|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
885-987 |
3.03e-67 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 224.40 E-value: 3.03e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 885 VKFRSSTQLHELTPHHQSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTACKENTSQYFFITP 964
Cdd:cd03277 111 VKFREGEQLQELDPHHQSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETACKEGTSQYFLITP 190
|
90 100
....*....|....*....|...
gi 358248353 965 KLLQNLPYSEKMTVLFVYNGPHM 987
Cdd:cd03277 191 KLLPGLNYHEKMTVLCVYNGPHI 213
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
1-120 |
1.03e-41 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 151.98 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 1 MIIGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFVKRGCSKGLVEIELFRTSGnliitreidviknqsfwfinkkpv 80
Cdd:cd03277 27 MIIGPNGSGKSSIVCAICLGLGGKPKLLGRAKKVGEFVKRGCDEGTIEIELYGNPG------------------------ 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 358248353 81 tqkiveeqvaalNIQVGNLCQFLPQDKVGEFAKLSKIELL 120
Cdd:cd03277 83 ------------NIQVDNLCQFLPQDRVGEFAKLSPIELL 110
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
120-963 |
1.21e-19 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 95.12 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 120 LEATEKSVGPPEMHRYHCELKNFREKEKQLETSCKEKTEYLE-----------KMVQRNERYKQDVERFYERKRHLDLIE 188
Cdd:TIGR02168 222 LRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQeleekleelrlEVSELEEEIEELQKELYALANEISRLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 189 MlEAKRPWVEYENVRQEYEGVKLIRDRVKEEVRKLKEGQIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDL 268
Cdd:TIGR02168 302 Q-QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 269 IERKDRQIKELQQALTVKQNE--ELDRQK-----RISNTRKMIEDLQSELKTAE------NCENLQPQIDTVTNDLRRVQ 335
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEieRLEARLerledRRERLQQEIEELLKKLEEAElkelqaELEELEEELEELQEELERLE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 336 EEKALCEGEIIDKQREKEMLEKQRRSVSDHITRFDNLMNQKEDKlrqryrdtYDAVLWLRNNRDRFKQRVcePIMLTINM 415
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF--------SEGVKALLKNQSGLSGIL--GVLSELIS 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 416 KDNKNAKYVENHISSNdLRAFVFESQEDMEIFLREVRDNKKLRVNAVIAPKISYADKAPSRSLNDLKQYGFFSYLRELFD 495
Cdd:TIGR02168 531 VDEGYEAAIEAALGGR-LQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVK 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 496 APD---PVMSYLCCQYHI-----------------------------------------HEVPVGTERTRERIERVIQE- 530
Cdd:TIGR02168 610 FDPklrKALSYLLGGVLVvddldnalelakklrpgyrivtldgdlvrpggvitggsaktNSSILERRREIEELEEKIEEl 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 531 ------------TRLKQIYTAEEKYVLKTSVYSNKVISSNTSLKVAQFLTVTVD--LEQRRHLEEQLKEMNRQLEAVDSG 596
Cdd:TIGR02168 690 eekiaelekalaELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqlEERIAQLSKELTELEAEIEELEER 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 597 LAALRDT-------------------------NRHLELKDNELRLKKKELLERKTRKRQLEQKISSKLASIRLMEQDTCN 651
Cdd:TIGR02168 770 LEEAEEElaeaeaeieeleaqieqlkeelkalREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 652 LEEEERKASTKIKEINVQKAKLVTELTGLVKICTSFQIQKVDLILQNTTVISEKNKLEADYMASSSQLRVTEQQFIELDD 731
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 732 NRQRLLQKCKELMKKARQVCNLSADQAVPQEFQTAFQdlpntLDEIDALLTEERSRASCFTGLNPSvVVEEYSkrevEIQ 811
Cdd:TIGR02168 930 RLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDD-----EEEARRRLKRLENKIKELGPVNLA-AIEEYE----ELK 999
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 812 QLTEELQGKKVELDEYREN----ISQVKERWLNPLKELVEKINEKFSNFFSSMQCAGEVDLHTENEEDYDKYGIRIRVKF 887
Cdd:TIGR02168 1000 ERYDFLTAQKEDLTEAKETleeaIEEIDREARERFKDTFDQVNENFQRVFPKLFGGGEAELRLTDPEDLLEAGIEIFAQP 1079
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 888 --RSSTQLHELtphhqSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVvntacKE--NTSQYFFIT 963
Cdd:TIGR02168 1080 pgKKNQNLSLL-----SGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLL-----KEfsKNTQFIVIT 1149
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2-963 |
3.38e-12 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 70.77 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 2 IIGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFV----KRGCSKGLVEI-------ELFRTSGNLIITREIdVIKNQ 70
Cdd:pfam02463 28 IVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIhsksGAFVNSAEVEItfdnedhELPIDKEEVSIRRRV-YRGGD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 71 SFWFINKKPVTQKIVEEQVAALNIQVGNLCQFLPQDKV--------------------GEFAKLSKIELLEATEKSVGPP 130
Cdd:pfam02463 107 SEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIeiiammkperrleieeeaagSRLKRKKKEALKKLIEETENLA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 131 EMHRYHCELKNFREKEKQLETSCKEKTEYLEKMVQRNERYKQDVERFYERKRHLDLIEMLEAKRPWVEYENVRQEYEG-- 208
Cdd:pfam02463 187 ELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEek 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 209 ---VKLIRDRVKEEVRKLKEGQIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQALTV 285
Cdd:pfam02463 267 laqVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 286 K------------------QNEELDRQKRISNTRKMIEDLQSELKTAEN---CENLQPQIDTVTNDLRRVQE-------- 336
Cdd:pfam02463 347 LeikreaeeeeeeeleklqEKLEQLEEELLAKKKLESERLSSAAKLKEEeleLKSEEEKEAQLLLELARQLEdllkeekk 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 337 ---EKALCEGEIIDKQREKEMLEKQRRSVSDHITRFDNLMNQKEDKLRQRYRDT------YDAVLWLRNNRDRFKQRVCE 407
Cdd:pfam02463 427 eelEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVklqeqlELLLSRQKLEERSQKESKAR 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 408 PimlTINMKDNKNAKYVENHISSNDLRAFVFESQEDME---IFLREVRDNKKLRVNAVIAPKISYADKAPSRSLNDLKQY 484
Cdd:pfam02463 507 S---GLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYkvaISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLL 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 485 GFFSYLRELFDAPDPVMSYL-CCQYHIHEVPVGTERTRERIERVIQETRLKQiyTAEEKYVLKTSVYSNKVISSNTSLKV 563
Cdd:pfam02463 584 IPKLKLPLKSIAVLEIDPILnLAQLDKATLEADEDDKRAKVVEGILKDTELT--KLKESAKAKESGLRKGVSLEEGLAEK 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 564 AQFLTVTVDLEQRRHLEEQLKEMNRQLEAVDSGLAALRDTNRHLELKDNELRLKKKELLERKTRKRQLEQKISSKLASIR 643
Cdd:pfam02463 662 SEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLL 741
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 644 LMEQDTCN-------------------------------------------------LEEEERKASTKIKEINVQKAKLV 674
Cdd:pfam02463 742 KQKIDEEEeeeeksrlkkeekeeekselslkekelaeerekteklkveeekeeklkaQEEELRALEEELKEEAELLEEEQ 821
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 675 TELTGLVKICT---------SFQIQKVDLILQNTTVISEKNKLEADYMASSSQLRVTEQQFIELDDN--RQRLLQKCKEL 743
Cdd:pfam02463 822 LLIEQEEKIKEeeleelaleLKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELesKEEKEKEEKKE 901
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 744 MKKARQVCNLSADQAVPQEFQTAFQDLPNT------------------LDEIDALLTEERS----RASCFTGLNPSVVVE 801
Cdd:pfam02463 902 LEEESQKLNLLEEKENEIEERIKEEAEILLkyeeepeellleeadekeKEENNKEEEEERNkrllLAKEELGKVNLMAIE 981
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 802 EYSKREVEIQQLTEELQGKKVELDEYRENISQVKERWLNPLKELVEKINEKFSNFFSSMQCAGEVDLHTENEEDYDKYGI 881
Cdd:pfam02463 982 EFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGI 1061
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 882 RIRVKFRSSTQLHELTphhQSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTAckeNTSQYFF 961
Cdd:pfam02463 1062 EISARPPGKGVKNLDL---LSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELS---KNAQFIV 1135
|
..
