|
Name |
Accession |
Description |
Interval |
E-value |
| rad24 |
TIGR00602 |
checkpoint protein rad24; All proteins in this family for which functions are known are ... |
2-641 |
0e+00 |
|
checkpoint protein rad24; All proteins in this family for which functions are known are involved in DNA damage tolerance (likely cell cycle checkpoints).This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129690 [Multi-domain] Cd Length: 637 Bit Score: 986.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 2 NQVTDWVDPSFDDFLECRDISTITATSLGVNNSSHRRKNGPSTLesskFPARKRGNLSsLEQIYGLENSKESLSENEPWV 81
Cdd:TIGR00602 1 MDVTDWVKPSFDDFLLSSLISTITKWSLSRPTSSHRRKNSPSTD----IHARKRGFLS-LEQDTGLELSSENLDGNEPWV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 82 DKYKPETQHELAVHKKKIEEVETWLKAQVLERQPKQggsILLITGPPGCGKTTTIKVLSKEHGIQVQEWINPVLPDFQKD 161
Cdd:TIGR00602 76 EKYKPETQHELAVHKKKIEEVETWLKAQVLENAPKR---ILLITGPSGCGKSTTIKILSKELGIQVQEWSNPTLPDFQKN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 162 DFREIFNTESSFHMFpyQSQIAVFKEFLLRATkyNKLQMLGDDLRTDKKIILVEDLPNQFYRDSHTLHEVLR-KYVRIGR 240
Cdd:TIGR00602 153 DHKVTLSLESCFSNF--QSQIEVFSEFLLRAT--NKLQMLGDDLMTDKKIILVEDLPNQFYRDTRALHEILRwKYVSIGR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 241 CPLIFVISDSLSGDNNQ-RLLFP------KEIQEECSISNISFNPVAPTIMMKFLNRIVTIEANKNGGKITVPDKTSLEL 313
Cdd:TIGR00602 229 CPLVFIITESLEGDNNQrRLLFPaetimnKEILEEPRVSNISFNPIAPTIMKKFLNRIVTIEAKKNGEKIKVPKKTSVEL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 314 LCQGCSGDIRSAINSLQFSSSKGenNLWPRKKGMSLKSDAVLSKSKRRKKPDRVFENQEVQAIGGKDVSLFLFRALGKIL 393
Cdd:TIGR00602 309 LCQGCSGDIRSAINSLQFSSSKS--GSLPIKKRMSTKSDAHASKSKIKGKHSSNNENQEIQALGGKDVSLFLFRALGKIL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 394 YCKRASLTELDSPRLPSHLSEYERDTLLVEPEEIVEMSHMPGD-LFNLYLHQNYIDFFMDIDDIVRASEFLSFADILSGD 472
Cdd:TIGR00602 387 YCKRATLNELDSPRLPSHLSELSRDTLMVGPEEVVEMSHMPGDkTFNLYSHQNYNDFFVEFDDEVKASEFLNFADILSGD 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 473 WNTCSLLREYSTSIATRGVIHSNKARGYAHCQGGGSSFRPLHKPQWFLIYKKYRENCLAAKALF--PDFCLPALCLQTQL 550
Cdd:TIGR00602 467 WNTRSLLREYSTSSARRGVMHSNKARGIAHCQGGKSSFRPLHKPQWFLISKKYRENCLAAKALFkvEDFCLPADCLQTQL 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 551 LPYLALLTIPMRNQAQISFIQDIGRLPLKRHFGRLKMEALTDREHGMIDPDSGDEAQLNGGHSTEESLGEPTQATAPETW 630
Cdd:TIGR00602 547 LPYLALDTIPMRNDAQISFIDDLGRLPLKRDFRRLKMEALTDREVGMIDPDSGDEETSFGDDPAVESDSDPSQAAGPETW 626
|
650
....*....|.
