|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3068-4378 |
0e+00 |
|
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: 633.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3068 VKIKDLMKNITKLTEELRSSIQISNETIHSILEANISHSKVLFSALTVALSG-KCDQEILHLLLTFPKGEKSWIAAEELC 3146
Cdd:TIGR01257 151 IRIRDILKDEEALTLFLMKNIGLSDSVVYLLVNSQVRPEQFAYGVPDLELKDiACSEALLERFIIFSQRRGAQTVRDALC 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3147 SLPGSKVYSLIVLLSRNLDV-RAF-IYKTLMPSEANGL-LNSLLDIVSSLSALLAKaqhvFEYLPEFLHTFKIT-ALLET 3222
Cdd:TIGR01257 231 SLSQGTLQWIEDTLYANVDFfKLFhVLPTLLDSRSQGInLRSWGGILSDMSPRIQE----FIHRPSVQDLLWVTrPLLQN 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3223 LDFQQVSQNVQARSSAF-------GSFQFVMkmvckdqaSFLSDSNMfinlprvKELLEDDKEK----FNIPEDSTPFCL 3291
Cdd:TIGR01257 307 GGPETFTQLMGILSDLLcgypeggGSRVFSF--------NWYEDNNY-------KAFLGIDSTRkdpiYSYDKRTTSFCN 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3292 KLYQEILQLPNGALVWTFLKPILHGKILYTPNTPEINKVIQKANYTFYIVDKLKTLSETLLEMSS----LFQRSGsgQMf 3367
Cdd:TIGR01257 372 ALIQSLESNPLTKIAWRAAKPLLMGKILFTPDSPAARRILKNANSTFEELERVRKLVKAWEEVGPqiwyFFDKST--QM- 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3368 NQLQEALRNKFVRNFVENQLH---IDVDKLTEKLQT--YGGLLDEMFNHAGAGRF----RFLGsiLVN-LSSCVALNRFQ 3437
Cdd:TIGR01257 449 TMIRDTLQNPTVKDFINRQLGeegITAEAVLNFLYNgpREKQADDMTNFDWRDIFnitdRFLR--LANqYLECLVLDKFE 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3438 ALQSVDILETKAHELLQQNSFLASIIFSNslfdknFRSESVKLPPHVSYTIRTNVLYSVRTDVVKNPSWKFHPQNLPADG 3517
Cdd:TIGR01257 527 SYDDEVQLTQRALSLLEENRFWAGVVFPD------MYPWTSSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVED 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3518 FKYNYV-FAPLQDMIERAIILVQTgQEALEPAAQTQAAPYPCHTSDLFLNNVGFFFPLIMMLTWMVSVASMVRKLVYEQE 3596
Cdd:TIGR01257 601 FRYIWGgFAYLQDMVEQGITRSQM-QAEPPVGIYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKE 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3597 IQIEEYMRMMGVHPVIHFLAWFLENMAVLTISSATLAIVLKTSGIFAHSNTFIVFLFLLDFGMSVVMLSYLLSAFFSQAN 3676
Cdd:TIGR01257 680 LRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFIMHGRILHYSDPFILFLFLLAFSTATIMQCFLLSTFFSKAS 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3677 TAALCTSLVYMISFLPYIVLLVLHNQLSFVNQTFLCLLSTTAFGQGVFFITFLEGQETGIQWNNMYQA-LEQGGMTFGWV 3755
Cdd:TIGR01257 760 LAAACSGVIYFTLYLPHILCFAWQDRMTADLKTAVSLLSPVAFGFGTEYLVRFEEQGLGLQWSNIGNSpLEGDEFSFLLS 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3756 CWMILFDSSLYFLCGWYLSNLIPGTFGLRKPWYFPFTASYWKSVGFLVEKRQYFLSSSLFFFNENFDNKGSSLQNR---E 3832
Cdd:TIGR01257 840 MKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLGGEGCSTREERALEKTEPLTEEMEDPEHPEGINDsffE 919
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3833 GELEGSAPGVTLVSVTKEYEGH-KAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLS 3911
Cdd:TIGR01257 920 RELPGLVPGVCVKNLVKIFEPSgRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLD 999
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3912 RVRMELGVCPQQDILLDNLTVREHLLLFASIKAPQWTKKELhqQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFM 3991
Cdd:TIGR01257 1000 AVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQL--EMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFV 1077
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3992 GMSRTVVLDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPPFCLKEAYGQGLRL 4071
Cdd:TIGR01257 1078 GDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYL 1157
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 4072 TLTRQPSVLEAH------------------------DLK-------DMACVTSLIKIYIPQAFLKDSSGSELTYTIP-KD 4119
Cdd:TIGR01257 1158 TLVRKMKNIQSQrggcegtcsctskgfstrcparvdEITpeqvldgDVNELMDLVYHHVPEAKLVECIGQELIFLLPnKN 1237
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 4120 TDKACLKGLFQALDENLHQLHLTGYGISDTTLEEVFLMLLQDSNKKSHIALGTESELQN---------------HRPTGH 4184
Cdd:TIGR01257 1238 FKQRAYASLFRELEETLADLGLSSFGISDTPLEEIFLKVTEDADSGSLFAGGAQQKRENanlrhpcsgptekagQTPQAS 1317
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 4185 LSGYCGSLARPATVQ--------------GVQLLRAQVAAILARRLRRTLRAGKSTLADLLLPVLFVALAMGLFMVRPLA 4250
Cdd:TIGR01257 1318 HTCSPGQPAAHPEGQpppepedpgvplntGARLILQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSIIIPPF 1397
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 4251 TEYPPLRLTPGHYQRAETYF-FSSSGGDNLD-LTRVLLRK--FRDQ--------DLPCAdlnprqkNSSCWRTdPFSHPE 4318
Cdd:TIGR01257 1398 GEYPALTLHPWMYGQQYTFFsMDEPNSEHLEvLADVLLNKpgFGNRclkeewlpEYPCG-------NSTPWKT-PSVSPN 1469
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 4319 ----FQD----------SCGCL---------KCPNRSAS--APYLTNHLGHTLLNLSGFNMEEYLLA--PS--------- 4362
Cdd:TIGR01257 1470 ithlFQKqkwtaahpspSCRCStrekltmlpECPEGAGGlpPPQRTQRSTEILQDLTDRNISDFLVKtyPAlirsslksk 1549
|
1450
....*....|....*....
gi 1034654212 4363 ---EKPRLGGWSFGLKIPS 4378
Cdd:TIGR01257 1550 fwvNEQRYGGISIGGKLPA 1568
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3842-4062 |
3.21e-93 |
|
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: 302.12 E-value: 3.21e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYE-GHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRMELGVC 3920
Cdd:cd03263 1 LQIRNLTKTYKkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3921 PQQDILLDNLTVREHLLLFASIKAPqwTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLD 4000
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGL--PKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034654212 4001 EPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPPFCLK 4062
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3842-4058 |
5.11e-77 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 256.14 E-value: 5.11e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYEGHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRMELGVCP 3921
Cdd:COG1131 1 IEVRGLTKRYGDKTAL-DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3922 QQDILLDNLTVREHLLLFASIKapQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDE 4001
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLY--GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034654212 4002 PTSGVDPCSRHSLWDILLKYR-EGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTP 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3842-4052 |
4.27e-60 |
|
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: 205.32 E-value: 4.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRMELGVCP 3921
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3922 QQDILLDNLTVREHLLlfasikapqwtkkelhqqvnqtlqdvdltqhqhkqtraLSGGLKRKLSLGIAFMGMSRTVVLDE 4001
Cdd:cd03230 80 EEPSLYENLTVRENLK--------------------------------------LSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1034654212 4002 PTSGVDPCSRHSLWDILLKYR-EGRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3843-4067 |
1.53e-56 |
|
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: 197.77 E-value: 1.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3843 TLVSVTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRMELGVCPQ 3922
Cdd:COG4555 3 EVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3923 QDILLDNLTVREHLLLFASIKapQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEP 4002
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELY--GLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654212 4003 TSGVDPCSRHSLWDILLKYR-EGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPPFCLKEAYGQ 4067
Cdd:COG4555 160 TNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3847-4062 |
4.32e-54 |
|
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: 189.89 E-value: 4.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEGHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRMELGVCPQQDIL 3926
Cdd:cd03265 6 LVKKYGDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3927 LDNLTVREHLLLFASIKAPQWtkKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGV 4006
Cdd:cd03265 85 DDELTGWENLYIHARLYGVPG--AERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034654212 4007 DPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPPFCLK 4062
Cdd:cd03265 163 DPQTRAHVWEYIekLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
3849-4158 |
2.17e-50 |
|
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: 182.20 E-value: 2.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3849 KEYEGHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRMELGVCPQQDILLD 3928
Cdd:TIGR01188 1 KVYGDFKAV-DGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3929 NLTVREHLLLFASIKApqWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDP 4008
Cdd:TIGR01188 80 DLTGRENLEMMGRLYG--LPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 4009 CSRHSLWDILLKYRE-GRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPPfclkeaygQGLRLTLTRQPSVLEAHDLKD 4087
Cdd:TIGR01188 158 RTRRAIWDYIRALKEeGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTP--------EELKRRLGKDTLESRPRDIQS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 4088 MACVTSLIKIYIPQAFLKDSSgseltytIPKDTDKA---------CLKGLFQALDENlhQLHLTGYGISDTTLEEVFLML 4158
Cdd:TIGR01188 230 LKVEVSMLIAELGETGLGLLA-------VTVDSDRIkilvpdgdeTVPEIVEAAIRN--GIRIRSISTERPSLDDVFLKL 300
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3847-4058 |
2.62e-47 |
|
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: 170.59 E-value: 2.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL-QTDLSRVRMELGVCPQQ-D 3924
Cdd:COG1122 6 LSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItKKNLRELRRKVGLVFQNpD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3925 ILLDNLTVREHLLLfasikAPQ---WTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSL-GIAFMGmSRTVVLD 4000
Cdd:COG1122 86 DQLFAPTVEEDVAF-----GPEnlgLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIaGVLAME-PEVLVLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034654212 4001 EPTSGVDPCSRHSLWDILLKY-REGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTP 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3842-4056 |
2.06e-45 |
|
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: 164.67 E-value: 2.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYeGHKAVVQDLSLTFyRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRMELGVCP 3921
Cdd:cd03264 1 LQLENLTKRY-GKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3922 QQDILLDNLTVREHLLLFASIKApqWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDE 4001
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKG--IPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034654212 4002 PTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCG 4056
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3585-4170 |
2.42e-45 |
|
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: 182.91 E-value: 2.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3585 ASMVRKLVYEQEIQIEEYMRMMGVHPVIHFLAWFLENMAVLTISSATLA---IVLKTSGIFAHSNTFIVFLFLLDFGMSV 3661
Cdd:TIGR01257 1695 ASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVgifIGFQKKAYTSPENLPALVALLMLYGWAV 1774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3662 VMLSYLLSAFF---SQANTAALCTSLVYMI--SFLPYIVLLVLHNQ----LSFVNQTFLCLLSTTAFGQGVFFITFLEG- 3731
Cdd:TIGR01257 1775 IPMMYPASFLFdvpSTAYVALSCANLFIGInsSAITFVLELFENNRtllrFNAMLRKLLIVFPHFCLGRGLIDLALSQAv 1854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3732 QETGIQWNNMYQALEQGGMTFGWVCWMILFDSSLYFLcgwyLSNLIPGTFGLRKPWYFPFTASYWKSVGFLVEKRQYFLS 3811
Cdd:TIGR01257 1855 TDVYAQFGEEHSANPFQWDLIGKNLVAMAVEGVVYFL----LTLLIQHHFFLSRWIAEPAKEPIFDEDDDVAEERQRIIS 1930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3812 SSlfffnenfdNKGSSLQNREgelegsapgvtlvsVTKEYEGHKA-VVQDLSLTFYRDQITALLGTNGAGKTTIISMLTG 3890
Cdd:TIGR01257 1931 GG---------NKTDILRLNE--------------LTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG 1987
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3891 LHPPTSGTIIINGKNLQTDLSRVRMELGVCPQQDILLDNLTVREHLLLFASIKAPqwTKKELHQQVNQTLQDVDLTQHQH 3970
Cdd:TIGR01257 1988 DTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGV--PAEEIEKVANWSIQSLGLSLYAD 2065
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3971 KQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLK-YREGRTIIFTTHHLDEAEALSDRVAVLQH 4049
Cdd:TIGR01257 2066 RLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSiIREGRAVVLTSHSMEECEALCTRLAIMVK 2145
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 4050 GRLRCCGPPFCLKEAYGQGLRLTLT-RQPsvlEAHDLKDMACVTSLIKIYIPQAFLKDSSGSELTYTIPKDTdkacLKGL 4128
Cdd:TIGR01257 2146 GAFQCLGTIQHLKSKFGDGYIVTMKiKSP---KDDLLPDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSSSS----LARI 2218
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1034654212 4129 FQALDENLHQLHLTGYGISDTTLEEVFLMLLQDSNKKSHIAL 4170
Cdd:TIGR01257 2219 FQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQTETYDLPL 2260
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3842-4163 |
8.41e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 166.05 E-value: 8.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYEGHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDlsrVRMELGVCP 3921
Cdd:COG4152 2 LELKGLTKRFGDKTAV-DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE---DRRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3922 QQDILLDNLTVREHLLLFASIKapQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDE 4001
Cdd:COG4152 78 EERGLYPKMKVGEQLVYLARLK--GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 4002 PTSGVDPCSRHSLWDILLKYRE-GRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPPFCLKEAYG-QGLRLTLTRQPSV 4079
Cdd:COG4152 156 PFSGLDPVNVELLKDVIRELAAkGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGrNTLRLEADGDAGW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 4080 LEAhdlkdmacvtslikiyIPQAFLKDSSGSELTYTIPKDTDKaclKGLFQALdenLHQLHLTGYGISDTTLEEVFLMLL 4159
Cdd:COG4152 236 LRA----------------LPGVTVVEEDGDGAELKLEDGADA---QELLRAL---LARGPVREFEEVRPSLNEIFIEVV 293
|
....
gi 1034654212 4160 QDSN 4163
Cdd:COG4152 294 GEKA 297
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3847-4053 |
1.43e-44 |
|
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: 162.00 E-value: 1.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQtDLSRVRMELGVCPQQDIL 3926
Cdd:cd03268 6 LTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ-KNIEALRRIGALIEAPGF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3927 LDNLTVREHLLLFAsiKAPQWTKKElhqqVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGV 4006
Cdd:cd03268 84 YPNLTARENLRLLA--RLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1034654212 4007 DPCSRHSLWDILLKYR-EGRTIIFTTHHLDEAEALSDRVAVLQHGRLR 4053
Cdd:cd03268 158 DPDGIKELRELILSLRdQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3847-4058 |
2.56e-44 |
|
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: 163.29 E-value: 2.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEGHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqTDLS---RVRMelGVC--- 3920
Cdd:COG0411 10 LTKRFGGLVAV-DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI-TGLPphrIARL--GIArtf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3921 --PQqdiLLDNLTVREHLLL----------FASIKAPQWTKK---ELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLS 3985
Cdd:COG0411 86 qnPR---LFPELTVLENVLVaaharlgrglLAALLRLPRARReerEARERAEELLERVGLADRADEPAGNLSYGQQRRLE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034654212 3986 LGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYRE--GRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:COG0411 163 IARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDerGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3838-4071 |
3.70e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 162.18 E-value: 3.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3838 SAPGVTLVSVTKEYEGHKaVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVrmel 3917
Cdd:COG1121 3 MMPAIELENLTVSYGGRP-VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRI---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3918 GVCPQQDILLDN--LTVREHLL--LFASIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGM 3993
Cdd:COG1121 78 GYVPQRAEVDWDfpITVRDVVLmgRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3994 SRTVVLDEPTSGVDPCSRHSLWDILLKYR-EGRTIIFTTHHLDEAEALSDRVAVLQHGRLrCCGPP------FCLKEAYG 4066
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLRELRrEGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPPeevltpENLSRAYG 236
|
....*
gi 1034654212 4067 QGLRL 4071
Cdd:COG1121 237 GPVAL 241
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3853-4058 |
1.54e-43 |
|
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: 160.98 E-value: 1.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3853 GHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqTDLSR--VRMELGVCPQQDILLDNL 3930
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL-ASLSRreLARRIAYVPQEPPAPFGL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3931 TVREHLLL--FASIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDP 4008
Cdd:COG1120 91 TVRELVALgrYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1034654212 4009 CSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:COG1120 171 AHQLEVLELLrrLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPP 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3847-4056 |
2.56e-43 |
|
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: 158.60 E-value: 2.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDlsrVRMELGVCPQQDIL 3926
Cdd:cd03269 6 VTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA---ARNRIGYLPEERGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3927 LDNLTVREHLLLFASIKApqWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGV 4006
Cdd:cd03269 82 YPKMKVIDQLVYLAQLKG--LKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034654212 4007 DPCSRHSLWDILLKY-REGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCG 4056
Cdd:cd03269 160 DPVNVELLKDVIRELaRAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3847-4058 |
2.25e-42 |
|
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: 156.83 E-value: 2.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEGHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqTDLS---RVRMELGVCPQQ 3923
Cdd:cd03219 6 LTKRFGGLVAL-DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI-TGLPpheIARLGIGRTFQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3924 DILLDNLTVREHLLL--------FASIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSR 3995
Cdd:cd03219 84 PRLFPELTVLENVMVaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034654212 3996 TVVLDEPTSGVDPCSRHSLWDILLKYRE-GRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:cd03219 164 LLLLDEPAAGLNPEETEELAELIRELRErGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3820-4061 |
1.53e-41 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 158.07 E-value: 1.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3820 NFDNKGSSLQNREGELEGSAPGVT--LVSVTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSG 3897
Cdd:PRK13536 18 PIERKHQGISEAKASIPGSMSTVAidLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3898 TIIINGKNLQTDLSRVRMELGVCPQQDILLDNLTVREHLLLFAsiKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALS 3977
Cdd:PRK13536 97 KITVLGVPVPARARLARARIGVVPQFDNLDLEFTVRENLLVFG--RYFGMSTREIEAVIPSLLEFARLESKADARVSDLS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3978 GGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDIL--LKYReGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCC 4055
Cdd:PRK13536 175 GGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLrsLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAE 253
|
....*.
gi 1034654212 4056 GPPFCL 4061
Cdd:PRK13536 254 GRPHAL 259
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3838-4058 |
2.25e-41 |
|
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: 153.98 E-value: 2.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3838 SAPGVTLVSVTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT----DLSRV 3913
Cdd:COG1127 2 SEPMIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlsekELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3914 RMELGVCPQQDILLDNLTV--------REHLLLfasikapqwTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLs 3985
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVfenvafplREHTDL---------SEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRV- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3986 lGIAfmgmsRTVVL-------DEPTSGVDPCSRHSLWDILLKYRE--GRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCG 4056
Cdd:COG1127 151 -ALA-----RALALdpeillyDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEG 224
|
..