gi 358248353 962 IT 963
Cdd:pfam02463 1136 IS 1137
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
168-784 |
9.12e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 9.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 168 ERYKQDVERFYERKRHLDLIEmleakRPWVEYENVRQEYEGVKLIRDRVKEEVRKLKEGQIpmTRRIEEIDRQRHTLEVR 247
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIR-----ELAERYAAARERLAELEYLRAALRLWFAQRRLELL--EAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 248 IKEKSTDIKEASQKCKQ-RQDLIERKDRQIKELQQALTVKQNEELDRQKRISNTRKMIEDLQSELKT-----AENCENLQ 321
Cdd:COG4913 311 LERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAsaeefAALRAEAA 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 322 PQIDTVTNDLRRVQEEKALCEGEIIDKQREKEMLEKQRRSvsdhitrfdnlmnqkedkLRQRyRDTYDAvlWLRNNRDRF 401
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS------------------LERR-KSNIPA--RLLALRDAL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 402 KQR----------VCEpiMLTINMKDNK--NAkyVENHISSNDLRAFVFESQEDMeiFLREVRDNK-KLRVNAVIAPKIS 468
Cdd:COG4913 450 AEAlgldeaelpfVGE--LIEVRPEEERwrGA--IERVLGGFALTLLVPPEHYAA--ALRWVNRLHlRGRLVYERVRTGL 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 469 YADKAPSRSLNDL------KQYGFFSYLRELFDAPdpvMSYLCCQyhihevpvgTERTRERIERVIQETRL-KQIYTAEE 541
Cdd:COG4913 524 PDPERPRLDPDSLagkldfKPHPFRAWLEAELGRR---FDYVCVD---------SPEELRRHPRAITRAGQvKGNGTRHE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 542 KYVlKTSVYSNKVISSNTSLKVAQFLTVTVDLEQRRH-LEEQLKEMNRQLEAVDSGLAALRdtnRHLELKDNELRLK--K 618
Cdd:COG4913 592 KDD-RRRIRSRYVLGFDNRAKLAALEAELAELEEELAeAEERLEALEAELDALQERREALQ---RLAEYSWDEIDVAsaE 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 619 KELLERKTRKRQLEQKiSSKLASIRLMEQDtcnLEEEERKASTKIKEINVQKAKLVTELTGLVKictsfQIQKVDLILQN 698
Cdd:COG4913 668 REIAELEAELERLDAS-SDDLAALEEQLEE---LEAELEELEEELDELKGEIGRLEKELEQAEE-----ELDELQDRLEA 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 699 TTVISEKNKLE------ADYMASSSQLRVTEQQFIELDDNRQRLLQKCKELMKKARQVCNlsADQAVPQEFQTAFQDLPN 772
Cdd:COG4913 739 AEDLARLELRAlleerfAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNR--EWPAETADLDADLESLPE 816
|
650
....*....|..
gi 358248353 773 TLDEIDALLTEE 784
Cdd:COG4913 817 YLALLDRLEEDG 828
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
2-162 |
1.50e-07 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 52.88 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 2 IIGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFV------KRGCSKGLVEIELFRTSG--NLIITREIDVIKN---- 69
Cdd:pfam13476 23 ITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKgdirigLEGKGKAYVEITFENNDGryTYAIERSRELSKKkgkt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 70 --QSFWFINKKPVTQKIVEEQVAALNIQVgNLCQFLPQDKVGEFAKLSKIELLEATEKSVGPPEmhryhcELKNFREKEK 147
Cdd:pfam13476 103 kkKEILEILEIDELQQFISELLKSDKIIL-PLLVFLGQEREEEFERKEKKERLEELEKALEEKE------DEKKLLEKLL 175
|
170
....*....|....*
gi 358248353 148 QLETSCKEKTEYLEK 162
Cdd:pfam13476 176 QLKEKKKELEELKEE 190
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
573-836 |
1.83e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 573 LEQRRHLEEQLKEMNRQLEAVDSGLAALRDTNRHLELKDNELRLKKKELLERKTRKRQLEQKISSKLASIRLMEQDTCNL 652
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 653 EEEERKASTKIKEINvQKAKLVTELTGLVKictsfqiQKVDLILQNTTVISEKNKLEADYMASSSQLRVTEQQFIELDDN 732
Cdd:PRK03918 265 EERIEELKKEIEELE-EKVKELKELKEKAE-------EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 733 RQRLlqkcKELMKKARQVcnlsadqavpQEFQTAFQDLPNTLDEIDALLTEERSRASCFTGLNPSVVVEEY---SKREVE 809
Cdd:PRK03918 337 EERL----EELKKKLKEL----------EKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELeelEKAKEE 402
|
250 260 270
....*....|....*....|....*....|.
gi 358248353 810 IQQLTEELQGKKVELD----EYRENISQVKE 836
Cdd:PRK03918 403 IEEEISKITARIGELKkeikELKKAIEELKK 433
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-62 |
2.13e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.46 E-value: 2.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 358248353 2 IIGANGTGKSSIVCAICLGLAGKPAfmGRADKVGFFVKRGCSKGLVEIELFRTSGNLIITR 62
Cdd:COG0419 28 IVGPNGAGKSTILEAIRYALYGKAR--SRSKLRSDLINVGSEEASVELEFEHGGKRYRIER 86
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
154-353 |
6.58e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 43.46 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 154 KEKTEYLEKMVQrnerykqDVERFYERKRH---LDLIEMLEA-KRPWVEYENVRQEYEGVKLIR----------DRVKEE 219
Cdd:NF033838 61 KEVESHLEKILS-------EIQKSLDKRKHtqnVALNKKLSDiKTEYLYELNVLKEKSEAELTSktkkeldaafEQFKKD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 220 VRKLKEGQIPMTRRIEEI----------DRQRH------TLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQAL 283
Cdd:NF033838 134 TLEPGKKVAEATKKVEEAekkakdqkeeDRRNYptntykTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQAKAKV 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 358248353 284 TVKQnEELDRQKRISNTRKMIEDLQSELKTAENCENLQPQIDTVTND-LRRVQEEKALCEGEIIDKQREKE 353
Cdd:NF033838 214 ESKK-AEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDkPKRRAKRGVLGEPATPDKKENDA 283
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
885-987 |
3.03e-67 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 224.40 E-value: 3.03e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 885 VKFRSSTQLHELTPHHQSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTACKENTSQYFFITP 964
Cdd:cd03277 111 VKFREGEQLQELDPHHQSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETACKEGTSQYFLITP 190
|
90 100
....*....|....*....|...