gi 1622945054 631 SLPLSQNSASE 641
Cdd:TIGR00602 627 SLPDSDNSLSE 637
|
|
| Rad17 |
pfam03215 |
Rad17 P-loop domain; |
72-259 |
1.93e-90 |
|
Rad17 P-loop domain;
Pssm-ID: 367398 [Multi-domain] Cd Length: 186 Bit Score: 279.15 E-value: 1.93e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 72 ESLSENEPWVDKYKPETQHELAVHKKKIEEVETWLKAQVLERQPKqggSILLITGPPGCGKTTTIKVLSKEHGIQVQEWI 151
Cdd:pfam03215 1 INDDGGEQWYEKYKPNCLEQLAVHKRKIKDVQEWLDAMFLENAKH---RILLISGPSGCGKSTVIKELSKELGPKYREWS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 152 NPVL---PDFQKDDFREIFNTESSFhmfpyQSQIAVFKEFLLRATKYNKLQMLGDDLRTDKKIILVEDLPNQFYRDSHTL 228
Cdd:pfam03215 78 NPTSfrsPPNQVTDFRGDCIVNSRF-----LSQMESFSEFELKGARYLVMQKRGKNAQGNKKLILIEDLPNVFHIDTRRF 152
|
170 180 190
....*....|....*....|....*....|....
gi 1622945054 229 HEVLRKYVRIGRC-PLIFVIS--DSLSGDNNQRL 259
Cdd:pfam03215 153 QQVIRQWLYSSEPlPLIICITecEILEGDNNQRK 186
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
79-491 |
4.35e-20 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 93.83 E-value: 4.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 79 PWVDKYKPETQHELAVHKKKIEEVETWLKAQvLERQPKQGgsiLLITGPPGCGKTTTIKVLSKEHGIQVQEwINpvlpdf 158
Cdd:PRK04195 3 PWVEKYRPKTLSDVVGNEKAKEQLREWIESW-LKGKPKKA---LLLYGPPGVGKTSLAHALANDYGWEVIE-LN------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 159 qKDDFReifNTEssfhmfpyqsqiaVFKEFLLRATKYNKLqmlgddLRTDKKIILVEDLPNQFYR-DSHTLHEVLrKYVR 237
Cdd:PRK04195 72 -ASDQR---TAD-------------VIERVAGEAATSGSL------FGARRKLILLDEVDGIHGNeDRGGARAIL-ELIK 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 238 IGRCPLIFVISDSLSgdnnqrlLFPKEIQEECSIsnISFNPVAPTIMMKFLNRIVTIEanknggKITVPDKTsLELLCQG 317
Cdd:PRK04195 128 KAKQPIILTANDPYD-------PSLRELRNACLM--IEFKRLSTRSIVPVLKRICRKE------GIECDDEA-LKEIAER 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 318 CSGDIRSAINSLQfSSSKGENNLwprkkgmslksdavlskskrrkkpdrvfENQEVQAIGGKDVSLFLFRALGKIL---Y 394
Cdd:PRK04195 192 SGGDLRSAINDLQ-AIAEGYGKL----------------------------TLEDVKTLGRRDREESIFDALDAVFkarN 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 395 CKRA--SLTELDsprlpshlseyerdtllVEPEEIVEmshmpgdlfnlYLHQNYIDFFMDIDDIVRASEFLSFADILSG- 471
Cdd:PRK04195 243 ADQAleASYDVD-----------------EDPDDLIE-----------WIDENIPKEYDDPEDIARAYDALSRADIFLGr 294
|
410 420
....*....|....*....|....*
gi 1622945054 472 -----DWntcSLLReYSTSIATRGV 491
Cdd:PRK04195 295 vkrtqNY---DLWR-YASDLMTAGV 315
|
|
| HLD_clamp_RarA |
cd18139 |
helical lid domain of recombination factor protein RarA; Recombination factor RarA ... |
281-339 |
3.92e-09 |
|
helical lid domain of recombination factor protein RarA; Recombination factor RarA (Replication associated recombination gene/protein A, also known as MgsA (Maintenance of genome stability A) or Mgs1 in yeast and WRNIP1 in mammals) is a member of the clamp-loader clade of the AAA+ superfamily. It functions as a tetramer. RarA co-localize with the replication fork throughout the cell cycle and may play a role in the rescue of stalled replication forks.