gi 1034654212 4057 PP 4058
Cdd:COG1127 225 TP 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3837-4064 |
4.71e-41 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 155.73 E-value: 4.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3837 GSAPGVTLVSVTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRME 3916
Cdd:PRK13537 3 MSVAPIDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3917 LGVCPQQDILLDNLTVREHLLLFAsiKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRT 3996
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVRENLLVFG--RYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3997 VVLDEPTSGVDPCSRHSLWDIL--LKYReGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPPFCLKEA 4064
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLrsLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3842-4047 |
1.21e-40 |
|
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: 151.09 E-value: 1.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYEGHKA---VVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKnlqtDLSRVRMELG 3918
Cdd:cd03293 1 LEVRNVSKTYGGGGGavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE----PVTGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3919 VCPQQDILLDNLTVREHLLLfaSIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVV 3998
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVAL--GLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034654212 3999 LDEPTSGVDPCSRHSLWDILLK--YREGRTIIFTTHHLDEAEALSDRVAVL 4047
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3840-4039 |
5.09e-40 |
|
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: 148.78 E-value: 5.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3840 PGVTLVSVTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRMELGV 3919
Cdd:COG4133 1 MMLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3920 CPQQDILLDNLTVREHLLLFASIKAPQWTkkelHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVL 3999
Cdd:COG4133 80 LGHADGLKPELTVRENLRFWAALYGLRAD----REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1034654212 4000 DEPTSGVDPCSRHSLWDILLKYRE-GRTIIFTTHHLDEAEA 4039
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLArGGAVLLTTHQPLELAA 196
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3847-4058 |
1.65e-39 |
|
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: 148.42 E-value: 1.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL----QTDLSRVRMELGVCPQ 3922
Cdd:cd03261 6 LTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRRRMGMLFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3923 QDILLDNLTV--------REHLLLfasikapqwTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMS 3994
Cdd:cd03261 85 SGALFDSLTVfenvafplREHTRL---------SEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654212 3995 RTVVLDEPTSGVDPCSRHSLWDILLKYRE--GRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTP 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3837-4047 |
2.92e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 148.70 E-value: 2.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3837 GSAPGVTLVSVTKEY---EGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKnlqtDLSRV 3913
Cdd:COG1116 3 AAAPALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK----PVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3914 RMELGVCPQQDILLDNLTVREHLLLfaSIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGM 3993
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVAL--GLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAND 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654212 3994 SRTVVLDEPTSGVDPCSRHSLWDILLKY--REGRTIIFTTHHLDEAEALSDRVAVL 4047
Cdd:COG1116 157 PEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3847-4051 |
3.60e-39 |
|
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: 146.84 E-value: 3.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEGH-KAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL-QTDLSRVRMELGVCPQQ- 3923
Cdd:cd03225 5 LSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLtKLSLKELRRKVGLVFQNp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3924 DILLDNLTVREHLLLfaSIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPT 4003
Cdd:cd03225 85 DDQFFGPTVEEEVAF--GLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1034654212 4004 SGVDPCSRHSLWDILLKY-REGRTIIFTTHHLDEAEALSDRVAVLQHGR 4051
Cdd:cd03225 163 AGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3847-4047 |
3.42e-38 |
|
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: 143.83 E-value: 3.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEGHKaVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVrmelGVCPQQ-DI 3925
Cdd:cd03235 5 LTVSYGGHP-VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRI----GYVPQRrSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3926 LLD-NLTVREHLL--LFASIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEP 4002
Cdd:cd03235 80 DRDfPISVRDVVLmgLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1034654212 4003 TSGVDPCSRHSLWDILLKYR-EGRTIIFTTHHLDEAEALSDRVAVL 4047
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRrEGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3842-4058 |
1.38e-37 |
|
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: 143.21 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKN-LQTDLSRVRMELGVC 3920
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDiREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3921 PQQDILLDNLTVREHLLLFASIKapQWTKKELHQQVNQTLQDVDL--TQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVV 3998
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLL--KWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034654212 3999 LDEPTSGVDPCSRHSLWDILLKYRE--GRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTP 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3842-4056 |
1.52e-37 |
|
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: 142.27 E-value: 1.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqTDLSRVRMELGVCP 3921
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3922 QQDILLDNLTVREHlLLFAsIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGiafmgmsRTVV--- 3998
Cdd:cd03259 79 QDYALFPHLTVAEN-IAFG-LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALA-------RALArep 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034654212 3999 ----LDEPTSGVDPCSRHSLWDILLKYRE--GRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCG 4056
Cdd:cd03259 150 slllLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3842-4053 |
5.91e-37 |
|
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: 140.58 E-value: 5.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYE---GHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRMELG 3918
Cdd:cd03266 2 ITADALTKRFRdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3919 VCPQQDILLDNLTVREHLLLFASIKAPQwtKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVV 3998
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLK--GDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654212 3999 LDEPTSGVDPCSRHSLWDILLKYRE-GRTIIFTTHHLDEAEALSDRVAVLQHGRLR 4053
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3836-4058 |
1.01e-36 |
|
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: 148.51 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3836 EGSAPGVTLVSVTKEYEGHKA----VVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT--- 3908
Cdd:COG1123 255 AAAEPLLEVRNLSKRYPVRGKggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlsr 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3909 -DLSRVRMELGVCPQ--QDILLDNLTVREHlLLFASIKAPQWTKKELHQQVNQTLQDVDL-TQHQHKQTRALSGGLKRKL 3984
Cdd:COG1123 335 rSLRELRRRVQMVFQdpYSSLNPRMTVGDI-IAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRV 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654212 3985 SLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYRE--GRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPT 489
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3843-4051 |
1.67e-36 |
|
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: 136.99 E-value: 1.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3843 TLVSVTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL-QTDLSRVRMELGVCP 3921
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIaKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3922 QqdilldnltvrehlllfasikapqwtkkelhqqvnqtlqdvdltqhqhkqtraLSGGLKRKLSLGIAFMGMSRTVVLDE 4001
Cdd:cd00267 80 Q-----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034654212 4002 PTSGVDPCSRHSLWDILLKY-REGRTIIFTTHHLDEAEALSDRVAVLQHGR 4051
Cdd:cd00267 107 PTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3857-4058 |
1.91e-35 |
|
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: 1.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3857 VVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqTDLS---RVRMELGVCPQQDILLDNLTVR 3933
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI-TGLPpheRARAGIGYVPEGRRIFPELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3934 EHLLLFASIKAPqwtkkelhQQVNQTLQDV-----DLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDP 4008
Cdd:cd03224 94 ENLLLGAYARRR--------AKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034654212 4009 CSRHSLWDILLKYR-EGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:cd03224 166 KIVEEIFEAIRELRdEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTA 216
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3842-4051 |
3.14e-34 |
|
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: 131.16 E-value: 3.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRV---RMELG 3918
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3919 VCPQQDILLDNLTVREHLLLfasikapqwtkkelhqqvnqtlqdvdltqhqhkqtrALSGGLKRKLSLGIAFMGMSRTVV 3998
Cdd:cd03229 80 MVFQDFALFPHLTVLENIAL------------------------------------GLSGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034654212 3999 LDEPTSGVDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGR 4051
Cdd:cd03229 124 LDEPTSALDPITRREVRALLksLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3842-4058 |
3.46e-34 |
|
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: 133.05 E-value: 3.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYEGHKaVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqTDL---SRVRMELG 3918
Cdd:cd03218 1 LRAENLSKRYGKRK-VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-TKLpmhKRARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3919 VCPQQDILLDNLTVREHLLLFASIKAPqwTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVV 3998
Cdd:cd03218 79 YLPQEASIFRKLTVEENILAVLEIRGL--SKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034654212 3999 LDEPTSGVDPCSRHSLWDILLKYRE-GRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDrGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3847-4051 |
4.56e-34 |
|
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: 130.58 E-value: 4.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEG-HKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT-DLSRVRMELGVCPQQD 3924
Cdd:cd03228 6 VSFSYPGrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAYVPQDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3925 ILLdNLTVREHLllfasikapqwtkkelhqqvnqtlqdvdltqhqhkqtraLSGGLKRKLSLGIAFMGMSRTVVLDEPTS 4004
Cdd:cd03228 86 FLF-SGTIRENI---------------------------------------LSGGQRQRIAIARALLRDPPILILDEATS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1034654212 4005 GVDPCSRHSLWDILLKYREGRTIIFTTHHLDEAEaLSDRVAVLQHGR 4051
Cdd:cd03228 126 ALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3838-4058 |
1.12e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 135.61 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3838 SAPGVTLVSVTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKnlqtDLSRVRME- 3916
Cdd:COG3842 2 AMPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR----DVTGLPPEk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3917 --LGVCPQQDILLDNLTVREHLllfA-SIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLgiAfmgm 3993
Cdd:COG3842 77 rnVGMVFQDYALFPHLTVAENV---AfGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVAL--A---- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034654212 3994 sRTVV-------LDEPTSGVDPCSRHSLWDILLKY--REGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:COG3842 148 -RALApeprvllLDEPLSALDAKLREEMREELRRLqrELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTP 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
3858-4004 |
1.20e-33 |
|
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: 128.53 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3858 VQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQ-TDLSRVRMELGVCPQQDILLDNLTVREHL 3936
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTdDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034654212 3937 LLFASIKApqWTKKELHQQVNQTLQDVDLT----QHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTS 4004
Cdd:pfam00005 81 RLGLLLKG--LSKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3842-4052 |
1.24e-33 |
|
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: 131.07 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYEG---HKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQ----TDLSRVR 3914
Cdd:cd03255 1 IELKNLSKTYGGggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISklseKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3915 ME-LGVCPQQDILLDNLTVREHLLL---FASIKapqwtKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAF 3990
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALENVELpllLAGVP-----KKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034654212 3991 MGMSRTVVLDEPTSGVDPCSRHSLWDILLKYRE--GRTIIFTTHHLDEAEaLSDRVAVLQHGRL 4052
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3849-4056 |
1.26e-33 |
|
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: 131.24 E-value: 1.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3849 KEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGL---HPPTSGTIIINGKNLQTDLsrVRMELGVCPQQDI 3925
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRKPDQ--FQKCVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3926 LLDNLTVREHLLLFASIKAPQWTKKELHQQVNQT--LQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPT 4003
Cdd:cd03234 92 LLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDvlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034654212 4004 SGVDPCSRHSLWDILLKY-REGRTIIFTTHH-LDEAEALSDRVAVLQHGRLRCCG 4056
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLaRRNRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3853-4056 |
2.56e-33 |
|
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: 128.71 E-value: 2.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3853 GHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQtdlsrvrmelgvcpqqdilldnltv 3932
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA------------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3933 rehlllfasikapQWTKKELHQQ---VNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPC 4009
Cdd:cd03214 65 -------------SLSPKELARKiayVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1034654212 4010 SRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCG 4056
Cdd:cd03214 132 HQIELLELLrrLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3838-4067 |
2.82e-33 |
|
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: 139.13 E-value: 2.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3838 SAPGVTLVSVTKEYEGH-KAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT-DLSRVRM 3915
Cdd:COG4987 330 GGPSLELEDVSFRYPGAgRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3916 ELGVCPQQDILLDNlTVREHLLLFAsikaPQWTKKELHQqvnqTLQDVDLTQHQHKQT-----------RALSGGLKRKL 3984
Cdd:COG4987 410 RIAVVPQRPHLFDT-TLRENLRLAR----PDATDEELWA----ALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3985 SLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDEAEALsDRVAVLQHGRLRCCGPPFCLKEA 4064
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLAQ 559
|
...
gi 1034654212 4065 YGQ 4067
Cdd:COG4987 560 NGR 562
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3842-4052 |
7.44e-33 |
|
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: 129.24 E-value: 7.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYEGHK---AVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT----DLSRVR 3914
Cdd:cd03258 2 IELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3915 MELGVCPQQDILLDNLTVREHLLLfaSIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKlsLGIA-FMGM 3993
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVAL--PLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQR--VGIArALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034654212 3994 SRTVVL-DEPTSGVDPCSRHSLWDILLKYRE--GRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:cd03258 158 NPKVLLcDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3837-4058 |
7.55e-33 |
|
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: 137.58 E-value: 7.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3837 GSAPGVTLVSVTKEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT-DLSRVRM 3915
Cdd:COG4988 332 AGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3916 ELGVCPQQDILLdNLTVREHLLLFasikAPQWTKKELHQQVNQT-LQDVDLTQHQHKQT------RALSGGLKRKLSLGI 3988
Cdd:COG4988 412 QIAWVPQNPYLF-AGTIRENLRLG----RPDASDEELEAALEAAgLDEFVAALPDGLDTplgeggRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3989 AFMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDEAeALSDRVAVLQHGRLRCCGPP 4058
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALL-AQADRILVLDDGRIVEQGTH 555
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3853-4058 |
1.90e-32 |
|
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: 128.18 E-value: 1.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3853 GHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqTDLS---RVRMELGVCPQQDILLDN 3929
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI-TGLPphrIARLGIGYVPEGRRIFPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3930 LTVREHLLLFASIKAPQwtkkelhQQVNQTLQDV-----DLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTS 4004
Cdd:COG0410 93 LTVEENLLLGAYARRDR-------AEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654212 4005 GVDPCSRHSLWDIL--LKyREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:COG0410 166 GLAPLIVEEIFEIIrrLN-REGVTILLVEQNARFALEIADRAYVLERGRIVLEGTA 220
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3844-4058 |
7.53e-32 |
|
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: 126.14 E-value: 7.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3844 LVSVTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHP-----PTSGTIIINGKN---LQTDLSRVRM 3915
Cdd:cd03260 3 LRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDiydLDVDVLELRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3916 ELGVCPQQDILLDnLTVREHLLLfasikAPQ----WTKKELHQQVNQTLQDVDLTQ--HQHKQTRALSGGLKRKLSLGIA 3989
Cdd:cd03260 82 RVGMVFQKPNPFP-GSIYDNVAY-----GLRlhgiKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034654212 3990 FMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3842-4052 |
3.91e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 124.01 E-value: 3.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT----DLSRVRMEL 3917
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3918 GVCPqQDI-LLDNLTVREHLLLfaSIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKlsLGIAfmgmsRT 3996
Cdd:COG2884 82 GVVF-QDFrLLPDRTVYENVAL--PLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQR--VAIA-----RA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034654212 3997 VV-------LDEPTSGVDPCSRHSLWDILLKY-REGRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:COG2884 152 LVnrpelllADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3847-4064 |
1.94e-30 |
|
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: 122.68 E-value: 1.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT----DLSRVRMELGVCPQ 3922
Cdd:cd03256 6 LSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgkALRQLRRQIGMIFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3923 QDILLDNLTVREHLL--------LFASIkaPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMS 3994
Cdd:cd03256 86 QFNLIERLSVLENVLsgrlgrrsTWRSL--FGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034654212 3995 RTVVLDEPTSGVDPCSRHSLWDILLKY--REGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPPFCLKEA 4064
Cdd:cd03256 164 KLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3842-4052 |
1.97e-30 |
|
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: 119.84 E-value: 1.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYEGHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRMELGVcp 3921
Cdd:cd03216 1 LELRGITKRFGGVKAL-DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3922 qqdilldnLTVrehlllfasikapqwtkkelHQqvnqtlqdvdltqhqhkqtraLSGGLKRKLSLGIAFMGMSRTVVLDE 4001
Cdd:cd03216 78 --------AMV--------------------YQ---------------------LSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034654212 4002 PTSGVDPCSRHSLWDIL--LKyREGRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:cd03216 109 PTAALTPAEVERLFKVIrrLR-AQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3837-4052 |
2.07e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 128.99 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3837 GSAPGVTLVSVTKEYEGHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRME 3916
Cdd:COG3845 1 MMPPALELRGITKRFGGVVAN-DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3917 LGV--CPQQDILLDNLTVREHLLL-FASIKAPQWTKKELHQQVNQTLQ----DVDLTQHQHKqtraLSGGLKRK------ 3983
Cdd:COG3845 80 LGIgmVHQHFMLVPNLTVAENIVLgLEPTKGGRLDRKAARARIRELSEryglDVDPDAKVED----LSVGEQQRveilka 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3984 LSLGiafmgmSRTVVLDEPTSGVDPCSRHSLWDILLKYR-EGRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:COG3845 156 LYRG------ARILILDEPTAVLTPQEADELFEILRRLAaEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
3847-4058 |
3.55e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 121.67 E-value: 3.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqTDLS---RVRMELGVCPQQ 3923
Cdd:COG1137 9 LVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THLPmhkRARLGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3924 DILLDNLTVREHLLLFASIKAPqwTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPT 4003
Cdd:COG1137 87 ASIFRKLTVEDNILAVLELRKL--SKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654212 4004 SGVDPCSRHSLWDILLKYRE-GRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:COG1137 165 AGVDPIAVADIQKIIRHLKErGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTP 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3845-4052 |
6.97e-30 |
|
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: 120.69 E-value: 6.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3845 VSVT-KEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqTDLSRVRM-----ELG 3918
Cdd:cd03257 7 LSVSfPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDL-LKLSRRLRkirrkEIQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3919 VCPQQDIL-LD-NLTVREHL---LLFASIKAPQWTKKElhqQVNQTLQDVDL-TQHQHKQTRALSGGLKRKLSLGIAFMG 3992
Cdd:cd03257 86 MVFQDPMSsLNpRMTIGEQIaepLRIHGKLSKKEARKE---AVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034654212 3993 MSRTVVLDEPTSGVDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:cd03257 163 NPKLLIADEPTSALDVSVQAQILDLLkkLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
3853-4058 |
8.09e-30 |
|
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: 121.60 E-value: 8.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3853 GHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT----DLSRVRME-LGVCPQQDILL 3927
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmsrkELRELRRKkISMVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3928 DNLTVREHLLLFASIKAPqwTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVD 4007
Cdd:cd03294 115 PHRTVLENVAFGLEVQGV--PRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034654212 4008 PCSRHSLWDILLKY--REGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:cd03294 193 PLIRREMQDELLRLqaELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTP 245
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3853-4077 |
1.23e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 120.99 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3853 GHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT----DLSRVRmelGVCPQQDILLD 3928
Cdd:COG4559 12 GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwspwELARRR---AVLPQHSSLAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3929 NLTVREHLLLFASikAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGG------LKRKLS-LGIAFMGMSRTVVLDE 4001
Cdd:COG4559 89 PFTVEEVVALGRA--PHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGeqqrvqLARVLAqLWEPVDGGPRWLFLDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 4002 PTSGVDPCSRHSLWDILLKY-REGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPPF------CLKEAYgqGLRLTLT 4074
Cdd:COG4559 167 PTSALDLAHQHAVLRLARQLaRRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEevltdeLLERVY--GADLRVL 244
|
...