gi 358248353 965 KLLQNLPYSEKMTVLFVYNGPHM 987
Cdd:cd03277 191 KLLPGLNYHEKMTVLCVYNGPHI 213
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
1-120 |
1.03e-41 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 151.98 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 1 MIIGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFVKRGCSKGLVEIELFRTSGnliitreidviknqsfwfinkkpv 80
Cdd:cd03277 27 MIIGPNGSGKSSIVCAICLGLGGKPKLLGRAKKVGEFVKRGCDEGTIEIELYGNPG------------------------ 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 358248353 81 tqkiveeqvaalNIQVGNLCQFLPQDKVGEFAKLSKIELL 120
Cdd:cd03277 83 ------------NIQVDNLCQFLPQDRVGEFAKLSPIELL 110
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
901-983 |
4.78e-28 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 111.63 E-value: 4.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 901 QSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTACkeNTSQYFFITPKLLQNLPYSEKMTVLF 980
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAK--HTSQFIVITLKKEMFENADKLIGVLF 172
|
...
gi 358248353 981 VYN 983
Cdd:cd03239 173 VHG 175
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
120-963 |
1.21e-19 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 95.12 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 120 LEATEKSVGPPEMHRYHCELKNFREKEKQLETSCKEKTEYLE-----------KMVQRNERYKQDVERFYERKRHLDLIE 188
Cdd:TIGR02168 222 LRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQeleekleelrlEVSELEEEIEELQKELYALANEISRLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 189 MlEAKRPWVEYENVRQEYEGVKLIRDRVKEEVRKLKEGQIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDL 268
Cdd:TIGR02168 302 Q-QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 269 IERKDRQIKELQQALTVKQNE--ELDRQK-----RISNTRKMIEDLQSELKTAE------NCENLQPQIDTVTNDLRRVQ 335
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEieRLEARLerledRRERLQQEIEELLKKLEEAElkelqaELEELEEELEELQEELERLE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 336 EEKALCEGEIIDKQREKEMLEKQRRSVSDHITRFDNLMNQKEDKlrqryrdtYDAVLWLRNNRDRFKQRVcePIMLTINM 415
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF--------SEGVKALLKNQSGLSGIL--GVLSELIS 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 416 KDNKNAKYVENHISSNdLRAFVFESQEDMEIFLREVRDNKKLRVNAVIAPKISYADKAPSRSLNDLKQYGFFSYLRELFD 495
Cdd:TIGR02168 531 VDEGYEAAIEAALGGR-LQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVK 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 496 APD---PVMSYLCCQYHI-----------------------------------------HEVPVGTERTRERIERVIQE- 530
Cdd:TIGR02168 610 FDPklrKALSYLLGGVLVvddldnalelakklrpgyrivtldgdlvrpggvitggsaktNSSILERRREIEELEEKIEEl 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 531 ------------TRLKQIYTAEEKYVLKTSVYSNKVISSNTSLKVAQFLTVTVD--LEQRRHLEEQLKEMNRQLEAVDSG 596
Cdd:TIGR02168 690 eekiaelekalaELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqlEERIAQLSKELTELEAEIEELEER 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 597 LAALRDT-------------------------NRHLELKDNELRLKKKELLERKTRKRQLEQKISSKLASIRLMEQDTCN 651
Cdd:TIGR02168 770 LEEAEEElaeaeaeieeleaqieqlkeelkalREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 652 LEEEERKASTKIKEINVQKAKLVTELTGLVKICTSFQIQKVDLILQNTTVISEKNKLEADYMASSSQLRVTEQQFIELDD 731
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 732 NRQRLLQKCKELMKKARQVCNLSADQAVPQEFQTAFQdlpntLDEIDALLTEERSRASCFTGLNPSvVVEEYSkrevEIQ 811
Cdd:TIGR02168 930 RLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDD-----EEEARRRLKRLENKIKELGPVNLA-AIEEYE----ELK 999
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 812 QLTEELQGKKVELDEYREN----ISQVKERWLNPLKELVEKINEKFSNFFSSMQCAGEVDLHTENEEDYDKYGIRIRVKF 887
Cdd:TIGR02168 1000 ERYDFLTAQKEDLTEAKETleeaIEEIDREARERFKDTFDQVNENFQRVFPKLFGGGEAELRLTDPEDLLEAGIEIFAQP 1079
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 888 --RSSTQLHELtphhqSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVvntacKE--NTSQYFFIT 963
Cdd:TIGR02168 1080 pgKKNQNLSLL-----SGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLL-----KEfsKNTQFIVIT 1149
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
899-987 |
1.27e-17 |
|
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: 81.25 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 899 HHQSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTACKenTSQYFFITPKLLQNLPYSEKMTV 978
Cdd:cd03227 76 LQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVK--GAQVIVITHLPELAELADKLIHI 153
|
....*....
gi 358248353 979 LFVYNGPHM 987
Cdd:cd03227 154 KKVITGVYK 162
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-962 |
2.85e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 87.43 E-value: 2.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 2 IIGANGTGKSSIVCAI--CLGLAGKPAFmgRADKVGFFV---KRGCSKGLVEIELF------RTSGNLIITREIDVIKN- 69
Cdd:TIGR02169 28 ISGPNGSGKSNIGDAIlfALGLSSSKAM--RAERLSDLIsngKNGQSGNEAYVTVTfknddgKFPDELEVVRRLKVTDDg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 70 -QSFWFINKKPVTQKIVEEQVAALNIQVGNLcQFLPQDKVGEFAKLSKIELLEATEKSVGPPEMHR----YHCELKNFRE 144
Cdd:TIGR02169 106 kYSYYYLNGQRVRLSEIHDFLAAAGIYPEGY-NVVLQGDVTDFISMSPVERRKIIDEIAGVAEFDRkkekALEELEEVEE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 145 KEKQLETSCKEKTEYLEKM-VQRN--ERYK--QDVERFYERKRHLDLIEMLEAKRPWVEYE--NVRQEYEGVK-LIRDRV 216
Cdd:TIGR02169 185 NIERLDLIIDEKRQQLERLrREREkaERYQalLKEKREYEGYELLKEKEALERQKEAIERQlaSLEEELEKLTeEISELE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 217 KE-------------EVRKLKEG-QIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQA 282
Cdd:TIGR02169 265 KRleeieqlleelnkKIKDLGEEeQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 283 LTVKQNEELDRQKRISNTRKMIEDLQSEL---------------KTAENCENLQPQIDTVTNDLRRVQEEKALCEGEI-- 345
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEELEDLRAELeevdkefaetrdelkDYREKLEKLKREINELKRELDRLQEELQRLSEELad 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 346 -------------------------IDKQREK-EMLEKQRRSVSDHITRFDNLMNQKEDKLRQRYRDTYDAVLWLRNNRD 399
Cdd:TIGR02169 425 lnaaiagieakineleeekedkaleIKKQEWKlEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 400 RFKQRVCEPIMLTINMK------------DNKNAKYVENhISSNDLRAFVFESQEDMEIFLREVRDNKKLRVNAVIAPKI 467
Cdd:TIGR02169 505 RVRGGRAVEEVLKASIQgvhgtvaqlgsvGERYATAIEV-AAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKM 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 468 syadKAPSRSLNDLKQYGFFSYLRELFDAPD---PVMSYLCCQYHIHE--------------------------VPVGTE 518
Cdd:TIGR02169 584 ----RDERRDLSILSEDGVIGFAVDLVEFDPkyePAFKYVFGDTLVVEdieaarrlmgkyrmvtlegelfeksgAMTGGS 659
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 519 RTRERIERVIQETRLKQIYTAEEKYVLKTSVYS---------NKVISSNTSLKVAQFLTVTVDLE------QRRHLEEQL 583
Cdd:TIGR02169 660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSlqselrrieNRLDELSQELSDASRKIGEIEKEieqleqEEEKLKERL 739
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 584 KEMNRQLEAVDSGLAALRDTNRHLE--LKDNELRLKKKELLERKTRKRQLEQKISSKLASIRLMEQDTCNLEEEERKAST 661
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEarIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 662 KIKEINVQKAKLVTELTGLVKICTSFQIQKVDLILQNTTVISEKNKLEADYMASSSQLRVTEQQFIELDDNRQRLLQKCK 741
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 742 ELMKKARQVcNLSADQAVPQ--EFQTAFQDLPNTLDEIDALLTEERSRASCFTGLNpsVVVEEYSKREVEIQQLTE---- 815
Cdd:TIGR02169 900 ELERKIEEL-EAQIEKKRKRlsELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE--DVQAELQRVEEEIRALEPvnml 976
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 816 -------------ELQGKKVELDEYRENISQVKERwLNPLK-----ELVEKINEKFSNFFSSMQcAGEVDLHTENEEDYD 877
Cdd:TIGR02169 977 aiqeyeevlkrldELKEKRAKLEEERKAILERIEE-YEKKKrevfmEAFEAINENFNEIFAELS-GGTGELILENPDDPF 1054
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 878 KYGIRIRVKFRSST--QLHELtphhqSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVvntacKEN 955
Cdd:TIGR02169 1055 AGGLELSAKPKGKPvqRLEAM-----SGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLI-----REK 1124
|
....*..