Pssm-ID: 350841 [Multi-domain] Cd Length: 75 Bit Score: 53.40 E-value: 3.92e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622945054 281 PTIMMKFLNRIVTIEANKNGGKITVPDKtSLELLCQGCSGDIRSAINSLQFSSSKGENN 339
Cdd:cd18139 3 EEDLEKLLKRALEDKERGGDRKVTIDDE-ALELLAEAADGDARSALNLLELAVLSAEED 60
|
|
| Kti12 |
COG4088 |
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ... |
119-189 |
5.41e-07 |
|
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];
Pssm-ID: 443264 [Multi-domain] Cd Length: 179 Bit Score: 50.11 E-value: 5.41e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622945054 119 GSILLITGPPGCGKTTTIKVLSKEHGiqVQEWINPVLPdfqKDDFREIFNTESsfhmFPYQSQIAVFKEFL 189
Cdd:COG4088 4 PMLLILTGPPGSGKTTFAKALAQRLY--AEGIAVALLH---SDDFRRFLVNES----FPKETYEEVVEDVR 65
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
119-142 |
1.10e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.05 E-value: 1.10e-03
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| rad24 |
TIGR00602 |
checkpoint protein rad24; All proteins in this family for which functions are known are ... |
2-641 |
0e+00 |
|
checkpoint protein rad24; All proteins in this family for which functions are known are involved in DNA damage tolerance (likely cell cycle checkpoints).This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129690 [Multi-domain] Cd Length: 637 Bit Score: 986.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 2 NQVTDWVDPSFDDFLECRDISTITATSLGVNNSSHRRKNGPSTLesskFPARKRGNLSsLEQIYGLENSKESLSENEPWV 81
Cdd:TIGR00602 1 MDVTDWVKPSFDDFLLSSLISTITKWSLSRPTSSHRRKNSPSTD----IHARKRGFLS-LEQDTGLELSSENLDGNEPWV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 82 DKYKPETQHELAVHKKKIEEVETWLKAQVLERQPKQggsILLITGPPGCGKTTTIKVLSKEHGIQVQEWINPVLPDFQKD 161
Cdd:TIGR00602 76 EKYKPETQHELAVHKKKIEEVETWLKAQVLENAPKR---ILLITGPSGCGKSTTIKILSKELGIQVQEWSNPTLPDFQKN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 162 DFREIFNTESSFHMFpyQSQIAVFKEFLLRATkyNKLQMLGDDLRTDKKIILVEDLPNQFYRDSHTLHEVLR-KYVRIGR 240
Cdd:TIGR00602 153 DHKVTLSLESCFSNF--QSQIEVFSEFLLRAT--NKLQMLGDDLMTDKKIILVEDLPNQFYRDTRALHEILRwKYVSIGR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 241 CPLIFVISDSLSGDNNQ-RLLFP------KEIQEECSISNISFNPVAPTIMMKFLNRIVTIEANKNGGKITVPDKTSLEL 313
Cdd:TIGR00602 229 CPLVFIITESLEGDNNQrRLLFPaetimnKEILEEPRVSNISFNPIAPTIMKKFLNRIVTIEAKKNGEKIKVPKKTSVEL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 314 LCQGCSGDIRSAINSLQFSSSKGenNLWPRKKGMSLKSDAVLSKSKRRKKPDRVFENQEVQAIGGKDVSLFLFRALGKIL 393
Cdd:TIGR00602 309 LCQGCSGDIRSAINSLQFSSSKS--GSLPIKKRMSTKSDAHASKSKIKGKHSSNNENQEIQALGGKDVSLFLFRALGKIL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 394 YCKRASLTELDSPRLPSHLSEYERDTLLVEPEEIVEMSHMPGD-LFNLYLHQNYIDFFMDIDDIVRASEFLSFADILSGD 472
Cdd:TIGR00602 387 YCKRATLNELDSPRLPSHLSELSRDTLMVGPEEVVEMSHMPGDkTFNLYSHQNYNDFFVEFDDEVKASEFLNFADILSGD 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 473 WNTCSLLREYSTSIATRGVIHSNKARGYAHCQGGGSSFRPLHKPQWFLIYKKYRENCLAAKALF--PDFCLPALCLQTQL 550
Cdd:TIGR00602 467 WNTRSLLREYSTSSARRGVMHSNKARGIAHCQGGKSSFRPLHKPQWFLISKKYRENCLAAKALFkvEDFCLPADCLQTQL 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 551 LPYLALLTIPMRNQAQISFIQDIGRLPLKRHFGRLKMEALTDREHGMIDPDSGDEAQLNGGHSTEESLGEPTQATAPETW 630
Cdd:TIGR00602 547 LPYLALDTIPMRNDAQISFIDDLGRLPLKRDFRRLKMEALTDREVGMIDPDSGDEETSFGDDPAVESDSDPSQAAGPETW 626
|
650
....*....|.