gi 1034654212 4075 RQP 4077
Cdd:COG4559 245 AHP 247
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3842-4058 |
3.11e-29 |
|
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: 118.88 E-value: 3.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqTDLSRVRMELGVCP 3921
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3922 QQDILLDNLTVREHLLLFASIKapQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDE 4001
Cdd:cd03300 79 QNYALFPHLTVFENIAFGLRLK--KLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034654212 4002 PTSGVDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:cd03300 157 PLGALDLKLRKDMQLELkrLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTP 215
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3842-4053 |
3.27e-29 |
|
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: 118.13 E-value: 3.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYEGHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqTDLSRVRMELGVCP 3921
Cdd:cd03301 1 VELENVTKRFGNVTAL-DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3922 QQDILLDNLTVREHLLLfaSIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDE 4001
Cdd:cd03301 79 QNYALYPHMTVYDNIAF--GLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1034654212 4002 PTSGVDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLR 4053
Cdd:cd03301 157 PLSNLDAKLRVQMRAELkrLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3838-4057 |
5.68e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 124.75 E-value: 5.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3838 SAPGVTLVSVTKEYEGHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRMEL 3917
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKAL-DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3918 GV-CPQQDI-LLDNLTVREHLLLFASIKAPQWT-KKELHQQVNQTLQDVDLTQHQHKQTRALSGGLK------RKLSLGi 3988
Cdd:COG1129 80 GIaIIHQELnLVPNLSVAENIFLGREPRRGGLIdWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQqlveiaRALSRD- 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034654212 3989 afmgmSRTVVLDEPTSGVDPCSRHSLWDIL--LKyREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGP 4057
Cdd:COG1129 159 -----ARVLILDEPTASLTEREVERLFRIIrrLK-AQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGP 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3853-4058 |
5.70e-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: 125.02 E-value: 5.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3853 GHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPT---SGTIIINGKNLQTDLSRVR-MELGVCPQQ-DILL 3927
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgRRIGMVFQDpMTQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3928 DNLTVREHLLLfaSIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVD 4007
Cdd:COG1123 97 NPVTVGDQIAE--ALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034654212 4008 PCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:COG1123 175 VTTQAEILDLLreLQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPP 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3842-4057 |
7.72e-29 |
|
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: 118.26 E-value: 7.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYEGhKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSG-TIIINGKNL-QTDLSRVRMELG- 3918
Cdd:COG1119 4 LELRNVTVRRGG-KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRgGEDVWELRKRIGl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3919 VCPQ-QDILLDNLTVREHLL--LFASIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSR 3995
Cdd:COG1119 83 VSPAlQLRFPRDETVLDVVLsgFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034654212 3996 TVVLDEPTSGVDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGP 4057
Cdd:COG1119 163 LLILDEPTAGLDLGARELLLALLdkLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGP 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3838-4052 |
2.31e-28 |
|
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: 114.96 E-value: 2.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3838 SAPGVTLVSVTKEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPP--TSGTIIINGKNLqtDLSRVRM 3915
Cdd:cd03213 5 SFRNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPL--DKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3916 ELGVCPQQDILLDNLTVREHLLLFASIkapqwtkkelhqqvnqtlqdvdltqhqhkqtRALSGGLKRKLSLGIAFMGMSR 3995
Cdd:cd03213 83 IIGYVPQDDILHPTLTVRETLMFAAKL-------------------------------RGLSGGERKRVSIALELVSNPS 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034654212 3996 TVVLDEPTSGVDPCSRHSLWDILLKYR-EGRTIIFTTHHL-DEAEALSDRVAVLQHGRL 4052
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLRRLAdTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3857-4052 |
4.53e-28 |
|
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: 115.51 E-value: 4.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3857 VVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqTDLSRVRMELGVCPQQDILLDNLTVREHL 3936
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQNYALFPHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3937 LLfaSIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWD 4016
Cdd:cd03299 93 AY--GLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLRE 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 1034654212 4017 ILLKYRE--GRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:cd03299 171 ELKKIRKefGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
3849-4058 |
5.40e-28 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 115.45 E-value: 5.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3849 KEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqTDL---SRVRMELGVCPQQDI 3925
Cdd:TIGR04406 9 KSY-KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDI-THLpmhERARLGIGYLPQEAS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3926 LLDNLTVREHLLLFASIKaPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSG 4005
Cdd:TIGR04406 87 IFRKLTVEENIMAVLEIR-KDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1034654212 4006 VDPCSRHSLWDILLKYRE-GRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:TIGR04406 166 VDPIAVGDIKKIIKHLKErGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTP 219
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3847-4050 |
5.74e-28 |
|
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: 114.28 E-value: 5.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDlSRVRMeLGVCPQ--QD 3924
Cdd:cd03226 5 ISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK-ERRKS-IGYVMQdvDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3925 ILLDNlTVREHLLLfasikapqwTKKELH---QQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDE 4001
Cdd:cd03226 83 QLFTD-SVREELLL---------GLKELDagnEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1034654212 4002 PTSGVDPCSRHSLWDILLK-YREGRTIIFTTHHLDEAEALSDRVAVLQHG 4050
Cdd:cd03226 153 PTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3842-4052 |
8.94e-28 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 117.87 E-value: 8.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYEGHKA---VVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT----DLSRVR 3914
Cdd:COG1135 2 IELENLSKTFPTKGGpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlserELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3915 MELGVCPQQDILLDNLTVREhlllfaSIKAP----QWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKlsLGIAf 3990
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAE------NVALPleiaGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQR--VGIA- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034654212 3991 mgmsR------TVVL-DEPTSGVDPCSRHSLWDILLKYRE--GRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:COG1135 153 ----RalannpKVLLcDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3853-4058 |
1.07e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 115.25 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3853 GHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQ----TDLSRVRmelGVCPQQDILLD 3928
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwspAELARRR---AVLPQHSSLSF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3929 NLTVREHLLLFASIkapqWT--KKELHQQVNQTLQDVDLTQHQHKQTRALSGG------LKRKLSLGIAFMGMSRTVVLD 4000
Cdd:PRK13548 90 PFTVEEVVAMGRAP----HGlsRAEDDALVAAALAQVDLAHLAGRDYPQLSGGeqqrvqLARVLAQLWEPDGPPRWLLLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 4001 EPTSGVDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:PRK13548 166 EPTSALDLAHQHHVLRLArqLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
3829-4052 |
1.42e-27 |
|
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: 114.35 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3829 QNREGELEGSAPGVtlvsVTKEYEgHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIING----K 3904
Cdd:cd03267 13 YSKEPGLIGSLKSL----FKRKYR-EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3905 NLQTDLSRVRMELGvcpQQDILLDNLTVREHLLLFASIKapQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKL 3984
Cdd:cd03267 88 RRKKFLRRIGVVFG---QKTQLWWDLPVIDSFYLLAAIY--DLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3985 SLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYREGR--TIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:cd03267 163 EIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3833-4052 |
4.87e-27 |
|
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: 121.09 E-value: 4.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3833 GELEGSapgVTLVSVTKEYEGH-KAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT-DL 3910
Cdd:COG2274 468 PRLKGD---IELENVSFRYPGDsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDP 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3911 SRVRMELGVCPQQDILLdNLTVREHLLLFASiKAPQwtkkelhQQVNQTLQDVDLT----QHQHK-QT------RALSGG 3979
Cdd:COG2274 545 ASLRRQIGVVLQDVFLF-SGTIRENITLGDP-DATD-------EEIIEAARLAGLHdfieALPMGyDTvvgeggSNLSGG 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034654212 3980 LKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLdEAEALSDRVAVLQHGRL 4052
Cdd:COG2274 616 QRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRL-STIRLADRIIVLDKGRI 687
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3845-4052 |
1.02e-26 |
|
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: 112.20 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3845 VSVT-KEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSR-----VRMelg 3918
Cdd:COG1124 7 LSVSyGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKafrrrVQM--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3919 VcpQQDIL--LD-NLTVREHLLLFASIKapqwTKKELHQQVNQTLQDVDLTQ-------HQhkqtraLSGGLKRKLSLGI 3988
Cdd:COG1124 84 V--FQDPYasLHpRHTVDRILAEPLRIH----GLPDREERIAELLEQVGLPPsfldrypHQ------LSGGQRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654212 3989 AFMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYRE--GRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
3869-4053 |
1.91e-26 |
|
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: 110.08 E-value: 1.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3869 QITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGK-----NLQTDLSRVRMELGVCPQQDILLDNLTVREHLLLFASIK 3943
Cdd:cd03297 24 EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGLKRK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3944 APqwtkKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRhslwDILLKYRE 4023
Cdd:cd03297 104 RN----REDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR----LQLLPELK 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 1034654212 4024 GR------TIIFTTHHLDEAEALSDRVAVLQHGRLR 4053
Cdd:cd03297 176 QIkknlniPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3842-4053 |
3.82e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 116.32 E-value: 3.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYEGHKaVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIInGKNLQtdlsrvrmeLGVCP 3921
Cdd:COG0488 316 LELEGLSKSYGDKT-LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK---------IGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3922 Q-QDILLDNLTVREHLLLFasikAPQWTKKELHqqvnQTLQDVDLT-QHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVL 3999
Cdd:COG0488 385 QhQEELDPDKTVLDELRDG----APGGTEQEVR----GYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLL 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654212 4000 DEPTSGVDPCSRHSLWDILLKYrEGrTIIFTTHhlDEA--EALSDRVAVLQHGRLR 4053
Cdd:COG0488 457 DEPTNHLDIETLEALEEALDDF-PG-TVLLVSH--DRYflDRVATRILEFEDGGVR 508
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
3858-4050 |
6.75e-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: 109.09 E-value: 6.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3858 VQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqTDLSRVRMelgVCPQQDILLDNLTVREHLL 3937
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI-TEPGPDRM---VVFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3938 LFASIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDI 4017
Cdd:TIGR01184 77 LAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 1034654212 4018 LLKYRE--GRTIIFTTHHLDEAEALSDRVAVLQHG 4050
Cdd:TIGR01184 157 LMQIWEehRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3842-4052 |
2.85e-25 |
|
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: 106.85 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL---QTDLSRVRMELG 3918
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3919 VCPQQDILLDNLTVREHLLLfASIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVV 3998
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITL-APIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034654212 3999 LDEPTSGVDPCSRHSLWDILLKY-REGRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3821-4047 |
3.50e-25 |
|
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: 113.54 E-value: 3.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3821 FDNKGSSLQNREGELEGSAPGVTLVSVTKEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTII 3900
Cdd:TIGR02857 301 LDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIA 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3901 INGKNLQT-DLSRVRMELGVCPQQDILLDNlTVREHLLLfasiKAPQWTKKELHQQVNQT-LQDVDLTQHQHKQTRA--- 3975
Cdd:TIGR02857 381 VNGVPLADaDADSWRDQIAWVPQHPFLFAG-TIAENIRL----ARPDASDAEIREALERAgLDEFVAALPQGLDTPIgeg 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034654212 3976 ---LSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDEAEALsDRVAVL 4047
Cdd:TIGR02857 456 gagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALA-DRIVVL 529
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3847-4052 |
5.45e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 109.02 E-value: 5.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEGHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRMELG-VCPQQDI 3925
Cdd:COG4586 28 FRREYREVEAV-DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGvVFGQRSQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3926 LLDNLTVREHLLLFASI-KAPqwtKKELHQQVNQtLQDV-DLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPT 4003
Cdd:COG4586 107 LWWDLPAIDSFRLLKAIyRIP---DAEYKKRLDE-LVELlDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034654212 4004 SGVDPCSRHSLWDILLKY--REGRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:COG4586 183 IGLDVVSKEAIREFLKEYnrERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3855-4052 |
5.67e-25 |
|
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: 104.82 E-value: 5.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3855 KAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRMELGVC-----PQQDILLDN 3929
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAyvpedRKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3930 LTVREHLLLfasikapqwtkkelhqqvnqtlqdvdltqhqhkqTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPC 4009
Cdd:cd03215 93 LSVAENIAL----------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1034654212 4010 SRHSLWDILLKYR-EGRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:cd03215 139 AKAEIYRLIRELAdAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3847-4052 |
8.25e-25 |
|
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: 105.57 E-value: 8.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqTDLSR-----VRMELGVCP 3921
Cdd:cd03292 6 VTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDV-SDLRGraipyLRRKIGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3922 QQDILLDNLTVREHLLLfaSIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDE 4001
Cdd:cd03292 85 QDFRLLPDRNVYENVAF--ALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1034654212 4002 PTSGVDPCSRHSLWDILLKYRE-GRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKINKaGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3858-4066 |
1.58e-24 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 113.68 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3858 VQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTI-----IINGKNLQTdlsrvRMELGVCPQQDILLDNLTV 3932
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDIAT-----RRRVGYMSQAFSLYGELTV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3933 REHLLLFAsiKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRH 4012
Cdd:NF033858 357 RQNLELHA--RLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARD 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034654212 4013 SLWDIL--LKYREGRTIIFTTHHLDEAEaLSDRVAvLQH-GRLRCCGPPFCLKEAYG 4066
Cdd:NF033858 435 MFWRLLieLSREDGVTIFISTHFMNEAE-RCDRIS-LMHaGRVLASDTPAALVAARG 489
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3841-4058 |
1.80e-24 |
|
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: 105.11 E-value: 1.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3841 GVTLVSVTKEYEGHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqTDLSRVRMELGVC 3920
Cdd:cd03296 2 SIEVRNVSKRFGDFVAL-DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3921 PQQDILLDNLTVREHLLLFASIK--APQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVV 3998
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034654212 3999 LDEPTSGVDPCSRHSL--WDILLKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:cd03296 160 LDEPFGALDAKVRKELrrWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTP 221
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
3845-4052 |
2.11e-24 |
|
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: 104.11 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3845 VSVTKEYEGHKAVvqDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqTDLSRVRMELGVCPQQD 3924
Cdd:cd03298 3 LDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRPVSMLFQEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3925 ILLDNLTVREHLLLFASikaPQWTKKELHQQ-VNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPT 4003
Cdd:cd03298 80 NLFAHLTVEQNVGLGLS---PGLKLTAEDRQaIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034654212 4004 SGVDPCSRHSLWDILLKYREGR--TIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:cd03298 157 AALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
3846-4071 |
3.07e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 104.59 E-value: 3.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3846 SVTKEYEGHKaVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINgknlQTDLS------RVRMELGV 3919
Cdd:PRK10895 8 NLAKAYKGRR-VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIID----DEDISllplhaRARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3920 CPQQDILLDNLTVREHLLLFASIKApQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVL 3999
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQIRD-DLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 4000 DEPTSGVDPCSRHSLWDILLKYRE-GRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPPFCL------KEAY-GQGLRL 4071
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRDsGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIlqdehvKRVYlGEDFRL 241
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3853-4058 |
4.91e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 104.33 E-value: 4.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3853 GHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT----DLSRvrmELGVCPQQDILLD 3928
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlssrQLAR---RLALLPQHHLTPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3929 NLTVREhllLFASIKAPQ---WTK--KELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKlslgiAFMGM-----SRTVV 3998
Cdd:PRK11231 90 GITVRE---LVAYGRSPWlslWGRlsAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQR-----AFLAMvlaqdTPVVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034654212 3999 LDEPTSGVDPCSRHSLWDILLKYR-EGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNtQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTP 222
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3840-4058 |
5.95e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 107.23 E-value: 5.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3840 PGVTLVSVTKEYEGHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKnlqtDLSRV---RME 3916
Cdd:PRK11607 18 PLLEIRNLTKSFDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV----DLSHVppyQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3917 LGVCPQQDILLDNLTVREHLLLfaSIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRT 3996
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAF--GLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654212 3997 VVLDEPTSGVDPCSR----HSLWDILlkYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:PRK11607 171 LLLDEPMGALDKKLRdrmqLEVVDIL--ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEP 234
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3847-4057 |
9.15e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 103.66 E-value: 9.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEGHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqTDLS---RVRMelGVCP-- 3921
Cdd:COG4674 16 LTVSFDGFKAL-NDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDL-TGLDeheIARL--GIGRkf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3922 QQDILLDNLTVREHLLL--------FASIKApqWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGM 3993
Cdd:COG4674 92 QKPTVFEELTVFENLELalkgdrgvFASLFA--RLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034654212 3994 SRTVVLDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGP 4057
Cdd:COG4674 170 PKLLLLDEPVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3842-4052 |
1.68e-23 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 105.27 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYEGHKAVV---QDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL----QTDLSRVR 3914
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3915 MELGVCPQQDILLDNLTVREHLLLfaSIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKlsLGIAFMGMS 3994
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVAL--PLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQR--VAIARALAS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034654212 3995 RTVVL--DEPTSGVDPCSRHSLWDiLLK--YRE-GRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:PRK11153 158 NPKVLlcDEATSALDPATTRSILE-LLKdiNRElGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3834-4052 |
3.40e-23 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 107.94 E-value: 3.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3834 ELEGSAPGVTLVSVTKEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT-DLSR 3912
Cdd:COG1132 332 PLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLES 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3913 VRMELGVCPQQDILLdNLTVREHlLLFASIKAPQwtkkelhQQVNQTLQDVDLTQHQHK-----QTR------ALSGGLK 3981
Cdd:COG1132 412 LRRQIGVVPQDTFLF-SGTIREN-IRYGRPDATD-------EEVEEAAKAAQAHEFIEAlpdgyDTVvgergvNLSGGQR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034654212 3982 RKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDEAEAlSDRVAVLQHGRL 4052
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRN-ADRILVLDDGRI 552
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3840-4056 |
5.62e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 106.41 E-value: 5.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3840 PGVTLVSVTKEYEGHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRMELG- 3918
Cdd:PRK09700 4 PYISMAGIGKSFGPVHAL-KSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3919 -VCPQQDILLDNLTVREHLLL-------FASIKAPQWtkKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAF 3990
Cdd:PRK09700 83 gIIYQELSVIDELTVLENLYIgrhltkkVCGVNIIDW--REMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034654212 3991 MGMSRTVVLDEPTSGVDPCSRHSLWDILLKYR-EGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCG 4056
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRkEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
3853-4056 |
6.02e-23 |
|
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: 100.30 E-value: 6.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3853 GHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGknlqtdlsRVR--MELGVCpqqdiLLDNL 3930
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--------RVSslLGLGGG-----FNPEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3931 TVREHLLLFASIKApqWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCS 4010
Cdd:cd03220 100 TGRENIYLNGRLLG--LSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1034654212 4011 RHSLWDILLKYRE-GRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCG 4056
Cdd:cd03220 178 QEKCQRRLRELLKqGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3858-4087 |
6.48e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 102.23 E-value: 6.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3858 VQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqtDLSR-----VRMELGVCPQQ-DILLDNLT 3931
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI--DYSRkglmkLRESVGMVFQDpDNQLFSAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3932 VREHLLLFA-SIKAPqwtKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCS 4010
Cdd:PRK13636 100 VYQDVSFGAvNLKLP---EDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 4011 RHSLWDILLKYRE--GRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP---FCLKEAYgQGLRLTLTRQPSVLEAHDL 4085
Cdd:PRK13636 177 VSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPkevFAEKEML-RKVNLRLPRIGHLMEILKE 255
|
..
gi 1034654212 4086 KD 4087
Cdd:PRK13636 256 KD 257
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
3845-4047 |
9.29e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 101.09 E-value: 9.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3845 VSVTkeYEGHKA---VVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSrvrmELGVCP 3921
Cdd:COG4525 9 VSVR--YPGGGQpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA----DRGVVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3922 QQDILLDNLTVREHL---LLFASIKapqwtKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVV 3998
Cdd:COG4525 83 QKDALLPWLNVLDNVafgLRLRGVP-----KAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034654212 3999 LDEPTSGVDPCSRHSLWDILLKY--REGRTIIFTTHHLDEAEALSDRVAVL 4047
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVwqRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3847-4052 |
1.28e-22 |
|
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: 99.61 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL-QTDLSRVRMELGVCPQQDI 3925
Cdd:cd03254 8 VNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIrDISRKSLRSMIGVVLQDTF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3926 LLdNLTVREHLLLFASIkapqwTKKELHQQVNQTLQDVDLTQHQHK--QTRA------LSGGLKRKLSLGIAFMGMSRTV 3997
Cdd:cd03254 88 LF-SGTIMENIRLGRPN-----ATDEEVIEAAKEAGAHDFIMKLPNgyDTVLgenggnLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034654212 3998 VLDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDEAEAlSDRVAVLQHGRL 4052
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKN-ADKILVLDDGKI 215
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3831-4034 |
1.33e-22 |
|
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: 105.52 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3831 REGELEGSAPGVTLVSVTKEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT-D 3909
Cdd:TIGR02868 324 AAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3910 LSRVRMELGVCPQQDILLDNlTVREHLLLfasiKAPQWTKKE---------LHQQVNQTLQDVDLTQHQHkqTRALSGGL 3980
Cdd:TIGR02868 404 QDEVRRRVSVCAQDAHLFDT-TVRENLRL----ARPDATDEElwaalervgLADWLRALPDGLDTVLGEG--GARLSGGE 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1034654212 3981 KRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHL 4034
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3857-4083 |
2.57e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 100.08 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3857 VVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL---QTDLSRVRMELGVC---PQQDILLDNL 3930
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdysKRGLLALRQQVATVfqdPEQQIFYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3931 tvrEHLLLFaSIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCS 4010
Cdd:PRK13638 96 ---DSDIAF-SLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034654212 4011 RHSLWDILLK-YREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP---FCLKEAYGQ-GLrltltRQPSVLEAH 4083
Cdd:PRK13638 172 RTQMIAIIRRiVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPgevFACTEAMEQaGL-----TQPWLVKLH 244
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3852-4052 |
7.36e-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: 95.84 E-value: 7.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3852 EGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRMELGVCPQQDILLDNlT 3931
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFDT-T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3932 VREHLllfasikapqwtkkelhqqvnqtlqdvdltqhqhkqTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSR 4011
Cdd:cd03247 91 LRNNL------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1034654212 4012 HSLWDILLKYREGRTIIFTTHHLDEAEALsDRVAVLQHGRL 4052
Cdd:cd03247 135 RQLLSLIFEVLKDKTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3842-4052 |
7.65e-22 |
|
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: 96.89 E-value: 7.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYEGHK-AVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL-QTDLSRVRMELGV 3919
Cdd:cd03245 3 IEFRNVSFSYPNQEiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIrQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3920 CPqQDILLDNLTVREHLLLFasikAPQWTKKELHQQVNQTLQDVDLTQHQH-------KQTRALSGGLKRKLSLGIAFMG 3992
Cdd:cd03245 83 VP-QDVTLFYGTLRDNITLG----APLADDERILRAAELAGVTDFVNKHPNgldlqigERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3993 MSRTVVLDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLdEAEALSDRVAVLQHGRL 4052
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP-SLLDLVDRIIVMDSGRI 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3847-4052 |
3.96e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 100.76 E-value: 3.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEGHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRMELGVC--PQQD 3924
Cdd:PRK11288 10 IGKTFPGVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAiiYQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3925 ILLDNLTVREHLLL------FASIKapqwtKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVV 3998
Cdd:PRK11288 89 HLVPEMTVAENLYLgqlphkGGIVN-----RRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034654212 3999 LDEPTSGVDpcSRHS--LWDILLKYR-EGRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:PRK11288 164 FDEPTSSLS--AREIeqLFRVIRELRaEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3869-4116 |
4.03e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 96.69 E-value: 4.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3869 QITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTD---LSRVRMELGVCPQQ-DILLDNLTVREHlLLFASIKA 3944
Cdd:PRK13639 29 EMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDkksLLEVRKTVGIVFQNpDDQLFAPTVEED-VAFGPLNL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3945 pQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSL-GIAFMGmSRTVVLDEPTSGVDPCSRHSLWDILLKY-R 4022
Cdd:PRK13639 108 -GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIaGILAMK-PEIIVLDEPTSGLDPMGASQIMKLLYDLnK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 4023 EGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPPfclKEAYgqglrltltRQPSVLEAHDLKdMACVTSLIKIYIPqa 4102
Cdd:PRK13639 186 EGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTP---KEVF---------SDIETIRKANLR-LPRVAHLIEILNK-- 250
|
250
....*....|....
