--GLPGHQIArmgvvrtfqhvrlf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1373 ----LWPNLTVRQHLEVYAAV-KGLRK--------GDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNP 1439
Cdd:PRK11300 93 remtVIENLLVAQHQQLKTGLfSGLLKtpafrraeSEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 1440 SVVLLDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1498
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1308-1506 |
1.54e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 78.29 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGGGE-------PLGfLGYCPQENALWPNLTVR 1380
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKldhklaaQLG-IGIIYQELSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1381 QHLEV------------YAAVKGLRKGDAMiaitrLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPS 1448
Cdd:PRK09700 99 ENLYIgrhltkkvcgvnIIDWREMRVRAAM-----MLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 1449 TGMDPEGQQQMWQVIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQ 1506
Cdd:PRK09700 174 SSLTNKEVDYLFLIMN-QLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
481-700 |
1.65e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.43 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYagkcERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGL----SVPTSgSVTVYNHTLSRMA---- 552
Cdd:PRK09984 5 IRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGS-HIELLGRTVQREGrlar 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 553 DIENISKFTGFCPQsnvQFGF---LTVKENLRLFAK-----IKGILPHEVEKEVQRVVQELE---MENIQDILAQNLSGG 621
Cdd:PRK09984 80 DIRKSRANTGYIFQ---QFNLvnrLSVLENVLIGALgstpfWRTCFSWFTREQKQRALQALTrvgMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 622 QNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-GKSDRVILFST-QFIDEADILADRKVFISNGKLKCAGS 699
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDiNQNDGITVVVTlHQVDYALRYCERIVALRQGHVFYDGS 236
|
.
gi 27477115 700 S 700
Cdd:PRK09984 237 S 237
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1299-1518 |
1.79e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 75.61 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1299 CFSKRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKgsggGEPL------------GFLGY 1366
Cdd:PRK13652 10 CYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIR----GEPItkenirevrkfvGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1367 CPQENALWPnlTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDE 1446
Cdd:PRK13652 86 NPDDQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477115 1447 PSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLkskFGKDYLL 1518
Cdd:PRK13652 164 PTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI---FLQPDLL 232
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1310-1518 |
1.82e-14 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 74.83 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGS--GGGEPLGF---LGYCPQENALWpNLTVRQHLE 1384
Cdd:cd03252 19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlALADPAWLrrqVGVVLQENVLF-NRSIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1385 VYAAVKGLRKgdaMIAITRLVDALKLQDQLKAPVKT--------LSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1456
Cdd:cd03252 98 LADPGMSMER---VIEAAKLAGAHDFISELPEGYDTivgeqgagLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477115 1457 QQMWQVIRATFRNteRGALLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFGKDYLL 1518
Cdd:cd03252 175 HAIMRNMHDICAG--RTVIIIAHRLSTVKNA-DRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
483-694 |
2.16e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 75.10 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 483 IKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVtvynhtlsrmadieniskFTG 562
Cdd:PRK11247 15 LNAVSKRYGER----TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------------------LAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 563 FCPQSNVQfgfltvkENLRLFAKIKGILPHeveKEV-------------QRVVQELEMENIQDiLAQN----LSGGQNRK 625
Cdd:PRK11247 73 TAPLAEAR-------EDTRLMFQDARLLPW---KKVidnvglglkgqwrDAALQALAAVGLAD-RANEwpaaLSGGQKQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 626 LTFGIAILGDPQVLLLDEPTAGLDPLSR-------HRIWnlLKEGKSdrvILFSTQFIDEADILADRKVFISNGKL 694
Cdd:PRK11247 142 VALARALIHRPGLLLLDEPLGALDALTRiemqdliESLW--QQHGFT---VLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
481-698 |
3.01e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 74.62 E-value: 3.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLS---------RM 551
Cdd:PRK10619 6 LNVIDLHKRYGEH----EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 552 ADIENI----SKFTGFCPQSNVqFGFLTVKEN-LRLFAKIKGILPHEVEKEVQRVVQELEM-ENIQDILAQNLSGGQNRK 625
Cdd:PRK10619 82 ADKNQLrllrTRLTMVFQHFNL-WSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 626 LTFGIAILGDPQVLLLDEPTAGLDPL---SRHRIWN-LLKEGKSDRVILFSTQFideADILADRKVFISNGKLKCAG 698
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPElvgEVLRIMQqLAEEGKTMVVVTHEMGF---ARHVSSHVIFLHQGKIEEEG 234
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1308-1494 |
3.48e-14 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 77.33 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPL---------GFLGYCPQENALWPNlT 1378
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAV----NGVPLadadadswrDQIAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1379 VRQHLEVYAAVKglrKGDAMIAITRLVDALKLQDQLKAPVKT--------LSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1450
Cdd:TIGR02857 412 IAENIRLARPDA---SDAEIREALERAGLDEFVAALPQGLDTpigeggagLSGGQAQRLALARAFLRDAPLLLLDEPTAH 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27477115 1451 MDPEGQQQMWQVIRATFRNteRGALLTTHYMAEAEAvCDRVAIM 1494
Cdd:TIGR02857 489 LDAETEAEVLEALRALAQG--RTVLLVTHRLALAAL-ADRIVVL 529
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1300-1529 |
4.36e-14 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 74.08 E-value: 4.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1300 FSKRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVilkgsgggEPLGFLGYCPQENALWPNLTV 1379
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV--------DRNGEVSVIAISAGLSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1380 RQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1459
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1460 WQVIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFgKDYLLEMKLKNLAQME 1529
Cdd:PRK13546 183 LDKIY-EFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKY-EAFLNDFKKKSKAEQK 250
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1305-1522 |
4.47e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 74.28 E-value: 4.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1305 KKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLgflgycpQENALWpnlTVRQHLE 1384
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV----GGMVL-------SEETVW---DVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1385 ----------VYAAVK-----GLRKG----DAMiaITRLVDALKL---QDQLKAPVKTLSEGIKRKLCFVLSILGNPSVV 1442
Cdd:PRK13635 85 mvfqnpdnqfVGATVQddvafGLENIgvprEEM--VERVDQALRQvgmEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1443 LLDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQHLkSKFGKDyLLEMKL 1522
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEI-FKSGHM-LQEIGL 239
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
499-693 |
4.58e-14 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 72.89 E-value: 4.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 499 ALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYnhtlSRMAdieniskftgFCPQSN-VQFGflTVK 577
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP----GSIA----------YVSQEPwIQNG--TIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 578 ENLrLFAKikgilPHEvEKEVQRVVQELEMENIQDILAQ-----------NLSGGQNRKLTFGIAILGDPQVLLLDEPTA 646
Cdd:cd03250 84 ENI-LFGK-----PFD-EERYEKVIKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27477115 647 GLDPLSRHRIWN--LLKEGKSDRVILFST---QFIDEadilADRKVFISNGK 693
Cdd:cd03250 157 AVDAHVGRHIFEncILGLLLNNKTRILVThqlQLLPH----ADQIVVLDNGR 204
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
481-698 |
5.23e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.03 E-value: 5.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGkcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRmADIENISKF 560
Cdd:PRK09536 4 IDVSDLSVEFGD----TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEA-LSARAASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQ-SNVQFGFlTVKENLRLfakikGILPHEV---------EKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGI 630
Cdd:PRK09536 79 VASVPQdTSLSFEF-DVRQVVEM-----GRTPHRSrfdtwtetdRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 631 AILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-GKSDRVILFSTQFIDEADILADRKVFISNGKLKCAG 698
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRlVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
496-694 |
6.21e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.49 E-value: 6.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 496 RVEALKG------VVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIENISKFTGFCPQSNV 569
Cdd:PRK11288 259 RLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDRK 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 570 QFGFL---TVKENL-----RLFAKIKGILPHEVEKE-VQRVVQELemeNI------QDILaqNLSGGQNRKltfgiAILG 634
Cdd:PRK11288 339 AEGIIpvhSVADNInisarRHHLRAGCLINNRWEAEnADRFIRSL---NIktpsreQLIM--NLSGGNQQK-----AILG 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 635 -----DPQVLLLDEPTAGLDPLSRHRIWNLLKE-GKSDRVILFSTQFIDEADILADRKVFISNGKL 694
Cdd:PRK11288 409 rwlseDMKVILLDEPTRGIDVGAKHEIYNVIYElAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
500-661 |
6.37e-14 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 72.30 E-value: 6.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 500 LKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPT---SGSVTVYNHTLSrmadiENISKFTG---FCPQSNVQFGF 573
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYK-----EFAEKYPGeiiYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 574 LTVKENLRLFAKIKGilpheveKEVQRVVqelemeniqdilaqnlSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSR 653
Cdd:cd03233 98 LTVRETLDFALRCKG-------NEFVRGI----------------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
....*...
gi 27477115 654 HRIWNLLK 661
Cdd:cd03233 155 LEILKCIR 162
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1280-1504 |
6.75e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 75.37 E-value: 6.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1280 TPVIIASCLRKEYAGKKkncfskrkkkiATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGgge 1359
Cdd:PRK09452 12 SPLVELRGISKSFDGKE-----------VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1360 plgfLGYCPQEN----------ALWPNLTVRQHLEVyaavkGLR---KGDAMIAiTRLVDALK---LQDQLKAPVKTLSE 1423
Cdd:PRK09452 78 ----ITHVPAENrhvntvfqsyALFPHMTVFENVAF-----GLRmqkTPAAEIT-PRVMEALRmvqLEEFAQRKPHQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1424 GIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1503
Cdd:PRK09452 148 GQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
.
gi 27477115 1504 S 1504
Cdd:PRK09452 228 T 228
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
500-656 |
7.01e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 76.84 E-value: 7.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 500 LKGVVFDIYEGQITALLGHSGAGKTTLLNILSGL--SVPTSGSVTVYNHTLSRmadieNISKFTGFCPQSNVQFGFLTVK 577
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRiqGNNFTGTILANNRKPTK-----QILKRTGFVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 578 ENLRLFAKIKgiLPHEVEKEV-----QRVVQELEMENIQDILAQN-----LSGGQNRKLTFGIAILGDPQVLLLDEPTAG 647
Cdd:PLN03211 159 ETLVFCSLLR--LPKSLTKQEkilvaESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
....*....
gi 27477115 648 LDPLSRHRI 656
Cdd:PLN03211 237 LDATAAYRL 245
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
477-699 |
7.36e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.50 E-value: 7.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 477 GKEAIRIKNLKKEYAGKC-ERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTV------------ 543
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKQeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 544 ---YNHTLSRMADIENISKFTGFCPQ-SNVQFGFLTVKENLrLFAKIK-GILPHEVEKEVQRVVQELEMEniQDILAQN- 617
Cdd:PRK13631 98 eliTNPYSKKIKNFKELRRRVSMVFQfPEYQLFKDTIEKDI-MFGPVAlGVKKSEAKKLAKFYLNKMGLD--DSYLERSp 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 618 --LSGGQNRKltfgIAILG----DPQVLLLDEPTAGLDPLSRHRIWNLLKEGK-SDRVILFSTQFIDEADILADRKVFIS 690
Cdd:PRK13631 175 fgLSGGQKRR----VAIAGilaiQPEILIFDEPTAGLDPKGEHEMMQLILDAKaNNKTVFVITHTMEHVLEVADEVIVMD 250
|
....*....
gi 27477115 691 NGKLKCAGS 699
Cdd:PRK13631 251 KGKILKTGT 259
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1289-1514 |
7.54e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 76.62 E-value: 7.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1289 RKEYAGKKKNCFSKRK-KKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGdtKPTAGqviLKGSGG----GEPLG- 1362
Cdd:TIGR00955 20 WKQLVSRLRGCFCRERpRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAF--RSPKG---VKGSGSvllnGMPIDa 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1363 -----FLGYCPQENALWPNLTVRQHLEVYAAVK---GLRKGDAMIAITRLVDALKLQD------QLKAPVKTLSEGIKRK 1428
Cdd:TIGR00955 95 kemraISAYVQQDDLFIPTLTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKcantriGVPGRVKGLSGGERKR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1429 LCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRAtFRNTERGALLTTHyMAEAEAVC--DRVAIMVSGRLRCIGSIQ 1506
Cdd:TIGR00955 175 LAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKG-LAQKGKTIICTIH-QPSSELFElfDKIILMAEGRVAYLGSPD 252
|
....*...
gi 27477115 1507 HLKSKFGK 1514
Cdd:TIGR00955 253 QAVPFFSD 260
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
481-712 |
8.01e-14 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 72.65 E-value: 8.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGkceRVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLsRMADIENISKF 560
Cdd:cd03253 1 IEFENVTFAYDP---GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI-REVTLDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQFGfLTVKENLRlFAKikgilPHEVEKEVQRVVqelEMENIQDILAQ--------------NLSGGQNRKL 626
Cdd:cd03253 77 IGVVPQDTVLFN-DTIGYNIR-YGR-----PDATDEEVIEAA---KAAQIHDKIMRfpdgydtivgerglKLSGGEKQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 627 TFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVILF-----STqfIDEADILadrkVFISNGKLKCAGSSL 701
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIViahrlST--IVNADKI----IVLKDGRIVERGTHE 220
|
250
....*....|.
gi 27477115 702 FLKKKWGIgYH 712
Cdd:cd03253 221 ELLAKGGL-YA 230
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
499-689 |
8.56e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.38 E-value: 8.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 499 ALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRmADIENIskfTGFCPQSN-VQFGFLTVK 577
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-ALQKNL---VAYVPQSEeVDWSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 578 ENLRLFAKI--KGILPHEVEKEVQRVVQELEMENIQDILAQN---LSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLS 652
Cdd:PRK15056 98 EDVVMMGRYghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQigeLSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 27477115 653 RHRIWNLLKEGKSD-RVILFSTQFIDEADILADRKVFI 689
Cdd:PRK15056 178 EARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMV 215
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1310-1504 |
1.03e-13 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 71.40 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITG--DTKPTAGQVILKGSgggeplgflgycpqenalwpNLTvrqHLEVYA 1387
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGE--------------------DIT---DLPPEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1388 -AVKGLrkgdaMIAITRLVD--ALKLQDQLKAPVKTLSEGiKRKLCFVLSILG-NPSVVLLDEPSTGMDPEGQQQMWQVI 1463
Cdd:cd03217 74 rARLGI-----FLAFQYPPEipGVKNADFLRYVNEGFSGG-EKKRNEILQLLLlEPDLAILDEPDSGLDIDALRLVAEVI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27477115 1464 RaTFRNTERGALLTTHYMAEAEAV-CDRVAIMVSGRLRCIGS 1504
Cdd:cd03217 148 N-KLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGD 188
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
505-678 |
1.32e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 75.65 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 505 FDIYEGQITALLGHSGAGKTTLLNILSGLsVPTSGSVTVYNHTLSRMaDIENISKFTGFCPQsNVQFGFLTVKENLRLfA 584
Cdd:PRK11174 371 FTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELREL-DPESWRKHLSWVGQ-NPQLPHGTLRDNVLL-G 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 585 KikgilPHEVEKEVQrvvQELEMENIQDILAQ--------------NLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDP 650
Cdd:PRK11174 447 N-----PDASDEQLQ---QALENAWVSEFLPLlpqgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180
....*....|....*....|....*...
gi 27477115 651 LSRHRIWNLLKEGKSDRVILFSTQFIDE 678
Cdd:PRK11174 519 HSEQLVMQALNAASRRQTTLMVTHQLED 546
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1310-1504 |
1.88e-13 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 70.90 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSG-GGEPLGFL----GYCPQENALWPNlTVRQHLE 1384
Cdd:cd03369 25 KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDiSTIPLEDLrsslTIIPQDPTLFSG-TIRSNLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1385 VYAavkglRKGDAMIaitrlVDALKLqdqlKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIR 1464
Cdd:cd03369 104 PFD-----EYSDEEI-----YGALRV----SEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27477115 1465 ATFRNTergALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1504
Cdd:cd03369 170 EEFTNS---TILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1299-1511 |
2.38e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 72.33 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1299 CFSKRK-KKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG-----SGGGEPLGFLGYCPQEna 1372
Cdd:PRK13632 14 SFSYPNsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskENLKEIRKKIGIIFQN-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1373 lwPN-----LTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCfVLSILG-NPSVVLLDE 1446
Cdd:PRK13632 92 --PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVA-IASVLAlNPEIIIFDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 1447 pSTGM-DPEGQQQMWQVIRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQH-LKSK 1511
Cdd:PRK13632 169 -STSMlDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEiLNNK 233
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1311-1517 |
3.09e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 71.20 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1311 NVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG------SGGGEPLGFL-----GYCPQENALWPNLTV 1379
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRElrrnvGMVFQQYNLWPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1380 RQHL-EVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1458
Cdd:PRK11124 100 QQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQ 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27477115 1459 MWQVIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLK----SKFgKDYL 1517
Cdd:PRK11124 180 IVSIIRE-LAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTqpqtEAF-KNYL 240
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1300-1513 |
3.42e-13 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 70.72 E-value: 3.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1300 FSKRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG-SGGGEPLGFL----GYCPQENALW 1374
Cdd:cd03254 10 FSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGiDIRDISRKSLrsmiGVVLQDTFLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1375 PNlTVRQHL----------EVYAAVKGLRkgdamiaITRLVDALK--LQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVV 1442
Cdd:cd03254 90 SG-TIMENIrlgrpnatdeEVIEAAKEAG-------AHDFIMKLPngYDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27477115 1443 LLDEPSTGMDPEGQQQMWQVIRATFRNteRGALLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFG 1513
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKG--RTSIIIAHRLSTIKNA-DKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
481-699 |
3.43e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 71.96 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKCE-RVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHT----LSRMADIE 555
Cdd:PRK13645 7 IILDNVSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAipanLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 556 NISKFTGFCPQ-SNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMEniQDILAQN---LSGGQNRKLTFGIA 631
Cdd:PRK13645 87 RLRKEIGLVFQfPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLP--EDYVKRSpfeLSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27477115 632 ILGDPQVLLLDEPTAGLDPLSRHRIWNL---LKEGKSDRVILFsTQFIDEADILADRKVFISNGKLKCAGS 699
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLferLNKEYKKRIIMV-THNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
480-699 |
3.43e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 74.48 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGkcERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADiENISK 559
Cdd:PRK11160 338 SLTLNNVSFTYPD--QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE-AALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 FTGFCPQSnVQFGFLTVKENLRLfAKikgilPHEVEKEVQRVVQELEMENiqdiLAQN--------------LSGGQNRK 625
Cdd:PRK11160 415 AISVVSQR-VHLFSATLRDNLLL-AA-----PNASDEALIEVLQQVGLEK----LLEDdkglnawlgeggrqLSGGEQRR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 626 LTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVILFST-------QFideadilaDRKVFISNGKLKCAG 698
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMIThrltgleQF--------DRICVMDNGQIIEQG 555
|
.