gi 1622945054 631 SLPLSQNSASE 641
Cdd:TIGR00602 627 SLPDSDNSLSE 637
|
|
| Rad17 |
pfam03215 |
Rad17 P-loop domain; |
72-259 |
1.93e-90 |
|
Rad17 P-loop domain;
Pssm-ID: 367398 [Multi-domain] Cd Length: 186 Bit Score: 279.15 E-value: 1.93e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 72 ESLSENEPWVDKYKPETQHELAVHKKKIEEVETWLKAQVLERQPKqggSILLITGPPGCGKTTTIKVLSKEHGIQVQEWI 151
Cdd:pfam03215 1 INDDGGEQWYEKYKPNCLEQLAVHKRKIKDVQEWLDAMFLENAKH---RILLISGPSGCGKSTVIKELSKELGPKYREWS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 152 NPVL---PDFQKDDFREIFNTESSFhmfpyQSQIAVFKEFLLRATKYNKLQMLGDDLRTDKKIILVEDLPNQFYRDSHTL 228
Cdd:pfam03215 78 NPTSfrsPPNQVTDFRGDCIVNSRF-----LSQMESFSEFELKGARYLVMQKRGKNAQGNKKLILIEDLPNVFHIDTRRF 152
|
170 180 190
....*....|....*....|....*....|....
gi 1622945054 229 HEVLRKYVRIGRC-PLIFVIS--DSLSGDNNQRL 259
Cdd:pfam03215 153 QQVIRQWLYSSEPlPLIICITecEILEGDNNQRK 186
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
79-491 |
4.35e-20 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 93.83 E-value: 4.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 79 PWVDKYKPETQHELAVHKKKIEEVETWLKAQvLERQPKQGgsiLLITGPPGCGKTTTIKVLSKEHGIQVQEwINpvlpdf 158
Cdd:PRK04195 3 PWVEKYRPKTLSDVVGNEKAKEQLREWIESW-LKGKPKKA---LLLYGPPGVGKTSLAHALANDYGWEVIE-LN------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 159 qKDDFReifNTEssfhmfpyqsqiaVFKEFLLRATKYNKLqmlgddLRTDKKIILVEDLPNQFYR-DSHTLHEVLrKYVR 237
Cdd:PRK04195 72 -ASDQR---TAD-------------VIERVAGEAATSGSL------FGARRKLILLDEVDGIHGNeDRGGARAIL-ELIK 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 238 IGRCPLIFVISDSLSgdnnqrlLFPKEIQEECSIsnISFNPVAPTIMMKFLNRIVTIEanknggKITVPDKTsLELLCQG 317
Cdd:PRK04195 128 KAKQPIILTANDPYD-------PSLRELRNACLM--IEFKRLSTRSIVPVLKRICRKE------GIECDDEA-LKEIAER 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 318 CSGDIRSAINSLQfSSSKGENNLwprkkgmslksdavlskskrrkkpdrvfENQEVQAIGGKDVSLFLFRALGKIL---Y 394
Cdd:PRK04195 192 SGGDLRSAINDLQ-AIAEGYGKL----------------------------TLEDVKTLGRRDREESIFDALDAVFkarN 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 395 CKRA--SLTELDsprlpshlseyerdtllVEPEEIVEmshmpgdlfnlYLHQNYIDFFMDIDDIVRASEFLSFADILSG- 471
Cdd:PRK04195 243 ADQAleASYDVD-----------------EDPDDLIE-----------WIDENIPKEYDDPEDIARAYDALSRADIFLGr 294
|
410 420
....*....|....*....|....*
gi 1622945054 472 -----DWntcSLLReYSTSIATRGV 491
Cdd:PRK04195 295 vkrtqNY---DLWR-YASDLMTAGV 315
|
|
| HLD_clamp_RarA |
cd18139 |
helical lid domain of recombination factor protein RarA; Recombination factor RarA ... |
281-339 |
3.92e-09 |
|
helical lid domain of recombination factor protein RarA; Recombination factor RarA (Replication associated recombination gene/protein A, also known as MgsA (Maintenance of genome stability A) or Mgs1 in yeast and WRNIP1 in mammals) is a member of the clamp-loader clade of the AAA+ superfamily. It functions as a tetramer. RarA co-localize with the replication fork throughout the cell cycle and may play a role in the rescue of stalled replication forks.