gi 1034654212 4103 flKDSSGSELTYTI 4116
Cdd:PRK13639 251 --EDNLPIKMGYTI 262
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3858-4059 |
4.63e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 96.62 E-value: 4.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3858 VQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDL------SRVRMELGVC---PQQDILLD 3928
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLkkikevKRLRKEIGLVfqfPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3929 NLtvrEHLLLFASIKAPQwTKKELHQQVNQTLQDVDLTQHQHKQTR-ALSGGLKRKLSL-GIAFMGmSRTVVLDEPTSGV 4006
Cdd:PRK13645 107 TI---EKDIAFGPVNLGE-NKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALaGIIAMD-GNTLVLDEPTGGL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034654212 4007 DPCSRHSLWDILLKYRE--GRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPPF 4059
Cdd:PRK13645 182 DPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPF 236
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3851-4052 |
4.78e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 95.61 E-value: 4.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3851 YEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTI---ISMLTGLHP--PTSGTIIINGKNL---QTDLSRVRMELGVCPQ 3922
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLlrsINRMNDLNPevTITGSIVYNGHNIyspRTDTVDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3923 QDilldN---LTVREHLLLFASIKAPQwTKKELHQQVNQTLQDV----DLTQHQHKQTRALSGGLKRKLSLGIAFMGMSR 3995
Cdd:PRK14239 94 QP----NpfpMSIYENVVYGLRLKGIK-DKQVLDEAVEKSLKGAsiwdEVKDRLHDSALGLSGGQQQRVCIARVLATSPK 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034654212 3996 TVVLDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:PRK14239 169 IILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
3855-4058 |
5.29e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 96.66 E-value: 5.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3855 KAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqTD----LSRVRMELGVCPQQDilldnl 3930
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI-TDkkvkLSDIRKKVGLVFQYP------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3931 tvrEHLLLFASIK-----APQ---WTKKELHQQVNQTLQDVDLTQHQHKQTRA--LSGGLKRKLSL-GIAFMgMSRTVVL 3999
Cdd:PRK13637 93 ---EYQLFEETIEkdiafGPInlgLSEEEIENRVKRAMNIVGLDYEDYKDKSPfeLSGGQKRRVAIaGVVAM-EPKILIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034654212 4000 DEPTSGVDPCSRHslwDILLKYRE-----GRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:PRK13637 169 DEPTAGLDPKGRD---EILNKIKElhkeyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3840-4052 |
5.73e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 94.95 E-value: 5.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3840 PGVTLVSVTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL-QTDLSRV-RMEL 3917
Cdd:PRK11614 4 VMLSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItDWQTAKImREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3918 GVCPQQDILLDNLTVREHLLL---FASikapqwtkKELHQQVNQTLQDV--DLTQHQHKQTRALSGGLKRKLSLGIAFMG 3992
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMggfFAE--------RDQFQERIKWVYELfpRLHERRIQRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034654212 3993 MSRTVVLDEPTSGVDPCSRHSLWDILLKYR-EGRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLReQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3852-4058 |
5.96e-21 |
|
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: 94.48 E-value: 5.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3852 EGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT-DLSRVRMELGVCPQQDILLDNl 3930
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISIIPQDPVLFSG- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3931 TVREHLLLFAsikapQWTKKELHqqvnQTLQDVDLTQHQHKQTRAL-----------SGGLKRKLSLGIAFMGMSRTVVL 3999
Cdd:cd03244 93 TIRSNLDPFG-----EYSDEELW----QALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034654212 4000 DEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDeAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:cd03244 164 DEATASVDPETDALIQKTIREAFKDCTVLTIAHRLD-TIIDSDRILVLDKGRVVEFDSP 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3840-4063 |
9.26e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 97.71 E-value: 9.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3840 PGVTLVSVTKEYEGhKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqTDLSRVRMELGV 3919
Cdd:PRK09452 13 PLVELRGISKSFDG-KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-THVPAENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3920 CPQQDILLDNLTVREHlLLFAsIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVL 3999
Cdd:PRK09452 91 VFQSYALFPHMTVFEN-VAFG-LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654212 4000 DEPTSGVDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPPFCLKE 4063
Cdd:PRK09452 169 DESLSALDYKLRKQMQNELkaLQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYE 234
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3855-4058 |
1.55e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 94.47 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3855 KAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRV-RMELGVCPQQDILLDNLTVR 3933
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfARKVAYLPQQLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3934 EhllLFASIKAPqWT------KKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVD 4007
Cdd:PRK10575 104 E---LVAIGRYP-WHgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654212 4008 PCsrHSLwDIL-----LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:PRK10575 180 IA--HQV-DVLalvhrLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTP 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3842-4106 |
1.58e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 94.67 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQ--TDLSRVRMELGV 3919
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGdfSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3920 CPQQ-DILLDNLTVREHLLLfasikAPQ---WTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSR 3995
Cdd:PRK13644 82 VFQNpETQFVGRTVEEDLAF-----GPEnlcLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3996 TVVLDEPTSGVDPCSRHSLWDILLK-YREGRTIIFTTHHLDEAEAlSDRVAVLQHGRLRCCG-PPFCLKEAYGQGLRLTL 4073
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKlHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGePENVLSDVSLQTLGLTP 235
|
250 260 270
....*....|....*....|....*....|....
gi 1034654212 4074 trqPSVLE-AHDLKDMACVTSLIKIYIPQAFLKD 4106
Cdd:PRK13644 236 ---PSLIElAENLKMHGVVIPWENTSSPSSFAEE 266
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3847-4052 |
2.70e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 93.92 E-value: 2.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEGHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGL---------HPPTSGTIIINGKNLQTDLSRVRMEL 3917
Cdd:PRK09984 10 LAKTFNQHQAL-HAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdksagsHIELLGRTVQREGRLARDIRKSRANT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3918 GVCPQQDILLDNLTVREHLLLFASIKAP------QWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFM 3991
Cdd:PRK09984 89 GYIFQQFNLVNRLSVLENVLIGALGSTPfwrtcfSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034654212 3992 GMSRTVVLDEPTSGVDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:PRK09984 169 QQAKVILADEPIASLDPESARIVMDTLrdINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
3872-4058 |
3.04e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 98.58 E-value: 3.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3872 ALLGTNGAGKTTIISMLTGLHPP---TSGTIIINGKNLQTDLSRVRMelGVCPQQDILLDNLTVREHLLLFASIKAP-QW 3947
Cdd:TIGR00955 55 AVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAIS--AYVQQDDLFIPTLTVREHLMFQAHLRMPrRV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3948 TKKELHQQVNQTLQDVDLTQHQH------KQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLKY 4021
Cdd:TIGR00955 133 TKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGL 212
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1034654212 4022 -REGRTIIFTTH----HLDEaeaLSDRVAVLQHGRLRCCGPP 4058
Cdd:TIGR00955 213 aQKGKTIICTIHqpssELFE---LFDKIILMAEGRVAYLGSP 251
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3830-4056 |
3.14e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 98.36 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3830 NREGELEGSAPGVTLVSVTKEY-EGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT 3908
Cdd:PRK11160 327 PTTSTAAADQVSLTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3909 -DLSRVRMELGVCPQQdILLDNLTVREHLLLfasiKAPQWTKKELHqqvnQTLQDVDLTQH-QHKQT---------RALS 3977
Cdd:PRK11160 407 ySEAALRQAISVVSQR-VHLFSATLRDNLLL----AAPNASDEALI----EVLQQVGLEKLlEDDKGlnawlgeggRQLS 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034654212 3978 GGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDEAEALsDRVAVLQHGRLRCCG 4056
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQG 555
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3846-4050 |
3.15e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 97.81 E-value: 3.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3846 SVTKEYEGhKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNlQTDLSRVRM-ELGV--CPQ 3922
Cdd:PRK15439 16 SISKQYSG-VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNP-CARLTPAKAhQLGIylVPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3923 QDILLDNLTVREHLLLfaSIKAPQWTKKELHQQVNQTLQDVDLtqhqHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEP 4002
Cdd:PRK15439 94 EPLLFPNLSVKENILF--GLPKRQASMQKMKQLLAALGCQLDL----DSSAGSLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1034654212 4003 TSGVDPCSRHSLWDILLKYR-EGRTIIFTTHHLDEAEALSDRVAVLQHG 4050
Cdd:PRK15439 168 TASLTPAETERLFSRIRELLaQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3852-4058 |
3.50e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 93.52 E-value: 3.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3852 EGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTD-LSRVRMELGVCPQQDillDN- 3929
Cdd:PRK13632 19 NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEIRKKIGIIFQNP---DNq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3930 ---LTVREHLLLfaSIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGV 4006
Cdd:PRK13632 96 figATVEDDIAF--GLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSML 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1034654212 4007 DPCSRHSLWDILLKYREGR--TIIFTTHHLDEAeALSDRVAVLQHGRLRCCGPP 4058
Cdd:PRK13632 174 DPKGKREIKKIMVDLRKTRkkTLISITHDMDEA-ILADKVIVFSEGKLIAQGKP 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3852-4076 |
3.92e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 93.65 E-value: 3.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3852 EGHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL-QTDLSRVRMELGVCPQQ-DILLDN 3929
Cdd:PRK13647 16 DGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnAENEKWVRSKVGLVFQDpDDQVFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3930 LTVREHLLLfasikAPQ---WTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSL-GIAFMgMSRTVVLDEPTSG 4005
Cdd:PRK13647 95 STVWDDVAF-----GPVnmgLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIaGVLAM-DPDVIVLDEPMAY 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034654212 4006 VDPCSRHSLWDILLK-YREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPPFCL--KEAYGQ-GLRLTLTRQ 4076
Cdd:PRK13647 169 LDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLtdEDIVEQaGLRLPLVAQ 243
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
3858-4058 |
4.61e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 96.26 E-value: 4.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3858 VQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL----QTDLSRVR-MELGVCPQQDILLDNLTV 3932
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakisDAELREVRrKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3933 REHL---LLFASIKAPQWTKKELhqqvnQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPC 4009
Cdd:PRK10070 124 LDNTafgMELAGINAEERREKAL-----DALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034654212 4010 SRHSLWDILLKY--REGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:PRK10070 199 IRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTP 249
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3842-4067 |
5.36e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 95.17 E-value: 5.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqTDLSrvrmelgvCP 3921
Cdd:PRK11432 7 VVLKNITKRF-GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-THRS--------IQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3922 QQDI--LLDNLTVREHLLLFASI----KAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSR 3995
Cdd:PRK11432 77 QRDIcmVFQSYALFPHMSLGENVgyglKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034654212 3996 TVVLDEPTSGVDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPPfclKEAYGQ 4067
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMREKIreLQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSP---QELYRQ 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3847-4071 |
6.01e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 93.16 E-value: 6.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEGHKA-VVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL-QTDLSRVRMELGVCPQQD 3924
Cdd:PRK13635 11 ISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLsEETVWDVRRQVGMVFQNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3925 illDN----LTVREHLLlFA--SIKAPqwtKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSlgIAFMGMSR--T 3996
Cdd:PRK13635 91 ---DNqfvgATVQDDVA-FGleNIGVP---REEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVA--IAGVLALQpdI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034654212 3997 VVLDEPTSGVDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAeALSDRVAVLQHGRLRCCGPPfclKEAYGQGLRL 4071
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVrqLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTP---EEIFKSGHML 234
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3858-4051 |
7.39e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 92.36 E-value: 7.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3858 VQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRMELGVCPQ-QDI-LLDNLTVREH 3935
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTfQHVrLFREMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3936 LL----------LFAS-IKAPQWTKKELH--QQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEP 4002
Cdd:PRK11300 101 LLvaqhqqlktgLFSGlLKTPAFRRAESEalDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034654212 4003 TSGVDPCSRHSLWDILLKYRE--GRTIIFTTHHLDEAEALSDRVAVLQHGR 4051
Cdd:PRK11300 181 AAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3846-4058 |
7.61e-20 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 92.08 E-value: 7.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3846 SVTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIING---KNLQTDLSRVRMELGVCPQ 3922
Cdd:PRK09493 6 NVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvNDPKVDERLIRQEAGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3923 QDILLDNLTVREHLLlFASIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEP 4002
Cdd:PRK09493 85 QFYLFPHLTALENVM-FGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034654212 4003 TSGVDPCSRHSLWDILLKY-REGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:PRK09493 164 TSALDPELRHEVLKVMQDLaEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDP 220
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
3860-4087 |
2.40e-19 |
|
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: 93.25 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3860 DLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT-----DLSRVRMELGVCPQQDILLDNLTVRE 3934
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgiFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3935 HLLLFASIKAPQWTKKELhQQVNQTLQDVDLTQhqhKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSL 4014
Cdd:TIGR02142 95 NLRYGMKRARPSERRISF-ERVIELLGIGHLLG---RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 4015 WDILLKYRE--GRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPPfclKEAYGQGLRLTLTRQP------SVLEAHDLK 4086
Cdd:TIGR02142 171 LPYLERLHAefGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPI---AEVWASPDLPWLAREDqgslieGVVAEHDQH 247
|
.
gi 1034654212 4087 D 4087
Cdd:TIGR02142 248 Y 248
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
3843-4058 |
2.53e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 90.53 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3843 TLVSVTKEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGknlqtdlsRVR--MELGVc 3920
Cdd:COG1134 27 LLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG--------RVSalLELGA- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3921 pqqdILLDNLTVREHLLLFASIkapqwtkkeL---HQQVNQTLQDV----DLTQHQHKQTRALSGGLKRKLSLGIAFMgm 3993
Cdd:COG1134 98 ----GFHPELTGRENIYLNGRL---------LglsRKEIDEKFDEIvefaELGDFIDQPVKTYSSGMRARLAFAVATA-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3994 srtvvldeptsgVDPcsrhslwDILL----------------------KYREGRTIIFTTHHLDEAEALSDRVAVLQHGR 4051
Cdd:COG1134 163 ------------VDP-------DILLvdevlavgdaafqkkclarireLRESGRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
....*..
gi 1034654212 4052 LRCCGPP 4058
Cdd:COG1134 224 LVMDGDP 230
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3842-4051 |
3.53e-19 |
|
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: 89.60 E-value: 3.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYEGHK-AVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT-DLSRVRMELGV 3919
Cdd:cd03251 1 VEFKNVTFRYPGDGpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3920 CpQQDILLDNLTVREHLllfaSIKAPQWTKKE---------LHQQVNQTLQDVDlTQHQHKQTRaLSGGLKRKLSLGIAF 3990
Cdd:cd03251 81 V-SQDVFLFNDTVAENI----AYGRPGATREEveeaaraanAHEFIMELPEGYD-TVIGERGVK-LSGGQRQRIAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034654212 3991 MGMSRTVVLDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDEAEAlSDRVAVLQHGR 4051
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIEN-ADRIVVLEDGK 213
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3852-4052 |
5.97e-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: 5.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3852 EGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL-QTDLSRVRMELGVCPQQDILLDNl 3930
Cdd:cd03246 12 GAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIsQWDPNELGDHVGYLPQDDELFSG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3931 TVREHLLlfasikapqwtkkelhqqvnqtlqdvdltqhqhkqtralSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCS 4010
Cdd:cd03246 91 SIAENIL---------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1034654212 4011 RHSLWDIL--LKYReGRTIIFTTHHLdEAEALSDRVAVLQHGRL 4052
Cdd:cd03246 132 ERALNQAIaaLKAA-GATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3860-4058 |
6.57e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.56 E-value: 6.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3860 DLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGT-----IIINGKNLQTDLSRVRMELGVC---PQQDILldnlt 3931
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKvtvgdIVVSSTSKQKEIKPVRKKVGVVfqfPESQLF----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3932 vrEHLLLFASIKAPQ---WTKKELHQQVNQTLQDVDLTQH-QHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVD 4007
Cdd:PRK13643 99 --EETVLKDVAFGPQnfgIPKEKAEKIAAEKLEMVGLADEfWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1034654212 4008 PCSRHSLWDILLK-YREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:PRK13643 177 PKARIEMMQLFESiHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTP 228
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3847-4052 |
9.56e-19 |
|
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: 88.44 E-value: 9.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL-QTDLSRVRMELGVCPqQDI 3925
Cdd:cd03253 6 VTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIrEVTLDSLRRAIGVVP-QDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3926 LLDNLTVREHLL---LFAS----IKAPQwtKKELHQQVNQTLQDVDlTQHQHKQTRaLSGGLKRKLSLGIAFMGMSRTVV 3998
Cdd:cd03253 85 VLFNDTIGYNIRygrPDATdeevIEAAK--AAQIHDKIMRFPDGYD-TIVGERGLK-LSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1034654212 3999 LDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDEAeALSDRVAVLQHGRL 4052
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTI-VNADKIIVLKDGRI 213
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3835-4058 |
1.42e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.04 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3835 LEGSAPGVTLVSVTKEYEGHKA-VVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL-QTDLSR 3912
Cdd:PRK13648 1 MEDKNSIIVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItDDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3913 VRMELGVCPQQ------------DIL--LDNLTVrehlllfasikapqwTKKELHQQVNQTLQDVDLTQHQHKQTRALSG 3978
Cdd:PRK13648 81 LRKHIGIVFQNpdnqfvgsivkyDVAfgLENHAV---------------PYDEMHRRVSEALKQVDMLERADYEPNALSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3979 GLKRKLSL-GIAFMGMSrTVVLDEPTSGVDPCSRHSLWDILLKYREGR--TIIFTTHHLDEAeALSDRVAVLQHGRLRCC 4055
Cdd:PRK13648 146 GQKQRVAIaGVLALNPS-VIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTVYKE 223
|
...
gi 1034654212 4056 GPP 4058
Cdd:PRK13648 224 GTP 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3847-4058 |
1.67e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.09 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL-QTDLSRVRMELGVCPQQ-D 3924
Cdd:PRK13652 9 LCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItKENIREVRKFVGLVFQNpD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3925 ILLDNLTVrEHLLLFASIKAPQWTKKELHqQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSL-GIAFMgMSRTVVLDEPT 4003
Cdd:PRK13652 89 DQIFSPTV-EQDIAFGPINLGLDEETVAH-RVSSALHMLGLEELRDRVPHHLSGGEKKRVAIaGVIAM-EPQVLVLDEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034654212 4004 SGVDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:PRK13652 166 AGLDPQGVKELIDFLndLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTV 222
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3855-4058 |
1.97e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 88.70 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3855 KAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTS---GTIIINGKNLQTD-LSRVRMELGVCPQQDillDN- 3929
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKtVWDIREKVGIVFQNP---DNq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3930 ---LTVREHLLLfaSIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSL-GIAFMGmSRTVVLDEPTSG 4005
Cdd:PRK13640 97 fvgATVGDDVAF--GLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIaGILAVE-PKIIILDESTSM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034654212 4006 VDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEaLSDRVAVLQHGRLRCCGPP 4058
Cdd:PRK13640 174 LDPAGKEQILKLIrkLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSP 227
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3857-4052 |
2.19e-18 |
|
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: 93.27 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3857 VVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT-DLSRVRMELGVCPQQDILLDNlTVREH 3935
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYLPQEPYIFSG-SILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3936 LLLFASikaPQWTKKELHQQVNQTLQDVDLTQ-HQHKQTR------ALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDP 4008
Cdd:TIGR01193 568 LLLGAK---ENVSQDEIWAACEIAEIKDDIENmPLGYQTElseegsSISGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1034654212 4009 CSRHSLWDILLKYREgRTIIFTTHHLDEAEaLSDRVAVLQHGRL 4052
Cdd:TIGR01193 645 ITEKKIVNNLLNLQD-KTIIFVAHRLSVAK-QSDKIIVLDHGKI 686
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3842-4056 |
2.26e-18 |
|
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: 87.54 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYEGHKAVV-QDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT-DLSRVRMELGV 3919
Cdd:cd03252 1 ITFEHVRFRYKPDGPVIlDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3920 CPQQDILLdNLTVREHLLL------------FASIKAPQWTKKELHQQVNQTLQDvdltqhqhkQTRALSGGLKRKLSLG 3987
Cdd:cd03252 81 VLQENVLF-NRSIRDNIALadpgmsmervieAAKLAGAHDFISELPEGYDTIVGE---------QGAGLSGGQRQRIAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034654212 3988 IAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDEAEAlSDRVAVLQHGRLRCCG 4056
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQG 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3847-4052 |
2.47e-18 |
|
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: 89.34 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEGHKAVVQ---DLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPP---TSGTIIINGKNLqTDLSRVRM----- 3915
Cdd:COG0444 7 LKVYFPTRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDL-LKLSEKELrkirg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3916 -ELGVCPQ------------QDILLDnlTVREHLLLfasikapqwTKKELHQQVNQTLQDVDLTQ---------HQhkqt 3973
Cdd:COG0444 86 rEIQMIFQdpmtslnpvmtvGDQIAE--PLRIHGGL---------SKAEARERAIELLERVGLPDperrldrypHE---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3974 raLSGGLKRKLslGIAfMGMS---RTVVLDEPTSGVDPCSRHSLWDILLKYRE--GRTIIFTTHHLDEAEALSDRVAVLQ 4048
Cdd:COG0444 151 --LSGGMRQRV--MIA-RALAlepKLLIADEPTTALDVTIQAQILNLLKDLQRelGLAILFITHDLGVVAEIADRVAVMY 225
|
....