gi 27477115 699 S 699
Cdd:PRK11160 556 T 556
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1310-1504 |
7.57e-13 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 69.44 E-value: 7.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTI----KMITgdtkPTAGQVILkgsgGGEPL---------GFLGYCPQEnalwPN 1376
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLlalfRLVE----LSSGSILI----DGVDIskiglhdlrSRISIIPQD----PV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1377 L---TVRQHL---------EVYAAVKglrkgdaMIAITRLVDAL--KLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVV 1442
Cdd:cd03244 89 LfsgTIRSNLdpfgeysdeELWQALE-------RVGLKEFVESLpgGLDTVVEEGGENLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 1443 LLDEPSTGMDPEGQQQMWQVIRATFRNTergALLT-THYMaeaEAV--CDRVAIMVSGRLRCIGS 1504
Cdd:cd03244 162 VLDEATASVDPETDALIQKTIREAFKDC---TVLTiAHRL---DTIidSDRILVLDKGRVVEFDS 220
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1308-1517 |
7.63e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 70.79 E-value: 7.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGGGEP---------LGFLGYCPQ--------- 1369
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsklqgirklVGIVFQNPEtqfvgrtve 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1370 -------ENALWPNLTVRQHLEVYAAVKGLRKGdamiaitrlvdalklqdQLKAPvKTLSEGIKRKLCFVLSILGNPSVV 1442
Cdd:PRK13644 97 edlafgpENLCLPPIEIRKRVDRALAEIGLEKY-----------------RHRSP-KTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 1443 LLDEPSTGMDPEGQQqmwQVIRATFRNTERGALL--TTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFGKDYL 1517
Cdd:PRK13644 159 IFDEVTSMLDPDSGI---AVLERIKKLHEKGKTIvyITHNLEELHDA-DRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
501-649 |
8.40e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 71.67 E-value: 8.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 501 KGVVFD-----IYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVynhtlsrmaDIENISKFT----GFCP--QSNV 569
Cdd:PRK11432 18 SNTVIDnlnltIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI---------DGEDVTHRSiqqrDICMvfQSYA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 570 QFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLD 649
Cdd:PRK11432 89 LFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
479-650 |
1.01e-12 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 70.21 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 479 EAIRIKNLKKEYAGkcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLsRM------- 551
Cdd:COG4598 7 PALEVRDLHKSFGD----LEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEI-RLkpdrdge 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 552 ---AD---IENISKFTGFCPQSNVQFGFLTVKENLrLFAKI--KGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQN 623
Cdd:COG4598 82 lvpADrrqLQRIRTRLGMVFQSFNLWSHMTVLENV-IEAPVhvLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQ 160
|
170 180
....*....|....*....|....*..
gi 27477115 624 RKLTFGIAILGDPQVLLLDEPTAGLDP 650
Cdd:COG4598 161 QRAAIARALAMEPEVMLFDEPTSALDP 187
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
500-650 |
1.05e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 69.05 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 500 LKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVP---TSGSVTVYNHTLSRMAdIEniSKFTGFCPQSNVQFGFLTV 576
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALP-AE--QRRIGILFQDDLLFPHLSV 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 577 KENLrLFAkikgiLPHEVEKE-----VQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDP 650
Cdd:COG4136 94 GENL-AFA-----LPPTIGRAqrrarVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1307-1479 |
1.25e-12 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 72.39 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1307 IATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG-----SGGGEPLGFLGYCPQENALWpNLTVRQ 1381
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssLDQDEVRRRVSVCAQDAHLF-DTTVRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1382 HL----------EVYAAVKGLRKGDamiaitrLVDALK--LQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPST 1449
Cdd:TIGR02868 428 NLrlarpdatdeELWAALERVGLAD-------WLRALPdgLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTE 500
|
170 180 190
....*....|....*....|....*....|
gi 27477115 1450 GMDPEGQQQMWQVIRATfrNTERGALLTTH 1479
Cdd:TIGR02868 501 HLDAETADELLEDLLAA--LSGRTVVLITH 528
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1280-1514 |
1.26e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 70.10 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1280 TPVIIASCLRKEYAGKkkNCFSKRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVilkgSGGGE 1359
Cdd:PRK10419 1 MTLLNVSGLSHHYAHG--GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNV----SWRGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1360 PLGFLGYCPQE--------------NALWPNLTVR-------QHLEVYAAVKGLRKGDAMIaitRLVDaLKLQDQLKAPv 1418
Cdd:PRK10419 75 PLAKLNRAQRKafrrdiqmvfqdsiSAVNPRKTVReiireplRHLLSLDKAERLARASEML---RAVD-LDDSVLDKRP- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1419 KTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1498
Cdd:PRK10419 150 PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQ 229
|
250
....*....|....*....
gi 27477115 1499 L---RCIGSIQHLKSKFGK 1514
Cdd:PRK10419 230 IvetQPVGDKLTFSSPAGR 248
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
481-670 |
1.37e-12 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 68.59 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKCERVeaLKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMaDIENISKF 560
Cdd:cd03369 7 IEVENLSVRYAPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI-PLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQF-GflTVKENLRLFAkikgilpHEVEKEVQRVVQELEMENiqdilaqNLSGGQNRKLTFGIAILGDPQVL 639
Cdd:cd03369 84 LTIIPQDPTLFsG--TIRSNLDPFD-------EYSDEEIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190
....*....|....*....|....*....|.
gi 27477115 640 LLDEPTAGLDPLSRHRIWNLLKEGKSDRVIL 670
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIREEFTNSTIL 178
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1296-1517 |
1.38e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 71.60 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1296 KKNCFSKRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGGGEPLGF---------LGY 1366
Cdd:PRK10070 31 KEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAelrevrrkkIAM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1367 CPQENALWPNLTVRQHLEVYAAVKGLRKGDAMiaiTRLVDALK---LQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVL 1443
Cdd:PRK10070 111 VFQSFALMPHMTVLDNTAFGMELAGINAEERR---EKALDALRqvgLENYAHSYPDELSGGMRQRVGLARALAINPDILL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477115 1444 LDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYL 1517
Cdd:PRK10070 188 MDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYV 261
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1310-1479 |
1.44e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 66.70 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGGgeplgfLGYCPQenalwpnltvrqhlevyaav 1389
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK------IGYFEQ-------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1390 kglrkgdamiaitrlvdalklqdqlkapvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQmwqvIRATFRN 1469
Cdd:cd03221 71 -------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEA----LEEALKE 115
|
170
....*....|
gi 27477115 1470 TERGALLTTH 1479
Cdd:cd03221 116 YPGTVILVSH 125
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
498-699 |
1.84e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 69.65 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 498 EALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTL--SRMADIENISKFTGFCPQSNVQFGFLT 575
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQVATVFQDPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 576 VKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHR 655
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27477115 656 IWNLLKE--GKSDRVILfSTQFIDEADILADRKVFISNGKLKCAGS 699
Cdd:PRK13638 175 MIAIIRRivAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
497-713 |
2.04e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 72.06 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 497 VEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMaDIENISKFTGFCPQSNVQFGfLTV 576
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY-DHHYLHRQVALVGQEPVLFS-GSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 577 KENlrlfakIKGILPHEVEKEVQRVVQE-------LEMENIQDIL----AQNLSGGQNRKLTFGIAILGDPQVLLLDEPT 645
Cdd:TIGR00958 572 REN------IAYGLTDTPDEEIMAAAKAanahdfiMEFPNGYDTEvgekGSQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 646 AGLDPLSRHriwnLLKEGKS--DRVILFSTQFIDEADiLADRKVFISNGKLKCAGSSLFLKKKWGIGYHL 713
Cdd:TIGR00958 646 SALDAECEQ----LLQESRSraSRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
506-662 |
2.60e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.86 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 506 DIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIEnISKFTGFCPQSNVQFGFLTVKEnlrLFAk 585
Cdd:PRK10253 29 EIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE-VARRIGLLAQNATTPGDITVQE---LVA- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 586 iKGILPH---------EVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRI 656
Cdd:PRK10253 104 -RGRYPHqplftrwrkEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
|
....*.
gi 27477115 657 WNLLKE 662
Cdd:PRK10253 183 LELLSE 188
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
448-694 |
3.24e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.85 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 448 RANHVVLENETDSDPTpNDCFEPVSPEFCGKEAIRIKNLKKEYAGkCERV---------------EALKGVVFDIYEGQI 512
Cdd:PRK15439 214 RDGTIALSGKTADLST-DDIIQAITPAAREKSLSASQKLWLELPG-NRRQqaagapvltvedltgEGFRNISLEVRAGEI 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 513 TALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIENISKFTGFCPQSNVQFG-FL----------------- 574
Cdd:PRK15439 292 LGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGlYLdaplawnvcalthnrrg 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 575 ----TVKENLRL--FAKIKGILPHEVEKEVQRvvqelemeniqdilaqnLSGGQNRKLTFGIAILGDPQVLLLDEPTAGL 648
Cdd:PRK15439 372 fwikPARENAVLerYRRALNIKFNHAEQAART-----------------LSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 27477115 649 DPLSRHRIWNLLKEGKSDRV-ILFSTQFIDEADILADRKVFISNGKL 694
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1314-1479 |
3.42e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 67.57 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1314 FCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG--SGGGEPLGFLGYCPQENALWPNLTVRQHLEVYAAVKG 1391
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGktATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1392 LRK----GDAMiAITRLVDalkLQDQLkapVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRATF 1467
Cdd:PRK13543 112 RRAkqmpGSAL-AIVGLAG---YEDTL---VRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHL 184
|
170
....*....|..
gi 27477115 1468 RnTERGALLTTH 1479
Cdd:PRK13543 185 R-GGGAALVTTH 195
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1310-1499 |
3.42e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.92 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKgsggGEPLGF-------------LGYCPQENALWPN 1376
Cdd:PRK11629 26 HNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFN----GQPMSKlssaakaelrnqkLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1377 LTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1456
Cdd:PRK11629 102 FTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27477115 1457 QQMWQVIRATFRNTERGALLTTHYMAEAEAVcDRVAIMVSGRL 1499
Cdd:PRK11629 182 DSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1316-1499 |
4.21e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 67.85 E-value: 4.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1316 VKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQvILKGS---GGGEPLG-----------FLGYCPQENALWPNLTVRQ 1381
Cdd:PRK11264 26 VKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGT-IRVGDitiDTARSLSqqkglirqlrqHVGFVFQNFNLFPHRTVLE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1382 H-LEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1460
Cdd:PRK11264 105 NiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVL 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 27477115 1461 QVIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:PRK11264 185 NTIRQ-LAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1310-1504 |
4.26e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 70.96 E-value: 4.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPL---------GFLGYCPQENALWpNLTVR 1380
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI----DGVDIrdltleslrRQIGVVPQDTFLF-SGTIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1381 QHL----------EVYAAVKglrkgdaMIAITRLVDALKlqDQLKAPV----KTLSEGIKRKLCFVLSILGNPSVVLLDE 1446
Cdd:COG1132 432 ENIrygrpdatdeEVEEAAK-------AAQAHEFIEALP--DGYDTVVgergVNLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 1447 PSTGMDPEGQQQMWQVIRATFRNteRGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGS 1504
Cdd:COG1132 503 ATSALDTETEALIQEALERLMKG--RTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1310-1479 |
4.39e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.90 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG-------SGGGEPLGFLGYcpqENALWPNLTVRQH 1382
Cdd:PRK13540 18 QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikkdlCTYQKQLCFVGH---RSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1383 levyaAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQV 1462
Cdd:PRK13540 95 -----CLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITK 169
|
170
....*....|....*..
gi 27477115 1463 IRAtFRNTERGALLTTH 1479
Cdd:PRK13540 170 IQE-HRAKGGAVLLTSH 185
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1313-1510 |
5.50e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 67.30 E-value: 5.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1313 SFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG------SGGGEPLGFLGycpQENALWPNLTVRQHLEVy 1386
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhtttPPSRRPVSMLF---QENNLFSHLTVAQNIGL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1387 aavkGLRKG--------DAMIAITRLVDALKLQDQLKApvkTLSEGIKRKL----CFVLSilgNPsVVLLDEPSTGMDPE 1454
Cdd:PRK10771 95 ----GLNPGlklnaaqrEKLHAIARQMGIEDLLARLPG---QLSGGQRQRValarCLVRE---QP-ILLLDEPFSALDPA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 1455 GQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKS 1510
Cdd:PRK10771 164 LRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
500-649 |
5.85e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.45 E-value: 5.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 500 LKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVtVYNHTLSrmadieniskfTGFCPQS-NVQFGF-LTVK 577
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-KRNGKLR-----------IGYVPQKlYLDTTLpLTVN 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477115 578 ENLRLFAKIKG--ILPhevekevqrVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLD 649
Cdd:PRK09544 88 RFLRLRPGTKKedILP---------ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1277-1524 |
5.91e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 68.50 E-value: 5.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1277 FDETPVIIASCLRKEYAgkKKNCFSKRkkkiATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVIL---K 1353
Cdd:PRK13645 1 FDFSKDIILDNVSYTYA--KKTPFEFK----ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1354 GSGGGEPLGFLGYCPQENAL---WPNL-----TVRQHLEVYAAVKGLRKGDAMIAITRLVDALKL-QDQLKAPVKTLSEG 1424
Cdd:PRK13645 75 IPANLKKIKEVKRLRKEIGLvfqFPEYqlfqeTIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1425 IKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1504
Cdd:PRK13645 155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
250 260 270
....*....|....*....|....*....|
gi 27477115 1505 I------QHLKSKFGKD----YLLEMKLKN 1524
Cdd:PRK13645 235 PfeifsnQELLTKIEIDppklYQLMYKLKN 264
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
496-649 |
6.57e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.56 E-value: 6.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 496 RVEALKGVVFDiyeGQITALLGHSGAGKTTLLNILSGLSvPTSGSVTVYNHTLSRMaDIENISKFTGFCPQSNVQFGFLT 575
Cdd:COG4138 11 RLGPISAQVNA---GELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDW-SAAELARHRAYLSQQQSPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 576 VKENLRLFAKIKGILPhEVEKEVQRVVQELemeNIQDILAQN---LSGG--QNRKLTfgiAIL--------GDPQVLLLD 642
Cdd:COG4138 86 VFQYLALHQPAGASSE-AVEQLLAQLAEAL---GLEDKLSRPltqLSGGewQRVRLA---AVLlqvwptinPEGQLLLLD 158
|
....*..
gi 27477115 643 EPTAGLD 649
Cdd:COG4138 159 EPMNSLD 165
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1316-1495 |
6.80e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 70.20 E-value: 6.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1316 VKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSgggeplgfLGYCPQENALWPNLTVRQHLevYAAVKglRKG 1395
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK--------ISYKPQYISPDYDGTVEEFL--RSANT--DDF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1396 DAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRATFRNTERGAL 1475
Cdd:COG1245 431 GSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAM 510
|
170 180
....*....|....*....|
gi 27477115 1476 LTTHYMAEAEAVCDRvaIMV 1495
Cdd:COG1245 511 VVDHDIYLIDYISDR--LMV 528
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1312-1465 |
7.16e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.27 E-value: 7.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1312 VSFCVKKGEVIGLLGHNGAGKSTTIKMITGdTKPTAGQVILkgsgGGEPLGFL---------GYCPQENALWPNLTVRQH 1382
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQF----AGQPLEAWsaaelarhrAYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1383 LEVYAAVkGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSIL-----GNPS--VVLLDEPSTGMDPEG 1455
Cdd:PRK03695 90 LTLHQPD-KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLLLLDEPMNSLDVAQ 168
|
170
....*....|
gi 27477115 1456 QQQMWQVIRA 1465
Cdd:PRK03695 169 QAALDRLLSE 178
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
477-694 |
7.53e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.81 E-value: 7.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 477 GKEAIRIKNLKKEYAGKcerveaLKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIEN 556
Cdd:PRK09700 262 HETVFEVRNVTSRDRKK------VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 557 ISKFTGFCPQSNVQFGFL---TVKENLRLFAKIK--------GILPHEVEK---EVQRVVQELEMENI-QDIlaQNLSGG 621
Cdd:PRK09700 336 VKKGMAYITESRRDNGFFpnfSIAQNMAISRSLKdggykgamGLFHEVDEQrtaENQRELLALKCHSVnQNI--TELSGG 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477115 622 QNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-GKSDRVILFSTQFIDEADILADRKVFISNGKL 694
Cdd:PRK09700 414 NQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1310-1498 |
8.21e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 66.13 E-value: 8.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGqviLKGS---GGGEPLGF-------LGYCPQENALWPNLTV 1379
Cdd:cd03233 24 KDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVS---VEGDihyNGIPYKEFaekypgeIIYVSEEDVHFPTLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1380 RQHLEvyAAVKGlrKGDAMiaitrlvdalklqdqlkapVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1459
Cdd:cd03233 101 RETLD--FALRC--KGNEF-------------------VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 27477115 1460 WQVIRaTFRNTERGALLTTHYMA--EAEAVCDRVAIMVSGR 1498
Cdd:cd03233 158 LKCIR-TMADVLKTTTFVSLYQAsdEIYDLFDKVLVLYEGR 197
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1304-1454 |
8.66e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 69.96 E-value: 8.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1304 KKKIaTRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgggEPLGFLGYCPQENALWPNLTVRQHL 1383
Cdd:TIGR03719 17 KKEI-LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP------QPGIKVGYLPQEPQLDPTKTVRENV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1384 ---------------EVYAAV--------KGLRKGDAMIAITRLVDALKLQDQLK------------APVKTLSEGIKRK 1428
Cdd:TIGR03719 90 eegvaeikdaldrfnEISAKYaepdadfdKLAAEQAELQEIIDAADAWDLDSQLEiamdalrcppwdADVTKLSGGERRR 169
|
170 180
....*....|....*....|....*...
gi 27477115 1429 --LCFVLsiLGNPSVVLLDEPSTGMDPE 1454
Cdd:TIGR03719 170 vaLCRLL--LSKPDMLLLDEPTNHLDAE 195
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1308-1508 |
8.77e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.88 E-value: 8.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAG--------------QVI---------LKGSGGGEplgfL 1364
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGlvqcdkmllrrrsrQVIelseqsaaqMRHVRGAD----M 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1365 GYCPQE--NALWPNLTV-RQHLEVYAAVKGLRKGDAMIAITRLVDALKL---QDQLKAPVKTLSEGIKRKLCFVLSILGN 1438
Cdd:PRK10261 107 AMIFQEpmTSLNPVFTVgEQIAESIRLHQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSCR 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1439 PSVVLLDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1508
Cdd:PRK10261 187 PAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1311-1508 |
1.19e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.21 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1311 NVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGGGEP--------LGFLGYcpqenALWPNLTVRQH 1382
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRsiqqrdicMVFQSY-----ALFPHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1383 LEVYAAVKGLRKGDAMiaiTRLVDALKLQDqLKA----PVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1458
Cdd:PRK11432 99 VGYGLKMLGVPKEERK---QRVKEALELVD-LAGfedrYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27477115 1459 MWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1508
Cdd:PRK11432 175 MREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1297-1512 |
1.51e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 69.06 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1297 KNCFSKRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITG--DTKPTAGQVILKGS-----GGGEPLGFLGY-CP 1368
Cdd:TIGR03269 4 KNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHVAlcekcGYVERPSKVGEpCP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1369 --------QENALW-PNLTVRQHLEVYAAVK------------------------GLRKGDAMIAITRLVDALKLQDQLK 1415
Cdd:TIGR03269 84 vcggtlepEEVDFWnLSDKLRRRIRKRIAIMlqrtfalygddtvldnvlealeeiGYEGKEAVGRAVDLIEMVQLSHRIT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1416 APVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMV 1495
Cdd:TIGR03269 164 HIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLE 243
|
250
....*....|....*..