gi 358248353 956 TSQYFFI 962
Cdd:TIGR02169 1125 AGEAQFI 1131
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
902-979 |
2.11e-13 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 69.93 E-value: 2.11e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 358248353 902 SGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTACKENTSQYFFITPKLLQNLPYSEKMTVL 979
Cdd:cd03276 111 SGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAKKQPGRQFIFITPQDISGLASSDDVKVF 188
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2-963 |
3.38e-12 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 70.77 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 2 IIGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFV----KRGCSKGLVEI-------ELFRTSGNLIITREIdVIKNQ 70
Cdd:pfam02463 28 IVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIhsksGAFVNSAEVEItfdnedhELPIDKEEVSIRRRV-YRGGD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 71 SFWFINKKPVTQKIVEEQVAALNIQVGNLCQFLPQDKV--------------------GEFAKLSKIELLEATEKSVGPP 130
Cdd:pfam02463 107 SEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIeiiammkperrleieeeaagSRLKRKKKEALKKLIEETENLA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 131 EMHRYHCELKNFREKEKQLETSCKEKTEYLEKMVQRNERYKQDVERFYERKRHLDLIEMLEAKRPWVEYENVRQEYEG-- 208
Cdd:pfam02463 187 ELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEek 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 209 ---VKLIRDRVKEEVRKLKEGQIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQALTV 285
Cdd:pfam02463 267 laqVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 286 K------------------QNEELDRQKRISNTRKMIEDLQSELKTAEN---CENLQPQIDTVTNDLRRVQE-------- 336
Cdd:pfam02463 347 LeikreaeeeeeeeleklqEKLEQLEEELLAKKKLESERLSSAAKLKEEeleLKSEEEKEAQLLLELARQLEdllkeekk 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 337 ---EKALCEGEIIDKQREKEMLEKQRRSVSDHITRFDNLMNQKEDKLRQRYRDT------YDAVLWLRNNRDRFKQRVCE 407
Cdd:pfam02463 427 eelEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVklqeqlELLLSRQKLEERSQKESKAR 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 408 PimlTINMKDNKNAKYVENHISSNDLRAFVFESQEDME---IFLREVRDNKKLRVNAVIAPKISYADKAPSRSLNDLKQY 484
Cdd:pfam02463 507 S---GLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYkvaISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLL 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 485 GFFSYLRELFDAPDPVMSYL-CCQYHIHEVPVGTERTRERIERVIQETRLKQiyTAEEKYVLKTSVYSNKVISSNTSLKV 563
Cdd:pfam02463 584 IPKLKLPLKSIAVLEIDPILnLAQLDKATLEADEDDKRAKVVEGILKDTELT--KLKESAKAKESGLRKGVSLEEGLAEK 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 564 AQFLTVTVDLEQRRHLEEQLKEMNRQLEAVDSGLAALRDTNRHLELKDNELRLKKKELLERKTRKRQLEQKISSKLASIR 643
Cdd:pfam02463 662 SEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLL 741
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 644 LMEQDTCN-------------------------------------------------LEEEERKASTKIKEINVQKAKLV 674
Cdd:pfam02463 742 KQKIDEEEeeeeksrlkkeekeeekselslkekelaeerekteklkveeekeeklkaQEEELRALEEELKEEAELLEEEQ 821
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 675 TELTGLVKICT---------SFQIQKVDLILQNTTVISEKNKLEADYMASSSQLRVTEQQFIELDDN--RQRLLQKCKEL 743
Cdd:pfam02463 822 LLIEQEEKIKEeeleelaleLKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELesKEEKEKEEKKE 901
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 744 MKKARQVCNLSADQAVPQEFQTAFQDLPNT------------------LDEIDALLTEERS----RASCFTGLNPSVVVE 801
Cdd:pfam02463 902 LEEESQKLNLLEEKENEIEERIKEEAEILLkyeeepeellleeadekeKEENNKEEEEERNkrllLAKEELGKVNLMAIE 981
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 802 EYSKREVEIQQLTEELQGKKVELDEYRENISQVKERWLNPLKELVEKINEKFSNFFSSMQCAGEVDLHTENEEDYDKYGI 881
Cdd:pfam02463 982 EFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGI 1061
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 882 RIRVKFRSSTQLHELTphhQSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTAckeNTSQYFF 961
Cdd:pfam02463 1062 EISARPPGKGVKNLDL---LSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELS---KNAQFIV 1135
|
..