gi 1034654212 4049 HGRL 4052
Cdd:COG0444 226 AGRI 229
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3854-4050 |
2.55e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 88.31 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3854 HKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQ-TDLS----RVRM-----ELGVCPQQ 3923
Cdd:PRK15112 25 TVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfGDYSyrsqRIRMifqdpSTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3924 DI--LLDnltvrEHLLLFASIKAPqwtkkELHQQVNQTLQDVDL-TQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLD 4000
Cdd:PRK15112 105 RIsqILD-----FPLRLNTDLEPE-----QREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIAD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1034654212 4001 EPTSGVDPCSRHSLWDILLKYREGRTI--IFTTHHLDEAEALSDRVAVLQHG 4050
Cdd:PRK15112 175 EALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVMHQG 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3853-4052 |
2.85e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 91.62 E-value: 2.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3853 GHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRMELGV--CP----QQDIL 3926
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIayVPedrkGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3927 LDnLTVREHLLLfASIKAPQW----TKKELHQQVNQTLQDVDL-TQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDE 4001
Cdd:COG1129 343 LD-LSIRENITL-ASLDRLSRggllDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDE 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1034654212 4002 PTSGVDPCSRHSLWDILLKY-REGRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:COG1129 421 PTRGIDVGAKAEIYRLIRELaAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
3860-4052 |
3.31e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 88.35 E-value: 3.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3860 DLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGK--NLQT---DLSRVRMELGVCPQ--QDILLDNlTV 3932
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhiTPETgnkNLKKLRKKVSLVFQfpEAQLFEN-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3933 REHLLL----F------ASIKAPQWTKKelhqqvnqtlqdVDL-TQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDE 4001
Cdd:PRK13641 104 LKDVEFgpknFgfsedeAKEKALKWLKK------------VGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1034654212 4002 PTSGVDPCSRHSLWDILLKY-REGRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
3841-4058 |
6.02e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 87.49 E-value: 6.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3841 GVTLVSVTKEYEG----HKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT-----DLS 3911
Cdd:PRK13649 2 GINLQNVSYTYQAgtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3912 RVRMELGVCPQ--QDILLDNlTVREHLLLfasikAPQ---WTKKELHQQVNQTLQDVDLTQHQ-HKQTRALSGGLKRKLS 3985
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEE-TVLKDVAF-----GPQnfgVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034654212 3986 L-GIAFMGMSrTVVLDEPTSGVDPCSRHSLWDILLK-YREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:PRK13649 156 IaGILAMEPK-ILVLDEPTAGLDPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKP 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3831-4058 |
6.16e-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: 91.02 E-value: 6.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3831 REGELEGSAPGVTLVSVTKEY----EGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL 3906
Cdd:TIGR03269 269 KECEVEVGEPIIKVRNVSKRYisvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3907 QTDLS--------RVRMELGVCPQQDILLDNLTVREHLLLFASIKAPqwtkKEL-HQQVNQTLQDVDLTQHQ-----HKQ 3972
Cdd:TIGR03269 349 WVDMTkpgpdgrgRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLELP----DELaRMKAVITLKMVGFDEEKaeeilDKY 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3973 TRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYRE--GRTIIFTTHHLDEAEALSDRVAVLQHG 4050
Cdd:TIGR03269 425 PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDVCDRAALMRDG 504
|
....*...
gi 1034654212 4051 RLRCCGPP 4058
Cdd:TIGR03269 505 KIVKIGDP 512
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
3838-4057 |
7.00e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 86.86 E-value: 7.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3838 SAPGVTLVSVTKEYE-GHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRme 3916
Cdd:PRK15056 3 QQAGIVVNDVTVTWRnGHTAL-RDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3917 LGVCPQQD-------ILLDNLTVREHLLLFASIKAPqwtKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIA 3989
Cdd:PRK15056 80 VAYVPQSEevdwsfpVLVEDVVMMGRYGHMGWLRRA---KKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034654212 3990 FMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYR-EGRTIIFTTHHLDEAEALSDrVAVLQHGRLRCCGP 4057
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGP 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
3853-4041 |
8.59e-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: 84.72 E-value: 8.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3853 GHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGknlqTDLSRVRMElgvcPQQDIL----LD 3928
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNG----TPLAEQRDE----PHENILylghLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3929 ----NLTVREHLLLFASIKAPQwtkkelHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTS 4004
Cdd:TIGR01189 83 glkpELSALENLHFWAAIHGGA------QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1034654212 4005 GVDPCSRHSLWDILLKYRE-GRTIIFTTHH---LDEAEALS 4041
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLArGGIVLLTTHQdlgLVEARELR 197
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3854-4052 |
1.34e-17 |
|
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: 84.83 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3854 HKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL-QTDLSRVRMELGVCPQQDILL----- 3927
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIsQYEHKYLHSKVSLVGQEPVLFarslq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3928 DNLTVREHLLLFASIKAPQwTKKELHQQVNQTLQDVDlTQHQHKQTRaLSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVD 4007
Cdd:cd03248 106 DNIAYGLQSCSFECVKEAA-QKAHAHSFISELASGYD-TEVGEKGSQ-LSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1034654212 4008 PCSRHSLWDILLKYREGRTIIFTTHHLDEAEAlSDRVAVLQHGRL 4052
Cdd:cd03248 183 AESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
3853-4033 |
1.36e-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: 84.08 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3853 GHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRMELGVCPQQDILLDNLTV 3932
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3933 REHLLLFASIKApqwtkkelHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRH 4012
Cdd:cd03231 91 LENLRFWHADHS--------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|..
gi 1034654212 4013 SLWDILLKYRE-GRTIIFTTHH 4033
Cdd:cd03231 163 RFAEAMAGHCArGGMVVLTTHQ 184
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3841-4061 |
2.52e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 87.39 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3841 GVTLVSVTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQtDLSRVRMELGVC 3920
Cdd:PRK11000 3 SVTLRNVTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-DVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3921 PQQDILLDNLTVREHL---LLFASIKapqwtKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTV 3997
Cdd:PRK11000 81 FQSYALYPHLSVAENMsfgLKLAGAK-----KEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654212 3998 VLDEPTSGVDPCSRHSL-WDIL-LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPPFCL 4061
Cdd:PRK11000 156 LLDEPLSNLDAALRVQMrIEISrLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3853-4083 |
2.58e-17 |
|
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: 85.24 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3853 GHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL-QTDLS---RVRMELGVCPQQDILLD 3928
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLyQLDRKqrrAFRRDVQLVFQDSPSAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3929 N--LTVREhlllfaSIKAP-----QWTKKELHQQVNQTLQDVDL-TQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLD 4000
Cdd:TIGR02769 102 NprMTVRQ------IIGEPlrhltSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 4001 EPTSGVDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRL---RCCGPPFCLKEAYGQGLrltltr 4075
Cdd:TIGR02769 176 EAVSNLDMVLQAVILELLrkLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIveeCDVAQLLSFKHPAGRNL------ 249
|
....*...
gi 1034654212 4076 QPSVLEAH 4083
Cdd:TIGR02769 250 QSAVLPEH 257
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
3857-4051 |
4.11e-17 |
|
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: 83.74 E-value: 4.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3857 VVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT-DLSRVRMELGVCPQQDILLDNlTVREH 3935
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVLFDG-TIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3936 lLLFASIKAPQWTKKELHQQVN-----QTLQDVDLTQHQHKQTRaLSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCS 4010
Cdd:cd03249 97 -IRYGKPDATDEEVEEAAKKANihdfiMSLPDGYDTLVGERGSQ-LSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1034654212 4011 RHSLWDILLKYREGRTIIFTTHHLDEAEAlSDRVAVLQHGR 4051
Cdd:cd03249 175 EKLVQEALDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQ 214
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
3853-4040 |
4.21e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.00 E-value: 4.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3853 GHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRME-LGvcpQQDILLDNLT 3931
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHyLG---HRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3932 VREHLLLFASIKAPqwtkKELHqqVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLgiAFMGMSRTVV--LDEPTSGVDPC 4009
Cdd:PRK13539 90 VAENLEFWAAFLGG----EELD--IAAALEAVGLAPLAHLPFGYLSAGQKRRVAL--ARLLVSNRPIwiLDEPTAALDAA 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1034654212 4010 SRHSLWDILLKYRE-GRTIIFTTHH---LDEAEAL 4040
Cdd:PRK13539 162 AVALFAELIRAHLAqGGIVIAATHIplgLPGAREL 196
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3853-4057 |
5.66e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 83.81 E-value: 5.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3853 GHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGL-----HPPTSGTIIINGKNL-QTDLSRVRMELGVCPQQDIL 3926
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIfKMDVIELRRRVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3927 LDNLTVREHLLLFASIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRA----LSGGLKRKLSLGIAFMGMSRTVVLDEP 4002
Cdd:PRK14247 94 IPNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDApagkLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034654212 4003 TSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGP 4057
Cdd:PRK14247 174 TANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGP 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3855-4086 |
5.94e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 84.37 E-value: 5.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3855 KAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIING--KNLQTDLSRVRMELGVCPQQDillDN--- 3929
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldTSDEENLWDIRNKAGMVFQNP---DNqiv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3930 LTVREHLLLFA--SIKAPQwtkKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSL-GIAFMgMSRTVVLDEPTSGV 4006
Cdd:PRK13633 100 ATIVEEDVAFGpeNLGIPP---EEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIaGILAM-RPECIIFDEPTAML 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 4007 DPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAeALSDRVAVLQHGRLRCCGPPfclKEAYGQ-------GLRLtltrqP 4077
Cdd:PRK13633 176 DPSGRREVVNTIkeLNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTP---KEIFKEvemmkkiGLDV-----P 246
|
250
....*....|
gi 1034654212 4078 SVLE-AHDLK 4086
Cdd:PRK13633 247 QVTElAYELK 256
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
3860-4058 |
6.03e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 84.69 E-value: 6.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3860 DLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTI------IINGKNlQTDLSRVRMELGVCPQqdilldnltVR 3933
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigervITAGKK-NKKLKPLRKKVGIVFQ---------FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3934 EHLLLFASIK-----APQ---WTKKELHQQVNQTLQDVDLTQH-QHKQTRALSGGLKRKLSlgIA-FMGMSRTV-VLDEP 4002
Cdd:PRK13634 95 EHQLFEETVEkdicfGPMnfgVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVA--IAgVLAMEPEVlVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034654212 4003 TSGVDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFykLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTP 230
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3849-4052 |
6.19e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 83.33 E-value: 6.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3849 KEY-EG--HKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRM-----ELGVC 3920
Cdd:PRK11629 13 KRYqEGsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnqKLGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3921 PQQDILLDNLTVREHL---LLFASIKapqwtKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTV 3997
Cdd:PRK11629 93 YQFHHLLPDFTALENVampLLIGKKK-----PAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034654212 3998 VLDEPTSGVDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAvLQHGRL 4052
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLgeLNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRL 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
3839-4058 |
9.39e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.05 E-value: 9.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3839 APGVTLVSVTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQ-TDLSRVRMEL 3917
Cdd:PRK09536 1 MPMIDVSDLSVEF-GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEaLSARAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3918 GVCPQQDILLDNLTVRE--------HLLLFASikapqWTKKElHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIA 3989
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQvvemgrtpHRSRFDT-----WTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034654212 3990 FMGMSRTVVLDEPTSGVDpcSRHSLWDILLKYR---EGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:PRK09536 154 LAQATPVLLLDEPTASLD--INHQVRTLELVRRlvdDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPP 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3849-4058 |
1.18e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 85.14 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3849 KEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKnlqtDLSRVRM---ELGVCPQQDI 3925
Cdd:PRK10851 9 KKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT----DVSRLHArdrKVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3926 LLDNLTVREHLLLFASI----KAPqwTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDE 4001
Cdd:PRK10851 85 LFRHMTVFDNIAFGLTVlprrERP--NAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034654212 4002 PTSGVDPCSRHSLWDIL------LKYregrTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:PRK10851 163 PFGALDAQVRKELRRWLrqlheeLKF----TSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTP 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3839-4052 |
1.69e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.23 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3839 APGVTLVSV----TKEYEGHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqTDLS-RV 3913
Cdd:COG3845 252 EPGEVVLEVenlsVRDDRGVPAL-KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI-TGLSpRE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3914 RMELGVC-----PQQDILLDNLTVREHLLLfASIKAPQWTK------KELHQQVNQTLQDVDL-TQHQHKQTRALSGGLK 3981
Cdd:COG3845 330 RRRLGVAyipedRLGRGLVPDMSVAENLIL-GRYRRPPFSRggfldrKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQ 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034654212 3982 RKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYR-EGRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:COG3845 409 QKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3841-4052 |
1.95e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 81.98 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3841 GVTLVSVTKEYEGHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGK--NLQTDLS-----RV 3913
Cdd:COG4161 2 SIQLKNINCFYGSHQAL-FDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSekairLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3914 RMELGVCPQQDILLDNLTVREHLllfasIKAPQW----TKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIA 3989
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTVMENL-----IEAPCKvlglSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034654212 3990 FMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYRE-GRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
3851-4072 |
1.96e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.91 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3851 YEgHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIING-----KNLQTDLSRVRMELGVC---PQ 3922
Cdd:PRK13646 18 YE-HQAI-HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithKTKDKYIRPVRKRIGMVfqfPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3923 QDILLDNLtvrEHLLLFASiKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTR-ALSGGLKRKLSLgIAFMGMS-RTVVLD 4000
Cdd:PRK13646 96 SQLFEDTV---EREIIFGP-KNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPfQMSGGQMRKIAI-VSILAMNpDIIVLD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034654212 4001 EPTSGVDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPPfclKEAYGQGLRLT 4072
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLksLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSP---KELFKDKKKLA 241
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3829-4057 |
2.26e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.84 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3829 QNREGELEGSAPGVTLVSVTKEYEGhKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSG-----TIIING 3903
Cdd:PRK14271 9 QSGAADVDAAAPAMAAVNLTLGFAG-KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3904 KNL--QTDLSRVRMELGVCPQQD-----ILLDNLT--VREHLLL----FASIKAPQWTKKELHQQVNQTLQDVDLTqhqh 3970
Cdd:PRK14271 88 RSIfnYRDVLEFRRRVGMLFQRPnpfpmSIMDNVLagVRAHKLVprkeFRGVAQARLTEVGLWDAVKDRLSDSPFR---- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3971 kqtraLSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDEAEALSDRVAVLQHG 4050
Cdd:PRK14271 164 -----LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDG 238
|
....*..
gi 1034654212 4051 RLRCCGP 4057
Cdd:PRK14271 239 RLVEEGP 245
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
3857-4051 |
5.81e-16 |
|
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: 79.44 E-value: 5.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3857 VVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKnlqtdlsrvrmeLGVCPQQDILLdNLTVREHl 3936
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------IAYVSQEPWIQ-NGTIREN- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3937 LLFASIKAPQWTKKELH----QQVNQTLQDVDLTQHQHKQTrALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRH 4012
Cdd:cd03250 86 ILFGKPFDEERYEKVIKacalEPDLEILPDGDLTEIGEKGI-NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034654212 4013 SLWD--ILLKYREGRTIIFTTHHLdeaEALS--DRVAVLQHGR 4051
Cdd:cd03250 165 HIFEncILGLLLNNKTRILVTHQL---QLLPhaDQIVVLDNGR 204
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3858-4071 |
5.95e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 81.32 E-value: 5.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3858 VQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTD-LSRVRMELGVCPQQDillDN----LTV 3932
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnVWDIRHKIGMVFQNP---DNqfvgATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3933 REHLLLFASIKApqWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRH 4012
Cdd:PRK13650 100 EDDVAFGLENKG--IPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034654212 4013 SLWDILLKYRE--GRTIIFTTHHLDEAeALSDRVAVLQHGRLRCCGPPfclKEAYGQGLRL 4071
Cdd:PRK13650 178 ELIKTIKGIRDdyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTP---RELFSRGNDL 234
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3851-4052 |
6.56e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 80.85 E-value: 6.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3851 YEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHP--P---TSGTIIINGKNL---QTDLSRVRMELGVCPQ 3922
Cdd:COG1117 20 YYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydpDVDVVELRRRVGMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3923 QDILL-----DNLT--VREHlllfaSIKapqwTKKELHQQVNQTLQDVDL---TQHQ-HKQTRALSGGLKRKLSlgIAfm 3991
Cdd:COG1117 100 KPNPFpksiyDNVAygLRLH-----GIK----SKSELDEIVEESLRKAALwdeVKDRlKKSALGLSGGQQQRLC--IA-- 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034654212 3992 gmsRT------VVL-DEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:COG1117 167 ---RAlavepeVLLmDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3827-4052 |
6.68e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 84.63 E-value: 6.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3827 SLQNREGElegsapgVTLVSVTKEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL 3906
Cdd:PRK13657 327 DLGRVKGA-------VEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3907 QT-DLSRVRMELGVCpQQDILLDNLTVREHLllfaSIKAPQWTKKELHQ--QVNQTLqDVDLTQHQHKQT------RALS 3977
Cdd:PRK13657 400 RTvTRASLRRNIAVV-FQDAGLFNRSIEDNI----RVGRPDATDEEMRAaaERAQAH-DFIERKPDGYDTvvgergRQLS 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654212 3978 GGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDE-AEAlsDRVAVLQHGRL 4052
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTvRNA--DRILVFDNGRV 547
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3846-4052 |
6.74e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 80.44 E-value: 6.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3846 SVTKEYEGHKAVVqDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIIngKNLQTDLSR---------VRME 3916
Cdd:PRK11124 7 GINCFYGAHQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNI--AGNHFDFSKtpsdkaireLRRN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3917 LGVCPQQDILLDNLTVREHLllfasIKAP----QWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMg 3992
Cdd:PRK11124 84 VGMVFQQYNLWPHLTVQQNL-----IEAPcrvlGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034654212 3993 MSRTVVL-DEPTSGVDPCSRHSLWDILLKYRE-GRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:PRK11124 158 MEPQVLLfDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3843-4037 |
9.05e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 80.51 E-value: 9.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3843 TLVSVTKEYEGhKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSrvrmELGVCPQ 3922
Cdd:PRK11248 3 QISHLYADYGG-KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA----ERGVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3923 QDILLDNLTVREHL---LLFASIkapqwTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVL 3999
Cdd:PRK11248 78 NEGLLPWRNVQDNVafgLQLAGV-----EKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1034654212 4000 DEPTSGVDPCSRHSLWDILLK--YREGRTIIFTTHHLDEA 4037
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKlwQETGKQVLLITHDIEEA 192
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
3869-4032 |
1.05e-15 |
|
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: 78.44 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3869 QITALLGTNGAGKTTIISML-----TGLhppTSGTIIINGKNLQTDLSRvrmELGVCPQQDILLDNLTVREHLLLFASIk 3943
Cdd:cd03232 34 TLTALMGESGAGKTTLLDVLagrktAGV---ITGEILINGRPLDKNFQR---STGYVEQQDVHSPNLTVREALRFSALL- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3944 apqwtkkelhqqvnqtlqdvdltqhqhkqtRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLKY-R 4022
Cdd:cd03232 107 ------------------------------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLaD 156
|
170
....*....|
gi 1034654212 4023 EGRTIIFTTH 4032
Cdd:cd03232 157 SGQAILCTIH 166
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
3855-4068 |
1.29e-15 |
|
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: 78.34 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3855 KAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGlHP---PTSGTIIINGKNLqTDLS---RVRMELGVCPQQDILLD 3928
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEGEILFKGEDI-TDLPpeeRARLGIFLAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3929 NLTVREHLllfasikapqwtkkelhQQVNQTlqdvdltqhqhkqtraLSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDP 4008
Cdd:cd03217 91 GVKNADFL-----------------RYVNEG----------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034654212 4009 CSRHSLWDILLKYR-EGRTIIFTTHHLDEAEAL-SDRVAVLQHGRLRCCGPPFCLKEAYGQG 4068
Cdd:cd03217 138 DALRLVAEVINKLReEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELALEIEKKG 199
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
3855-4056 |
1.52e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 84.00 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3855 KAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL-QTDLSRVRMELGVCpQQDILLDNLTVR 3933
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLvQYDHHYLHRQVALV-GQEPVLFSGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3934 EHL---LLFASIKAPQWTKKE--LHQQVNQTLQDVDLTQHQHKQTraLSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDP 4008
Cdd:TIGR00958 573 ENIaygLTDTPDEEIMAAAKAanAHDFIMEFPNGYDTEVGEKGSQ--LSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1034654212 4009 CSRHSLWDilLKYREGRTIIFTTHHLDEAEAlSDRVAVLQHGRLRCCG 4056
Cdd:TIGR00958 651 ECEQLLQE--SRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3849-4058 |
1.89e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 79.63 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3849 KEYEGHKaVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL--------------QTDLSRVR 3914
Cdd:PRK10619 13 KRYGEHE-VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvadKNQLRLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3915 MELGVCPQQDILLDNLTVREHLLLfASIKAPQWTKKELHQQVNQTLQDVDLTQH-QHKQTRALSGGLKRKLSLGIAFMGM 3993
Cdd:PRK10619 92 TRLTMVFQHFNLWSHMTVLENVME-APIQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654212 3994 SRTVVLDEPTSGVDPCSRHSLWDILLKY-REGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3842-4052 |
1.99e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 79.34 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINgknlQTDLSRVRMELGVCP 3921
Cdd:PRK11247 13 LLLNAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG----TAPLAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3922 QQDILL------DN--LTVREHlllfasikapqWTKKELhqqvnQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGM 3993
Cdd:PRK11247 88 QDARLLpwkkviDNvgLGLKGQ-----------WRDAAL-----QALAAVGLADRANEWPAALSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654212 3994 SRTVVLDEPTSGVDPCSR-------HSLWDillkyREGRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRiemqdliESLWQ-----QHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3838-4056 |
2.63e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 78.94 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3838 SAPGVTLVSVTKEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL-------QTDL 3910
Cdd:PRK14246 6 SAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdifQIDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3911 SRVRMELGVCPQQDILLDNLTVREHL---LLFASIKapqwTKKELHQQVNQTLQDVDLTQHQHKQTRA----LSGGLKRK 3983
Cdd:PRK14246 86 IKLRKEVGMVFQQPNPFPHLSIYDNIaypLKSHGIK----EKREIKKIVEECLRKVGLWKEVYDRLNSpasqLSGGQQQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034654212 3984 LSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCG 4056
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWG 234
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
3853-4058 |
5.00e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.49 E-value: 5.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3853 GHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSR-VRMELGVCPQQDILLDNLT 3931
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKeVARRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3932 VREhllLFASIKAP------QWtKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSG 4005
Cdd:PRK10253 98 VQE---LVARGRYPhqplftRW-RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034654212 4006 VDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:PRK10253 174 LDISHQIDLLELLseLNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAP 228
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3842-4058 |
5.17e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.85 E-value: 5.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKnlqtdlsrvrMELGVCP 3921
Cdd:PRK09544 5 VSLENVSVSF-GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK----------LRIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3922 QQdILLDN---LTVREHLLLFASIKA----PQWTKKELHQQVNQTLQDvdltqhqhkqtraLSGGLKRKLSLGIAFMGMS 3994
Cdd:PRK09544 74 QK-LYLDTtlpLTVNRFLRLRPGTKKedilPALKRVQAGHLIDAPMQK-------------LSGGETQRVLLARALLNRP 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654212 3995 RTVVLDEPTSGVDPCSRHSLWDILLKYRE--GRTIIFTTHHLDEAEALSDRVAVLQHgRLRCCGPP 4058
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTP 204
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3844-4052 |
7.42e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 81.69 E-value: 7.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3844 LVSVTKEY---EGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT----DLSRVRME 3916
Cdd:PRK10535 7 LKDIRRSYpsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadALAQLRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3917 -LGVCPQQDILLDNLTVREHL---LLFASIKapqwtKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMG 3992
Cdd:PRK10535 87 hFGFIFQRYHLLSHLTAAQNVevpAVYAGLE-----RKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034654212 3993 MSRTVVLDEPTSGVDPCSRHSLWDILLKYRE-GRTIIFTTHHLDEAeALSDRVAVLQHGRL 4052
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVA-AQAERVIEIRDGEI 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3847-4053 |
7.70e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.88 E-value: 7.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGknlqtdlsrvRMELGVCPQQDIL 3926
Cdd:COG0488 4 LSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK----------GLRIGYLPQEPPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3927 LDNLTVREHLLL-FASIKApqwTKKELHQ--------------------------------QVNQTLQDVDLTQHQH-KQ 3972
Cdd:COG0488 73 DDDLTVLDTVLDgDAELRA---LEAELEEleaklaepdedlerlaelqeefealggweaeaRAEEILSGLGFPEEDLdRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3973 TRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYReGrTIIFTTH--H-LDeaeALSDRVAVLQH 4049
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYP-G-TVLVVSHdrYfLD---RVATRILELDR 224
|
....