gi 27477115 1496 SGRLRCIGSIQHLKSKF 1512
Cdd:TIGR03269 244 NGEIKEEGTPDEVVAVF 260
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1308-1499 |
1.57e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 65.67 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSG----GGEPLGFL----GYCPQENALWPNLTV 1379
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrlKNREVPFLrrqiGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1380 RQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1459
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27477115 1460 WQVIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:PRK10908 177 LRLFE-EFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1321-1504 |
1.58e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.57 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1321 VIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKgsggGEPLGFlgycpQENALwpnLTVRQHLEV----------YAAVK 1390
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQ----GKPLDY-----SKRGL---LALRQQVATvfqdpeqqifYTDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1391 -----GLRK-GDAMIAITRLVD-ALKLQDQL---KAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1460
Cdd:PRK13638 97 sdiafSLRNlGVPEAEITRRVDeALTLVDAQhfrHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27477115 1461 QVIRATFRNTERgALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1504
Cdd:PRK13638 177 AIIRRIVAQGNH-VIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
476-670 |
1.80e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.68 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 476 CGKEAIRIKNLKKEYAGKCerVEALKGVVFDIY------EGQITALLGHSGAGKTTLLNILSGLSVPTSGSVtvynhtlS 549
Cdd:PRK13409 61 CPFDAISIVNLPEELEEEP--VHRYGVNGFKLYglpipkEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY-------E 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 550 RMADIEN-ISKFTGfcpqSNVQFGFLTVKEN-LRLFAKI----------KGILPHEVEKEVQR-----VVQELEMENIQD 612
Cdd:PRK13409 132 EEPSWDEvLKRFRG----TELQNYFKKLYNGeIKVVHKPqyvdlipkvfKGKVRELLKKVDERgkldeVVERLGLENILD 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 613 ILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVIL 670
Cdd:PRK13409 208 RDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVL 265
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
470-695 |
1.88e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 68.70 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 470 PVSPEFCGKEAIRIKNLKKeYAGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGlSVPT--SGSVTVYNHT 547
Cdd:TIGR02633 247 PHEPHEIGDVILEARNLTC-WDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGkfEGNVFINGKP 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 548 LSRMADIENISKFTGFCPQSNVQFGF---LTVKENLRL-----FAKIKGILPHEVEKEVQRVVQELEMENIQDILA-QNL 618
Cdd:TIGR02633 325 VDIRNPAQAIRAGIAMVPEDRKRHGIvpiLGVGKNITLsvlksFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRL 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 619 SGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLL----KEGKSdrVILFSTQfIDEADILADRKVFISNGKL 694
Cdd:TIGR02633 405 SGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLInqlaQEGVA--IIVVSSE-LAEVLGLSDRVLVIGEGKL 481
|
.
gi 27477115 695 K 695
Cdd:TIGR02633 482 K 482
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1312-1504 |
2.00e-11 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 65.98 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1312 VSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGF----------------------LGYCPQ 1369
Cdd:COG4598 27 VSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRV----GGEEIRLkpdrdgelvpadrrqlqrirtrLGMVFQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1370 ENALWPNLTVRQHL-EVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEG------IKRKLCFvlsilgNPSVV 1442
Cdd:COG4598 103 SFNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGqqqraaIARALAM------EPEVM 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477115 1443 LLDEPSTGMDPEGQQQMWQVIRATfrnTERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1504
Cdd:COG4598 177 LFDEPTSALDPELVGEVLKVMRDL---AEEGRtmLVVTHEMGFARDVSSHVVFLHQGRIEEQGP 237
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
506-685 |
2.00e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 65.89 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 506 DIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLS-RMADIEniSKFTGfcpqsnvqfgflTVKENLRLFA 584
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSyKPQYIK--ADYEG------------TVRDLLSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 585 KIKGILPH-EVEkevqrVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKeg 663
Cdd:cd03237 87 KDFYTHPYfKTE-----IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR-- 159
|
170 180
....*....|....*....|....*....
gi 27477115 664 ksdRVILF--STQFIDEADI-----LADR 685
Cdd:cd03237 160 ---RFAENneKTAFVVEHDIimidyLADR 185
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1310-1499 |
2.02e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 66.26 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKP----TAGQVILKGsgggEPL------GFLGYCPQEN---ALWPN 1376
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDG----KPVapcalrGRKIATIMQNprsAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1377 LTVRQH-LEVYAAVKGLRKGDAMIAItrlVDALKLQDQ---LKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1452
Cdd:PRK10418 96 HTMHTHaRETCLALGKPADDATLTAA---LEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27477115 1453 PEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:PRK10418 173 VVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
478-682 |
2.44e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 68.51 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 478 KEAIRIKNLKKEYAGKCERveALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHtlsrmadieNI 557
Cdd:PRK11176 339 KGDIEFRNVTFTYPGKEVP--ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGH---------DL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 558 SKFTgfcpQSNVQFGFLTVKENLRLF----------AKIKGILPHEVEKeVQRVVQELE----MENIQD-ILAQN---LS 619
Cdd:PRK11176 408 RDYT----LASLRNQVALVSQNVHLFndtianniayARTEQYSREQIEE-AARMAYAMDfinkMDNGLDtVIGENgvlLS 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 620 GGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVIL-----FSTqfIDEAD-IL 682
Cdd:PRK11176 483 GGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLviahrLST--IEKADeIL 549
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1310-1454 |
2.77e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.99 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVilKGSGGGEplgfLGYCPQENALW--PNLTVRQHLEVYA 1387
Cdd:PRK15064 336 KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--KWSENAN----IGYYAQDHAYDfeNDLTLFDWMSQWR 409
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 1388 AVKGlrkGDAMI--AITRLvdaLKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1454
Cdd:PRK15064 410 QEGD---DEQAVrgTLGRL---LFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDME 472
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
494-649 |
3.19e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.44 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 494 CERVEAL--KGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIEN-----ISKFTGFCPQ 566
Cdd:PRK13538 9 CERDERIlfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHqdllyLGHQPGIKTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 567 snvqfgfLTVKENLRLFAKIKGILphevekEVQRVVQELEMENIQ---DILAQNLSGGQNRKltfgIAI----LGDPQVL 639
Cdd:PRK13538 89 -------LTALENLRFYQRLHGPG------DDEALWEALAQVGLAgfeDVPVRQLSAGQQRR----VALarlwLTRAPLW 151
|
170
....*....|
gi 27477115 640 LLDEPTAGLD 649
Cdd:PRK13538 152 ILDEPFTAID 161
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
480-694 |
3.59e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 65.89 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGKCerveALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSG-----SVTVYNHTLSRMADI 554
Cdd:PRK14271 21 AMAAVNLTLGFAGKT----VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 555 ENISKFTGFCPQSNVQFGfLTVKENLRLFAKIKGILPhevEKEVQRVVQELEME-----NIQDILAQN---LSGGQNRKL 626
Cdd:PRK14271 97 LEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVP---RKEFRGVAQARLTEvglwdAVKDRLSDSpfrLSGGQQQLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 627 TFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVILFSTQFIDEADILADRKVFISNGKL 694
Cdd:PRK14271 173 CLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
481-662 |
3.82e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 65.48 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYA-----GKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMA--- 552
Cdd:PRK10419 4 LNVSGLSHHYAhgglsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 553 ------DIENI--SKFTGFCPQSNVQFgflTVKENLRlfaKIKGILPHEVEKEVQRVVQELEM-ENIQDILAQNLSGGQN 623
Cdd:PRK10419 84 rkafrrDIQMVfqDSISAVNPRKTVRE---IIREPLR---HLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQL 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 27477115 624 RKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE 662
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKK 196
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1322-1454 |
3.94e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.84 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1322 IGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgggEPlGF-LGYCPQENALWPNLTVRQHLEvyAAVkglrkGDAMIA 1400
Cdd:PRK11819 36 IGVLGLNGAGKSTLLRIMAGVDKEFEGEARP------AP-GIkVGYLPQEPQLDPEKTVRENVE--EGV-----AEVKAA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1401 ITRL-------------VDAL-----KLQDQLKA------------------------PVKTLSEGIKRK--LCFVLsiL 1436
Cdd:PRK11819 102 LDRFneiyaayaepdadFDALaaeqgELQEIIDAadawdldsqleiamdalrcppwdaKVTKLSGGERRRvaLCRLL--L 179
|
170
....*....|....*...
gi 27477115 1437 GNPSVVLLDEPSTGMDPE 1454
Cdd:PRK11819 180 EKPDMLLLDEPTNHLDAE 197
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1278-1498 |
4.32e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 65.33 E-value: 4.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1278 DETPVIIASCLRKEYAGKKkncfskrkkkiATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGG 1357
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRK-----------GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1358 G-EPLGFLGYcPQENAL----WPnlTVRQHlevyaAVKGLRK--------GDAMIAI----------------TRL-VDA 1407
Cdd:PRK11701 71 QlRDLYALSE-AERRRLlrteWG--FVHQH-----PRDGLRMqvsaggniGERLMAVgarhygdiratagdwlERVeIDA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1408 LKLQDQlkaPvKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAV 1487
Cdd:PRK11701 143 ARIDDL---P-TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLL 218
|
250
....*....|.
gi 27477115 1488 CDRVAIMVSGR 1498
Cdd:PRK11701 219 AHRLLVMKQGR 229
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
500-656 |
5.69e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.35 E-value: 5.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 500 LKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADiENISKFTGFCPQSNVQFGfLTVKEN 579
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYRQQVSYCAQTPTLFG-DTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 580 LRLFAKIKGILPHevEKEVQRVVQELEMEniQDILAQN---LSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRI 656
Cdd:PRK10247 101 LIFPWQIRNQQPD--PAIFLDDLERFALP--DTILTKNiaeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNV 176
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1302-1464 |
6.14e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 63.42 E-value: 6.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1302 KRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITG--DTKPTAGQVILKGSGGGEPLG-FLGYCPQENALWPNLT 1378
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNFQrSTGYVEQQDVHSPNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1379 VRQHLEVYAAVKGLrkgdamiaitrlvdalklqdqlkapvkTLSEgiKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1458
Cdd:cd03232 96 VREALRFSALLRGL---------------------------SVEQ--RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
....*.
gi 27477115 1459 MWQVIR 1464
Cdd:cd03232 147 IVRFLK 152
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1303-1497 |
6.82e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.90 E-value: 6.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1303 RKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGGGEPL--GFLGYCPQ-ENALWPNLTV 1379
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALqkNLVAYVPQsEEVDWSFPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1380 RQHLEV---YAAVKGLRKGDAM------IAITRlVDALKLQDQlkaPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1450
Cdd:PRK15056 97 VEDVVMmgrYGHMGWLRRAKKRdrqivtAALAR-VDMVEFRHR---QIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27477115 1451 MDPEGQQQMWQVIRaTFRNTERGALLTTHYMAEAEAVCDrVAIMVSG 1497
Cdd:PRK15056 173 VDVKTEARIISLLR-ELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1316-1495 |
7.49e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.76 E-value: 7.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1316 VKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVI--LKGSgggeplgflgYCPQENALWPNLTVRQHLEvyaAVKGlR 1393
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDpeLKIS----------YKPQYIKPDYDGTVEDLLR---SITD-D 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1394 KGDAMIaITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRATFRNTERG 1473
Cdd:PRK13409 428 LGSSYY-KSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREAT 506
|
170 180
....*....|....*....|..
gi 27477115 1474 ALLTTHYMAEAEAVCDRvaIMV 1495
Cdd:PRK13409 507 ALVVDHDIYMIDYISDR--LMV 526
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1310-1540 |
7.63e-11 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 64.88 E-value: 7.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTT----IKMITgdtkpTAGQVILKG-SGGGEPL----GFLGYCPQENALWPNlTVR 1380
Cdd:cd03289 21 ENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGvSWNSVPLqkwrKAFGVIPQKVFIFSG-TFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1381 QHLEVYAAVKG--LRKGDAMIAITRLVDAL--KLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPegq 1456
Cdd:cd03289 95 KNLDPYGKWSDeeIWKVAEEVGLKSVIEQFpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP--- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1457 qQMWQVIRATFRNTERGA--LLTTHYMaEAEAVCDRVAIMVSGRLRCIGSIQHLKSKfgkdyllemklKNLAQMEPLHAE 1534
Cdd:cd03289 172 -ITYQVIRKTLKQAFADCtvILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLNE-----------KSHFKQAISPSD 238
|
....*.
gi 27477115 1535 ILRLFP 1540
Cdd:cd03289 239 RLKLFP 244
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1308-1508 |
7.66e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.42 E-value: 7.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVK-------------KGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLG------F---LG 1365
Cdd:PRK10575 13 ALRNVSFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILL----DAQPLEswsskaFarkVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1366 YCPQENALWPNLTVRQHLEV-----YAAVKGLRKGD---AMIAITrLVDALKLQDQLkapVKTLSEGIKRKLCFVLSILG 1437
Cdd:PRK10575 89 YLPQQLPAAEGMTVRELVAIgrypwHGALGRFGAADrekVEEAIS-LVGLKPLAHRL---VDSLSGGERQRAWIAMLVAQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27477115 1438 NPSVVLLDEPSTGMDPEGQQQMWQVIRATFRntERGALLTT--HYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1508
Cdd:PRK10575 165 DSRCLLLDEPTSALDIAHQVDVLALVHRLSQ--ERGLTVIAvlHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1308-1522 |
8.57e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 66.77 E-value: 8.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGFLGycpqENALWPNLT-VRQHLEVY 1386
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL----NGQPIADYS----EAALRQAISvVSQRVHLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1387 AAVkgLRKG----------DAMIAITRLVDALKLQDQLKaPVKT--------LSEGIKRKLCFVLSILGNPSVVLLDEPS 1448
Cdd:PRK11160 427 SAT--LRDNlllaapnasdEALIEVLQQVGLEKLLEDDK-GLNAwlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPT 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477115 1449 TGMDPEGQQQMWQVIRATFRNteRGALLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFGKDYLLEMKL 1522
Cdd:PRK11160 504 EGLDAETERQILELLAEHAQN--KTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1278-1354 |
9.04e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 65.14 E-value: 9.04e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 1278 DETPVIIASCLRKEYAgKKKNCFSKRKKKI-ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG 1354
Cdd:COG4608 3 MAEPLLEVRDLKKHFP-VRGGLFGRTVGVVkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDG 79
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1312-1507 |
9.75e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.09 E-value: 9.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1312 VSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKgsggGEPLGF----------LGYCPQ---ENALWPNLT 1378
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLD----GKPIDIrsprdairagIMLCPEdrkAEGIIPVHS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1379 VRQHLEVYAAVKGLRKG-------DAMIAiTRLVDALKLQ----DQlkaPVKTLSEGIKRKlcfvlSILG-----NPSVV 1442
Cdd:PRK11288 348 VADNINISARRHHLRAGclinnrwEAENA-DRFIRSLNIKtpsrEQ---LIMNLSGGNQQK-----AILGrwlseDMKVI 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 1443 LLDEPSTGMDPEGQQQMWQVIratFRNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRLRciGSIQH 1507
Cdd:PRK11288 419 LLDEPTRGIDVGAKHEIYNVI---YELAAQGvaVLFVSSDLPEVLGVADRIVVMREGRIA--GELAR 480
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1310-1499 |
1.02e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.22 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGS-------GGGEPLGF-----------LGYCPQEN 1371
Cdd:PRK10619 22 KGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdKDGQLKVAdknqlrllrtrLTMVFQHF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1372 ALWPNLTVRQH-LEVYAAVKGLRKGDAMIAITRLVDALKLQD--QLKAPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPS 1448
Cdd:PRK10619 102 NLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDEraQGKYPVH-LSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27477115 1449 TGMDPEgqqQMWQVIRATFRNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:PRK10619 181 SALDPE---LVGEVLRIMQQLAEEGKtmVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1282-1454 |
1.04e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.11 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1282 VIIASCLRKEYAGKkkncfskrkkkIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsggGEPL 1361
Cdd:TIGR03719 322 VIEAENLTKAFGDK-----------LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-----GETV 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1362 GfLGYCPQE-NALWPNLTVRQhlEVYAAVKGLRKGDAMIAITRLVDA--LKLQDQLKaPVKTLSEGIKRKLCFVLSILGN 1438
Cdd:TIGR03719 386 K-LAYVDQSrDALDPNKTVWE--EISGGLDIIKLGKREIPSRAYVGRfnFKGSDQQK-KVGQLSGGERNRVHLAKTLKSG 461
|
170
....*....|....*.
gi 27477115 1439 PSVVLLDEPSTGMDPE 1454
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVE 477
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
476-665 |
1.05e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 66.35 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 476 CGKEAIRIKNLKKEYAGKCervealkgvV-------FDIY------EGQITALLGHSGAGKTTLLNILSGLSVPTSGSVT 542
Cdd:COG1245 61 CPFDAISIVNLPEELEEDP---------VhrygengFRLYglpvpkKGKVTGILGPNGIGKSTALKILSGELKPNLGDYD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 543 ----------------VYNHtLSRMAD-----------IENISK-FTGfcpqsnvqfgflTVKEnlrLFAKI--KGILPH 592
Cdd:COG1245 132 eepswdevlkrfrgteLQDY-FKKLANgeikvahkpqyVDLIPKvFKG------------TVRE---LLEKVdeRGKLDE 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 593 evekevqrVVQELEMENI--QDIlaQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHR----IWNLLKEGKS 665
Cdd:COG1245 196 --------LAEKLGLENIldRDI--SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNvarlIRELAEEGKY 264
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
510-652 |
1.07e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 64.02 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 510 GQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNH---TLSRMAdIENISKFTGFCPQSNVQFGFLTVKENLRLFAKI 586
Cdd:PRK11831 33 GKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipAMSRSR-LYTVRKRMSMLFQSGALFTDMNVFDNVAYPLRE 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 587 KGILPHEVEKEVqrVVQELE---MENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLS 652
Cdd:PRK11831 112 HTQLPAPLLHST--VMMKLEavgLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPIT 178
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1303-1479 |
1.13e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.05 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1303 RKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITG--DTKPTAGQVILkgsgggeplgflgycpQENALWPNLTVR 1380
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDV----------------PDNQFGREASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1381 QHLevyaavkgLRKGDAMIAITRLVDAlKLQDQ--LKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1458
Cdd:COG2401 104 DAI--------GRKGDFKDAVELLNAV-GLSDAvlWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKR 174
|
170 180
....*....|....*....|.