Pssm-ID: 350841 [Multi-domain] Cd Length: 75 Bit Score: 53.40 E-value: 3.92e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622945054 281 PTIMMKFLNRIVTIEANKNGGKITVPDKtSLELLCQGCSGDIRSAINSLQFSSSKGENN 339
Cdd:cd18139 3 EEDLEKLLKRALEDKERGGDRKVTIDDE-ALELLAEAADGDARSALNLLELAVLSAEED 60
|
|
| PRK12402 |
PRK12402 |
replication factor C small subunit 2; Reviewed |
80-338 |
3.79e-07 |
|
replication factor C small subunit 2; Reviewed
Pssm-ID: 237090 [Multi-domain] Cd Length: 337 Bit Score: 52.68 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 80 WVDKYKPETQHELAVHkkkiEEVETWLKAQVLERQPKQggsiLLITGPPGCGKTTTIKVLSKE-HGiqvQEWINPvLPDF 158
Cdd:PRK12402 5 WTEKYRPALLEDILGQ----DEVVERLSRAVDSPNLPH----LLVQGPPGSGKTAAVRALARElYG---DPWENN-FTEF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 159 QKDDF-----REIFNTEsSFHMF------PYQSQIAVFKEFLLRATKYNKLQmlgddlrTDKKIILV---EDLPNQFyrd 224
Cdd:PRK12402 73 NVADFfdqgkKYLVEDP-RFAHFlgtdkrIRSSKIDNFKHVLKEYASYRPLS-------ADYKTILLdnaEALREDA--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 225 SHTLHEVLRKYVRIGRcpliFVISDSlsgdNNQRLLFPkeIQEECsiSNISFNPVAPTIMMKFLNRIVTIEanknggKIT 304
Cdd:PRK12402 142 QQALRRIMEQYSRTCR----FIIATR----QPSKLIPP--IRSRC--LPLFFRAPTDDELVDVLESIAEAE------GVD 203
|
250 260 270
....*....|....*....|....*....|....