gi 1034654212 4050 GRLR 4053
Cdd:COG0488 225 GKLT 228
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3844-4050 |
1.08e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.43 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3844 LVSVTKEYEGHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRME--LGVCP 3921
Cdd:PRK10762 7 LKGIDKAFPGVKAL-SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEagIGIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3922 QQDILLDNLTVREHLLL-------FASIkapQWtkKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMS 3994
Cdd:PRK10762 86 QELNLIPQLTIAENIFLgrefvnrFGRI---DW--KKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034654212 3995 RTVVLDEPTSGVDPCSRHSLWDILLKYR-EGRTIIFTTHHLDEAEALSDRVAVLQHG 4050
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLFRVIRELKsQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3842-4057 |
1.20e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 77.10 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYEGHkAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTI------IINGKNL---QTDLSR 3912
Cdd:PRK11264 4 IEVKNLVKKFHGQ-TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditIDTARSLsqqKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3913 VRMELGVCPQQDILLDNLTVREHLllfasIKAPQWTKKELHQQV----NQTLQDVDLTQHQHKQTRALSGGLKRKLSLGI 3988
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENI-----IEGPVIVKGEPKEEAtaraRELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034654212 3989 AfMGMSRTVVL-DEPTSGVDPcsrHSLWDILLKYR----EGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGP 4057
Cdd:PRK11264 158 A-LAMRPEVILfDEPTSALDP---ELVGEVLNTIRqlaqEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGP 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
3847-4052 |
1.40e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 77.82 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEG----HKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRMELGVcpq 3922
Cdd:PRK13651 8 IVKIFNKklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVL--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3923 QDILLDNLTVR-------------------EHLLLFASIK-----APQ---WTKKELHQQVNQTLQDVDLTQ-HQHKQTR 3974
Cdd:PRK13651 85 EKLVIQKTRFKkikkikeirrrvgvvfqfaEYQLFEQTIEkdiifGPVsmgVSKEEAKKRAAKYIELVGLDEsYLQRSPF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3975 ALSGGLKRKLSL-GIAFMGmSRTVVLDEPTSGVDPCSRHSLWDILLK-YREGRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:PRK13651 165 ELSGGQKRRVALaGILAME-PDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
3853-4070 |
1.56e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.03 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3853 GHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqTDLSRVRME-------------LG- 3918
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPL-AKLNRAQRKafrrdiqmvfqdsISa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3919 VCPQQDIlldNLTVRE---HLLlfasikapQWTKKELHQQVNQTLQDVDLT-QHQHKQTRALSGGLKRKLSLGIAFMGMS 3994
Cdd:PRK10419 102 VNPRKTV---REIIREplrHLL--------SLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3995 RTVVLDEPTSGVDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRL---RCCGPPFCLKEAYGQGL 4069
Cdd:PRK10419 171 KLLILDEAVSNLDLVLQAGVIRLLkkLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIvetQPVGDKLTFSSPAGRVL 250
|
.
gi 1034654212 4070 R 4070
Cdd:PRK10419 251 Q 251
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3869-4050 |
1.63e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 81.31 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3869 QITALLGTNGAGKTTIISML-----TGLhpPTSGTIIINGKNLQTDLSRVrmeLGVCPQQDILLDNLTVREHLLLFASIK 3943
Cdd:TIGR00956 790 TLTALMGASGAGKTTLLNVLaervtTGV--ITGGDRLVNGRPLDSSFQRS---IGYVQQQDLHLPTSTVRESLRFSAYLR 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3944 APQ-WTKKELHQQVNQTLQDVDLTQHQHkqtrALSG----GL----KRKLSLGIAFMGMSRTVV-LDEPTSGVDpcSRhS 4013
Cdd:TIGR00956 865 QPKsVSKSEKMEYVEEVIKLLEMESYAD----AVVGvpgeGLnveqRKRLTIGVELVAKPKLLLfLDEPTSGLD--SQ-T 937
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1034654212 4014 LWDILLKYRE----GRTIIFTTHH-----LDEAealsDRVAVLQHG 4050
Cdd:TIGR00956 938 AWSICKLMRKladhGQAILCTIHQpsailFEEF----DRLLLLQKG 979
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3928-4052 |
1.81e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 78.24 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3928 DNLTVREHLLLFAsiKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVD 4007
Cdd:NF000106 99 ESFSGRENLYMIG--R*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1034654212 4008 PCSRHSLWD-ILLKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:NF000106 177 PRTRNEVWDeVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3840-4053 |
1.86e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 76.61 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3840 PGVTLVSVTKEYEGHKaVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTS-----GTIIINGKNL---QTDLS 3911
Cdd:PRK14258 6 PAIKVNNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3912 RVRMELG-VCPQQDI----LLDNLTVrehlllfaSIKAPQWTKK-ELHQQVNQTLQDVDL---TQHQ-HKQTRALSGGLK 3981
Cdd:PRK14258 85 RLRRQVSmVHPKPNLfpmsVYDNVAY--------GVKIVGWRPKlEIDDIVESALKDADLwdeIKHKiHKSALDLSGGQQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034654212 3982 RKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLR 4053
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENR 230
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3853-4042 |
2.09e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 76.73 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3853 GHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTdLSR-----VRMELGVCPQQDILL 3927
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPA-MSRsrlytVRKRMSMLFQSGALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3928 DNLTV--------REHLLLFASIkapqwtkkeLHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVL 3999
Cdd:PRK11831 97 TDMNVfdnvayplREHTQLPAPL---------LHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1034654212 4000 DEPTSGVDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSD 4042
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLIseLNSALGVTCVVVSHDVPEVLSIAD 212
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3851-4057 |
5.70e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 74.88 E-value: 5.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3851 YEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTII---SMLTGLHPPT--SGTIIINGKNL---QTDLSRVRMELGVCPQ 3922
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfNRLLELNEEArvEGEVRLFGRNIyspDVDPIEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3923 QDILLDNLTVREHLLLFASIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTR----ALSGGLKRKLSLGIAFMGMSRTVV 3998
Cdd:PRK14267 93 YPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALWDEVKDRLNdypsNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034654212 3999 LDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGP 4057
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGP 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3860-4052 |
6.60e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.78 E-value: 6.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3860 DLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRMELGVC--P---QQDIL-LD----- 3928
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylPedrQSSGLyLDaplaw 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3929 ---NLTVREhLLLFASIKAPQWTKKELHQQVNQTLQDVDltqhqhKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSG 4005
Cdd:PRK15439 361 nvcALTHNR-RGFWIKPARENAVLERYRRALNIKFNHAE------QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1034654212 4006 VDPCSRHSLWDILLKY-REGRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:PRK15439 434 VDVSARNDIYQLIRSIaAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3843-4051 |
7.32e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.66 E-value: 7.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3843 TLVSVTKEYEGHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHP--PTSGTIIINGKNLQTDLSRVRMELGVC 3920
Cdd:PRK13549 7 EMKNITKTFGGVKAL-DNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASNIRDTERAGIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3921 --PQQDILLDNLTVREHLLLFAsikapQWTKK------ELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMG 3992
Cdd:PRK13549 86 iiHQELALVKELSVLENIFLGN-----EITPGgimdydAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034654212 3993 MSRTVVLDEPTSGVDPCSRHSLWDIL--LKyREGRTIIFTTHHLDEAEALSDRVAVLQHGR 4051
Cdd:PRK13549 161 QARLLILDEPTASLTESETAVLLDIIrdLK-AHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
3527-3728 |
7.84e-14 |
|
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: 76.27 E-value: 7.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3527 LQDMIERAIILVQTGQEALEPAAQTQAAPYPCHTSDLF---LNNVGFFFPLIMMLTWMVSVASMVRKLVYEQEIQIEEYM 3603
Cdd:pfam12698 116 ILNALQSLLQQLNASALVLLLEALSTSAPIPVESTPLFnpqSGYAYYLVGLILMIIILIGAAIIAVSIVEEKESRIKERL 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3604 RMMGVHPVIHFLAWFLENMAVLTISSATLAIVLKTSGIFAHSNTFIVFLFLLdFGMSVVMLSYLLSAFFSQAnTAALCTS 3683
Cdd:pfam12698 196 LVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGIGIPFGNLGLLLLLFLL-YGLAYIALGYLLGSLFKNS-EDAQSII 273
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1034654212 3684 LVYMISFLPYIVLLVLHNQLSFVNQTFLCLLSTTAFGQGVFFITF 3728
Cdd:pfam12698 274 GIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGLLRLIY 318
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3842-4051 |
1.38e-13 |
|
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: 70.94 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYEGHKaVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKnlqtdlsrvrMELGVCP 3921
Cdd:cd03221 1 IELENLSKTYGGKL-LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST----------VKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3922 QqdilldnltvrehlllfasikapqwtkkelhqqvnqtlqdvdltqhqhkqtraLSGGLKRKLSLGIAFMGMSRTVVLDE 4001
Cdd:cd03221 70 Q-----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1034654212 4002 PTSGVDPCSRHSLWDILLKYRegRTIIFTTHHLDEAEALSDRVAVLQHGR 4051
Cdd:cd03221 97 PTNHLDLESIEALEEALKEYP--GTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3857-4059 |
1.59e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.89 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3857 VVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTI----IINGKNLQT-------------DLSRVRMELGV 3919
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNhelitnpyskkikNFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3920 C---PQQDILLDNLtvrEHLLLFASIKAPQwTKKELHQQVNQTLQDVDL-TQHQHKQTRALSGGLKRKLSLGIAFMGMSR 3995
Cdd:PRK13631 121 VfqfPEYQLFKDTI---EKDIMFGPVALGV-KKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034654212 3996 TVVLDEPTSGVDPCSRHSLWDILLKYR-EGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPPF 4059
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKaNNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPY 261
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3842-4051 |
1.60e-13 |
|
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: 76.79 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYEGHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHP--PTSGTIIINGKNLQTDLSRVRMELGV 3919
Cdd:TIGR02633 2 LEMKGIVKTFGGVKAL-DGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3920 C--PQQDILLDNLTVREHLLLFASIKAP--QWTKKELHQQVNQTLQDVDLT-QHQHKQTRALSGGLKRKLSLGIAFMGMS 3994
Cdd:TIGR02633 81 ViiHQELTLVPELSVAENIFLGNEITLPggRMAYNAMYLRAKNLLRELQLDaDNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034654212 3995 RTVVLDEPTSGVDPCSRHSLWDIL--LKyREGRTIIFTTHHLDEAEALSDRVAVLQHGR 4051
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIrdLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3858-4052 |
2.02e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.20 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3858 VQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTdlsrvrmelgVCPQQ-------------- 3923
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVT----------RSPQDglangivyisedrk 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3924 -DILLDNLTVREHLLLFASIKAPQWTKKELHQQVNQTLQD-VDL----TQHQHKQTRALSGGLKRKLSLGIAFMGMSRTV 3997
Cdd:PRK10762 338 rDGLVLGMSVKENMSLTALRYFSRAGGSLKHADEQQAVSDfIRLfnikTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654212 3998 VLDEPTSGVDPCSRHSLWDILLKYR-EGRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
3861-4066 |
2.50e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.04 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3861 LSLTFYRDQITALLGTNGAGKTTIISMLTGLhPPTSGTIIINGKNLQT----DLSRVRMELGvcpQQDILLDNLTVREHL 3936
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAwsaaELARHRAYLS---QQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3937 LLFASIKAPqwtKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTV-------VLDEPTSGVDpC 4009
Cdd:PRK03695 91 TLHQPDKTR---TEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDInpagqllLLDEPMNSLD-V 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034654212 4010 SRHSLWDILLKY--REGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGP------PFCLKEAYG 4066
Cdd:PRK03695 167 AQQAALDRLLSElcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRrdevltPENLAQVFG 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3853-4051 |
2.58e-13 |
|
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: 76.26 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3853 GHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPpTSGTIIINGKNLQT----DLSRVRMELGVCPQ------ 3922
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGlsrrALRPLRRRMQVVFQdpfgsl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3923 ------QDIlldnltVREHLLlfasIKAPQWTKKELHQQVNQTLQDVDLT-QHQHKQTRALSGG------------LKRK 3983
Cdd:COG4172 376 sprmtvGQI------IAEGLR----VHGPGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGqrqriaiaraliLEPK 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3984 LslgiafmgmsrtVVLDEPTSGVDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGR 4051
Cdd:COG4172 446 L------------LVLDEPTSALDVSVQAQILDLLrdLQREHGLAYLFISHDLAVVRALAHRVMVMKDGK 503
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3847-4052 |
6.76e-13 |
|
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: 75.14 E-value: 6.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEGH-KAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT-DLSRVRMELGVCPQQD 3924
Cdd:TIGR02203 336 VTFRYPGRdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADyTLASLRRQVALVSQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3925 ILLDNlTVREHLLLFASIKAPQwtkkelhQQVNQTLQDVDLTQ---------HQHKQTRA--LSGGLKRKLSLGIAFMGM 3993
Cdd:TIGR02203 416 VLFND-TIANNIAYGRTEQADR-------AEIERALAAAYAQDfvdklplglDTPIGENGvlLSGGQRQRLAIARALLKD 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034654212 3994 SRTVVLDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDEAEAlSDRVAVLQHGRL 4052
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEK-ADRIVVMDDGRI 545
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3850-4052 |
8.80e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 72.05 E-value: 8.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3850 EYEGHKAVVQ--DLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTD-LSRVRMELGVCPQQ-DI 3925
Cdd:PRK13642 13 KYEKESDVNQlnGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnVWNLRRKIGMVFQNpDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3926 LLDNLTVREHLLLfaSIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSG 4005
Cdd:PRK13642 93 QFVGATVEDDVAF--GMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1034654212 4006 VDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAeALSDRVAVLQHGRL 4052
Cdd:PRK13642 171 LDPTGRQEIMRVIheIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
3872-4058 |
1.61e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.38 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3872 ALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNlQTDLSRVRMELGVCPQQDILLDNLTVREH--LLLFASIK--APQw 3947
Cdd:PRK10771 29 AILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRPVSMLFQENNLFSHLTVAQNigLGLNPGLKlnAAQ- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3948 tkkelHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYREGR-- 4025
Cdd:PRK10771 107 -----REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERql 181
|
170 180 190
....*....|....*....|....*....|...
gi 1034654212 4026 TIIFTTHHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:PRK10771 182 TLLMVSHSLEDAARIAPRSLVVADGRIAWDGPT 214
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3855-4052 |
1.75e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.41 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3855 KAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRMELGV--CP----QQDIL-- 3926
Cdd:PRK11288 266 PGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGImlCPedrkAEGIIpv 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3927 ---LDNLTV--REHLLLFASIKAPQWTKKELHQQVnqtlQDVDL-TQHQHKQTRALSGG------LKRKLSLGIafmgms 3994
Cdd:PRK11288 346 hsvADNINIsaRRHHLRAGCLINNRWEAENADRFI----RSLNIkTPSREQLIMNLSGGnqqkaiLGRWLSEDM------ 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034654212 3995 RTVVLDEPTSGVDPCSRHSLWDILLKYRE-GRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:PRK11288 416 KVILLDEPTRGIDVGAKHEIYNVIYELAAqGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3856-4053 |
1.84e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.81 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3856 AVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRMEL-----GVCPQQDILLDNL 3930
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakhvGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3931 TVREHLLLFASIKAPqwTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCS 4010
Cdd:PRK10584 104 NALENVELPALLRGE--SSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1034654212 4011 RHSLWDIL--LKYREGRTIIFTTHHLDEAeALSDRVAVLQHGRLR 4053
Cdd:PRK10584 182 GDKIADLLfsLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQ 225
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
3855-4057 |
7.15e-12 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 71.70 E-value: 7.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3855 KAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL----QTDLSRVrmeLGVCPQqDILLDNL 3930
Cdd:COG4618 345 RPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsqwdREELGRH---IGYLPQ-DVELFDG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3931 TVREHLLLFAS------IKAPQwtkkelhqqvnqtLQDV-DLTQHQHK--QTR------ALSGGLKRKLSLGIAFMGMSR 3995
Cdd:COG4618 421 TIAENIARFGDadpekvVAAAK-------------LAGVhEMILRLPDgyDTRigeggaRLSGGQRQRIGLARALYGDPR 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034654212 3996 TVVLDEPTSGVDPCSRHSLWDILLKYRE-GRTIIFTTHHLdEAEALSDRVAVLQHGRLRCCGP 4057
Cdd:COG4618 488 LVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGP 549
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3847-4051 |
1.04e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.91 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEGHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKN---------LQTDLSRVRMEL 3917
Cdd:PRK10982 4 ISKSFPGVKAL-DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfksskeaLENGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3918 GVCPQQDIlLDNLTVREHLLlfasiKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTV 3997
Cdd:PRK10982 83 NLVLQRSV-MDNMWLGRYPT-----KGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034654212 3998 VLDEPTSGVDPCSRHSLWDILLKYRE-GRTIIFTTHHLDEAEALSDRVAVLQHGR 4051
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLKErGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-82 |
1.51e-11 |
|
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: 71.58 E-value: 1.51e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654212 7 QFKALLWKNWLCRLRNPVLFLAEFFWPCILFVILTVLRFQEPPRYRDICYLQPRDLPSCGVIPFVQSLLCNTGSRC 82
Cdd:TIGR01257 6 QIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNANPLYSQHECHFPNKAMPSAGMLPWLQGIFCNVNNPC 81
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
3869-4051 |
1.53e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 70.68 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3869 QITALLGTNGAGKTTIISMLTG-LHPPT-SGTIIINGKNLQTDLSRvrmELGVCPQQDILLDNLTVREHLLLFASIKAPQ 3946
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGrIQGNNfTGTILANNRKPTKQILK---RTGFVTQDDILYPHLTVRETLVFCSLLRLPK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3947 -WTKKELHQQVNQTLQDVDLTQHQHKQT-----RALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLK 4020
Cdd:PLN03211 172 sLTKQEKILVAESVISELGLTKCENTIIgnsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS 251
|
170 180 190
....*....|....*....|....*....|...