gi 27477115 1459 MWQVIRATFRNTERGALLTTH 1479
Cdd:COG2401 175 VARNLQKLARRAGITLVVATH 195
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
483-659 |
1.30e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 63.55 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 483 IKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSV--PTSGSVTVYNHTLSRMaDIENISK- 559
Cdd:COG0396 3 IKNLHVSVEGK----EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILEL-SPDERARa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 --FTGFcpQSNVQFGFLTVKENLRLFAKIKG---ILPHEVEKEVQRVVQELEMEniQDILAQNL----SGGQnRKLT--F 628
Cdd:COG0396 78 giFLAF--QYPVEIPGVSVSNFLRTALNARRgeeLSAREFLKLLKEKMKELGLD--EDFLDRYVnegfSGGE-KKRNeiL 152
|
170 180 190
....*....|....*....|....*....|.
gi 27477115 629 GIAILgDPQVLLLDEPTAGLDplsrhrIWNL 659
Cdd:COG0396 153 QMLLL-EPKLAILDETDSGLD------IDAL 176
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1312-1499 |
1.41e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 63.96 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1312 VSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGS--------GGGEPLGFLGYCPQENALwpNLTVRQHL 1383
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGElltaenvwNLRRKIGMVFQNPDNQFV--GATVEDDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1384 EVYAAVKGLRKGDAMIAITRLVDALKLQD-QLKAPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQV 1462
Cdd:PRK13642 104 AFGMENQGIPREEMIKRVDEALLAVNMLDfKTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 27477115 1463 IRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSGRL 1499
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
479-695 |
1.42e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 63.68 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 479 EAIRIKNLKKEY---AGKCERVE-------------ALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVT 542
Cdd:PRK13546 3 VSVNIKNVTKEYriyRTNKERMKdalipkhknktffALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 543 vynhtlsRMADIENISKFTGFCPQsnvqfgfLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQ 622
Cdd:PRK13546 83 -------RNGEVSVIAISAGLSGQ-------LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477115 623 NRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGK-SDRVILFSTQFIDEADILADRKVFISNGKLK 695
Cdd:PRK13546 149 RAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKeQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLK 222
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
481-700 |
1.46e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 63.66 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKC-----ERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLS------ 549
Cdd:PRK15112 5 LEVRNLSKTFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdysy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 550 RMADIENISK--FTGFCPQSNV-QFGFLTVKENLRLfakikgilphEVEKEVQRVVQELEMENIQDILA----QNLSGGQ 622
Cdd:PRK15112 85 RSQRIRMIFQdpSTSLNPRQRIsQILDFPLRLNTDL----------EPEQREKQIIETLRQVGLLPDHAsyypHMLAPGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 623 NRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVI--LFSTQFIDEADILADRKVFISNGKLKCAGSS 700
Cdd:PRK15112 155 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVMHQGEVVERGST 234
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1310-1499 |
2.23e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.02 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKgsggGEPLgfLGYCPQE---------------NALW 1374
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLD----GHEV--VTRSPQDglangivyisedrkrDGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1375 PNLTVRQHLEVYA------AVKGLRKGDAMIAITRLVDALKL----QDQlkaPVKTLSEGIKRKLCFVLSILGNPSVVLL 1444
Cdd:PRK10762 343 LGMSVKENMSLTAlryfsrAGGSLKHADEQQAVSDFIRLFNIktpsMEQ---AIGLLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 1445 DEPSTGMDPEGQQQMWQVIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLIN-QFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1308-1545 |
2.40e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 63.22 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGggeplgflgyCPQENALWpnltVRQHL---- 1383
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRE----------VNAENEKW----VRSKVglvf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1384 -----EVYAAV-----------KGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1447
Cdd:PRK13647 86 qdpddQVFSSTvwddvafgpvnMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1448 STGMDPEGQQQMWQvIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGsiqhlkskfGKDYLLEMKLKNLAQ 1527
Cdd:PRK13647 166 MAYLDPRGQETLME-ILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG---------DKSLLTDEDIVEQAG 235
|
250
....*....|....*....
gi 27477115 1528 ME-PLHAEILRLFPQAAQQ 1545
Cdd:PRK13647 236 LRlPLVAQIFEDLPELGQS 254
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
499-694 |
2.68e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.75 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 499 ALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIENIS----------KFTGFcpQSN 568
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINhgfalvteerRSTGI--YAY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 569 VQFGFLTVKENLRLFAKIKGILPHE-VEKEVQRVVQELEMEN-IQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTA 646
Cdd:PRK10982 341 LDIGFNSLISNIRNYKNKVGLLDNSrMKSDTQWVIDSMRVKTpGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTR 420
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27477115 647 GLDPLSRHRIWNLLKE-GKSDRVILFSTQFIDEADILADRKVFISNGKL 694
Cdd:PRK10982 421 GIDVGAKFEIYQLIAElAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1292-1504 |
3.16e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.21 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1292 YAGKKKNCFSKRkkkiATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQV------ILKGSGGGE------ 1359
Cdd:PRK13643 9 YTYQPNSPFASR----ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdivVSSTSKQKEikpvrk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1360 PLGFLGYCPqENALWPNlTVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQL--KAPVKtLSEGIKRKLCFVLSILG 1437
Cdd:PRK13643 85 KVGVVFQFP-ESQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFweKSPFE-LSGGQMRRVAIAGILAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 1438 NPSVVLLDEPSTGMDPEGQQQMWQVIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1504
Cdd:PRK13643 162 EPEVLVLDEPTAGLDPKARIEMMQLFE-SIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
483-662 |
3.46e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.57 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 483 IKNLKKEYAGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIENISKftg 562
Cdd:PRK15079 20 IKDGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAV--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 563 fcpQSNVQFGF----------LTV----KENLRLFAkikgilPHEVEKEVQRVVQELEM-----ENIQDILAQNLSGGQN 623
Cdd:PRK15079 97 ---RSDIQMIFqdplaslnprMTIgeiiAEPLRTYH------PKLSRQEVKDRVKAMMLkvgllPNLINRYPHEFSGGQC 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27477115 624 RKLtfGIA---ILgDPQVLLLDEPTAGLDPLSRHRIWNLLKE 662
Cdd:PRK15079 168 QRI--GIAralIL-EPKLIICDEPVSALDVSIQAQVVNLLQQ 206
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1306-1484 |
4.34e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 62.02 E-value: 4.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1306 KIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGGGEPLGFLGYCPQENALWPNLTVRQHLEV 1385
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNVAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1386 YAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRA 1465
Cdd:PRK11248 94 GLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLK 173
|
170
....*....|....*....
gi 27477115 1466 TFRNTERGALLTTHYMAEA 1484
Cdd:PRK11248 174 LWQETGKQVLLITHDIEEA 192
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1306-1522 |
4.73e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 62.73 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1306 KIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsggGE-------------PL----GFLGYCP 1368
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-----GErvitagkknkklkPLrkkvGIVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1369 qENALWPNlTVR-------QHLEVYAAvKGLRKGDAMIAITRLVDALkLQdqlKAPVKtLSEGIKRKLCF--VLSIlgNP 1439
Cdd:PRK13634 95 -EHQLFEE-TVEkdicfgpMNFGVSEE-DAKQKAREMIELVGLPEEL-LA---RSPFE-LSGGQMRRVAIagVLAM--EP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1440 SVVLLDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKfgKDYLLE 1519
Cdd:PRK13634 165 EVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD--PDELEA 242
|
...
gi 27477115 1520 MKL 1522
Cdd:PRK13634 243 IGL 245
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1310-1499 |
5.35e-10 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 61.33 E-value: 5.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG----------------SGGGEPLGFLGYCpQENAL 1373
Cdd:cd03248 31 QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkylhskvsLVGQEPVLFARSL-QDNIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1374 WpNLTVRQHLEVYAAVKGLRKGDamiAITRLvdALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP 1453
Cdd:cd03248 110 Y-GLQSCSFECVKEAAQKAHAHS---FISEL--ASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27477115 1454 EGQQQMWQVIRATfrNTERGALLTTHYMAEAEAVcDRVAIMVSGRL 1499
Cdd:cd03248 184 ESEQQVQQALYDW--PERRTVLVIAHRLSTVERA-DQILVLDGGRI 226
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1307-1452 |
5.90e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 61.39 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1307 IATR--NVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTkPTAGQVILkgsgGGEPLG---------FLGYCPQENALWP 1375
Cdd:COG4138 8 VAGRlgPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILL----NGRPLSdwsaaelarHRAYLSQQQSPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1376 NLTVRQHLEVYAAvKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSIL-----GNPS--VVLLDEPS 1448
Cdd:COG4138 83 AMPVFQYLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqLLLLDEPM 161
|
....
gi 27477115 1449 TGMD 1452
Cdd:COG4138 162 NSLD 165
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
510-1479 |
6.46e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.36 E-value: 6.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 510 GQITALLGHSGAGKTTLLNILS----GLSVPTSGSVTVYNHTLsrmADIENisKFTG---FCPQSNVQFGFLTVKENLRL 582
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITP---EEIKK--HYRGdvvYNAETDVHFPHLTVGETLDF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 583 FAKIKGI--LPHEVEKEVQRV-VQELEME----------NIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLD 649
Cdd:TIGR00956 162 AARCKTPqnRPDGVSREEYAKhIADVYMAtyglshtrntKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 650 PLSRHRIWNLLKEGKSdrvILFSTQFI------DEADILADRKVFISNGKLKCAGSS-----LFLKkkwgIGYhlslhln 718
Cdd:TIGR00956 242 SATALEFIRALKTSAN---ILDTTPLVaiyqcsQDAYELFDKVIVLYEGYQIYFGPAdkakqYFEK----MGF------- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 719 eRCDPESITSLVKQHISDAK--LTAQSEEKLVYILPLE---RTNKFPElYRDLDRcsnqGIEDYGVSITTLNEvflkleg 793
Cdd:TIGR00956 308 -KCPDRQTTADFLTSLTSPAerQIKPGYEKKVPRTPQEfetYWRNSPE-YAQLMK----EIDEYLDRCSESDT------- 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 794 KSTIDESDIgiwgQLQTDGAKDigslveleqvlSSFHEtrktisgVALWrQQVCAIAKVRFLKLKkeRKSLWTILLLFGI 873
Cdd:TIGR00956 375 KEAYRESHV----AKQSKRTRP-----------SSPYT-------VSFS-MQVKYCLARNFLRMK--GNPSFTLFMVFGN 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 874 SFIPQLLEHLFYEsyqksypweLSPNTyflspgqqpqdplthllvinktgstidnflhslrrqniaieVDAFgtrngtdd 953
Cdd:TIGR00956 430 IIMALILSSVFYN---------LPKNT-----------------------------------------SDFY-------- 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 954 pSYNGAIIvsgdekdhrFSIAcntkrLNCFpvlldvisNGLLGIFNSSEHiqtdRStFFEEHMDYEYgYRSNTFFWIPMA 1033
Cdd:TIGR00956 452 -SRGGALF---------FAIL-----FNAF--------SSLLEIASMYEA----RP-IVEKHRKYAL-YHPSADAIASII 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1034 ASFTPYIAMSSIGDYKKKAHSQLRISglyPSAYWFgqalvdvslYFLILLL-MQIMDYIFspeEIIFIIQNLLIQ--ILC 1110
Cdd:TIGR00956 503 SEIPFKIIESVVFNIILYFMVNFRRT---AGRFFF---------YLLILFIcTLAMSHLF---RSIGAVTKTLSEamTPA 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1111 SIGYVSSLVFLTYVISfifrngRKNSGIWSFFflivvifsIVATDLNEYGFLGLFFGTMLippftliGSLFIFSEISPDS 1190
Cdd:TIGR00956 568 AILLLALSIYTGFAIP------RPSMLGWSKW--------IYYVNPLAYAFESLMVNEFH-------GRRFECSQYVPSG 626
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1191 MDYLGASESEIV-----------------YLALLIPYLH------------FLIFLFILRCLEMNCRKKLMRKDPVFrIS 1241
Cdd:TIGR00956 627 GGYDNLGVTNKVctvvgaepgqdyvdgddYLKLSFQYYNshkwrnfgiiigFTVFFFFVYILLTEFNKGAKQKGEIL-VF 705
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1242 PRSNAIFpnpeepegeeediqMERMRTVNAMAVRDFDETPVIIASCLRKEY----------AGKKKNCFS---------- 1301
Cdd:TIGR00956 706 RRGSLKR--------------AKKAGETSASNKNDIEAGEVLGSTDLTDESddvndekdmeKESGEDIFHwrnltyevki 771
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1302 KRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGdtKPTAGqVILKGS--GGGEPL--GF---LGYCPQENALW 1374
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTG-VITGGDrlVNGRPLdsSFqrsIGYVQQQDLHL 848
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1375 PNLTVRQHLEVYAAV---KGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGI----KRKLCFVLSILGNP-SVVLLDE 1446
Cdd:TIGR00956 849 PTSTVRESLRFSAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPkLLLFLDE 928
|
1050 1060 1070
....*....|....*....|....*....|....*.
gi 27477115 1447 PSTGMDpegQQQMWQVIRaTFRNTE---RGALLTTH 1479
Cdd:TIGR00956 929 PTSGLD---SQTAWSICK-LMRKLAdhgQAILCTIH 960
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1305-1525 |
7.09e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 61.74 E-value: 7.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1305 KKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGdtkptagqVILKGSGGGEPLGFLGYCPQENALWpnlTVRQHLE 1384
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLING--------LLLPDDNPNSKITVDGITLTAKTVW---DIREKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1385 ----------VYAAVK-----GLRK----GDAMIAITRLVDA-LKLQDQLKAPVKTLSEGIKRKLCfVLSILG-NPSVVL 1443
Cdd:PRK13640 88 ivfqnpdnqfVGATVGddvafGLENravpRPEMIKIVRDVLAdVGMLDYIDSEPANLSGGQKQRVA-IAGILAvEPKIII 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1444 LDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEA-----VCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLL 1518
Cdd:PRK13640 167 LDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMadqvlVLDDGKLLAQGSPVEIFSKVEMLKEIGLDIPF 246
|
....*..
gi 27477115 1519 EMKLKNL 1525
Cdd:PRK13640 247 VYKLKNK 253
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
482-649 |
7.29e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.48 E-value: 7.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 482 RIKNLKKEYAGkcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTvYnhtlsRMADIENISKFT 561
Cdd:PRK11701 8 SVRGLTKLYGP----RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH-Y-----RMRDGQLRDLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 562 --------------GFCPQS-------NVQFGfLTVKENL-----RLFAKIKGilphEVEKEVQRVvqELEMENIQDiLA 615
Cdd:PRK11701 78 lseaerrrllrtewGFVHQHprdglrmQVSAG-GNIGERLmavgaRHYGDIRA----TAGDWLERV--EIDAARIDD-LP 149
|
170 180 190
....*....|....*....|....*....|....
gi 27477115 616 QNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLD 649
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
986-1219 |
8.63e-10 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 62.41 E-value: 8.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 986 LLDVISNGLLGIFNSSEHIQTDRSTFFEEHMDYEYGYrsntFFWIPMAASFTP--YIAMSSIGDYKKKAHSQLRISGLYP 1063
Cdd:pfam12698 127 LNASALVLLLEALSTSAPIPVESTPLFNPQSGYAYYL----VGLILMIIILIGaaIIAVSIVEEKESRIKERLLVSGVSP 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1064 SAYWFGQALVDVSLYFLILLLMQIM--DYIFSPEEIIFIiqnlliqILCSIGYVSSLVFLTYVISFIFRNGRKNSGIWSF 1141
Cdd:pfam12698 203 LQYWLGKILGDFLVGLLQLLIILLLlfGIGIPFGNLGLL-------LLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGI 275
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 1142 FFLIVVIFSIVATDLNE-YGFLGLFFgtmLIPPFTLIGSLFIFSeispdsmdYLGASESEIvYLALLIPYLHFLIFLFI 1219
Cdd:pfam12698 276 VILLLSGFFGGLFPLEDpPSFLQWIF---SIIPFFSPIDGLLRL--------IYGDSLWEI-APSLIILLLFAVVLLLL 342
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
478-699 |
9.26e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 63.44 E-value: 9.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 478 KEAIRIKNLKKEYAGKcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVynhtlsrmaDIENI 557
Cdd:PRK13657 332 KGAVEFDDVSFSYDNS---RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILI---------DGTDI 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 558 SKFTGFCPQSNVQFGFL-------TVKENLRLfAKikgilPHEVEKEVQRVvqeLEMENIQDILAQN------------- 617
Cdd:PRK13657 400 RTVTRASLRRNIAVVFQdaglfnrSIEDNIRV-GR-----PDATDEEMRAA---AERAQAHDFIERKpdgydtvvgergr 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 618 -LSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRvilfsTQFIDeADIL-----ADRKVFISN 691
Cdd:PRK13657 471 qLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGR-----TTFII-AHRLstvrnADRILVFDN 544
|
....*...