gi 358248353 962 IT 963
Cdd:pfam02463 1136 IS 1137
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1-51 |
4.85e-11 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 62.71 E-value: 4.85e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 358248353 1 MIIGANGTGKSSIVCAICLGLAGKPAFMGRADKV---GFFVKRGCSKGLVEIEL 51
Cdd:cd03239 26 AIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLflaGGGVKAGINSASVEITF 79
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
168-784 |
9.12e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 9.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 168 ERYKQDVERFYERKRHLDLIEmleakRPWVEYENVRQEYEGVKLIRDRVKEEVRKLKEGQIpmTRRIEEIDRQRHTLEVR 247
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIR-----ELAERYAAARERLAELEYLRAALRLWFAQRRLELL--EAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 248 IKEKSTDIKEASQKCKQ-RQDLIERKDRQIKELQQALTVKQNEELDRQKRISNTRKMIEDLQSELKT-----AENCENLQ 321
Cdd:COG4913 311 LERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAsaeefAALRAEAA 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 322 PQIDTVTNDLRRVQEEKALCEGEIIDKQREKEMLEKQRRSvsdhitrfdnlmnqkedkLRQRyRDTYDAvlWLRNNRDRF 401
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS------------------LERR-KSNIPA--RLLALRDAL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 402 KQR----------VCEpiMLTINMKDNK--NAkyVENHISSNDLRAFVFESQEDMeiFLREVRDNK-KLRVNAVIAPKIS 468
Cdd:COG4913 450 AEAlgldeaelpfVGE--LIEVRPEEERwrGA--IERVLGGFALTLLVPPEHYAA--ALRWVNRLHlRGRLVYERVRTGL 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 469 YADKAPSRSLNDL------KQYGFFSYLRELFDAPdpvMSYLCCQyhihevpvgTERTRERIERVIQETRL-KQIYTAEE 541
Cdd:COG4913 524 PDPERPRLDPDSLagkldfKPHPFRAWLEAELGRR---FDYVCVD---------SPEELRRHPRAITRAGQvKGNGTRHE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 542 KYVlKTSVYSNKVISSNTSLKVAQFLTVTVDLEQRRH-LEEQLKEMNRQLEAVDSGLAALRdtnRHLELKDNELRLK--K 618
Cdd:COG4913 592 KDD-RRRIRSRYVLGFDNRAKLAALEAELAELEEELAeAEERLEALEAELDALQERREALQ---RLAEYSWDEIDVAsaE 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 619 KELLERKTRKRQLEQKiSSKLASIRLMEQDtcnLEEEERKASTKIKEINVQKAKLVTELTGLVKictsfQIQKVDLILQN 698
Cdd:COG4913 668 REIAELEAELERLDAS-SDDLAALEEQLEE---LEAELEELEEELDELKGEIGRLEKELEQAEE-----ELDELQDRLEA 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 699 TTVISEKNKLE------ADYMASSSQLRVTEQQFIELDDNRQRLLQKCKELMKKARQVCNlsADQAVPQEFQTAFQDLPN 772
Cdd:COG4913 739 AEDLARLELRAlleerfAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNR--EWPAETADLDADLESLPE 816
|
650
....*....|..
gi 358248353 773 TLDEIDALLTEE 784
Cdd:COG4913 817 YLALLDRLEEDG 828
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
2-162 |
1.50e-07 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 52.88 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 2 IIGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFV------KRGCSKGLVEIELFRTSG--NLIITREIDVIKN---- 69
Cdd:pfam13476 23 ITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKgdirigLEGKGKAYVEITFENNDGryTYAIERSRELSKKkgkt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 70 --QSFWFINKKPVTQKIVEEQVAALNIQVgNLCQFLPQDKVGEFAKLSKIELLEATEKSVGPPEmhryhcELKNFREKEK 147
Cdd:pfam13476 103 kkKEILEILEIDELQQFISELLKSDKIIL-PLLVFLGQEREEEFERKEKKERLEELEKALEEKE------DEKKLLEKLL 175
|
170
....*....|....*
gi 358248353 148 QLETSCKEKTEYLEK 162
Cdd:pfam13476 176 QLKEKKKELEELKEE 190
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
232-386 |
3.28e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 232 RRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQALTVKQNEELDRQKRISNTRKMIEDLQSEL 311
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 358248353 312 K-TAENCENLQPQIDTVTNDLRRVQEEKALCEGEIIDKQREKEMLEKQRRSVSDHITRFDNLMNQKEDKLRQRYRD 386
Cdd:COG1196 312 ReLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
2-51 |
8.43e-07 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 50.67 E-value: 8.43e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 358248353 2 IIGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFVKRGCSKGLVEIEL 51
Cdd:cd03276 26 IVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLIKDGESSAKITVTL 75
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
155-383 |
1.11e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.82 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 155 EKTEYLEKMvqRNERYKQDVERFYERKRHLDLIEMLEAKRPWVEY----ENVRQEYEGVKLIRDRVKEEVRKLKEGQIPM 230
Cdd:pfam17380 345 ERERELERI--RQEERKRELERIRQEEIAMEISRMRELERLQMERqqknERVRQELEAARKVKILEEERQRKIQQQKVEM 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 231 TR-RIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQALTVKQNEELDRQKRISNTRKMIEDLQS 309
Cdd:pfam17380 423 EQiRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELE 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 310 ELKTA----ENCENL------QPQIDTVTNDLRRVQEEKALCEGEIIDKQREKEMLEK--QRRSVSDHITRFDNLMNQKE 377
Cdd:pfam17380 503 ERKQAmieeERKRKLlekemeERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKatEERSRLEAMEREREMMRQIV 582
|
....*.
gi 358248353 378 DKLRQR 383
Cdd:pfam17380 583 ESEKAR 588
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1-51 |
1.39e-06 |
|
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: 49.28 E-value: 1.39e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 358248353 1 MIIGANGTGKSSIVCAICLGLAGKPAFMGRadkvGFFVKRGCSKGLVEIEL 51
Cdd:cd03227 25 IITGPNGSGKSTILDAIGLALGGAQSATRR----RSGVKAGCIVAAVSAEL 71
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
573-836 |
1.83e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 573 LEQRRHLEEQLKEMNRQLEAVDSGLAALRDTNRHLELKDNELRLKKKELLERKTRKRQLEQKISSKLASIRLMEQDTCNL 652
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 653 EEEERKASTKIKEINvQKAKLVTELTGLVKictsfqiQKVDLILQNTTVISEKNKLEADYMASSSQLRVTEQQFIELDDN 732
Cdd:PRK03918 265 EERIEELKKEIEELE-EKVKELKELKEKAE-------EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 733 RQRLlqkcKELMKKARQVcnlsadqavpQEFQTAFQDLPNTLDEIDALLTEERSRASCFTGLNPSVVVEEY---SKREVE 809
Cdd:PRK03918 337 EERL----EELKKKLKEL----------EKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELeelEKAKEE 402
|
250 260 270
....*....|....*....|....*....|.
gi 358248353 810 IQQLTEELQGKKVELD----EYRENISQVKE 836
Cdd:PRK03918 403 IEEEISKITARIGELKkeikELKKAIEELKK 433
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
143-383 |
1.92e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 143 REKEKQLETsckekteyLEKMVQRNERYKQDVERFYERKRHLDLIEMLEAKRpwvEYENVRQEYEGVKLIRDRVKEEVRK 222
Cdd:COG1196 196 GELERQLEP--------LERQAEKAERYRELKEELKELEAELLLLKLRELEA---ELEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 223 LKEgqipmtrRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQ--------RQDLIERKDRqIKELQQALTVKQNEELDRQ 294
Cdd:COG1196 265 LEA-------ELEELRLELEELELELEEAQAEEYELLAELARleqdiarlEERRRELEER-LEELEEELAELEEELEELE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 295 KRISNTRKMIEDLQSELKTAENcenlqpQIDTVTNDLRRVQEEKALCEGEIIDKQREKEMLEKQRRSVSDHITRFDNLMN 374
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEA------ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
....*....