gi 1622945054 305 VPDKtSLELLCQGCSGDIRSAINSLQFSSSKGEN 338
Cdd:PRK12402 204 YDDD-GLELIAYYAGGDLRKAILTLQTAALAAGE 236
|
|
| Kti12 |
COG4088 |
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ... |
119-189 |
5.41e-07 |
|
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];
Pssm-ID: 443264 [Multi-domain] Cd Length: 179 Bit Score: 50.11 E-value: 5.41e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622945054 119 GSILLITGPPGCGKTTTIKVLSKEHGiqVQEWINPVLPdfqKDDFREIFNTESsfhmFPYQSQIAVFKEFL 189
Cdd:COG4088 4 PMLLILTGPPGSGKTTFAKALAQRLY--AEGIAVALLH---SDDFRRFLVNES----FPKETYEEVVEDVR 65
|
|
| rfc |
PRK00440 |
replication factor C small subunit; Reviewed |
76-338 |
1.11e-05 |
|
replication factor C small subunit; Reviewed
Pssm-ID: 234763 [Multi-domain] Cd Length: 319 Bit Score: 47.95 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 76 ENEPWVDKYKPETQHELAVHkkkiEEVETWLKAQVLERQ-PKqggsiLLITGPPGCGKTTTIKVLSKEhgiqvqewinpV 154
Cdd:PRK00440 3 MEEIWVEKYRPRTLDEIVGQ----EEIVERLKSYVKEKNmPH-----LLFAGPPGTGKTTAALALARE-----------L 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 155 LPDFQKDDFREIfNTESsfhmfpyQSQIAV----FKEFLlratkynKLQMLGDdlrTDKKIILVeDLPNQFYRDS-HTLH 229
Cdd:PRK00440 63 YGEDWRENFLEL-NASD-------ERGIDVirnkIKEFA-------RTAPVGG---APFKIIFL-DEADNLTSDAqQALR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 230 EVLRKYVRIGRcpliFVISDSLSgdnnQRLLFPkeIQEECSIsnISFNPVAPTIMMKFLNRIVTIEanknggKITVPDKt 309
Cdd:PRK00440 124 RTMEMYSQNTR----FILSCNYS----SKIIDP--IQSRCAV--FRFSPLKKEAVAERLRYIAENE------GIEITDD- 184
|
250 260
....*....|....*....|....*....
gi 1622945054 310 SLELLCQGCSGDIRSAINSLQFSSSKGEN 338
Cdd:PRK00440 185 ALEAIYYVSEGDMRKAINALQAAAATGKE 213
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
96-142 |
1.30e-05 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 47.98 E-value: 1.30e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1622945054 96 KKKIEEVETWLKAQVLERQ---PKQGGSILLiTGPPGCGKTTTIKVLSKE 142
Cdd:COG0464 166 KEELRELVALPLKRPELREeygLPPPRGLLL-YGPPGTGKTLLARALAGE 214
|
|
| HLD_clamp_RFC |
cd18140 |
helical lid domain of replication factor C subunit; Replication factor C (RFC) is five-protein ... |
284-338 |
1.33e-05 |
|
helical lid domain of replication factor C subunit; Replication factor C (RFC) is five-protein clamp loader complex that forms a stable ATP-dependent complex with the sliding clamp, PCNA, which binds specifically to primed DNA. RFC subunits belong to the clamp loader clade of the AAA+ superfamily.
Pssm-ID: 350842 [Multi-domain] Cd Length: 63 Bit Score: 43.29 E-value: 1.33e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1622945054 284 MMKFLNRIVTIEanknggKITVPDKtSLELLCQGCSGDIRSAINSLQFSSSKGEN 338
Cdd:cd18140 6 IVKRLREICKKE------GVKIDEE-ALEAIAEKSEGDMRKAINDLQAAAAGGGV 53
|
|
| PLN03025 |
PLN03025 |
replication factor C subunit; Provisional |
79-142 |
5.86e-05 |
|
replication factor C subunit; Provisional
Pssm-ID: 178596 [Multi-domain] Cd Length: 319 Bit Score: 45.49 E-value: 5.86e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622945054 79 PWVDKYKPETQHELAVHKKKIEevetwlKAQVLERqpkqGGSI--LLITGPPGCGKTTTIKVLSKE 142
Cdd:PLN03025 2 PWVEKYRPTKLDDIVGNEDAVS------RLQVIAR----DGNMpnLILSGPPGTGKTTSILALAHE 57
|
|
| AAA_18 |
pfam13238 |
AAA domain; |
123-224 |
6.85e-05 |
|
AAA domain;
Pssm-ID: 433052 [Multi-domain] Cd Length: 128 Bit Score: 43.19 E-value: 6.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 123 LITGPPGCGKTTTIKVLSKEHGIQvqewinpvlpDFQKDDFREIFNTESSFHmfpyqsQIAVFKEFLLRATKYNKLQMLG 202
Cdd:pfam13238 2 LITGTPGVGKTTLAKELSKRLGFG----------DNVRDLALENGLVLGDDP------ETRESKRLDEDKLDRLLDLLEE 65
|
90 100
....*....|....*....|..