gi 27477115 692 GKLKCAGS 699
Cdd:PRK13657 545 GRVVESGS 552
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1305-1499 |
1.32e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.80 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1305 KKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLG---------FLGYCPQE----- 1370
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFL----GDKPISmlssrqlarRLALLPQHhltpe 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1371 ---------------NALWPNLTVRQHLEVYAAvkglrkgdamIAITRLVDalkLQDQlkaPVKTLSEGiKRKLCFVLSI 1435
Cdd:PRK11231 90 gitvrelvaygrspwLSLWGRLSAEDNARVNQA----------MEQTRINH---LADR---RLTDLSGG-QRQRAFLAMV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 1436 LG-NPSVVLLDEPSTGMDPEGQQQMWQVIRAtfRNTERGALLTT-HYMAEAEAVCDRVAIMVSGRL 1499
Cdd:PRK11231 153 LAqDTPVVLLDEPTTYLDINHQVELMRLMRE--LNTQGKTVVTVlHDLNQASRYCDHLVVLANGHV 216
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
505-650 |
1.45e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.86 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 505 FDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRmADIENISKFTGFCPQSNVQfgfLTVKENLRLFA 584
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR-GDRSRFMAYLGHLPGLKAD---LSTLENLHFLC 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 585 KIKGILPHEVEKEVQRVVQeleMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDP 650
Cdd:PRK13543 108 GLHGRRAKQMPGSALAIVG---LAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1308-1508 |
2.04e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.41 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIK----MITGDTKPTAGQVIL------KGSGGGE---PLGFLGYCPQENALW 1374
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLgrtvqrEGRLARDirkSRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1375 PNLTVRQHLEVYAA------------VKGLRKGDAMIAITRlVDALKLQDQlkaPVKTLSEGIKRKLCFVLSILGNPSVV 1442
Cdd:PRK09984 99 NRLSVLENVLIGALgstpfwrtcfswFTREQKQRALQALTR-VGMVHFAHQ---RVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 1443 LLDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1508
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1312-1500 |
2.80e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.41 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1312 VSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKgsggGEPLGFL-------------GYCPQENALWPNLT 1378
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLV----GQPLHQMdeearaklrakhvGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1379 VRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1458
Cdd:PRK10584 105 ALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27477115 1459 MWQVIRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSGRLR 1500
Cdd:PRK10584 185 IADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQ 225
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1299-1513 |
2.97e-09 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 59.17 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1299 CFSKRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPL---------GFLGYCPQ 1369
Cdd:cd03253 7 TFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILI----DGQDIrevtldslrRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1370 ENALWpNLTVRQHL----------EVYAAVKGlrkgdAMI--AITRLVDA---------LKlqdqlkapvktLSEGIKRK 1428
Cdd:cd03253 83 DTVLF-NDTIGYNIrygrpdatdeEVIEAAKA-----AQIhdKIMRFPDGydtivgergLK-----------LSGGEKQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1429 LCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRATFRNteRGALLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQHL 1508
Cdd:cd03253 146 VAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKG--RTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEEL 222
|
....*
gi 27477115 1509 KSKFG 1513
Cdd:cd03253 223 LAKGG 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1311-1506 |
3.38e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 60.48 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1311 NVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG------SGGGEPLGFLGycpQENALWPNLTVRQHLE 1384
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsrlHARDRKVGFVF---QHYALFRHMTVFDNIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1385 VYAAVKGLRKGDAMIAITRLVDALKLQDQL-----KAPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1459
Cdd:PRK10851 97 FGLTVLPRRERPNAAAIKAKVTQLLEMVQLahladRYPAQ-LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKEL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27477115 1460 WQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQ 1506
Cdd:PRK10851 176 RRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1310-1499 |
3.55e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.20 E-value: 3.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGF----------LGYCPQE---NALWPN 1376
Cdd:COG3845 275 KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRL----DGEDITGlsprerrrlgVAYIPEDrlgRGLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1377 LTVRQH--LEVYAAVKGLRKG----DAMIAIT-RLVDALKLQ-DQLKAPVKTLSEGIKRKlcFVLS--ILGNPSVVLLDE 1446
Cdd:COG3845 351 MSVAENliLGRYRRPPFSRGGfldrKAIRAFAeELIEEFDVRtPGPDTPARSLSGGNQQK--VILAreLSRDPKLLIAAQ 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 1447 PSTGMDPEGQQQMWQVIRATfRNteRGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:COG3845 429 PTRGLDVGAIEFIHQRLLEL-RD--AGAavLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1303-1499 |
3.59e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.46 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1303 RKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGD-TKPTA-------GQVILKgsggGEPLGFL---------G 1365
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDlTGGGAprgarvtGDVTLN----GEPLAAIdaprlarlrA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1366 YCPQENALWPNLTVRQ--------HLEVYAAVKGLRKGDAMIAITRL-VDALKLQDqlkapVKTLSEGIKRKLCF--VLS 1434
Cdd:PRK13547 87 VLPQAAQPAFAFSAREivllgrypHARRAGALTHRDGEIAWQALALAgATALVGRD-----VTTLSGGELARVQFarVLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477115 1435 IL-------GNPSVVLLDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:PRK13547 162 QLwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAI 233
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1316-1493 |
3.65e-09 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 57.97 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1316 VKKGEVIGLLGHNGAGKSTTIKMITGDTKPTagqvilkgsgggeplgflgycpQENALWPNLTVrqhleVYaavkglrkg 1395
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPN----------------------GDNDEWDGITP-----VY--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1396 damiaitrlvdalklqdqlKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRATFRNTERGAL 1475
Cdd:cd03222 66 -------------------KPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTAL 126
|
170
....*....|....*...
gi 27477115 1476 LTTHYMAEAEAVCDRVAI 1493
Cdd:cd03222 127 VVEHDLAVLDYLSDRIHV 144
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1311-1497 |
3.72e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 59.38 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1311 NVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVIlkgsgggeplgFLGYCPQENalwpNLT-VRQHLEV---- 1385
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIF-----------YNNQAITDD----NFEkLRKHIGIvfqn 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1386 -----------YAAVKGLRKG----DAMIAIT-RLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPST 1449
Cdd:PRK13648 92 pdnqfvgsivkYDVAFGLENHavpyDEMHRRVsEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27477115 1450 GMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSG 1497
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKG 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1310-1357 |
3.96e-09 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 58.60 E-value: 3.96e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGG 1357
Cdd:COG4778 28 DGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGG 75
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
470-662 |
5.84e-09 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 60.47 E-value: 5.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 470 PVSPEfcGKEAIRIKNLKKEYAGK-------CERVEALKGVVFDIYEGQITALLGHSGAGKTTL-LNILsGLsVPTSGSV 541
Cdd:COG4172 267 PVPPD--APPLLEARDLKVWFPIKrglfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL-RL-IPSEGEI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 542 TVYNHTLSRMadienisKFTGFCP-QSNVQ------FGFL--------TVKENLRLFAkiKGILPHEVEKEVQRVVQELE 606
Cdd:COG4172 343 RFDGQDLDGL-------SRRALRPlRRRMQvvfqdpFGSLsprmtvgqIIAEGLRVHG--PGLSAAERRARVAEALEEVG 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477115 607 MeniqDILAQN-----LSGGQNRKLtfGIA---ILgDPQVLLLDEPTAGLDPLSRHRIWNLLKE 662
Cdd:COG4172 414 L----DPAARHrypheFSGGQRQRI--AIAralIL-EPKLLVLDEPTSALDVSVQAQILDLLRD 470
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1308-1499 |
6.08e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 58.35 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSG---------GGEPLGFLgycPQENALWPNLT 1378
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDitdwqtakiMREAVAIV---PEGRRVFSRMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1379 VRQHLevyaAVKGL--RKGDAMIAITRLVDAL-KLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEG 1455
Cdd:PRK11614 97 VEENL----AMGGFfaERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27477115 1456 QQQMWQVIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:PRK11614 173 IQQIFDTIE-QLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
493-662 |
6.37e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 61.02 E-value: 6.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 493 KCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGL---SVPTSGSVTVYNHTLSRMADIenisKFTGFCPQSNV 569
Cdd:PLN03140 174 KKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKldpSLKVSGEITYNGYRLNEFVPR----KTSAYISQNDV 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 570 QFGFLTVKENLRLFAKIKGI-----LPHEV-----------EKEVQRVVQELEMENIQ---------------------- 611
Cdd:PLN03140 250 HVGVMTVKETLDFSARCQGVgtrydLLSELarrekdagifpEAEVDLFMKATAMEGVKsslitdytlkilgldickdtiv 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27477115 612 -DILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE 662
Cdd:PLN03140 330 gDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQ 381
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1310-1499 |
8.13e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 58.39 E-value: 8.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITG--DTKPTA---GQVILKGSGGGE-PLGFLGYCPQ-----ENALwPNLT 1378
Cdd:PRK14247 20 DGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEArvsGEVYLDGQDIFKmDVIELRRRVQmvfqiPNPI-PNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1379 VRQHLEVYAAVKGLRKGDAMIAiTRLVDALK-------LQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGM 1451
Cdd:PRK14247 99 IFENVALGLKLNRLVKSKKELQ-ERVRWALEkaqlwdeVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27477115 1452 DPEGQQQmwqvIRATF--RNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:PRK14247 178 DPENTAK----IESLFleLKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
481-695 |
8.73e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 58.33 E-value: 8.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKCERVeaLKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLsVPTSGSVTVYNHTLSRMAdIENISKF 560
Cdd:cd03289 3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVP-LQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 561 TGFCPQSNVQFGFlTVKENLRLFAKIKgilphevEKEVQRVVQELEMENIQDILAQNL-----------SGGQNRKLTFG 629
Cdd:cd03289 79 FGVIPQKVFIFSG-TFRKNLDPYGKWS-------DEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 630 IAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVILFSTQFIdEADILADRKVFISNGKLK 695
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKVR 215
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1404-1510 |
1.03e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 58.18 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1404 LVDALKlqDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRATFRNTErgALLTTHYMAE 1483
Cdd:PRK14271 149 LWDAVK--DRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLT--VIIVTHNLAQ 224
|
90 100
....*....|....*....|....*..
gi 27477115 1484 AEAVCDRVAIMVSGRLRCIGSIQHLKS 1510
Cdd:PRK14271 225 AARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1310-1498 |
1.23e-08 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 56.71 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSgggeplgfLGYCPQENalW-PNLTVRQHL----- 1383
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--------IAYVSQEP--WiQNGTIRENIlfgkp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1384 ---EVYAAVkglrkgdamiaitrlVDALKLQDQLKAPVK-----------TLSEGIKRKLCFVLSILGNPSVVLLDEPST 1449
Cdd:cd03250 92 fdeERYEKV---------------IKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27477115 1450 GMDPE-GQQQMWQVIRATFRNtERGALLTTHYMAEAEAvCDRVAIMVSGR 1498
Cdd:cd03250 157 AVDAHvGRHIFENCILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
480-649 |
1.42e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.52 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 480 AIRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTvynhtLSRMADIenisk 559
Cdd:PRK15064 319 ALEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK-----WSENANI----- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 ftGFCPQ-SNVQF-GFLTVKENLRLFAK-------IKGIL------PHEVEKEVQrvvqelemeniqdilaqNLSGGQNR 624
Cdd:PRK15064 385 --GYYAQdHAYDFeNDLTLFDWMSQWRQegddeqaVRGTLgrllfsQDDIKKSVK-----------------VLSGGEKG 445
|
170 180
....*....|....*....|....*
gi 27477115 625 KLTFGIAILGDPQVLLLDEPTAGLD 649
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1308-1508 |
1.51e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 58.20 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGdtkPTAGQVILKGSG---GGEPLGFlgycPQE-------------- 1370
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMG---LLAANGRIGGSAtfnGREILNL----PEKelnklraeqismif 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1371 ----NALWPNLTV-RQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKA----PvKTLSEGIKRKLCFVLSILGNPSV 1441
Cdd:PRK09473 104 qdpmTSLNPYMRVgEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRmkmyP-HEFSGGMRQRVMIAMALLCRPKL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 1442 VLLDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1508
Cdd:PRK09473 183 LIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1280-1499 |
1.57e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 57.38 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1280 TPVIIAScLRKEYAGKKkncfskrkkkiATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQvILKGSGgge 1359
Cdd:PRK11247 11 TPLLLNA-VSKRYGERT-----------VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1360 PLG---------FlgycpQENALWPNLTVRQHLEVyaavkGLrKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLC 1430
Cdd:PRK11247 75 PLAearedtrlmF-----QDARLLPWKKVIDNVGL-----GL-KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 1431 FVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
500-656 |
1.62e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.53 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 500 LKGVVFDIYEGQITALLGHSGAGKTTLLNILSG--------LSVPTSGSVTVYNHTLSRMaDIENISKFTGFCPQ-SNVQ 570
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgggapRGARVTGDVTLNGEPLAAI-DAPRLARLRAVLPQaAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 571 FGFlTVKENLRL----FAKIKGILPHEvEKEVqrVVQELEMENIQDILAQN---LSGGQNRKLTFGIAI---------LG 634
Cdd:PRK13547 96 FAF-SAREIVLLgrypHARRAGALTHR-DGEI--AWQALALAGATALVGRDvttLSGGELARVQFARVLaqlwpphdaAQ 171
|
170 180
....*....|....*....|..
gi 27477115 635 DPQVLLLDEPTAGLDPLSRHRI 656
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRL 193
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1300-1561 |
1.64e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.74 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1300 FSKRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDT----KPTAGQVILKGSGGGEPL----GFLGYCPQEN 1371
Cdd:TIGR00956 68 FRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgfhIGVEGVITYDGITPEEIKkhyrGDVVYNAETD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1372 ALWPNLTVRQHLEVYAAVKGlrKGDAMIAITRLVDALKLQDQLKAP---------------VKTLSEGIKRKLCFVLSIL 1436
Cdd:TIGR00956 148 VHFPHLTVGETLDFAARCKT--PQNRPDGVSREEYAKHIADVYMATyglshtrntkvgndfVRGVSGGERKRVSIAEASL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1437 GNPSVVLLDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTThYMAEAEA--VCDRVAIMVSGRLRCIGSIQHLKSKFGK 1514
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAI-YQCSQDAyeLFDKVIVLYEGYQIYFGPADKAKQYFEK 304
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27477115 1515 ------------DYLLEmkLKNLAQMEPLhAEILRLFPQAAQQ--ERFSSLMVYKLPVEDV 1561
Cdd:TIGR00956 305 mgfkcpdrqttaDFLTS--LTSPAERQIK-PGYEKKVPRTPQEfeTYWRNSPEYAQLMKEI 362
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
510-649 |
1.79e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 57.49 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 510 GQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMaDIENISKFTGFCPQSNVQFGFLTVKEnlrLFAKIK-- 587
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESW-SSKAFARKVAYLPQQLPAAEGMTVRE---LVAIGRyp 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 588 --GILPHEVEKEVQRVVQELEMENIQDI---LAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLD 649
Cdd:PRK10575 113 whGALGRFGAADREKVEEAISLVGLKPLahrLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1319-1457 |
2.30e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.03 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1319 GEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVIL-KGSGggeplgfLGYCPQENA--LWPNLTVRQHLeVYAAVKGLRKg 1395
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIK-------LGYFAQHQLefLRADESPLQHL-ARLAPQELEQ- 408
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 1396 damiaitRLVDAL---KLQ-DQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1457
Cdd:PRK10636 409 -------KLRDYLggfGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQ 467
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
470-694 |
2.31e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.83 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 470 PVSPEFCGKEAIRIKNLKKEYAgkcERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNhtls 549
Cdd:PRK10522 312 PRPQAFPDWQTLELRNVTFAYQ---DNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG---- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 550 RMADIENISKFTGFcpqsnvqfgFLTVKENLRLFAKIKGILPHEVEKE-VQRVVQELEMEN---IQD--ILAQNLSGGQN 623
Cdd:PRK10522 385 KPVTAEQPEDYRKL---------FSAVFTDFHLFDQLLGPEGKPANPAlVEKWLERLKMAHkleLEDgrISNLKLSKGQK 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 624 RKLTFGIAILGDPQVLLLDEPTAGLDPLSR----HRIWNLLKE-GKSdrviLFSTQFIDEADILADRKVFISNGKL 694
Cdd:PRK10522 456 KRLALLLALAEERDILLLDEWAADQDPHFRrefyQVLLPLLQEmGKT----IFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1303-1454 |
2.57e-08 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 56.39 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1303 RKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGFL---------GYCPQENAL 1373
Cdd:cd03249 13 RPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILL----DGVDIRDLnlrwlrsqiGLVSQEPVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1374 WPNlTVRQHLevyaavkGLRKGDA----MIAITRLVDA----LKLQDQLKAPV----KTLSEGIKRKLCFVLSILGNPSV 1441
Cdd:cd03249 89 FDG-TIAENI-------RYGKPDAtdeeVEEAAKKANIhdfiMSLPDGYDTLVgergSQLSGGQKQRIAIARALLRNPKI 160
|
170
....*....|...
gi 27477115 1442 VLLDEPSTGMDPE 1454
Cdd:cd03249 161 LLLDEATSALDAE 173
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
477-649 |
3.14e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 58.26 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 477 GKEAIRIKNLKKEYAGKCERVEAlkGvvfDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTvynhtlsrmADIEn 556
Cdd:COG1245 338 EETLVEYPDLTKSYGGFSLEVEG--G---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD---------EDLK- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 557 ISkftgFCPQSNVQFGFLTVKENLRlfAKIKGILPHEVEKEvqRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDP 636
Cdd:COG1245 403 IS----YKPQYISPDYDGTVEEFLR--SANTDDFGSSYYKT--EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDA 474
|
170
....*....|...
gi 27477115 637 QVLLLDEPTAGLD 649
Cdd:COG1245 475 DLYLLDEPSAHLD 487
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1309-1503 |
3.60e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 57.35 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1309 TRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGGEPLGFL-------GYCPQENALWPNLTVRQ 1381
Cdd:PRK11000 19 SKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI----GEKRMNDVppaergvGMVFQSYALYPHLSVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1382 HLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ 1461
Cdd:PRK11000 95 NMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27477115 1462 VIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1503
Cdd:PRK11000 175 EISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
505-649 |
3.66e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.04 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 505 FDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVtVYNHTL--SRM-ADieniskftgfcPQSNVQ---FGFltVKE 578
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI-IYEQDLivARLqQD-----------PPRNVEgtvYDF--VAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 579 NLRLFA---KIKGILPHEVE--------KEVQRVVQELEMEN-------IQDILAQ----------NLSGGQNRKLTFGI 630
Cdd:PRK11147 90 GIEEQAeylKRYHDISHLVEtdpseknlNELAKLQEQLDHHNlwqlenrINEVLAQlgldpdaalsSLSGGWLRKAALGR 169
|
170
....*....|....*....
gi 27477115 631 AILGDPQVLLLDEPTAGLD 649
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLD 188
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1311-1499 |
4.93e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 55.87 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1311 NVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGGGEPLGFL-------GYCPQENALWPNLTVrqhL 1383
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlirqeaGMVFQQFYLFPHLTA---L 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1384 EVYA----AVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1459
Cdd:PRK09493 96 ENVMfgplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27477115 1460 WQVIRATfrnTERG--ALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:PRK09493 176 LKVMQDL---AEEGmtMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1310-1479 |
5.20e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 58.32 E-value: 5.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGdtKPTAGQVilkgSGGGEPLGF----------LGYCPQENALWPNLTV 1379
Cdd:PLN03140 897 REVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYI----EGDIRISGFpkkqetfariSGYCEQNDIHSPQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1380 RQHLeVYAAV----KGLRKGDAMIAITRLVDALKLqDQLK------APVKTLSEGIKRKLCFVLSILGNPSVVLLDEPST 1449
Cdd:PLN03140 971 RESL-IYSAFlrlpKEVSKEEKMMFVDEVMELVEL-DNLKdaivglPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
170 180 190
....*....|....*....|....*....|
gi 27477115 1450 GMDPEGQQQMWQVIRATFrNTERGALLTTH 1479
Cdd:PLN03140 1049 GLDARAAAIVMRTVRNTV-DTGRTVVCTIH 1077
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
503-695 |
6.05e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 503 VVFDIYEGQITALLGHSGAGKTTLLNILSGlSVP--TSGSVTVYNHTLSRMADIENISKFTGFCPQSNVQFGFLT---VK 577
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPgrWEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPvmgVG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 578 ENLRL-----FAKIkGILPHEVE-KEVQRVVQELEMENIQDILA-QNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDP 650
Cdd:PRK13549 360 KNITLaaldrFTGG-SRIDDAAElKTILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27477115 651 LSRHRIWNLL----KEGKSdrVILFSTQFideADIL--ADRKVFISNGKLK 695
Cdd:PRK13549 439 GAKYEIYKLInqlvQQGVA--IIVISSEL---PEVLglSDRVLVMHEGKLK 484
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
483-787 |
6.65e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 57.61 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 483 IKNLKKEYAGKCERVeaLKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLsVPTSGSVTVYNHTLSRMAdIENISKFTG 562
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVT-LQTWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 563 FCPQSNVQFGFlTVKENLRlfakikgilPHE--VEKEVQRVVQELEMENIQDILAQNL-----------SGGQNRKLTFG 629
Cdd:TIGR01271 1296 VIPQKVFIFSG-TFRKNLD---------PYEqwSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLA 1365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 630 IAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRVILFSTQFIdEADILADRKVFISNGKLKCAGSslflkkkwgi 709
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV-EALLECQQFLVIEGSSVKQYDS---------- 1434
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 710 gyhLSLHLNERcdpesitSLVKQHISdakltaqseeklvyilPLERTNKFPELYRDLDRCSNQGiedygvSITTLNEV 787
Cdd:TIGR01271 1435 ---IQKLLNET-------SLFKQAMS----------------AADRLKLFPLHRRNSSKRKPQP------KITALREE 1480
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
499-643 |
7.34e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.21 E-value: 7.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 499 ALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVtvynhtlsrmaDIENISKFTGFCPQSNVQfgfLTVKE 578
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----------DIKGSAALIAISSGLNGQ---LTGIE 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 579 NLRLfakiKGILPHEVEKEVQRVVQE-LEMENIQDILAQ---NLSGGQNRKLTFGIAILGDPQVLLLDE 643
Cdd:PRK13545 105 NIEL----KGLMMGLTKEKIKEIIPEiIEFADIGKFIYQpvkTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
500-674 |
7.64e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.57 E-value: 7.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 500 LKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRmaDIENISKFTGFCPQSNVQFGFLTVKEN 579
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK--DLCTYQKQLCFVGHRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 580 LrLFakikGILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNL 659
Cdd:PRK13540 95 C-LY----DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITK 169
|
170
....*....|....*..