gi 358248353 375 QKEDKLRQR 383
Cdd:COG1196 411 ALLERLERL 419
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-360 |
2.09e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 1 MIIGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFVKRGCSKGLVEIELFRTSGNLIITREIDviKNQSFWFINKKPV 80
Cdd:PRK03918 27 LIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGGSGTEIELKFEKNGRKYRIVRSFN--RGESYLKYLDGSE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 81 TQKIVEEQVAALNIQVGNLCQFLPQDKV--GEFAKLskIELLEATEKSVGP-PEMHRYHCELKNFREKEKQLETSCKEKT 157
Cdd:PRK03918 105 VLEEGDSSVREWVERLIPYHVFLNAIYIrqGEIDAI--LESDESREKVVRQiLGLDDYENAYKNLGEVIKEIKRRIERLE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 158 EYLEKMVQRNERYKQDVERFYERKRHLDLIEMLEAKRPwVEYENVRQEYEGVKLIRDRVkEEVRKLKEGQIPMTRRIEEI 237
Cdd:PRK03918 183 KFIKRTENIEELIKEKEKELEEVLREINEISSELPELR-EELEKLEKEVKELEELKEEI-EELEKELESLEGSKRKLEEK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 238 DRQrhtLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKelQQALTVKQNEELDR-QKRISNTRKMIEDLQSELKTAEN 316
Cdd:PRK03918 261 IRE---LEERIEELKKEIEELEEKVKELKELKEKAEEYIK--LSEFYEEYLDELREiEKRLSRLEEEINGIEERIKELEE 335
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 358248353 317 CENlqpQIDTVTNDLRRVQEEKALCEGEIIDKQREKEMLEKQRR 360
Cdd:PRK03918 336 KEE---RLEELKKKLKELEKRLEELEERHELYEEAKAKKEELER 376
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
574-852 |
5.73e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 574 EQRRHLEEQLKEMNRQLEAVDSGLAALRDTNRHLELKDNELRLKKKELLERKTRKRQLEQKISSKLASIRLMEQDTCNLE 653
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 654 EEERKASTKIKEINVQKAKLVTELTGLVKICTSFQIQKVDLILQNTTVISEKNKLEADYMASSSQLRVTEQQFIELDDNR 733
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 734 QRLLQkckELMKKARQVCNLSADQAVPQE-FQTAFQDLPNTLDEIDALLTEERSRAScftglnpsvVVEEYSKREVEIQQ 812
Cdd:COG1196 382 EELAE---ELLEALRAAAELAAQLEELEEaEEALLERLERLEEELEELEEALAELEE---------EEEEEEEALEEAAE 449
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 358248353 813 LTEELQGKKVELDEYRENISQVKERWLNPLKELVEKINEK 852
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
138-379 |
9.74e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 9.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 138 ELKNFREKEKQLETSCKEKTEYLEKMVQRNERYKQDVERFYERKRHLDL---------------IEMLEAkrpwvEYENV 202
Cdd:TIGR04523 350 ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESkiqnqeklnqqkdeqIKKLQQ-----EKELL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 203 RQEYEGVKLIRDRVKEEVRKLKEGQIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQA 282
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 283 LTVKQNEELDRQKRISNTRKMIEDLQSELKTAENcenlqpQIDTVTNDLRRVQEE--KALCEGEIIDKQREKEMLEKQRR 360
Cdd:TIGR04523 505 KKELEEKVKDLTKKISSLKEKIEKLESEKKEKES------KISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQK 578
|
250
....*....|....*....
gi 358248353 361 SVSDHITRFDNLMNQKEDK 379
Cdd:TIGR04523 579 SLKKKQEEKQELIDQKEKE 597
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
138-316 |
1.02e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 138 ELKNFREKEKQLETSCKEKTEYLEKMVQRNERYKQDVERFYERKRHLDliEMLEAKRPWVEYENVRQEYEGVKLIRDRVK 217
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE--KLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 218 EEVRKLKEGQIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRqdlIERKDRQIKELQQALTVKQNEELDRQKRI 297
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE---LEELQQRLAELEEELEEAQEELEELEEEL 229
|
170
....*....|....*....
gi 358248353 298 SNTRKMIEDLQSELKTAEN 316
Cdd:COG4717 230 EQLENELEAAALEERLKEA 248
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
214-375 |
1.19e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 214 DRVKEEVRKLKEgqipMTRRIEEIDRQRHTLEvRIKEKSTDIKEASQKCKQRQDLIERkdRQIKELQQALTVKQNEeldr 293
Cdd:COG4913 228 DALVEHFDDLER----AHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAA--LRLWFAQRRLELLEAE---- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 294 qkrisntrkmIEDLQSELKTAEN-CENLQPQIDTVTNDLRRVQEEKALCEGEIIDK-QREKEMLEKQRRSVSDHITRFDN 371
Cdd:COG4913 297 ----------LEELRAELARLEAeLERLEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEA 366
|
....
gi 358248353 372 LMNQ 375
Cdd:COG4913 367 LLAA 370
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
146-364 |
1.24e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.66 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 146 EKQLETSCKEKTEYLekmvQRNERYKQDVERfyERKRHLDLIEMLEAKRPWVEYENVRQEyEGVKLIRDRVKEEVRKLKE 225
Cdd:pfam07888 33 QNRLEECLQERAELL----QAQEAANRQREK--EKERYKRDREQWERQRRELESRVAELK-EELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 226 GQIPMTRRIEEID---RQRHTLEVRIKEKSTDIKEASQKCKQRQDLIER-KDRQikelQQALTVKQNEELDRQKRISNTR 301
Cdd:pfam07888 106 LSASSEELSEEKDallAQRAAHEARIRELEEDIKTLTQRVLERETELERmKERA----KKAGAQRKEEEAERKQLQAKLQ 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 358248353 302 KMIEDLQSELKTAENCENLQPQIDTVTNDLRRVQEEKALCEGEIIDKQREKEMLEKQRRSVSD 364
Cdd:pfam07888 182 QTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQE 244
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
235-310 |
1.38e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 1.38e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 358248353 235 EEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQALTVKQNEELDRQKRISNTRKMIEDLQSE 310
Cdd:PRK12704 64 EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
186-364 |
1.90e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 186 LIEMLEAKRPWVEYENVRQEYEGVKLIRDrVKEEVRKLKEGQ---IPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKC 262
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKE-LEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 263 KQRQDLIERKD--RQIKELQ---QALTVKQNEELDRQKRISNTRKMIEDLQSELKTAENCENLQ--PQIDTVTNDLRRVQ 335
Cdd:COG4717 126 QLLPLYQELEAleAELAELPerlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAteEELQDLAEELEELQ 205
|
170 180
....*....|....*....|....*....
gi 358248353 336 EEKALCEGEIIDKQREKEMLEKQRRSVSD 364
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLEN 234
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-62 |
2.13e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.46 E-value: 2.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 358248353 2 IIGANGTGKSSIVCAICLGLAGKPAfmGRADKVGFFVKRGCSKGLVEIELFRTSGNLIITR 62
Cdd:COG0419 28 IVGPNGAGKSTILEAIRYALYGKAR--SRSKLRSDLINVGSEEASVELEFEHGGKRYRIER 86
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
204-313 |
2.28e-04 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 43.27 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 204 QEYEGVKLIRDRVKE---EVRKLKEGQIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRqdlIERKDRQIKELQ 280
Cdd:pfam06785 80 LDAEGFKILEETLEElqsEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEEQ---LAEKQLLINEYQ 156
|
90 100 110
....*....|....*....|....*....|....
gi 358248353 281 QAlTVKQNEELD-RQKRISNTRKMIEDLQSELKT 313
Cdd:pfam06785 157 QT-IEEQRSVLEkRQDQIENLESKVRDLNYEIKT 189
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
902-963 |
2.43e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 43.22 E-value: 2.43e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 358248353 902 SGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTAckeNTSQYFFIT 963
Cdd:cd03278 115 SGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFS---KETQFIVIT 173
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
213-382 |
3.86e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 213 RDRVKEEVRKLKEGQIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQALTVKQNEELD 292
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 293 R----QKRISNTRKMI----EDLQSELKTAENCENLQP----QIDTVTNDLRRVQEEKALCEGEIIDKQREKEMLEKQRR 360
Cdd:COG4942 109 LlralYRLGRQPPLALllspEDFLDAVRRLQYLKYLAParreQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180
....*....|....*....|..