gi 1622945054 203 DDLRTDKKIILVEDLPNQFYRD 224
Cdd:pfam13238 66 NAALEEGGNLIIDGHLAELEPE 87
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
92-147 |
1.23e-04 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 43.04 E-value: 1.23e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622945054 92 LAVHKKKIEEVETWLKAQVLERQPKQGgsILLItGPPGCGKTTTIKVLSKEHGIQV 147
Cdd:cd19481 2 KASLREAVEAPRRGSRLRRYGLGLPKG--ILLY-GPPGTGKTLLAKALAGELGLPL 54
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
106-176 |
1.88e-04 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 42.13 E-value: 1.88e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622945054 106 LKAQVLERQPKQGGSILLITGPPGCGKTTTIKVLSKEhgiqVQEWINPVL----PDF-QKDDFREIFNTESSFHMF 176
Cdd:cd00009 6 AIEALREALELPPPKNLLLYGPPGTGKTTLARAIANE----LFRPGAPFLylnaSDLlEGLVVAELFGHFLVRLLF 77
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
122-147 |
4.96e-04 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 40.65 E-value: 4.96e-04
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
119-142 |
1.10e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.05 E-value: 1.10e-03
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
118-147 |
1.91e-03 |
|
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350691 [Multi-domain] Cd Length: 155 Bit Score: 39.46 E-value: 1.91e-03
10 20 30
....*....|....*....|....*....|...
gi 1622945054 118 GGSILLITGPPGCGKTTTIKVL---SKEHGIQV 147
Cdd:cd17933 11 RNRVSVLTGGAGTGKTTTLKALlaaLEAEGKRV 43
|
|
| dNK |
pfam01712 |
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2. ... |
124-182 |
2.34e-03 |
|
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2.7.1.74, guanosine EC:2.7.1.113, adenosine EC:2.7.1.76 and thymidine kinase EC:2.7.1.21 (which also phosphorylates deoxyuridine and deoxycytosine.) These enzymes catalyze the production of deoxynucleotide 5'-monophosphate from a deoxynucleoside. Using ATP and yielding ADP in the process.
Pssm-ID: 396326 Cd Length: 201 Bit Score: 39.61 E-value: 2.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622945054 124 ITGPPGCGKTTTIKVLSKEHGIQ-----VQEWINPVLPDFQKDDFREIF--NTESSFHMFPYQSQI 182
Cdd:pfam01712 3 IEGNIGAGKSTLTKILSKRLGFKvfeepVDRWTNPYLDKFYKDPSRWSFalQTYFLNSRFKQQLEA 68
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
96-142 |
2.47e-03 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 40.25 E-value: 2.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1622945054 96 KKKIEEV-ETWLKAQVLER---QPKQGgsiLLITGPPGCGKTTTIKVLSKE 142
Cdd:COG1223 11 KKKLKLIiKELRRRENLRKfglWPPRK---ILFYGPPGTGKTMLAEALAGE 58
|
|
| PRK13768 |
PRK13768 |
GTPase; Provisional |
120-252 |
2.74e-03 |
|
GTPase; Provisional
Pssm-ID: 237498 [Multi-domain] Cd Length: 253 Bit Score: 39.85 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 120 SILLITGPPGCGKTTTIKVLSK---EHGIQVQ--------EWInPVLPDFqkdDFREIFNTES---SFHMFPYQSQIAVF 185
Cdd:PRK13768 3 YIVFFLGTAGSGKTTLTKALSDwleEQGYDVAivnldpavEYL-PYTPDF---DVRDYVTAREimkKYGLGPNGALIASV 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622945054 186 kEFLLraTKYNKLQMLGDDLRTDkkIILVeDLPNQ---F-YRDSHTlhEVLRKYVRIGRCPLIFVISDSLS 252