gi 27477115 660 LKE--GKSDRVILFSTQ 674
Cdd:PRK13540 170 IQEhrAKGGAVLLTSHQ 186
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1308-1503 |
8.53e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.17 E-value: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG-------SGGGEPL----GFLGYCPQEnALWPN 1376
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqridtlsPGKLQALrrdiQFIFQDPYA-SLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1377 LTVRQHLEVYAAVKGLRKGDAMIA-ITRLVD--ALKLQDQLKAPvKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP 1453
Cdd:PRK10261 418 QTVGDSIMEPLRVHGLLPGKAAAArVAWLLErvGLLPEHAWRYP-HEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27477115 1454 EGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1503
Cdd:PRK10261 497 SIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
481-662 |
8.58e-08 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 57.00 E-value: 8.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKCERVEALKGVVFDIYEGQITALLGHSGAGKT----TLLNILSGLSVPTSGSVTVYNHTLSRM----- 551
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLserel 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 552 -----ADIENIskF----TGFCPQSNV--QfgfltVKENLRLFAKIKGilphevEKEVQRVVQELEMENIQD---ILAQ- 616
Cdd:COG4172 87 rrirgNRIAMI--FqepmTSLNPLHTIgkQ-----IAEVLRLHRGLSG------AAARARALELLERVGIPDperRLDAy 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27477115 617 --NLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE 662
Cdd:COG4172 154 phQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKD 201
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
481-699 |
9.31e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 54.07 E-value: 9.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLS--VPTSGSVTVYNHTLSRMADIENIS 558
Cdd:cd03217 1 LEIKDLHVSVGGK----EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 559 KFTGFCPQSNVQFGFLTVKENLRlfakikgilphEVEKevqrvvqelemeniqdilaqNLSGGQNRKLTFGIAILGDPQV 638
Cdd:cd03217 77 LGIFLAFQYPPEIPGVKNADFLR-----------YVNE--------------------GFSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 639 LLLDEPTAGLD----PLSRHRIWNLLKEGKSdrvILFSTQFIDEAD-ILADRKVFISNGKLKCAGS 699
Cdd:cd03217 126 AILDEPDSGLDidalRLVAEVINKLREEGKS---VLIITHYQRLLDyIKPDRVHVLYDGRIVKSGD 188
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
481-648 |
9.46e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.55 E-value: 9.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGkcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGS-------VTVYNHTLSRMAD 553
Cdd:PRK10762 5 LQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSilylgkeVTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 554 IENISKFTGFCPQsnvqfgfLTVKENL---RLFAKIKG-ILPHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFG 629
Cdd:PRK10762 81 IGIIHQELNLIPQ-------LTIAENIflgREFVNRFGrIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIA 153
|
170
....*....|....*....
gi 27477115 630 IAILGDPQVLLLDEPTAGL 648
Cdd:PRK10762 154 KVLSFESKVIIMDEPTDAL 172
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1305-1499 |
1.03e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 54.78 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1305 KKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMIT--GDTKP---TAGQVILKGSGGGEPLG-------FLGYCPQENA 1372
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNGHNIYSPRTdtvdlrkEIGMVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1373 LWPnltvrqhLEVYA-AVKGLR-KG--DAMIAITRLVDALK-------LQDQLKAPVKTLSEGIKRKLCFVLSILGNPSV 1441
Cdd:PRK14239 97 PFP-------MSIYEnVVYGLRlKGikDKQVLDEAVEKSLKgasiwdeVKDRLHDSALGLSGGQQQRVCIARVLATSPKI 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1442 VLLDEPSTGMDPEGQQQmwqvIRATFRNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:PRK14239 170 ILLDEPTSALDPISAGK----IEETLLGLKDDytMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
505-649 |
1.09e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 54.94 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 505 FDIYEGQITALLGHSGAGKTTLLNILSGLSvPTSGSVTVYNHTLSRMADIENISKFTGFCPQSNVQFGfLTVKENLRLFA 584
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFA-MPVFQYLTLHQ 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 585 KIKGILpHEVEKEVQRVVQELemeNIQDILA---QNLSGGQNRKLTFGIAIL-----GDP--QVLLLDEPTAGLD 649
Cdd:PRK03695 95 PDKTRT-EAVASALNEVAEAL---GLDDKLGrsvNQLSGGEWQRVRLAAVVLqvwpdINPagQLLLLDEPMNSLD 165
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1308-1520 |
1.11e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.55 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKgsggGEPLGF----------LGYCPQENALWPNL 1377
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYL----GKEVTFngpkssqeagIGIIHQELNLIPQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1378 TVRQHL----EVYAAVkGLRKGDAMIA-ITRLVDALKLQDQLKAPVKTLSEG------IKRKLCFvlsilgNPSVVLLDE 1446
Cdd:PRK10762 95 TIAENIflgrEFVNRF-GRIDWKKMYAeADKLLARLNLRFSSDKLVGELSIGeqqmveIAKVLSF------ESKVIIMDE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477115 1447 PSTGMDPEGQQQMWQVIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLrcIGsiQHLKSKFGKDYLLEM 1520
Cdd:PRK10762 168 PTDALTDTETESLFRVIR-ELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF--IA--EREVADLTEDSLIEM 236
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1299-1518 |
1.26e-07 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 54.54 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1299 CFSKRKKKI-ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGGGE-PLGFL----GYCPQENA 1372
Cdd:cd03251 7 TFRYPGDGPpVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLrrqiGLVSQDVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1373 LWpNLTVRQHLeVYAAVKGLRkgDAMIAITRLVDAL----KLQDQLKAPVK----TLSEGIKRKLCFVLSILGNPSVVLL 1444
Cdd:cd03251 87 LF-NDTVAENI-AYGRPGATR--EEVEEAARAANAHefimELPEGYDTVIGergvKLSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477115 1445 DEPSTGMDPEGQQQMWQVIRATFRNteRGALLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFGKDYLL 1518
Cdd:cd03251 163 DEATSALDTESERLVQAALERLMKN--RTTFVIAHRLSTIENA-DRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1310-1540 |
1.26e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.84 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITgDTKPTAGQVILKG-SGGGEPL----GFLGYCPQENALWPNlTVRQHLE 1384
Cdd:TIGR01271 1236 QDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGvSWNSVTLqtwrKAFGVIPQKVFIFSG-TFRKNLD 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1385 VYA--AVKGLRKGDAMIAITRLVDAL--KLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1460
Cdd:TIGR01271 1314 PYEqwSDEEIWKVAEEVGLKSVIEQFpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIR 1393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1461 QVIRATFRNTErgALLTTHYMaEAEAVCDRVAIMVSGRLRCIGSIQHLKSKfgkdyllemklKNLAQMEPLHAEILRLFP 1540
Cdd:TIGR01271 1394 KTLKQSFSNCT--VILSEHRV-EALLECQQFLVIEGSSVKQYDSIQKLLNE-----------TSLFKQAMSAADRLKLFP 1459
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1311-1454 |
1.30e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1311 NVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsggGEPLGfLGYCPQE-NALWPNLTvrqhleVYAAV 1389
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-----GETVK-LAYVDQSrDALDPNKT------VWEEI 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 1390 KGlrkGDAMIAI-TRLVDA--------LKLQDQLKaPVKTLSEGiKRK---LCFVLSILGNpsVVLLDEPSTGMDPE 1454
Cdd:PRK11819 410 SG---GLDIIKVgNREIPSrayvgrfnFKGGDQQK-KVGVLSGG-ERNrlhLAKTLKQGGN--VLLLDEPTNDLDVE 479
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1308-1499 |
1.43e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 54.79 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGsgggeplgflgycpqenalwpnLTVrQHLEVYA 1387
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDD----------------------ITI-THKTKDK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1388 AVKGLRKGDAMI-----------AITRLV----------------DALKLQDQL--------KAPVKtLSEGIKRKLCFV 1432
Cdd:PRK13646 79 YIRPVRKRIGMVfqfpesqlfedTVEREIifgpknfkmnldevknYAHRLLMDLgfsrdvmsQSPFQ-MSGGQMRKIAIV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 1433 lSILG-NPSVVLLDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:PRK13646 158 -SILAmNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1311-1479 |
1.47e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.95 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1311 NVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKgsggGEPLGFL---------GYCPQENALWPNlTVRQ 1381
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFE----GEDISTLkpeiyrqqvSYCAQTPTLFGD-TVYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1382 HLEVYAAVKGlrKGDAMIAITRLVDALKLQDQ-LKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1460
Cdd:PRK10247 100 NLIFPWQIRN--QQPDPAIFLDDLERFALPDTiLTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVN 177
|
170
....*....|....*....
gi 27477115 1461 QVIRATFRNTERGALLTTH 1479
Cdd:PRK10247 178 EIIHRYVREQNIAVLWVTH 196
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1297-1502 |
1.53e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.89 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1297 KNCFSKRKKKIatRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGS-----------GGGEPL---- 1361
Cdd:PRK10982 254 RNLTSLRQPSI--RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKkinnhnaneaiNHGFALvtee 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1362 ----GFLGYCPQE-NALWPNLtvrqhlEVYAAVKGLRKGDAMIAITRLV-DALKLQD-QLKAPVKTLSEGIKRKLCFVLS 1434
Cdd:PRK10982 332 rrstGIYAYLDIGfNSLISNI------RNYKNKVGLLDNSRMKSDTQWViDSMRVKTpGHRTQIGSLSGGNQQKVIIGRW 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 1435 ILGNPSVVLLDEPSTGMDPEGQQQMWQVIrATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCI 1502
Cdd:PRK10982 406 LLTQPEILMLDEPTRGIDVGAKFEIYQLI-AELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGI 472
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1308-1499 |
1.69e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 54.86 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSGGGEPLGFLGYCPQENA--------------- 1372
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSkkiknfkelrrrvsm 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1373 --LWPNL-----TVRQHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQL--KAPVKtLSEGIKRKLCF--VLSIlgNPSV 1441
Cdd:PRK13631 121 vfQFPEYqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYleRSPFG-LSGGQKRRVAIagILAI--QPEI 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 1442 VLLDEPSTGMDPEGQQQMWQVIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:PRK13631 198 LIFDEPTAGLDPKGEHEMMQLIL-DAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
509-649 |
1.75e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 54.29 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 509 EGQITALLGHSGAGKTTLLNILSGLSVPTSGsvtvyNHTLSRMADiENISKFTGfcpqSNVQFGFLTVKE-NLRLFAK-- 585
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLG-----KFDDPPDWD-EILDEFRG----SELQNYFTKLLEgDVKVIVKpq 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 586 --------IKG----ILPHEVEKEVQ-RVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLD 649
Cdd:cd03236 95 yvdlipkaVKGkvgeLLKKKDERGKLdELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1310-1513 |
2.27e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 55.88 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKgsggGEPLGFLGYC---------PQENALWpNLTVR 1380
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD----GVPLVQYDHHylhrqvalvGQEPVLF-SGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1381 QHLevyaaVKGLRKG--DAMIAITRLVDALKLQDQLKAPVKT--------LSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1450
Cdd:TIGR00958 573 ENI-----AYGLTDTpdEEIMAAAKAANAHDFIMEFPNGYDTevgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27477115 1451 MDPEGQQQMWQVIRAtfrnTERGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSKFG 1513
Cdd:TIGR00958 648 LDAECEQLLQESRSR----ASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
481-670 |
2.33e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGKcERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYN--------------- 545
Cdd:PTZ00265 383 IQFKNVRFHYDTR-KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlkdinlkwwrsk 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 546 --------------------HTLSRMADIENISKFT---GFCPQSNVQFGFLTVKENLRLFAKIKGILPH----EVEKEV 598
Cdd:PTZ00265 462 igvvsqdpllfsnsiknnikYSLYSLKDLEALSNYYnedGNDSQENKNKRNSCRAKCAGDLNDMSNTTDSneliEMRKNY 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 599 QrVVQELEMEN------IQDIL--------------AQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRH---R 655
Cdd:PTZ00265 542 Q-TIKDSEVVDvskkvlIHDFVsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYlvqK 620
|
250
....*....|....*
gi 27477115 656 IWNLLKeGKSDRVIL 670
Cdd:PTZ00265 621 TINNLK-GNENRITI 634
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1319-1452 |
4.12e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.89 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1319 GEVIGLLGHNGAGKSTTIKMITGDTKPT--AGQVILKGSGGGEP-LGFLGYCPQENALWPNLTVRQHLeVYAAV----KG 1391
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQiLKRTGFVTQDDILYPHLTVRETL-VFCSLlrlpKS 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 1392 LRKGDAMIAITRLVDAL---KLQDQL--KAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1452
Cdd:PLN03211 173 LTKQEKILVAESVISELgltKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1326-1463 |
4.80e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.18 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1326 GHNGAGKSTTIKMITGDTKPTAGQVILKGSGGGE-PLGFLGYCPQENALWPNLTVRQHLEVYAAVKglrkgDAMIAITRL 1404
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNiAKPYCTYIGHNLGLKLEMTVFENLKFWSEIY-----NSAETLYAA 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 1405 VDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQVI 1463
Cdd:PRK13541 108 IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1306-1504 |
5.28e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 52.74 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1306 KIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITG-----DTK-PTAGQVILKGSGGGEPLGF-----LGYCPQENALW 1374
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRlieiyDSKiKVDGKVLYFGKDIFQIDAIklrkeVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1375 PNLTVRQHLEVYAAVKGLRKGDAMIAIT----RLVDALK-LQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPST 1449
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKKIVeeclRKVGLWKeVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 1450 GMDPEGQQQMWQVIraTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1504
Cdd:PRK14246 183 MIDIVNSQAIEKLI--TELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
500-651 |
5.56e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 52.27 E-value: 5.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 500 LKGVVFDIYEGQITALLGHSGAGKTTLLNILSG--LSVPTSGSVTVYNHTLSR-MADIENISKFTGFcpqsNVQFGFLT- 575
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFGReASLIDAIGRKGDF----KDAVELLNa 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 576 --VKENLRLFAKIKgilphevekevqrvvqelemeniqdilaqNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPL 651
Cdd:COG2401 122 vgLSDAVLWLRRFK-----------------------------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
454-661 |
7.55e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.94 E-value: 7.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 454 LENETDSDPTPNDcfEPVSPefcgkeAIRIKNLKKEYAGK---CERV----EALKGVVFDIYEGQITALLGHSGAGKTTl 526
Cdd:PRK15134 257 LNSEPSGDPVPLP--EPASP------LLDVEQLQVAFPIRkgiLKRTvdhnVVVKNISFTLRPGETLGLVGESGSGKST- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 527 lnilSGLS----VPTSGSVTVYN---HTLSRMADIENISKF--------TGFCPQSNVQfgfLTVKENLRLFAKIkgILP 591
Cdd:PRK15134 328 ----TGLAllrlINSQGEIWFDGqplHNLNRRQLLPVRHRIqvvfqdpnSSLNPRLNVL---QIIEEGLRVHQPT--LSA 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477115 592 HEVEKEVQRVVQE--LEMENIQDILAQnLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLK 661
Cdd:PRK15134 399 AQREQQVIAVMEEvgLDPETRHRYPAE-FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLK 469
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1310-1503 |
7.99e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 52.15 E-value: 7.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITG--DTKPTA---GQVILKG----SGGGEPLGF---LGYCPQENALWPNL 1377
Cdd:PRK14267 21 KGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllELNEEArveGEVRLFGrniySPDVDPIEVrreVGMVFQYPNPFPHL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1378 TVRQHLEVYAAVKGLRKGDAMIAiTRLVDALK-------LQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1450
Cdd:PRK14267 101 TIYDNVAIGVKLNGLVKSKKELD-ERVEWALKkaalwdeVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27477115 1451 MDPEGQQQMWQVIRATfrNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1503
Cdd:PRK14267 180 IDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1311-1500 |
8.05e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 53.68 E-value: 8.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1311 NVSFCVKKGEVIGLLGHNGAGKSTTIKMITG------------DTKPTAGQVILKGSGGGeplgfLGYCPQE---NALWP 1375
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGaypgkfegnvfiNGKPVDIRNPAQAIRAG-----IAMVPEDrkrHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1376 NLTVRQHLEVYAAvkglrkgDAMIAITRLVDALKLQ------DQLKA-------PVKTLSEGIKRKLCFVLSILGNPSVV 1442
Cdd:TIGR02633 353 ILGVGKNITLSVL-------KSFCFKMRIDAAAELQiigsaiQRLKVktaspflPIGRLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1443 LLDEPSTGMDPEGQQQMWQVIRATFRnteRGA--LLTTHYMAEAEAVCDRVAIMVSGRLR 1500
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQLAQ---EGVaiIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1310-1499 |
9.61e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.52 E-value: 9.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG------SGGGEPLGFLGYCPQEnalwpnltvRQ-- 1381
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGkeinalSTAQRLARGLVYLPED---------RQss 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1382 --HLE--VYAAVKGLRKGDAMIAITRLVDALKLQ----------DQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1447
Cdd:PRK15439 351 glYLDapLAWNVCALTHNRRGFWIKPARENAVLEryrralnikfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27477115 1448 STGMDPEGQQQMWQVIRA-TFRNTerGALLTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSiAAQNV--AVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1316-1464 |
1.02e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.98 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1316 VKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAG--------QVILKGSGGGEPLGFLGYCpQENALWPNLTVRQHLEVYA 1387
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwDEILDEFRGSELQNYFTKL-LEGDVKVIVKPQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1388 AVKG-----LRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQV 1462
Cdd:cd03236 102 AVKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARL 181
|
..