gi 358248353 361 SVSDHITRFDNLMNQKEDKLRQ 382
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAE 210
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
154-353 |
6.58e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 43.46 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 154 KEKTEYLEKMVQrnerykqDVERFYERKRH---LDLIEMLEA-KRPWVEYENVRQEYEGVKLIR----------DRVKEE 219
Cdd:NF033838 61 KEVESHLEKILS-------EIQKSLDKRKHtqnVALNKKLSDiKTEYLYELNVLKEKSEAELTSktkkeldaafEQFKKD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 220 VRKLKEGQIPMTRRIEEI----------DRQRH------TLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQAL 283
Cdd:NF033838 134 TLEPGKKVAEATKKVEEAekkakdqkeeDRRNYptntykTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQAKAKV 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 358248353 284 TVKQnEELDRQKRISNTRKMIEDLQSELKTAENCENLQPQIDTVTND-LRRVQEEKALCEGEIIDKQREKE 353
Cdd:NF033838 214 ESKK-AEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDkPKRRAKRGVLGEPATPDKKENDA 283
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
138-374 |
9.86e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.50 E-value: 9.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 138 ELKNFREKEKQLETSCKEKTEYLEKMVQRNERYKQDV-------------ERFYERKRHLDLI--EMLEAKRPWV-EYEN 201
Cdd:TIGR01612 1487 ELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVtellnkysalaikNKFAKTKKDSEIIikEIKDAHKKFIlEAEK 1566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 202 VRQEYEGVKLIRDRVKEEVRKLKEGQipmtRRIEEIDRQRHTLEVRIKeKSTDIKEASQKCKQRQDLIERKDRQIKELQQ 281
Cdd:TIGR01612 1567 SEQKIKEIKKEKFRIEDDAAKNDKSN----KAAIDIQLSLENFENKFL-KISDIKKKINDCLKETESIEKKISSFSIDSQ 1641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 282 ALTVKQNEELDRQ-----KRISNTRKMIEDLQSELktaencENLQPQIDTVTNDlrrVQEEKALCEGEIIDKQRE----- 351
Cdd:TIGR01612 1642 DTELKENGDNLNSlqeflESLKDQKKNIEDKKKEL------DELDSEIEKIEID---VDQHKKNYEIGIIEKIKEiaian 1712
|
250 260
....*....|....*....|...
gi 358248353 352 KEMLEKQRRSVSDHITRFDNLMN 374
Cdd:TIGR01612 1713 KEEIESIKELIEPTIENLISSFN 1735
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
138-302 |
1.13e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 138 ELKNFREKEKQLEtscKEKTEYLEKMVQRNERYKQDVERFYERKRHLDLIEM-LEAKRPwveyENVRQEYEGVKLIRDRV 216
Cdd:COG3883 59 ELEALQAEIDKLQ---AEIAEAEAEIEERREELGERARALYRSGGSVSYLDVlLGSESF----SDFLDRLSALSKIADAD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 217 KEEVRKLKEGQIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQALTVKQNEELDRQKR 296
Cdd:COG3883 132 ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
....*.
gi 358248353 297 ISNTRK 302
Cdd:COG3883 212 AAAAAA 217
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
232-366 |
1.28e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 232 RRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQALTVKQNEELDRQKRISNTR--KMIEDLQS 309
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 358248353 310 ELKTA---------------ENCENLQPQIDTVTNDL----RRVQEEKALCEGEIIDKQREKEMLEKQRRSVSDHI 366
Cdd:COG1579 97 EIESLkrrisdledeilelmERIEELEEELAELEAELaeleAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
105-377 |
2.04e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 105 QDKVGEFAKLSKIELLEATEKSVGPPEMHRYHCELKNFREKEKQLETSCKEKTEYLEKMVQ---RNERYKQDVERFYERK 181
Cdd:PRK03918 289 KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHELYEEAK 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 182 RHLDLIEMLEAKRPWVEYENVRQEYEGVKLIRDRVKEEVRKLkegqipmTRRIEEIDRQRHTLEVRIKEkstdIKEASQK 261
Cdd:PRK03918 369 AKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKI-------TARIGELKKEIKELKKAIEE----LKKAKGK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 262 C---------KQRQDLIERKDRQIKELQ---QALTVKQNEELDRQKRISNTRKMIEDLQSELKTAEncenlqpQIDTVTN 329
Cdd:PRK03918 438 CpvcgrelteEHRKELLEEYTAELKRIEkelKEIEEKERKLRKELRELEKVLKKESELIKLKELAE-------QLKELEE 510
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 358248353 330 DLRRVQEEKALCEGEIIDKQREKEM-LEKQRRSVSDHITRFDNLMNQKE 377
Cdd:PRK03918 511 KLKKYNLEELEKKAEEYEKLKEKLIkLKGEIKSLKKELEKLEELKKKLA 559
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
198-383 |
2.34e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 198 EYENVRQEYEGVKLIRDRVKEEVRKLKEgqipmtrRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIK 277
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQA-------ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 278 E--------------LQQALTVKQNEE-LDRQKRIS----NTRKMIEDLQSELKTAENCE-NLQPQIDTVTNDLRRVQEE 337
Cdd:COG3883 90 EraralyrsggsvsyLDVLLGSESFSDfLDRLSALSkiadADADLLEELKADKAELEAKKaELEAKLAELEALKAELEAA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 358248353 338 KALCEGEIIDKQREKEMLEKQRRSVSDHITRFDNLMNQKEDKLRQR 383
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
247-665 |
3.12e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 247 RIKEKSTDIKEASQKCKQRQDLIERKDR---QIKELQQALTVKQNE--ELDRQKRISNTRKMIEDLQSELKTAENC-ENL 320
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEEleeELEELEAELEELREEleKLEKLLQLLPLYQELEALEAELAELPERlEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 321 QPQIDTvtndLRRVQEEKALCEGEIIDKQREKEMLEKQ-----RRSVSDHITRFDNLMNQKEdKLRQRYRDTYDAVLWLR 395
Cdd:COG4717 152 EERLEE----LRELEEELEELEAELAELQEELEELLEQlslatEEELQDLAEELEELQQRLA-ELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 396 NNRDRFKQRVcepimltinMKDNKNAKYVENHISSNDLRAFVFESQEDMEIFLREVRDNKKLRVNAVIAPKISY------ 469
Cdd:COG4717 227 EELEQLENEL---------EAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLllarek 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 470 -------ADKAPSRSLNDLKQYGFFSYLREL----FDAPDPVMSYLCCQYHIHEVPVGTERTRERIERVIQETRLKQIYT 538
Cdd:COG4717 298 aslgkeaEELQALPALEELEEEELEELLAALglppDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 539 AeekyvlktsvysNKVISsntslkVAQFLTVTVDLEQRRHLEEQLKEMNRQLEAVDSGLAALRDTNRHLELKDnELRLKK 618
Cdd:COG4717 378 E------------AGVED------EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEE-ELEELE 438
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 358248353 619 KELLERKTRKRQLEQKISSKLASIRLMEQDTC--NLEEEERKASTKIKE 665
Cdd:COG4717 439 EELEELEEELEELREELAELEAELEQLEEDGElaELLQELEELKAELRE 487
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
574-673 |
3.94e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 574 EQRRHLEEQLKEMNRQLEAVDSGLAALRDTNRHLELKDNELRLKKKELLERKTRKRQLEQKISSKLASI----------R 643
Cdd:PRK12704 79 ERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsgltaeeakeI 158
|
90 100 110
....*....|....*....|....*....|.