gi 1034654212 4021 Y-REGRTIIFTTHH-LDEAEALSDRVAVLQHGR 4051
Cdd:PLN03211 252 LaQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3842-4066 |
1.56e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.92 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIIngknLQTDLSRVRMELGVCP 3921
Cdd:NF033858 2 ARLEGVSHRY-GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEV----LGGDMADARHRRAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3922 QqdI----------LLDNLTVREHLLLFA-----SikapqwtKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSL 3986
Cdd:NF033858 77 R--IaympqglgknLYPTLSVFENLDFFGrlfgqD-------AAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3987 GIAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYREGR---TIIFTTHHLDEAEALsDRVAVLQHGRLRCCGPPFCLKE 4063
Cdd:NF033858 148 CCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpgmSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLA 226
|
...
gi 1034654212 4064 AYG 4066
Cdd:NF033858 227 RTG 229
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3847-4051 |
2.37e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.13 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTdLSRVRMELGVC-PQQD- 3924
Cdd:PRK10790 346 VSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSS-LSHSVLRQGVAmVQQDp 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3925 -ILLDNltvrehllLFASIKAPQWTKKELHQQVNQTLQDVDLTQ------HQH--KQTRALSGGLKRKLSLGIAFMGMSR 3995
Cdd:PRK10790 425 vVLADT--------FLANVTLGRDISEEQVWQALETVQLAELARslpdglYTPlgEQGNNLSVGQKQLLALARVLVQTPQ 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034654212 3996 TVVLDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDE-AEAlsDRVAVLQHGR 4051
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTiVEA--DTILVLHRGQ 551
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3853-4048 |
2.69e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.66 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3853 GHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTdLS--RVRMELGVCPQQDILLDNl 3930
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST-LKpeIYRQQVSYCAQTPTLFGD- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3931 TVREHLLLFASI--KAPQwtkkelHQQVNQTLQDVDLTQHQ-HKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVD 4007
Cdd:PRK10247 96 TVYDNLIFPWQIrnQQPD------PAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034654212 4008 PCSRHSLWDILLKYREGRTI--IFTTHHLDEAEAlSDRVAVLQ 4048
Cdd:PRK10247 170 ESNKHNVNEIIHRYVREQNIavLWVTHDKDEINH-ADKVITLQ 211
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3851-4052 |
2.94e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.87 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3851 YEGhKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTsGTIIINGKNL-QTDLSRVRMELGVCPQQDILLDN 3929
Cdd:PRK11174 360 PDG-KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELrELDPESWRKHLSWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3930 lTVREHLLLfASIKAPQwtkkelhQQVNQTLQDVDLTQHQHK-----------QTRALSGGLKRKLSLGIAFMGMSRTVV 3998
Cdd:PRK11174 438 -TLRDNVLL-GNPDASD-------EQLQQALENAWVSEFLPLlpqgldtpigdQAAGLSVGQAQRLALARALLQPCQLLL 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1034654212 3999 LDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDEAEALsDRVAVLQHGRL 4052
Cdd:PRK11174 509 LDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQI 561
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3851-4045 |
3.70e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 66.73 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3851 YEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTII---SMLTGLHPP--TSGTIIINGKNL---QTDLSRVRMELGVCPQ 3922
Cdd:PRK14243 19 YYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPGfrVEGKVTFHGKNLyapDVDPVEVRRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3923 QDILLDNlTVREHLLLFASIKAPQWTKKELhqqVNQTLQDV---DLTQHQHKQT-RALSGGLKRKLSLGIAFMGMSRTVV 3998
Cdd:PRK14243 99 KPNPFPK-SIYDNIAYGARINGYKGDMDEL---VERSLRQAalwDEVKDKLKQSgLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1034654212 3999 LDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDEAEALSDRVA 4045
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3853-4048 |
6.47e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.83 E-value: 6.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3853 GHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKnlqtDLSRVRMELgvcpQQDILL----- 3927
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGE----PIRRQRDEY----HQDLLYlghqp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3928 ---DNLTVREHLLLFASIKAPQWTkkelhQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLgiAFMGMSRTV--VLDEP 4002
Cdd:PRK13538 84 gikTELTALENLRFYQRLHGPGDD-----EALWEALAQVGLAGFEDVPVRQLSAGQQRRVAL--ARLWLTRAPlwILDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034654212 4003 -----TSGVDPCSRHslwdILLKYREGRTIIFTTHHldEAEALSDRVAVLQ 4048
Cdd:PRK13538 157 ftaidKQGVARLEAL----LAQHAEQGGMVILTTHQ--DLPVASDKVRKLR 201
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3854-4058 |
8.85e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.00 E-value: 8.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3854 HKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPT--------SGTIIINGKNL-QTDLSRVRMELGVCPQQD 3924
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLaAIDAPRLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3925 ILLDNLTVREHLLL--FASIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGG-LKR--------KLSLGIAFMGM 3993
Cdd:PRK13547 93 QPAFAFSAREIVLLgrYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGeLARvqfarvlaQLWPPHDAAQP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034654212 3994 SRTVVLDEPTSGVDPCSRHSLWDILLKY-REGRTIIFT-THHLDEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAiVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3854-4053 |
1.11e-10 |
|
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: 67.54 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3854 HKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPT-SGTIIINGK--NLQTDLSRVRMELGVCPQ---QDILL 3927
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDIRNPAQAIRAGIAMVPEdrkRHGIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3928 DNLTVREHLLL-----FASIKAPQWTKKElhQQVNQTLQDVDL-TQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDE 4001
Cdd:TIGR02633 352 PILGVGKNITLsvlksFCFKMRIDAAAEL--QIIGSAIQRLKVkTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034654212 4002 PTSGVDPCSRHSLWDILLKY-REGRTIIFTTHHLDEAEALSDRVAVLQHGRLR 4053
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3847-4052 |
1.54e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 64.13 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSR----VRMELGVCPQ 3922
Cdd:PRK10908 7 VSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpfLRRQIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3923 QDILLDNLTVREHLLLFASIKAPqwTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEP 4002
Cdd:PRK10908 87 DHHLLMDRTVYDNVAIPLIIAGA--SGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034654212 4003 TSGVDPCSRHSLWDILLKY-REGRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:PRK10908 165 TGNLDDALSEGILRLFEEFnRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3854-4053 |
1.93e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.88 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3854 HKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHP-PTSGTIIINGKNLQTDLSRVRMELGVC------PQQDIL 3926
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQGIAmvpedrKRDGIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3927 LDnLTVREHLLLfASIKapQWTK-------KELHQqVNQTLQDVDL-TQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVV 3998
Cdd:PRK13549 354 PV-MGVGKNITL-AALD--RFTGgsriddaAELKT-ILESIQRLKVkTASPELAIARLSGGNQQKAVLAKCLLLNPKILI 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654212 3999 LDEPTSGVDPCSRHSLWDILLKY-REGRTIIFTTHHLDEAEALSDRVAVLQHGRLR 4053
Cdd:PRK13549 429 LDEPTRGIDVGAKYEIYKLINQLvQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
3842-4053 |
2.64e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 64.45 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYE---------------GHKA----VVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIIN 3902
Cdd:PRK13546 5 VNIKNVTKEYRiyrtnkermkdalipKHKNktffALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3903 GknlqtDLSRVRMELGVCPQQdILLDNLTVREHLLLFasikapqwTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKR 3982
Cdd:PRK13546 85 G-----EVSVIAISAGLSGQL-TGIENIEFKMLCMGF--------KRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034654212 3983 KLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYRE-GRTIIFTTHHLDEAEALSDRVAVLQHGRLR 4053
Cdd:PRK13546 151 KLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEqNKTIFFVSHNLGQVRQFCTKIAWIEGGKLK 222
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
3863-4008 |
2.72e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.33 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3863 LTFYRDQITALL--GTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT-DLSRVRMELGVCP--QQDI-LLDNLtvreHL 3936
Cdd:PRK13543 30 LDFHVDAGEALLvqGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRgDRSRFMAYLGHLPglKADLsTLENL----HF 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034654212 3937 LLFASIKAPQwtkkelhQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDP 4008
Cdd:PRK13543 106 LCGLHGRRAK-------QMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3857-4058 |
2.94e-10 |
|
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: 63.20 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3857 VVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT-DLSRVRMELGVCPQQDILLDNlTVREH 3935
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTIIPQDPTLFSG-TIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3936 LLLFAsikapQWTKKELHQQVNQTLQDVDLTQHQhkqtralsgglKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLW 4015
Cdd:cd03369 102 LDPFD-----EYSDEEIYGALRVSEGGLNLSQGQ-----------RQLLCLARALLKRPRVLVLDEATASIDYATDALIQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034654212 4016 DILLKYREGRTIIFTTHHLdEAEALSDRVAVLQHGRLRCCGPP 4058
Cdd:cd03369 166 KTIREEFTNSTILTIAHRL-RTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3858-4052 |
6.96e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.19 E-value: 6.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3858 VQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL--QTDLSRVRMELGVCPQ---QDILLDNLTV 3932
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAYITEsrrDNGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3933 REHLLLFASIKAPQW-------TKKELHQQVNQTLQDVDLTQHQHKQT-RALSGGLKRKLSLGIAFMGMSRTVVLDEPTS 4004
Cdd:PRK09700 359 AQNMAISRSLKDGGYkgamglfHEVDEQRTAENQRELLALKCHSVNQNiTELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1034654212 4005 GVDPCSRHSLWDILLKY-REGRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:PRK09700 439 GIDVGAKAEIYKVMRQLaDDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
3852-4057 |
1.15e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.41 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3852 EGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPP----TSGTIIINGKNLQTDLSRVRMELGVcpqqdilL 3927
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRKIATI-------M 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3928 DN--------LTVREHLL--LFASIKAPQwtkkelHQQVNQTLQDVDLTQHQhkqtRAL-------SGGLKRKLSLGIAF 3990
Cdd:PRK10418 86 QNprsafnplHTMHTHARetCLALGKPAD------DATLTAALEAVGLENAA----RVLklypfemSGGMLQRMMIALAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034654212 3991 MGMSRTVVLDEPTSGVDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGRLRCCGP 4057
Cdd:PRK10418 156 LCEAPFIIADEPTTDLDVVAQARILDLLesIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGD 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3842-4058 |
1.73e-09 |
|
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: 63.67 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYEGhKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGL--HPPTSGTIIIN----------------- 3902
Cdd:TIGR03269 1 IEVKNLTKKFDG-KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3903 ------GKNLQT------DLS-----RVRMELGVCPQQDI-LLDNLTVREHLllfasIKAPQWTKKELHQQVNQTLQDVD 3964
Cdd:TIGR03269 80 epcpvcGGTLEPeevdfwNLSdklrrRIRKRIAIMLQRTFaLYGDDTVLDNV-----LEALEEIGYEGKEAVGRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3965 LTQHQHKQT---RALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLK--YREGRTIIFTTHHLDEAEA 4039
Cdd:TIGR03269 155 MVQLSHRIThiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIED 234
|
250
....*....|....*....
gi 1034654212 4040 LSDRVAVLQHGRLRCCGPP 4058
Cdd:TIGR03269 235 LSDKAIWLENGEIKEEGTP 253
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3853-4050 |
1.92e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.57 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3853 GHKAVVQDLSLTFYRDQITALLGTNGAGKTTiismlTGLH----PPTSGTIIINGKNLQTdLSR-----VRMELGVCPQ- 3922
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKST-----TGLAllrlINSQGEIWFDGQPLHN-LNRrqllpVRHRIQVVFQd 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3923 -----------QDILLDNLTVREhlllfasikaPQWTKKELHQQVNQTLQDVDL-TQHQHKQTRALSGGLKRKLSLGIAF 3990
Cdd:PRK15134 371 pnsslnprlnvLQIIEEGLRVHQ----------PTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARAL 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034654212 3991 MGMSRTVVLDEPTSGVDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHG 4050
Cdd:PRK15134 441 ILKPSLIILDEPTSSLDKTVQAQILALLksLQQKHQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3857-4051 |
2.16e-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: 60.91 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3857 VVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRvrmelgvCPQQDILldnlTVREHL 3936
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQ-------ASPREIL----ALRRRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3937 LLFAS-----IkaPQWTKKELhqqVNQTLQDVDLTQHQ-HKQTRAL------------------SGGLKRKLSLGIAFMG 3992
Cdd:COG4778 95 IGYVSqflrvI--PRVSALDV---VAEPLLERGVDREEaRARARELlarlnlperlwdlppatfSGGEQQRVNIARGFIA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3993 MSRTVVLDEPTSGVDPCSRHSLWDILLKY-REGRTIIFTTHHLDEAEALSDRVAVLQHGR 4051
Cdd:COG4778 170 DPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3838-4051 |
2.97e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.10 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3838 SAPGVTLVSVTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKN-LQTDLSR---- 3912
Cdd:PRK11701 3 DQPLLSVRGLTKLY-GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgQLRDLYAlsea 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3913 -----VRMELGVCPQQDilLDNL--------TVREHLLL-----FASI--KAPQWtkkelhqqvnqtLQDVDLTQHQ-HK 3971
Cdd:PRK11701 82 errrlLRTEWGFVHQHP--RDGLrmqvsaggNIGERLMAvgarhYGDIraTAGDW------------LERVEIDAARiDD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3972 QTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQH 4049
Cdd:PRK11701 148 LPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLrgLVRELGLAVVIVTHDLAVARLLAHRLLVMKQ 227
|
..
gi 1034654212 4050 GR 4051
Cdd:PRK11701 228 GR 229
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
3854-4052 |
3.63e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 62.81 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3854 HKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL-QTDLSRVRMELGVCPQQDILLDNlTV 3932
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtKLQLDSWRSRLAVVSQTPFLFSD-TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3933 REHLLLfasiKAPQWTKKELHQQVN-QTLQDVDLTQHQHKQTRA------LSGGLKRKLSLGIAFMGMSRTVVLDEPTSG 4005
Cdd:PRK10789 406 ANNIAL----GRPDATQQEIEHVARlASVHDDILRLPQGYDTEVgergvmLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1034654212 4006 VDPCSRHSLWDILLKYREGRTIIFTTHHLdEAEALSDRVAVLQHGRL 4052
Cdd:PRK10789 482 VDGRTEHQILHNLRQWGEGRTVIISAHRL-SALTEASEILVMQHGHI 527
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3846-4051 |
6.93e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 61.73 E-value: 6.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3846 SVTKEYEGHKAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTS--GTIIINGKNLQ-TDLSR--------VR 3914
Cdd:NF040905 6 GITKTFPGVKAL-DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRfKDIRDsealgiviIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3915 MELGVCPQqdilldnLTVREHLLL---FASIKAPQWtkKELHQQVNQTLQDVDLtqHQHKQTRALSGGL-KRKLsLGIAf 3990
Cdd:NF040905 85 QELALIPY-------LSIAENIFLgneRAKRGVIDW--NETNRRARELLAKVGL--DESPDTLVTDIGVgKQQL-VEIA- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654212 3991 MGMSRTV---VLDEPTSGV-DPCSRHsLWDILLKYRE-GRTIIFTTHHLDEAEALSDRVAVLQHGR 4051
Cdd:NF040905 152 KALSKDVkllILDEPTAALnEEDSAA-LLDLLLELKAqGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3852-4066 |
9.71e-09 |
|
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: 62.27 E-value: 9.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3852 EGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNL-QTDLSRVRMELGVCPQQDILLDNl 3930
Cdd:TIGR00957 1296 EDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIaKIGLHDLRFKITIIPQDPVLFSG- 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3931 TVREHLLLFASIKAPQ-WTKKEL-HQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDP 4008
Cdd:TIGR00957 1375 SLRMNLDPFSQYSDEEvWWALELaHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034654212 4009 CSRHSLWDILLKYREGRTIIFTTHHLDEAEALSdRVAVLQHGRLRCCGPPFCLKEAYG 4066
Cdd:TIGR00957 1455 ETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQRG 1511
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3857-4033 |
9.92e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.42 E-value: 9.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3857 VVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRMELGVCPQQDILLDNLTVREHL 3936
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3937 LLfasikapqwtkkELH-----QQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSR 4011
Cdd:PRK13540 96 LY------------DIHfspgaVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSL 163
|
170 180
....*....|....*....|...
gi 1034654212 4012 HSLWDILLKYR-EGRTIIFTTHH 4033
Cdd:PRK13540 164 LTIITKIQEHRaKGGAVLLTSHQ 186
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
3870-4082 |
9.96e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 60.66 E-value: 9.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3870 ITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqtdlsrVRMELGVC--PQ--------QDI-LLDNLTVREHLLL 3938
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVL------FDAEKGIClpPEkrrigyvfQDArLFPHYKVRGNLRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3939 fasikapqWTKKELHQQVNQTlqdVDLTQHQHKQTR---ALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVD-PCSRHsl 4014
Cdd:PRK11144 100 --------GMAKSMVAQFDKI---VALLGIEPLLDRypgSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRE-- 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034654212 4015 wdiLLKY-----REGRT-IIFTTHHLDEAEALSDRVAVLQHGRLRCCGPpfcLKEAYG-QGLR--LTLTRQPSVLEA 4082
Cdd:PRK11144 167 ---LLPYlerlaREINIpILYVSHSLDEILRLADRVVVLEQGKVKAFGP---LEEVWAsSAMRpwLPKEEQSSILKV 237
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3849-4035 |
4.27e-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: 59.92 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3849 KEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLhPPTSGTIIINGKNLQT-DLSRVRMELGVCPQQDILL 3927
Cdd:TIGR01271 1226 KYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSvTLQTWRKAFGVIPQKVFIF 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3928 DNlTVREHLLLFAsikapQWTKKELHQQVNQTLQDVDLTQHQHKQT-------RALSGGLKRKLSLGIAFMGMSRTVVLD 4000
Cdd:TIGR01271 1305 SG-TFRKNLDPYE-----QWSDEEIWKVAEEVGLKSVIEQFPDKLDfvlvdggYVLSNGHKQLMCLARSILSKAKILLLD 1378
|
170 180 190
....*....|....*....|....*....|....*
gi 1034654212 4001 EPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLD 4035
Cdd:TIGR01271 1379 EPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVE 1413
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
3870-4057 |
6.45e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.47 E-value: 6.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3870 ITALLGTNGAGKTTIISMLTGLHPP--TSGTIIING--KNLQTdLSRVRmelGVCPQQDILLDNLTVREHLLLFASIKAP 3945
Cdd:PLN03140 908 LTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGfpKKQET-FARIS---GYCEQNDIHSPQVTVRESLIYSAFLRLP 983
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3946 -QWTKKELHQQVNQTLQDVDLTQHQHK-----QTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDpcSRHSLwdILL 4019
Cdd:PLN03140 984 kEVSKEEKMMFVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD--ARAAA--IVM 1059
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1034654212 4020 K-----YREGRTIIFTTHH--LDEAEALSDRVAVLQHGRLRCCGP 4057
Cdd:PLN03140 1060 RtvrntVDTGRTVVCTIHQpsIDIFEAFDELLLMKRGGQVIYSGP 1104
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
3852-4050 |
6.99e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.12 E-value: 6.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3852 EGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSgtiiingknlqtDLSRVRMELGVCPQQDILLDnlt 3931
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTP------------VAGCVDVPDNQFGREASLID--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3932 vreHLLLFASIKApqwtKKELHQQVNqtLQDVDLTQhqhKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDP--- 4008
Cdd:COG2401 105 ---AIGRKGDFKD----AVELLNAVG--LSDAVLWL---RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRqta 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1034654212 4009 --CSR--HSLWDillkyREGRTIIFTTHHLDEAEALS-DRVAVLQHG 4050
Cdd:COG2401 173 krVARnlQKLAR-----RAGITLVVATHHYDVIDDLQpDLLIFVGYG 214
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3842-4032 |
7.41e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.75 E-value: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEYEGhKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNlqtdlsrvrmELGVCP 3921
Cdd:PRK15064 320 LEVENLTKGFDN-GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA----------NIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3922 Q--QDILLDNLTVREHLllfasikaPQWTK-KELHQQVNQTLQDVDLTQHQ-HKQTRALSGGLKRKLSLGIAFMGMSRTV 3997
Cdd:PRK15064 389 QdhAYDFENDLTLFDWM--------SQWRQeGDDEQAVRGTLGRLLFSQDDiKKSVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170 180 190
....*....|....*....|....*....|....*
gi 1034654212 3998 VLDEPTSGVDPCSRHSLWDILLKYrEGrTIIFTTH 4032
Cdd:PRK15064 461 VMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSH 493
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
3841-4051 |
7.42e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.93 E-value: 7.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3841 GVTLVSVTKEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKnlqtdlsRV-RMElgv 3919
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGR-------VVnELE--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3920 cP-QQDI--------LLDNLTVREHLllfA-SIKAPQWTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSlgia 3989
Cdd:PRK11650 73 -PaDRDIamvfqnyaLYPHMSVRENM---AyGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVA---- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034654212 3990 fmgMSRTVV-------LDEPTSGVDPCSR-HSLWDIL-LKYREGRTIIFTTHhlDEAEA--LSDRVAVLQHGR 4051
Cdd:PRK11650 145 ---MGRAIVrepavflFDEPLSNLDAKLRvQMRLEIQrLHRRLKTTSLYVTH--DQVEAmtLADRVVVMNGGV 212
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
3837-4051 |
1.30e-07 |
|
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: 54.96 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3837 GSAPGVTLVSVTKEYEGHKA-VVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPT---SGTIIINGKNLQTDLSR 3912
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIpILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3913 VRMELGVCPQQDILLDNLTVREhLLLFAsikapqwtkkeLHQQVNQTLqdvdltqhqhkqtRALSGGLKRKLSLGIAFMG 3992
Cdd:cd03233 81 YPGEIIYVSEEDVHFPTLTVRE-TLDFA-----------LRCKGNEFV-------------RGISGGERKRVSIAEALVS 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034654212 3993 MSRTVVLDEPTSGVDPCSRHslwDILLKYRE-----GRTIIFTTHHL-DEAEALSDRVAVLQHGR 4051
Cdd:cd03233 136 RASVLCWDNSTRGLDSSTAL---EILKCIRTmadvlKTTTFVSLYQAsDEIYDLFDKVLVLYEGR 197
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3830-4034 |
1.41e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.12 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3830 NREGELEGSAPGVTLVSVTK--------EYEGHKAV--VQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTI 3899
Cdd:PTZ00265 363 NRKPLVENNDDGKKLKDIKKiqfknvrfHYDTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3900 IIN-GKNLQ-TDLSRVRMELGVCPQQDILLDNLTVREHLLLFASIKAPQWTKKELHQQVN-------------------- 3957
Cdd:PTZ00265 443 IINdSHNLKdINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYSLKDLEALSNYYNEDGNdsqenknkrnscrakcagdl 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3958 -------------------QTLQDVDLTQHQHK--------------------QTRALSGGLKRKLSLGIAFMGMSRTVV 3998
Cdd:PTZ00265 523 ndmsnttdsneliemrknyQTIKDSEVVDVSKKvlihdfvsalpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILI 602
|
250 260 270
....*....|....*....|....*....|....*...