gi 27477115 1463 IR 1464
Cdd:cd03236 182 IR 183
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
484-660 |
1.06e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 52.66 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 484 KNLKKEYA------GKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRmADIENI 557
Cdd:PRK11308 9 IDLKKHYPvkrglfKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK-ADPEAQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 558 SKFtgfcpQSNVQFGFLTVKENLRLFAKIKGIL--PHEVEKEV---QRVVQELEMeniqdiLAQ-------------NLS 619
Cdd:PRK11308 88 KLL-----RQKIQIVFQNPYGSLNPRKKVGQILeePLLINTSLsaaERREKALAM------MAKvglrpehydryphMFS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 27477115 620 GGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLL 660
Cdd:PRK11308 157 GGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLM 197
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
464-705 |
1.22e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 464 PNDCFEPVSPefcgkeAIRIKNLKKEYAGKCERvEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTV 543
Cdd:PLN03232 604 QNPPLQPGAP------AISIKNGYFSWDSKTSK-PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 544 YNHTLSRMADIENISKFTgfcPQSNVQFGflTVKENLRLFAKIKGI-LPHEVEKEVQRVVQELEMENIqdilaqNLSGGQ 622
Cdd:PLN03232 677 IRGSVAYVPQVSWIFNAT---VRENILFG--SDFESERYWRAIDVTaLQHDLDLLPGRDLTEIGERGV------NISGGQ 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 623 NRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWN-LLKE---GKSDRVILFSTQFIDeadiLADRKVFISNGKLKCAG 698
Cdd:PLN03232 746 KQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDsCMKDelkGKTRVLVTNQLHFLP----LMDRIILVSEGMIKEEG 821
|
....*..
gi 27477115 699 SSLFLKK 705
Cdd:PLN03232 822 TFAELSK 828
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1311-1498 |
1.23e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.17 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1311 NVSFCVKKGEVIGLLGHNGAGKSTTIKMI------------TGDTKpTAGQVILKGS--------GGGEPLGFlgycpQE 1370
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSVTALSIlrllpsppvvypSGDIR-FHGESLLHASeqtlrgvrGNKIAMIF-----QE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1371 N--ALWPNLTVRQHL-EVYAAVKGLRKGDAMIAITRLVDALKLQD---QLKAPVKTLSEGIKRKLCFVLSILGNPSVVLL 1444
Cdd:PRK15134 101 PmvSLNPLHTLEKQLyEVLSLHRGMRREAARGEILNCLDRVGIRQaakRLTDYPHQLSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27477115 1445 DEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1498
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
484-648 |
1.29e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.01 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 484 KNLKKEYAGkcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGlsVPTSGS-----------VTVYNHTLSRMA 552
Cdd:PRK13549 9 KNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG--VYPHGTyegeiifegeeLQASNIRDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 553 DIENISKFTGFCPQsnvqfgfLTVKENLRLFAKI--KGILPH-EVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFG 629
Cdd:PRK13549 83 GIAIIHQELALVKE-------LSVLENIFLGNEItpGGIMDYdAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIA 155
|
170
....*....|....*....
gi 27477115 630 IAILGDPQVLLLDEPTAGL 648
Cdd:PRK13549 156 KALNKQARLLILDEPTASL 174
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
454-543 |
1.41e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.02 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 454 LENETDSDPTPNDCFEPVSPEFcGKEAIRIKNLKKEYAGKCerveALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGL 533
Cdd:TIGR03719 297 LSQEFQKRNETAEIYIPPGPRL-GDKVIEAENLTKAFGDKL----LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQ 371
|
90
....*....|
gi 27477115 534 SVPTSGSVTV 543
Cdd:TIGR03719 372 EQPDSGTIEI 381
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1288-1504 |
1.53e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.15 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1288 LRKEYAGKKKncfskrkkkiATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsgGG------EP- 1360
Cdd:PRK11650 9 VRKSYDGKTQ----------VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWI----GGrvvnelEPa 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1361 -----LGFLGYcpqenALWPNLTVRQHLEvYA-AVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLS 1434
Cdd:PRK11650 75 drdiaMVFQNY-----ALYPHMSVRENMA-YGlKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1435 ILGNPSVVLLDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1504
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1305-1476 |
1.57e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.53 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1305 KKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGS-----GGGEPLGFLGYCPQeNALWP-NLT 1378
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiqhyASKEVARRIGLLAQ-NATTPgDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1379 VRQ--------HLEVYAAvkgLRKGDAMiAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1450
Cdd:PRK10253 98 VQElvargrypHQPLFTR---WRKEDEE-AVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180
....*....|....*....|....*.
gi 27477115 1451 MDPEGQQQMWQVIRATfrNTERGALL 1476
Cdd:PRK10253 174 LDISHQIDLLELLSEL--NREKGYTL 197
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1308-1498 |
1.57e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 52.52 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGdTKPTA---GQVILKGS-------GGGEPLGfLGYCPQENALWPNL 1377
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYWSGSplkasniRDTERAG-IVIIHQELTLVPEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1378 TVRQHL----EVyaAVKGLRKGDAmiAITRLVDALKLQDQLKA-----PVKTLSEGIKRKLCFVLSILGNPSVVLLDEPS 1448
Cdd:TIGR02633 94 SVAENIflgnEI--TLPGGRMAYN--AMYLRAKNLLRELQLDAdnvtrPVGDYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27477115 1449 TGMDPEGQQQMWQVIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1498
Cdd:TIGR02633 170 SSLTEKETEILLDIIR-DLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1312-1513 |
1.80e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.03 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1312 VSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSgggeplgfLGYCPQEnALWPNLTVRQHLEVYAAVKG 1391
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------VAYVPQQ-AWIQNDSLRENILFGKALNE 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1392 LRKGDAMIAITRLVD--ALKLQDQLKAPVK--TLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE-GQQQMWQVI--R 1464
Cdd:TIGR00957 728 KYYQQVLEACALLPDleILPSGDRTEIGEKgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIgpE 807
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27477115 1465 ATFRNTERgaLLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFG 1513
Cdd:TIGR00957 808 GVLKNKTR--ILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDG 853
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
500-657 |
1.85e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 51.40 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 500 LKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVtvyNHtlsrmadieniSKFTGFCPQ-SNVQFGflTVKE 578
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI---KH-----------SGRISFSSQfSWIMPG--TIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 579 NLrlfakIKGILPHEVekEVQRVVQELEMEniQDILA-------------QNLSGGQNRKLTFGIAILGDPQVLLLDEPT 645
Cdd:cd03291 117 NI-----IFGVSYDEY--RYKSVVKACQLE--EDITKfpekdntvlgeggITLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170
....*....|..
gi 27477115 646 AGLDPLSRHRIW 657
Cdd:cd03291 188 GYLDVFTEKEIF 199
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
512-660 |
1.94e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 50.26 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 512 ITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNhtlsrmADIENISKftGFCPQSNVQFGF---LTVKENLRLFAKIkg 588
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKN------CNINNIAK--PYCTYIGHNLGLkleMTVFENLKFWSEI-- 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477115 589 ilpHEVEKEVQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLL 660
Cdd:PRK13541 98 ---YNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1310-1517 |
1.97e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.18 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITG--DTKPTAGQVILKGSG--GGEP-----LG-FLGYcpQENALWPNLTV 1379
Cdd:CHL00131 24 KGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESilDLEPeerahLGiFLAF--QYPIEIPGVSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1380 RQHLE-VYAAVK---GLRKGDAMIAITRLVDALKLQDqLKAPV--KTLSEGI-----KRKLCFVLSILgNPSVVLLDEPS 1448
Cdd:CHL00131 102 ADFLRlAYNSKRkfqGLPELDPLEFLEIINEKLKLVG-MDPSFlsRNVNEGFsggekKRNEILQMALL-DSELAILDETD 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477115 1449 TGMDPEGQQQMWQVIRaTFRNTERGALLTTHYMAEAEAVC-DRVAIMVSGRLRCIGSIQ--HLKSKFGKDYL 1517
Cdd:CHL00131 180 SGLDIDALKIIAEGIN-KLMTSENSIILITHYQRLLDYIKpDYVHVMQNGKIIKTGDAElaKELEKKGYDWL 250
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
497-671 |
2.52e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.17 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 497 VEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADieniSKFTGFcpQSNVQFGF--- 573
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSP----GKLQAL--RRDIQFIFqdp 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 574 -------LTVKENLRLFAKIKGILPHEVEKEvqRVVQELEMENIQDILA----QNLSGGQNRKLTFGIAILGDPQVLLLD 642
Cdd:PRK10261 411 yasldprQTVGDSIMEPLRVHGLLPGKAAAA--RVAWLLERVGLLPEHAwrypHEFSGGQRQRICIARALALNPKVIIAD 488
|
170 180
....*....|....*....|....*....
gi 27477115 643 EPTAGLDPLSRHRIWNLLKEGKSDRVILF 671
Cdd:PRK10261 489 EAVSALDVSIRGQIINLLLDLQRDFGIAY 517
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
517-662 |
2.67e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 52.12 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 517 GHSGAGKTTLLNILSGLSVPTSGSVTVynHTLSRMAdieniskftgFCPQ-SNVQFGflTVKENLrlfakikgILPHEVE 595
Cdd:COG4178 396 GPSGSGKSTLLRAIAGLWPYGSGRIAR--PAGARVL----------FLPQrPYLPLG--TLREAL--------LYPATAE 453
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 596 K----EVQRVVQELEMENIQDIL------AQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE 662
Cdd:COG4178 454 AfsdaELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE 530
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
470-699 |
3.12e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.78 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 470 PVSPEFCGKEAIRIKNLKKEYAGKCERVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLS 549
Cdd:PRK10261 2 PHSDELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 550 RM--------------------ADIENISK--FTGFCPQSNVQfgfLTVKENLRLFakiKGILPHEVEKEVQRVVQELEM 607
Cdd:PRK10261 82 RRsrqvielseqsaaqmrhvrgADMAMIFQepMTSLNPVFTVG---EQIAESIRLH---QGASREEAMVEAKRMLDQVRI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 608 ENIQDILAQ---NLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDR---VILFSTQFIDEADI 681
Cdd:PRK10261 156 PEAQTILSRyphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMsmgVIFITHDMGVVAEI 235
|
250
....*....|....*...
gi 27477115 682 lADRKVFISNGKLKCAGS 699
Cdd:PRK10261 236 -ADRVLVMYQGEAVETGS 252
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1311-1499 |
3.67e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 50.51 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1311 NVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQV------ILKGSGGGE------PLGFLGYCPQEN------- 1371
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVrvddtlITSTSKNKDikqirkKVGLVFQFPESQlfeetvl 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1372 ---ALWP-NLTVRQHlevyAAVKGLRKGDAMIAITR-LVDalklqdqlKAPVKtLSEGIKRKLCfVLSILG-NPSVVLLD 1445
Cdd:PRK13649 105 kdvAFGPqNFGVSQE----EAEALAREKLALVGISEsLFE--------KNPFE-LSGGQMRRVA-IAGILAmEPKILVLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 1446 EPSTGMDPEGQQQMWQViratFRNTERGAL---LTTHYMAEAEAVCDRVAIMVSGRL 1499
Cdd:PRK13649 171 EPTAGLDPKGRKELMTL----FKKLHQSGMtivLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1308-1498 |
4.40e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.08 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGdTKPTA---GQVILKgsggGEPLGFLGYCP----------QENALW 1374
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHGtyeGEIIFE----GEELQASNIRDteragiaiihQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1375 PNLTVRQHL----EVYAAvkGLRKGDAMIA-ITRLVDALKLQDQLKAPVKTLSEGiKRKLCFVLSILG-NPSVVLLDEPS 1448
Cdd:PRK13549 95 KELSVLENIflgnEITPG--GIMDYDAMYLrAQKLLAQLKLDINPATPVGNLGLG-QQQLVEIAKALNkQARLLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27477115 1449 TGMDPEGQQQMWQVIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1498
Cdd:PRK13549 172 ASLTESETAVLLDIIR-DLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1310-1479 |
4.58e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.40 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSG---------------GGEPLGFLGYC-PQEnal 1373
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVrmavfsqhhvdgldlSSNPLLYMMRCfPGV--- 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1374 wPNLTVRQHLEVYAavkglrkgdamiaitrLVDALKLQdqlkaPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP 1453
Cdd:PLN03073 603 -PEQKLRAHLGSFG----------------VTGNLALQ-----PMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL 660
|
170 180
....*....|....*....|....*.
gi 27477115 1454 EGQQQMWQVIrATFRNterGALLTTH 1479
Cdd:PLN03073 661 DAVEALIQGL-VLFQG---GVLMVSH 682
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1302-1366 |
5.21e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 49.79 E-value: 5.21e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 1302 KRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKgsggGEPLGFLGY 1366
Cdd:PRK15112 22 RRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLID----DHPLHFGDY 82
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
481-693 |
5.28e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 50.98 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 481 IRIKNLKKEYAGkcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGL--------SVPTSGSVTVYNHTL-SRM 551
Cdd:TIGR02633 2 LEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgtwdgEIYWSGSPLKASNIRdTER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 552 ADIENISKFTGFCPQsnvqfgfLTVKENLRLFAKI--KGILPH--EVEKEVQRVVQELEMENIQDILA-QNLSGGQNRKL 626
Cdd:TIGR02633 78 AGIVIIHQELTLVPE-------LSVAENIFLGNEItlPGGRMAynAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 627 TFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKSDRV-ILFSTQFIDEADILADRKVFISNGK 693
Cdd:TIGR02633 151 EIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVaCVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
500-649 |
5.50e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.66 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 500 LKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMAdIENISKFTGFCPQSNVQFGFlTVKEN 579
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG-LMDLRKVLGIIPQAPVLFSG-TVRFN 1332
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 580 LRLF-----AKIKGILPHEVEKEV-QRVVQELEMENIQDilAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLD 649
Cdd:PLN03130 1333 LDPFnehndADLWESLERAHLKDViRRNSLGLDAEVSEA--GENFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1300-1500 |
5.95e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 49.65 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1300 FSKRKKKIaTRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITgDTKPTAGQVILKGSgggepLGFLGYCPQENALWPNLTV 1379
Cdd:PRK14258 15 FYYDTQKI-LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVRVEGR-----VEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1380 RQ-----------HLEVYAAVK------GLRKGDAMIAITR-LVDALKLQDQLKAPVKT----LSEGIKRKLCFVLSILG 1437
Cdd:PRK14258 88 RQvsmvhpkpnlfPMSVYDNVAygvkivGWRPKLEIDDIVEsALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27477115 1438 NPSVVLLDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLR 1500
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENR 230
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
500-699 |
5.97e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 51.48 E-value: 5.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 500 LKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHT--LSRMADIENISKftgfcpQSNVQFG----- 572
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVayVPQQAWIQNDSL------RENILFGkalne 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 573 --FLTVKENLRLFAKIKgILPHEVEKEVQRVvqelemeniqdilAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDP 650
Cdd:TIGR00957 728 kyYQQVLEACALLPDLE-ILPSGDRTEIGEK-------------GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 651 -LSRHRIWNL-----LKEGKSDRVILFSTQFIDEADILadrkVFISNGKLKCAGS 699
Cdd:TIGR00957 794 hVGKHIFEHVigpegVLKNKTRILVTHGISYLPQVDVI----IVMSGGKISEMGS 844
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1306-1454 |
6.05e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 6.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1306 KIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILkgsggGEPLGfLGYCPQENA-LWPNLTVRQHLe 1384
Cdd:PRK11147 332 KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-----GTKLE-VAYFDQHRAeLDPEKTVMDNL- 404
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 1385 vyaavkGLRKGDAMI-AITRLVDALkLQDQL------KAPVKTLSEGIKRKLcFVLSILGNPSVVL-LDEPSTGMDPE 1454
Cdd:PRK11147 405 ------AEGKQEVMVnGRPRHVLGY-LQDFLfhpkraMTPVKALSGGERNRL-LLARLFLKPSNLLiLDEPTNDLDVE 474
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1310-1452 |
6.69e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 49.86 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVilKGSGGgeplgfLGYCPQENALWPNlTVRQHLEVYAAV 1389
Cdd:cd03291 54 KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--KHSGR------ISFSSQFSWIMPG-TIKENIIFGVSY 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 1390 KGLRKGDAMIAITRLVDALKLQDQLKAPVK----TLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1452
Cdd:cd03291 125 DEYRYKSVVKACQLEEDITKFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
500-649 |
8.82e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.74 E-value: 8.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 500 LKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMAdIENISKFTGFCPQSNVQFGFlTVKEN 579
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG-LTDLRRVLSIIPQSPVLFSG-TVRFN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 580 LRLFAkikgilphevEKEVQRVVQELEMENIQDIL--------------AQNLSGGQNRKLTFGIAILGDPQVLLLDEPT 645
Cdd:PLN03232 1330 IDPFS----------EHNDADLWEALERAHIKDVIdrnpfgldaevsegGENFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
....
gi 27477115 646 AGLD 649
Cdd:PLN03232 1400 ASVD 1403
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
483-649 |
1.32e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.48 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 483 IKNLKkeyAGKCERvEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSG---LSVpTSGSVTVYNHTLSRMaDIENISK 559
Cdd:CHL00131 10 IKNLH---ASVNEN-EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaYKI-LEGDILFKGESILDL-EPEERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 ---FTGFcpQSNVQFGFLTVKENLRLFAKIKGILPHEVEKE----VQRVVQELEMENIQDI-LAQNL----SGGQNRKLT 627
Cdd:CHL00131 84 lgiFLAF--QYPIEIPGVSNADFLRLAYNSKRKFQGLPELDplefLEIINEKLKLVGMDPSfLSRNVnegfSGGEKKRNE 161
|
170 180
....*....|....*....|..
gi 27477115 628 FGIAILGDPQVLLLDEPTAGLD 649
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLD 183
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
439-674 |
1.35e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 48.93 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 439 KSCFWFQHGRANHVVLENETDSDPTPNDCFEPVSPEFCGKEAIRIKNLKKEYAGKCERVEALKGVVFDIYEGQITALLGH 518
Cdd:pfam13304 57 PIEFEISEFLEDGVRYRYGLDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 519 SGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMADIENISKFtgfcPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEV 598
Cdd:pfam13304 137 DLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALF----PDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 599 QRVVQE-----LEMENIQDILAQNLSGGQNRKLTFGIAILGDPQ---VLLLDEPTAGLDPLSRHRIWNLLKEGKSDRV-I 669
Cdd:pfam13304 213 DDRLRErglilLENGGGGELPAFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGAqL 292
|
....*
gi 27477115 670 LFSTQ 674
Cdd:pfam13304 293 ILTTH 297
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
500-657 |
1.38e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.29 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 500 LKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVtvyNHtlsrmadieniSKFTGFCPQ-SNVQFGflTVKE 578
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI---KH-----------SGRISFSPQtSWIMPG--TIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 579 NLrLFAkikgiLPHEvEKEVQRVVQELEMENIQDILAQ-----------NLSGGQNRKLTFGIAILGDPQVLLLDEPTAG 647
Cdd:TIGR01271 506 NI-IFG-----LSYD-EYRYTSVIKACQLEEDIALFPEkdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170
....*....|
gi 27477115 648 LDPLSRHRIW 657
Cdd:TIGR01271 579 LDVVTEKEIF 588
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1310-1464 |
1.38e-05 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 48.54 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG-----SGGGE---PLGFLgycPQENALWPNLTVRQ 1381
Cdd:COG4604 18 DDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvatTPSRElakRLAIL---RQENHINSRLTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1382 hLeV----YAAVKG-LRKGDAMIaITRLVDALKLQDQLKAPVKTLSEGiKRKLCFVLSILG-NPSVVLLDEPSTGMDPEG 1455
Cdd:COG4604 95 -L-VafgrFPYSKGrLTAEDREI-IDEAIAYLDLEDLADRYLDELSGG-QRQRAFIAMVLAqDTDYVLLDEPLNNLDMKH 170
|
....*....