gi 358248353 644 LMEQdtcnLEEE-ERKASTKIKEInVQKAKL 673
Cdd:PRK12704 159 LLEK----VEEEaRHEAAVLIKEI-EEEAKE 184
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
87-377 |
6.21e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.49 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 87 EQVAALNIQVGNLCQFLpqDKVGEFAKLSKIELlEATEKSVGPPEmhryhcelKNFREKEKQLETSCKEKTeyleKMVQR 166
Cdd:pfam15921 461 EKVSSLTAQLESTKEML--RKVVEELTAKKMTL-ESSERTVSDLT--------ASLQEKERAIEATNAEIT----KLRSR 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 167 NERYKQDVERFYERKRHLdliemleakrpwveyENVRQEYEGVKLI---RDRVKEEVRKLKEGqipMTRRIEEIDRQRHT 243
Cdd:pfam15921 526 VDLKLQELQHLKNEGDHL---------------RNVQTECEALKLQmaeKDKVIEILRQQIEN---MTQLVGQHGRTAGA 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 244 LEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQALTVKQNEELDRQKRISNTRKMIEDLQSELktaencENLQPQ 323
Cdd:pfam15921 588 MQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQER------DQLLNE 661
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 358248353 324 IDTVTNDLRRVQEEKALCEGEIIDKQREKEM----LEKQRRSVSDHITRFDNLMNQKE 377
Cdd:pfam15921 662 VKTSRNELNSLSEDYEVLKRNFRNKSEEMETttnkLKMQLKSAQSELEQTRNTLKSME 719
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
253-336 |
6.22e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 253 TDIKEASQKCKQRQDLIERKDRQIKELQQALTVKQNEELDRQKRISNTRKMIEDLQSELKTAEncENLQPQIDTVTNDLR 332
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE--AEIEERREELGERAR 93
|
....
gi 358248353 333 RVQE 336
Cdd:COG3883 94 ALYR 97
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
862-984 |
6.58e-03 |
|
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: 38.38 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 862 CAGEVDLHTENEEDYDKYGIRIRVKFRSstQLheltphhqSGGERSVSTMLYLMALQelnrCPFRVVDEINQGMDPINER 941
Cdd:cd00267 52 TSGEILIDGKDIAKLPLEELRRRIGYVP--QL--------SGGQRQRVALARALLLN----PDLLLLDEPTSGLDPASRE 117
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 358248353 942 RVFEMVVNTACKENTsqYFFITPKLLQNLPYSEKmtVLFVYNG 984
Cdd:cd00267 118 RLLELLRELAEEGRT--VIIVTHDPELAELAADR--VIVLKDG 156
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
132-364 |
7.17e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 132 MHRYHCELKNFREKEKQL---ETSCKEKTEYLEKMVQRNER---YKQDVERFYERKRHLDLIEMLEAKRPWVEYENVRQE 205
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIeekERKLRKELRELEKVLKKESElikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEK 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 206 YEGVKLIRDRVKEEVRKLKE---GQIPMTRRIEEIDRQRHTLEVRIKEKS------------------------------ 252
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGfesveeleerlkelepfyneylelkdaeke 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 253 ------------TDIKEASQKCKQRQDLIERKDRQIKELQQALTVKQNEELDRQKRisNTRKMIEDLQSELKTAENcenl 320
Cdd:PRK03918 614 lereekelkkleEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYL--ELSRELAGLRAELEELEK---- 687
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 358248353 321 qpQIDTVTNDLRRVQEEKalceGEIIDKQREKEMLEKQRRSVSD 364
Cdd:PRK03918 688 --RREEIKKTLEKLKEEL----EEREKAKKELEKLEKALERVEE 725
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
138-392 |
7.76e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 138 ELKNFREKEKQLETSCKEKTEYLEKmVQRNERYKQDVERFYERKRHLDLIEMLEAKRpwveYENVRQEYEGVKLIR--DR 215
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELKKAEE-KKKAEEAKKAEEDKNMALRKAEEAKKAEEAR----IEEVMKLYEEEKKMKaeEA 1612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 216 VKEEVRKLKEGQIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKelQQALTVKQNEELDRQK 295
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK--KKAEEAKKAEEDEKKA 1690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 296 RISNTRKmiedlQSELKTAENCENLQPQIDTVTNDLRRVQEEKALcEGEIIDKQREKEMLEKQRRSVSDHITRFDNLMNQ 375
Cdd:PTZ00121 1691 AEALKKE-----AEEAKKAEELKKKEAEEKKKAEELKKAEEENKI-KAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKK 1764
|
250
....*....|....*..
gi 358248353 376 KEDKLRQRYRDTYDAVL 392
Cdd:PTZ00121 1765 EEEKKAEEIRKEKEAVI 1781
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
143-333 |
8.03e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 40.01 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 143 REKEKQLETSCKEKTEYLEKMVQRNERYKQDVERfyeRKRHLDLIEmlEAKrpwveyENVRQEYEGVKLIRDRVKEEVRK 222
Cdd:pfam05667 355 EKEIKKLESSIKQVEEELEELKEQNEELEKQYKV---KKKTLDLLP--DAE------ENIAKLQALVDASAQRLVELAGQ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 223 LKEGQIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQALTvKQNEELDRQ---KRI-- 297
Cdd:pfam05667 424 WEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYE-RLPKDVSRSaytRRIle 502
|
170 180 190
....*....|....*....|....*....|....*...
gi 358248353 298 --SNTRKMIEDLQselKTAENCENLQPQIDTVTNDLRR 333
Cdd:pfam05667 503 ivKNIKKQKEEIT---KILSDTKSLQKEINSLTGKLDR 537
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
2-75 |
9.14e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 38.74 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 2 IIGANGTGKSSIVCAICLGLAG-KPAFMGRADKVGFFVKRGCSKGLVEIELFRTSGN-LIITREIDVIKN-------QSF 72
Cdd:cd03240 27 IVGQNGAGKTTIIEALKYALTGeLPPNSKGGAHDPKLIREGEVRAQVKLAFENANGKkYTITRSLAILENvifchqgESN 106
|
...
gi 358248353 73 WFI 75
Cdd:cd03240 107 WPL 109
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
138-296 |
9.16e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 138 ELKNFREKEKQLETSCKEKTEYLEKMV---QRNERYK--------QDVERFYERKRHLDLIemleakrpwveYENVRQEY 206
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELLralYRLGRQPplalllspEDFLDAVRRLQYLKYL-----------APARREQA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 207 EGVKLIRDRVKEEVRKLKEGQIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQALTVK 286
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
170
....*....|
gi 358248353 287 QNEELDRQKR 296
Cdd:COG4942 233 EAEAAAAAER 242
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
212-383 |
9.71e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 212 IRDRVKEEVRKLKEGQIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQALTVKQNEEL 291
Cdd:COG4372 18 LRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248353 292 DRQKRISNTRKMIEDLQSELktaencENLQPQIDTVTNDLRRVQEEKALCEGEIIDKQREKEMLEKQRRSVSDHITRFDN 371
Cdd:COG4372 98 QAQEELESLQEEAEELQEEL------EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170
....*....|..
gi 358248353 372 LMNQKEDKLRQR 383
Cdd:COG4372 172 ELQALSEAEAEQ 183
|
|
| |