Cdd:PRK13768 79 -DLLL--TKADEIKEEIESLDAD--YVLV-DTPGQmelFaFRESGR--KLVERLSGSSKSVVVFLIDAVLA 141
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
108-249 |
3.96e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 38.64 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 108 AQVLERQPKQGGSILLITGPPGCGKTTTIKVLSKEHGIQvqewinpvlpdfqkddfREIFNTESSFHMFPYQSQIAVFKE 187
Cdd:pfam13191 13 LDALDRVRSGRPPSVLLTGEAGTGKTTLLRELLRALERD-----------------GGYFLRGKCDENLPYSPLLEALTR 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622945054 188 FLLRATKYNKLQMLGDDLRTDKKIILVEDLPNQFYRDSHTLHEVLRKYVRIGRC---PLIFVISD 249
Cdd:pfam13191 76 EGLLRQLLDELESSLLEAWRAALLEALAPVPELPGDLAERLLDLLLRLLDLLARgerPLVLVLDD 140
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
117-139 |
4.23e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 39.39 E-value: 4.23e-03
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
50-194 |
4.27e-03 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 40.14 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 50 FPARKRGNLSSLEQIYGLENSKESLSENEPWVDKYkpetqhelaVHKKKIEEVETWLKAqvLERQPkqggsILLITGPPG 129
Cdd:COG1401 168 APEDLSADALAAELSAAEELYSEDLESEDDYLKDL---------LREKFEETLEAFLAA--LKTKK-----NVILAGPPG 231
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622945054 130 CGKTTTIKVLSKEHGIQVQEWIN--PVLPDFQKDDFRE-IFNTESSFHmfpYQSQIAVFKEFLLRATK 194
Cdd:COG1401 232 TGKTYLARRLAEALGGEDNGRIEfvQFHPSWSYEDFLLgYRPSLDEGK---YEPTPGIFLRFCLKAEK 296
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
20-142 |
4.73e-03 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 39.60 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945054 20 DISTITATSLGVNNSSHRRKNGPSTLESSKFPARKRGNLSSLEQIYGLENSKESLSENEPWVDKYKPE-TQHELAVHKKK 98
Cdd:COG1222 7 IDENIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDvTFDDIGGLDEQ 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1622945054 99 IEE----VETWLK-AQVLER---QPKQGgsILLiTGPPGCGKTTTIKVLSKE 142
Cdd:COG1222 87 IEEireaVELPLKnPELFRKygiEPPKG--VLL-YGPPGTGKTLLAKAVAGE 135
|
|
| 44 |
PHA02544 |
clamp loader, small subunit; Provisional |
80-147 |
6.39e-03 |
|
clamp loader, small subunit; Provisional
Pssm-ID: 222866 [Multi-domain] Cd Length: 316 Bit Score: 39.20 E-value: 6.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622945054 80 WVDKYKPETQHE--LAVHKKKIeevetwLKAQVlerqpKQGG--SILLITGPPGCGKTTTIKVLSKEHGIQV 147
Cdd:PHA02544 11 WEQKYRPSTIDEciLPAADKET------FKSIV-----KKGRipNMLLHSPSPGTGKTTVAKALCNEVGAEV 71
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
119-140 |
6.99e-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: 37.61 E-value: 6.99e-03
|
| AAA_28 |
pfam13521 |
AAA domain; |
124-147 |
9.01e-03 |
|
AAA domain;
Pssm-ID: 433278 [Multi-domain] Cd Length: 164 Bit Score: 37.63 E-value: 9.01e-03
|
| Fap7 |
COG1936 |
Broad-specificity NMP kinase [Nucleotide transport and metabolism]; |
121-147 |
9.15e-03 |
|
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
Pssm-ID: 441539 [Multi-domain] Cd Length: 173 Bit Score: 37.49 E-value: 9.15e-03
10 20
....*....|....*....|....*..
gi 1622945054 121 ILLITGPPGCGKTTTIKVLSKEHGIQV 147
Cdd:COG1936 2 RIAITGTPGTGKTTVAKLLAERLGLEV 28
|
|
|