gi 27477115 1456 QQQMWQVIR 1464
Cdd:COG4604 171 SVQMMKLLR 179
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1307-1492 |
1.83e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 48.24 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1307 IATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMI--TGDTKPTA---GQVILKGS----GGGEPLGF---LGYCPQENALW 1374
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGFrveGKVTFHGKnlyaPDVDPVEVrrrIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1375 PNlTVRQHLEVYAAVKGLrKGDAMIAITRLVDALKLQDQLKAPVKT----LSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1450
Cdd:PRK14243 104 PK-SIYDNIAYGARINGY-KGDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27477115 1451 MDPEGQQQMWQVIRATFRntERGALLTTHYMAEAEAVCDRVA 1492
Cdd:PRK14243 182 LDPISTLRIEELMHELKE--QYTIIIVTHNMQQAARVSDMTA 221
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1310-1452 |
1.86e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 49.34 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSG----GGEPLGFL-----GYCPQENALWPNLTVR 1380
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvatlDADALAQLrrehfGFIFQRYHLLSHLTAA 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477115 1381 QHLEVYAAVKGLRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1452
Cdd:PRK10535 105 QNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD 176
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1310-1452 |
2.02e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.52 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1310 RNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVilKGSGGgeplgfLGYCPQENALWPNlTVRQHLEVYAAV 1389
Cdd:TIGR01271 443 KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI--KHSGR------ISFSPQTSWIMPG-TIKDNIIFGLSY 513
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 1390 KGLRKGDAMIAITRLVDALKLQDQLKAPVK----TLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1452
Cdd:TIGR01271 514 DEYRYTSVIKACQLEEDIALFPEKDKTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
464-699 |
2.05e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.74 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 464 PNDCFEPVSPefcgkeAIRIKNLKKEYAGKCERvEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTV 543
Cdd:PLN03130 604 PNPPLEPGLP------AISIKNGYFSWDSKAER-PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 544 YNHTLSrmadieniskftgFCPQSNVQFGfLTVKENLrLFAkikgiLPHEVEKeVQRVVQELEMENIQDILAQ------- 616
Cdd:PLN03130 677 IRGTVA-------------YVPQVSWIFN-ATVRDNI-LFG-----SPFDPER-YERAIDVTALQHDLDLLPGgdlteig 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 617 ----NLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDP-LSRHRIWNLLKE--GKSDRViLFSTQ--FIDEadilADRKV 687
Cdd:PLN03130 736 ergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVFDKCIKDelRGKTRV-LVTNQlhFLSQ----VDRII 810
|
250
....*....|..
gi 27477115 688 FISNGKLKCAGS 699
Cdd:PLN03130 811 LVHEGMIKEEGT 822
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
45-408 |
2.34e-05 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 48.54 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 45 YLFFSNlhqvhDTPQMSSMDLGRVDSFNDTNYviafapeskttQEIMNKVASAPFLKGRTImgWPDEKSMDELDLNYSID 124
Cdd:pfam12698 19 GLIFSN-----AVNDPEELPVAVVDEDNSSLS-----------RQLVRALEASPTVNLVQY--VDSEEEAKEALKNGKID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 125 AVRVIFTDTFSYHLKFSWGHRIPMMKEHRDHSAhcQAVNEKMKCEGSEFWEKGFVAFQAAINAAIIEIATNHSVMEQLMS 204
Cdd:pfam12698 81 GLLVIPKGFSKDLLKGESATVTVYINSSNLLVS--KLILNALQSLLQQLNASALVLLLEALSTSAPIPVESTPLFNPQSG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 205 VTGVHMKILPFVAQggvatdffiffciisfSTFIYYVSVNVTQER-QYITSLMTMMGLRESAFWLSWGLMYAGFILIMAT 283
Cdd:pfam12698 159 YAYYLVGLILMIII----------------LIGAAIIAVSIVEEKeSRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 284 LMALIVKSAQIvVLTGFVMVFTLFLLYGLSLITLAFLMSVLIKKPFLTGLVVFLLI-VFWGILGFPALYTRLPAFLEWTL 362
Cdd:pfam12698 223 IILLLLFGIGI-PFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVIlLLSGFFGGLFPLEDPPSFLQWIF 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 27477115 363 CLLSPFAFTVGMAQLIHldYDVNSNAHLDSSqnpYLIIATLFMLVF 408
Cdd:pfam12698 302 SIIPFFSPIDGLLRLIY--GDSLWEIAPSLI---ILLLFAVVLLLL 342
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1316-1452 |
2.39e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.04 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1316 VKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQV--------ILKGSGGGEPLGFL----------GYCPQENALWPNl 1377
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdeVLKRFRGTELQNYFkklyngeikvVHKPQYVDLIPK- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1378 tvrqhlevyaAVKG-----LRKGDAMIAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1452
Cdd:PRK13409 175 ----------VFKGkvrelLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1317-1350 |
2.75e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 48.63 E-value: 2.75e-05
10 20 30
....*....|....*....|....*....|....
gi 27477115 1317 KKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQV 1350
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDY 130
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1312-1354 |
2.80e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 48.64 E-value: 2.80e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 27477115 1312 VSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG 1354
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG 393
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
505-662 |
3.55e-05 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 45.99 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 505 FDIYEGQITALLGHSGAGKTTLLNILSGLSvpTSGSVTVYNHTLSRMAdieniskftgFCPQSNVqFGFLTVKENLrlfa 584
Cdd:cd03223 22 FEIKPGDRLLITGPSGTGKSSLFRALAGLW--PWGSGRIGMPEGEDLL----------FLPQRPY-LPLGTLREQL---- 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 585 kikgILPhevekevqrvvqelemeniqdiLAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE 662
Cdd:cd03223 85 ----IYP----------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKE 136
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
482-532 |
3.76e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.25 E-value: 3.76e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 27477115 482 RIKNLKKEYAGkcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSG 532
Cdd:NF040905 3 EMRGITKTFPG----VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1278-1354 |
4.51e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 47.65 E-value: 4.51e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 1278 DETPVIIASCLRKEYAgKKKNCFSKRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG 1354
Cdd:PRK11308 1 SQQPLLQAIDLKKHYP-VKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQG 76
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1299-1500 |
8.28e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 47.27 E-value: 8.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1299 CFSKRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKgsggGEPLGFLG---YCPQENALWP 1375
Cdd:PRK10522 329 TFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLD----GKPVTAEQpedYRKLFSAVFT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1376 NLTVRQHL---EVYAAVKGLrkGDAMIAITRLVDALKLQDQLKAPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1452
Cdd:PRK10522 405 DFHLFDQLlgpEGKPANPAL--VEKWLERLKMAHKLELEDGRISNLK-LSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27477115 1453 PEGQQQMWQVIRATFRNTERGALLTTH---YMAEAeavcDRVAIMVSGRLR 1500
Cdd:PRK10522 482 PHFRREFYQVLLPLLQEMGKTIFAISHddhYFIHA----DRLLEMRNGQLS 528
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1311-1364 |
9.14e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.19 E-value: 9.14e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 1311 NVSfcVKKGE--VIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKgsgGGEPLGFL 1364
Cdd:PRK15064 19 NIS--VKFGGgnRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD---PNERLGKL 69
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1295-1504 |
9.26e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.47 E-value: 9.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1295 KKKNCFSKRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKGSgggeplgfLGYCPQEnALW 1374
Cdd:PTZ00243 662 MKTDDFFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS--------IAYVPQQ-AWI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1375 PNLTVRQHL----EVYAAvkglrkgdamiaitRLVDALKLQdQLKAPVKTLSEGI---------------KRKLCFVLSI 1435
Cdd:PTZ00243 733 MNATVRGNIlffdEEDAA--------------RLADAVRVS-QLEADLAQLGGGLeteigekgvnlsggqKARVSLARAV 797
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1436 LGNPSVVLLDEPSTGMDPE-GQQQMWQVIRATFRNTERgaLLTTHYMaEAEAVCDRVAIMVSGRLRCIGS 1504
Cdd:PTZ00243 798 YANRDVYLLDDPLSALDAHvGERVVEECFLGALAGKTR--VLATHQV-HVVPRADYVVALGDGRVEFSGS 864
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
497-532 |
1.11e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 45.08 E-value: 1.11e-04
10 20 30
....*....|....*....|....*....|....*.
gi 27477115 497 VEALKGVVfdiyEGQITALLGHSGAGKTTLLNILSG 532
Cdd:cd01854 76 LDELRELL----KGKTSVLVGQSGVGKSTLLNALLP 107
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
505-684 |
1.37e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 505 FDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHTLSRMAdIENISKFTGFCPQSNV---------QFGfLT 575
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLS-FEQLQKLVSDEWQRNNtdmlspgedDTG-RT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 576 VKEnlrlfakikgILPHEVEKEvQRVVQELEMENIQDILAQN---LSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLS 652
Cdd:PRK10938 102 TAE----------IIQDEVKDP-ARCEQLAQQFGITALLDRRfkyLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27477115 653 RHRIWNLL----KEGKSDRVIL--FST--QFIDEADILAD 684
Cdd:PRK10938 171 RQQLAELLaslhQSGITLVLVLnrFDEipDFVQFAGVLAD 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
618-693 |
1.59e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.24 E-value: 1.59e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 618 LSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKEGKS--DRVILFSTQFIDEADILADRKVFISNGK 693
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
470-543 |
2.61e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.49 E-value: 2.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477115 470 PVSPEFcGKEAIRIKNLKKEYAgkcERVeALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTV 543
Cdd:PRK11819 315 PPGPRL-GDKVIEAENLSKSFG---DRL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1300-1354 |
2.66e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 45.72 E-value: 2.66e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 1300 FSKRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG 1354
Cdd:PRK13657 342 FSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDG 396
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1278-1354 |
3.33e-04 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 45.06 E-value: 3.33e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 1278 DETPVIIASCLRKEYAGKKKNCFSKRKKKIATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTkPTAGQVILKG 1354
Cdd:COG4172 271 DAPPLLEARDLKVWFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDG 346
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
510-692 |
5.06e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 42.36 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 510 GQITALLGHSGAGKTTLLNILSGLSVPTSGSVtvynhtlsRMADIENIskftgfcpqsnvqfgfltvkenlrlfakikgi 589
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV--------IYIDGEDI-------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 590 lphevekevQRVVQELEMENIQDILAQNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLL-------KE 662
Cdd:smart00382 42 ---------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllllLK 112
|
170 180 190
....*....|....*....|....*....|....*
gi 27477115 663 GKSDRVILFSTQFIDEAD-----ILADRKVFISNG 692
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGpallrRRFDRRIVLLLI 147
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1306-1516 |
9.83e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.54 E-value: 9.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1306 KIATRNVSFCVKKGEVIGLLGHNGAGKSTT----IKMItgdtkPTAGQVILKGSgggePLGFLG--------------YC 1367
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLI-----NSQGEIWFDGQ----PLHNLNrrqllpvrhriqvvFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1368 PQENALWPNLTVRQ----HLEV-YAAVKGLRKGDAMIAITRLVdALKLQDQLKAPVKtLSEGIKRKLCFVLSILGNPSVV 1442
Cdd:PRK15134 370 DPNSSLNPRLNVLQiieeGLRVhQPTLSAAQREQQVIAVMEEV-GLDPETRHRYPAE-FSGGQRQRIAIARALILKPSLI 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477115 1443 LLDEPSTGMDPEGQQQMWQVIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDY 1516
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
509-539 |
1.15e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 41.76 E-value: 1.15e-03
10 20 30
....*....|....*....|....*....|..
gi 27477115 509 EGQITALLGHSGAGKTTLLN-ILSGLSVPTSG 539
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNaLLPELDLRTGE 136
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1308-1341 |
1.19e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.24 E-value: 1.19e-03
10 20 30
....*....|....*....|....*....|....
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITG 1341
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
515-653 |
1.25e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.46 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 515 LLGHSGAGKTTLLNILSGlSVPT--SGSVTVYNHTLSRMADIENISKFTGFCPQS------------NVQF-GFltvken 579
Cdd:PRK10938 291 IVGPNGAGKSTLLSLITG-DHPQgySNDLTLFGRRRGSGETIWDIKKHIGYVSSSlhldyrvstsvrNVILsGF------ 363
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27477115 580 lrlFAKIkGILPHEVEKEVQRVVQELEMENIQDILA----QNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSR 653
Cdd:PRK10938 364 ---FDSI-GIYQAVSDRQQKLAQQWLDILGIDKRTAdapfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNR 437
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1308-1498 |
1.65e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.79 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1308 ATRNVSFCVKKGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKgsggGEPLGF----------LGYCPQENALWPNL 1377
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQ----GKEIDFksskealengISMVHQELNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1378 TVRQHLEV--YAAVKGLRKGDAMIAITRLV-DALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1454
Cdd:PRK10982 89 SVMDNMWLgrYPTKGMFVDQDKMYRDTKAIfDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27477115 1455 GQQQMWQVIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1498
Cdd:PRK10982 169 EVNHLFTIIR-KLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
483-649 |
1.79e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.09 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 483 IKNLKKEYAGKcervEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLS--VPTSGSVTVYNHTLSRMADIENISK- 559
Cdd:PRK09580 4 IKDLHVSVEDK----AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 560 -FTGF-----CPQSNVQFGFLTVKENLRLFAKIKGILPHEVEKEVQRVVQELEMEniQDILAQNL----SGGQ-NRKLTF 628
Cdd:PRK09580 80 iFMAFqypveIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMP--EDLLTRSVnvgfSGGEkKRNDIL 157
|
170 180
....*....|....*....|.
gi 27477115 629 GIAILgDPQVLLLDEPTAGLD 649
Cdd:PRK09580 158 QMAVL-EPELCILDESDSGLD 177
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
491-537 |
1.97e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 42.11 E-value: 1.97e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 27477115 491 AGKCERVEALKgvvfDIYEGQITALLGHSGAGKTTLLN-ILSGLSVPT 537
Cdd:PRK00098 149 AKEGEGLDELK----PLLAGKVTVLAGQSGVGKSTLLNaLAPDLELKT 192
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
477-672 |
2.02e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 477 GKEAIRIKNLKKEYAGKCERVeALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSVTVYNHtlSRMADIEN 556
Cdd:NF040905 254 GEVVFEVKNWTVYHPLHPERK-VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRNISGTVFKD--GKEVDVST 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 557 ISKFTG----FCPQSNVQFGFL---TVKENLRLfAKIKGILPHEV--EKEVQRVVQEL--EMeNIQ--DILAQ--NLSGG 621
Cdd:NF040905 331 VSDAIDaglaYVTEDRKGYGLNlidDIKRNITL-ANLGKVSRRGVidENEEIKVAEEYrkKM-NIKtpSVFQKvgNLSGG 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27477115 622 QNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWN----LLKEGKSdrVILFS 672
Cdd:NF040905 409 NQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTiineLAAEGKG--VIVIS 461
|
|
| Bax1-I |
pfam01027 |
Inhibitor of apoptosis-promoting Bax1; Programmed cell-death involves a set of Bcl-2 family ... |
266-341 |
2.06e-03 |
|
Inhibitor of apoptosis-promoting Bax1; Programmed cell-death involves a set of Bcl-2 family proteins, some of which inhibit apoptosis (Bcl-2 and Bcl-XL) and some of which promote it (Bax and Bak). Human Bax inhibitor, BI-1, is an evolutionarily conserved integral membrane protein containing multiple membrane-spanning segments predominantly localized to intracellular membranes. It has 6-7 membrane-spanning domains. The C termini of the mammalian BI-1 proteins are comprised of basic amino acids resembling some nuclear targeting sequences, but otherwise the predicted proteins lack motifs that suggest a function. As plant BI-1 appears to localize predominantly to the ER, we hypothesized that plant BI-1 could also regulate cell death triggered by ER stress. BI-1 appears to exert its effect through an interaction with calmodulin. The budding yeast member of this family has been found unexpectedly to encode a BH3 domain-containing protein (Ybh3p) that regulates the mitochondrial pathway of apoptosis in a phylogenetically conserved manner. Examination of the crystal structure of a bacterial member of this family shows that these proteins mediate a calcium leak across the membrane that is pH-dependent. Calcium homoeostasis balances passive calcium leak with active calcium uptake. The structure exists in a pore-closed and pore-open conformation, at pHs of 8 and 6 respectively, and the pore can be opened by intracrystalline transition; together these findings suggest that pH controls the conformational transition.
Pssm-ID: 460029 Cd Length: 207 Bit Score: 41.39 E-value: 2.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 266 FWLSWGLMYAGFILIMATLMALIVKSAQIVVLTGFVMVFTLFLLYGLSLITLAFLMSVLIKKPFLTGLVVFLLIVF 341
Cdd:pfam01027 38 PPLFWVLIIAPLGLLFGALLLARKRKYSSNVALLLLLAFTLLMGLTLGPLLLVYTGAIIATAFLGTAAIFGGLSLY 113
|
|
| NosY |
COG1277 |
ABC-type transport system involved in multi-copper enzyme maturation, permease component ... |
265-350 |
2.06e-03 |
|
ABC-type transport system involved in multi-copper enzyme maturation, permease component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440888 [Multi-domain] Cd Length: 201 Bit Score: 41.34 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 265 AFWLSWGLMYAGFILIMATLMALIVKSAQIVVLTgFVMVFTLFLLYGLSLITLAFLMSVLIKKPFLT-GLVVFLLIVFWG 343
Cdd:COG1277 102 GALLVLLLALLITFLLALLLGLLLFGSPPPDLGA-ILGFYLGLLLLGLAFLAIGLFISALTRNQIVAaILAIALWLLLVI 180
|
....*..
gi 27477115 344 ILGFPAL 350
Cdd:COG1277 181 LLAWIVL 187
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
616-670 |
2.40e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 2.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 27477115 616 QNLSGGQNRKLTFGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--GKSDRVIL 670
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDikDKADKTII 1413
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1318-1352 |
5.87e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.89 E-value: 5.87e-03
10 20 30
....*....|....*....|....*....|....*
gi 27477115 1318 KGEVIGLLGHNGAGKSTTIKMITGDTKPTAGQVIL 1352
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY 35
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1321-1447 |
6.41e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 40.63 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477115 1321 VIGLLGHNGAGKSTTIKMITGDTKPTAGQVILKG-----SGGGEPLG----FLGYCPQENALWPNLTVRQHLEvYaavkG 1391
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdAEKGICLPpekrRIGYVFQDARLFPHYKVRGNLR-Y----G 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 27477115 1392 LRKGDAMiAITRLVDALKLQDQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1447
Cdd:PRK11144 101 MAKSMVA-QFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
483-541 |
8.48e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 8.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 27477115 483 IKNLKKEYAGkcerVEALKGVVFDIYEGQITALLGHSGAGKTTLLNILSGLSVPTSGSV 541
Cdd:PRK10982 1 MSNISKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI 55
|
|
| |