gi 1034654212 3999 LDEPTSGVDPCSRHSLWDIL--LKYREGRTIIFTTHHL 4034
Cdd:PTZ00265 603 LDEATSSLDNKSEYLVQKTInnLKGNENRITIIIAHRL 640
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3847-3901 |
2.02e-07 |
|
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: 57.25 E-value: 2.02e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1034654212 3847 VTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIII 3901
Cdd:TIGR03719 328 LTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3840-4053 |
2.41e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.68 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3840 PGVTLVSVTKEY-----EGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIIngknlqtdlsrVR 3914
Cdd:PLN03232 610 PGAPAISIKNGYfswdsKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV-----------IR 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3915 MELGVCPQQDILLdNLTVREHLLlFASIKAPQWTKKELHQQVNQTLQDV----DLTQHQHKQTRaLSGGLKRKLSLGIAF 3990
Cdd:PLN03232 679 GSVAYVPQVSWIF-NATVRENIL-FGSDFESERYWRAIDVTALQHDLDLlpgrDLTEIGERGVN-ISGGQKQRVSMARAV 755
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034654212 3991 MGMSRTVVLDEPTSGVDPCSRHSLWDILLKYR-EGRTIIFTTHHLdEAEALSDRVAVLQHGRLR 4053
Cdd:PLN03232 756 YSNSDIYIFDDPLSALDAHVAHQVFDSCMKDElKGKTRVLVTNQL-HFLPLMDRIILVSEGMIK 818
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3847-4052 |
4.20e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.18 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEG-HKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQT-DLSRVRMELGVCPQQd 3924
Cdd:PRK11176 347 VTFTYPGkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDyTLASLRNQVALVSQN- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3925 ILLDNLTVREHLllfASIKAPQWTKKELHQQ---------VNQTLQDVDLTQHQHKQTraLSGGLKRKLSLGIAFMGMSR 3995
Cdd:PRK11176 426 VHLFNDTIANNI---AYARTEQYSREQIEEAarmayamdfINKMDNGLDTVIGENGVL--LSGGQRQRIAIARALLRDSP 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034654212 3996 TVVLDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLDEAEAlSDRVAVLQHGRL 4052
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEK-ADEILVVEDGEI 556
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3857-4051 |
6.67e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.48 E-value: 6.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3857 VVQDLSLTFYRDQITALLGTNGAGKT-TIISMLTGLHPP----TSGTIIINGKNL-----QTdLSRVR-MELGVCPQQDI 3925
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLlhaseQT-LRGVRgNKIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3926 L----LDNL--TVREHLLLFASIKapqwtKKELHQQVNQTLQDVDLTQ---------HQhkqtraLSGGLKRKLSLGIAF 3990
Cdd:PRK15134 103 VslnpLHTLekQLYEVLSLHRGMR-----REAARGEILNCLDRVGIRQaakrltdypHQ------LSGGERQRVMIAMAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034654212 3991 MGMSRTVVLDEPTSGVDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGR 4051
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLreLQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
3861-4053 |
7.06e-07 |
|
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: 55.57 E-value: 7.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3861 LSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKnlqtdlsrvrmelgvcpqqdiLLDNLTVREHLLLFA 3940
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ---------------------PVTADNREAYRQLFS 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3941 SI--------KAPQWTKKELHQQVNQTLQDVDLtqhQHK--------QTRALSGGLKRKLSLGIAFMgMSRTV-VLDEPT 4003
Cdd:COG4615 410 AVfsdfhlfdRLLGLDGEADPARARELLERLEL---DHKvsvedgrfSTTDLSQGQRKRLALLVALL-EDRPIlVFDEWA 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1034654212 4004 SGVDPCSRHSLW-DIL--LKyREGRTIIFTTHhlDEAE-ALSDRVAVLQHGRLR 4053
Cdd:COG4615 486 ADQDPEFRRVFYtELLpeLK-ARGKTVIAISH--DDRYfDLADRVLKMDYGKLV 536
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
3818-4056 |
9.98e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.56 E-value: 9.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3818 NENFDNKGSSLQNREGELEGSAPGVTLVSVTKEYEGH-KAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTS 3896
Cdd:PTZ00243 635 SRHIVEGGTGGGHEATPTSERSAKTPKMKTDDFFELEpKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISE 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3897 GtiiingknlqtdlsRVRME--LGVCPQQDILLdNLTVREHLLLFASIKApqwtkKELHQQVNQTLQDVDLTQ------- 3967
Cdd:PTZ00243 715 G--------------RVWAErsIAYVPQQAWIM-NATVRGNILFFDEEDA-----ARLADAVRVSQLEADLAQlggglet 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3968 HQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDP-CSRHSLWDILLKYREGRTIIFTTHHLdEAEALSDRVAV 4046
Cdd:PTZ00243 775 EIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAhVGERVVEECFLGALAGKTRVLATHQV-HVVPRADYVVA 853
|
250
....*....|
gi 1034654212 4047 LQHGRLRCCG 4056
Cdd:PTZ00243 854 LGDGRVEFSG 863
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3847-3901 |
1.28e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 1.28e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1034654212 3847 VTKEYeGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIII 3901
Cdd:PRK11819 330 LSKSF-GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3858-4052 |
1.82e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3858 VQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTD------------LSRVRMELGVCPQQDI 3925
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHnaneainhgfalVTEERRSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3926 LLDNL--TVREH-----LLLFASIKA-PQWTKKELHQQvnqtlqdvdlTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTV 3997
Cdd:PRK10982 344 GFNSLisNIRNYknkvgLLDNSRMKSdTQWVIDSMRVK----------TPGHRTQIGSLSGGNQQKVIIGRWLLTQPEIL 413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654212 3998 VLDEPTSGVDPCSRHSLWDILLKY-REGRTIIFTTHHLDEAEALSDRVAVLQHGRL 4052
Cdd:PRK10982 414 MLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3842-4053 |
3.88e-06 |
|
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: 51.78 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3842 VTLVSVTKEY-EGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLhPPTSGTIIINGKNLQT-DLSRVRMELGV 3919
Cdd:cd03289 3 MTVKDLTAKYtEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSvPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3920 CPQQdILLDNLTVREHLLLFAsikapQWTKKELHQQVNQTLQDVDLTQHQHKQT-------RALSGGLKRKLSLGIAFMG 3992
Cdd:cd03289 82 IPQK-VFIFSGTFRKNLDPYG-----KWSDEEIWKVAEEVGLKSVIEQFPGQLDfvlvdggCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034654212 3993 MSRTVVLDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHLdEAEALSDRVAVLQHGRLR 4053
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKVR 215
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3855-4051 |
5.22e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.02 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3855 KAVvQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLqTDLSRVRMELGVCPQQDILLDNLTVRE 3934
Cdd:PRK15079 35 KAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDL-LGMKDDEWRAVRSDIQMIFQDPLASLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3935 HLLLFASIKA-------PQWTKKELHQQVNQTLQDVDL-----TQHQHKqtraLSGGLKRKLSLGIAFMGMSRTVVLDEP 4002
Cdd:PRK15079 113 PRMTIGEIIAeplrtyhPKLSRQEVKDRVKAMMLKVGLlpnliNRYPHE----FSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034654212 4003 TSGVDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGR 4051
Cdd:PRK15079 189 VSALDVSIQAQVVNLLqqLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 239
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
3856-4034 |
6.36e-06 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 50.41 E-value: 6.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3856 AVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKN-----LQTDLSRVRMELGVCPQQDILLdNL 3930
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNesepsFEATRSRNRYSVAYAAQKPWLL-NA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3931 TVREHLLLFASIKapqwtkKELHQQVNQ--TLQ-DVDLTQHQhKQTRA------LSGGLKRKLSLGIAFMGMSRTVVLDE 4001
Cdd:cd03290 94 TVEENITFGSPFN------KQRYKAVTDacSLQpDIDLLPFG-DQTEIgerginLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 1034654212 4002 PTSGVD-PCSRHSLWDILLKY--REGRTIIFTTHHL 4034
Cdd:cd03290 167 PFSALDiHLSDHLMQEGILKFlqDDKRTLVLVTHKL 202
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3847-4053 |
1.18e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.51 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3847 VTKEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKnlqtdlsrvrmelgvcpqqdiL 3926
Cdd:PRK10522 328 VTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK---------------------P 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3927 LDNLTVREHLLLFASI------------KAPQWTKKELHQQVNQTLQDVDLTQHQHKQ--TRALSGGLKRKLSLGIAFMG 3992
Cdd:PRK10522 387 VTAEQPEDYRKLFSAVftdfhlfdqllgPEGKPANPALVEKWLERLKMAHKLELEDGRisNLKLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034654212 3993 MSRTVVLDEPTSGVDPCSRHSLWDILLKY-RE-GRTIIFTTHHlDEAEALSDRVAVLQHGRLR 4053
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFYQVLLPLlQEmGKTIFAISHD-DHYFIHADRLLEMRNGQLS 528
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3843-4032 |
2.47e-05 |
|
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: 50.32 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3843 TLVSVTKEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIingknLQTDLSrvrmeLGVCPQ 3922
Cdd:TIGR03719 6 TMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR-----PQPGIK-----VGYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3923 QDILLDNLTVREHLLL-FASIKAPQWTKKELHQQVNQ-------------TLQD----VDLTQHQHKQTRA--------- 3975
Cdd:TIGR03719 76 EPQLDPTKTVRENVEEgVAEIKDALDRFNEISAKYAEpdadfdklaaeqaELQEiidaADAWDLDSQLEIAmdalrcppw 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034654212 3976 ------LSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYrEGrTIIFTTH 4032
Cdd:TIGR03719 156 dadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY-PG-TVVAVTH 216
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
3860-4032 |
9.87e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.40 E-value: 9.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3860 DLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIIngKNLQTDlSRVRMELGVCPQQDILLDNLTVREHLLLF 3939
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY--KNCNIN-NIAKPYCTYIGHNLGLKLEMTVFENLKFW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3940 ASIKAPQWTkkelhqqVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWD-IL 4018
Cdd:PRK13541 95 SEIYNSAET-------LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNlIV 167
|
170
....*....|....
gi 1034654212 4019 LKYREGRTIIFTTH 4032
Cdd:PRK13541 168 MKANSGGIVLLSSH 181
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3869-4007 |
1.49e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3869 QITALLGTNGAGKTT----IISMLTGLHPPTSGTIIINGKNLQTDLSRVRMELGVCPQQDILLDNLTVREHLLLFASIKA 3944
Cdd:TIGR00956 88 ELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAARCKT 167
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034654212 3945 PQWTKKELHQQV-NQTLQDVDLTQHQHKQT----------RALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVD 4007
Cdd:TIGR00956 168 PQNRPDGVSREEyAKHIADVYMATYGLSHTrntkvgndfvRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3873-4034 |
1.86e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3873 LLGTNGAGKTTIISMLTGLHPPTSGTIiingknlqtDLSRvRMELGVCPQQDilLDNLTVREHLLLFASIKAPQwtkkEL 3952
Cdd:PRK10636 343 LLGRNGAGKSTLIKLLAGELAPVSGEI---------GLAK-GIKLGYFAQHQ--LEFLRADESPLQHLARLAPQ----EL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3953 HQQVNQTLQDVDLTQHQ-HKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHSLWDILLKYREGRTIIFTT 4031
Cdd:PRK10636 407 EQKLRDYLGGFGFQGDKvTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHD 486
|
...
gi 1034654212 4032 HHL 4034
Cdd:PRK10636 487 RHL 489
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3855-4007 |
2.43e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.25 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3855 KAVVQDLSLTFYR-DQItALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQTDLSRVRMELGvcPQQDIlLDNLT-- 3931
Cdd:PRK11147 332 KQLVKDFSAQVQRgDKI-ALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELD--PEKTV-MDNLAeg 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3932 --------VREHLLLFasikapqwtkkelhqqvnqtLQDVdLTQHQHKQT--RALSGGLKRKLSLGIAFMGMSRTVVLDE 4001
Cdd:PRK11147 408 kqevmvngRPRHVLGY--------------------LQDF-LFHPKRAMTpvKALSGGERNRLLLARLFLKPSNLLILDE 466
|
....*.
gi 1034654212 4002 PTSGVD 4007
Cdd:PRK11147 467 PTNDLD 472
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3843-3934 |
5.26e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.27 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3843 TLVSVTKEYEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIingknLQTDLSrvrmeLGVCPQ 3922
Cdd:PRK11819 8 TMNRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR-----PAPGIK-----VGYLPQ 77
|
90
....*....|..
gi 1034654212 3923 QDILLDNLTVRE 3934
Cdd:PRK11819 78 EPQLDPEKTVRE 89
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
3976-4038 |
6.48e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.50 E-value: 6.48e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034654212 3976 LSGGLKRKLSLGIAFMGMSR----TVVLDEPTSGVDPCSRHSLWDILLKYR-EGRTIIFTTHHLDEAE 4038
Cdd:cd03227 78 LSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAE 145
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3857-4007 |
1.28e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.35 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3857 VVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKNLQ----TDLSRVrmeLGVCPQQDILLDNlTV 3932
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfglTDLRRV---LSIIPQSPVLFSG-TV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3933 REHLLLFASIK-APQWtkKELHQQvnqTLQDV------DLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSG 4005
Cdd:PLN03232 1327 RFNIDPFSEHNdADLW--EALERA---HIKDVidrnpfGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
..
gi 1034654212 4006 VD 4007
Cdd:PLN03232 1402 VD 1403
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3872-4007 |
1.66e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.73 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3872 ALLGTNGAGKTTIISMLTGLHPPTSGTIIIngknlqtdlsrVRMELGVCPQQDILLdNLTVREHLLLFASIKAPQWTK-- 3949
Cdd:PLN03130 647 AIVGSTGEGKTSLISAMLGELPPRSDASVV-----------IRGTVAYVPQVSWIF-NATVRDNILFGSPFDPERYERai 714
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3950 --KELHQQVnQTLQDVDLTQHQHKQTRaLSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVD 4007
Cdd:PLN03130 715 dvTALQHDL-DLLPGGDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
3869-4047 |
2.00e-03 |
|
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: 43.12 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3869 QITALLGTNGAGKTTIISMLTGLHPPTSG---------TIIIN--GKNLQTDLSRVR---MELGVCPQQ-DILLDNLTVR 3933
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdEILDEfrGSELQNYFTKLLegdVKVIVKPQYvDLIPKAVKGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3934 EHLLLfasikapqwTKKELHQQVNQTLQDVDLTQHQHKQTRALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPCSRHS 4013
Cdd:cd03236 107 VGELL---------KKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLN 177
|
170 180 190
....*....|....*....|....*....|....*
gi 1034654212 4014 LWDILLKY-REGRTIIFTTHHLDEAEALSDRVAVL 4047
Cdd:cd03236 178 AARLIRELaEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3857-4050 |
4.54e-03 |
|
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: 43.36 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3857 VVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKnlqtdlsrvrmeLGVCPQQDILLDNlTVREHL 3936
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR------------ISFSPQTSWIMPG-TIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3937 LLFASIKAPQWTkkelhQQVNQTLQDVDLTQHQHKQTR-------ALSGGLKRKLSLGIAFMGMSRTVVLDEPTSGVDPC 4009
Cdd:TIGR01271 508 IFGLSYDEYRYT-----SVIKACQLEEDIALFPEKDKTvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1034654212 4010 SRHSLWD-ILLKYREGRTIIFTTHHLDEAEAlSDRVAVLQHG 4050
Cdd:TIGR01271 583 TEKEIFEsCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3856-4051 |
4.64e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.92 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3856 AVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTI--------------IINGKNLQTDLSRVR-MELGVC 3920
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqvIELSEQSAAQMRHVRgADMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3921 PQQDILLDN--LTVREHLLlfASIKAPQ-WTKKELHQQVNQTLQDVDLTQHQHKQTR---ALSGGLKRKLSLGIAFMGMS 3994
Cdd:PRK10261 110 FQEPMTSLNpvFTVGEQIA--ESIRLHQgASREEAMVEAKRMLDQVRIPEAQTILSRyphQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034654212 3995 RTVVLDEPTSGVDPCSRHSLWDIL--LKYREGRTIIFTTHHLDEAEALSDRVAVLQHGR 4051
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIkvLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
3840-4050 |
4.81e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3840 PGVTLVSVTKE---YEGHKAVVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKnlqtdlsrVRMe 3916
Cdd:PLN03073 504 PGPPIISFSDAsfgYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK--------VRM- 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3917 lGVCPQQDIllDNLTVREHLLLFASIKAPqwtkKELHQQVNQTLQDVDLTQHQHKQTR-ALSGGLKRKLSLGIAFMGMSR 3995
Cdd:PLN03073 575 -AVFSQHHV--DGLDLSSNPLLYMMRCFP----GVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPH 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3996 TVVLDEPTSGVDPCSRHSLWDILLKYREGRTIIFTTHHL-----DEAEALSDRVAVLQHG 4050
Cdd:PLN03073 648 ILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLisgsvDELWVVSEGKVTPFHG 707
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
3857-4050 |
5.51e-03 |
|
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: 42.15 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3857 VVQDLSLTFYRDQITALLGTNGAGKTTIISMLTGLHPPTSGTIIINGKnlqtdlsrvrmeLGVCPQQDILLDNlTVREHL 3936
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR------------ISFSSQFSWIMPG-TIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654212 3937 LLFAS---------IKAPQWTKK--ELHQQVNQTLQDVDLTqhqhkqtraLSGGLKRKLSLGIAFMGMSRTVVLDEPTSG 4005
Cdd:cd03291 119 IFGVSydeyryksvVKACQLEEDitKFPEKDNTVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1034654212 4006 VDPCSRHSLWD-ILLKYREGRTIIFTTHHLDEAEAlSDRVAVLQHG 4050
Cdd:cd03291 190 LDVFTEKEIFEsCVCKLMANKTRILVTSKMEHLKK-ADKILILHEG 234
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
3976-4032 |
8.24e-03 |
|
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: 41.61 E-value: 8.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034654212 3976 LSGGLKRKLSLGIAFMGM---SRTVVLDEPTSGVDPCSRHSLWDILLKYREGRT-IIFTTH 4032
Cdd:pfam13304 237 LSDGTKRLLALLAALLSAlpkGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAqLILTTH 297
|
|
| |
