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Conserved domains on  [gi|1907092987|ref|XP_036013813|]
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cell cycle checkpoint protein RAD17 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
rad24 TIGR00602
checkpoint protein rad24; All proteins in this family for which functions are known are ...
 13-653 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: 979.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987  13 TKVTDWVAPAFDDFEANTAITTITASSLTFSNSSHRRKYLPSTLesnrLSARKRGRLSLEQTHGLETSRERLSDNEPWVD 92
Cdd:TIGR00602   1 MDVTDWVKPSFDDFLLSSLISTITKWSLSRPTSSHRRKNSPSTD----IHARKRGFLSLEQDTGLELSSENLDGNEPWVE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987  93 KYKPETQHELAVHKKKIEEVETWLKAQVLEVKPKQggsVLLITGPPGCGKTTTIKILSKELGIQVQEWVNPILPDFQKDD 172
Cdd:TIGR00602  77 KYKPETQHELAVHKKKIEEVETWLKAQVLENAPKR---ILLITGPSGCGKSTTIKILSKELGIQVQEWSNPTLPDFQKND 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 173 YKELLSLESNFSVVpyQSQIAVFNDFLLRATkySKLQMLGDDLTTDKKIILVEELPNQFYRDPNALHEILR-KHVQIGRC 251
Cdd:TIGR00602 154 HKVTLSLESCFSNF--QSQIEVFSEFLLRAT--NKLQMLGDDLMTDKKIILVEDLPNQFYRDTRALHEILRwKYVSIGRC 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 252 PLVFIVSDSVSGDNNQ-RLLFP------RNIQEECSVSNISFNPVAPTIMMKFLNRIVTIEASKNGEKIIVPNKTSLELL 324
Cdd:TIGR00602 230 PLVFIITESLEGDNNQrRLLFPaetimnKEILEEPRVSNISFNPIAPTIMKKFLNRIVTIEAKKNGEKIKVPKKTSVELL 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 325 CQGCSGDIRSAINSLQFSSSKGenSSWSKKKRMSLKSDAAISKSKQKKKHNSTLENQEIQAIGGKDVSLFLFRALGKILY 404
Cdd:TIGR00602 310 CQGCSGDIRSAINSLQFSSSKS--GSLPIKKRMSTKSDAHASKSKIKGKHSSNNENQEIQALGGKDVSLFLFRALGKILY 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 405 CKRAPLTELDSPRLPAHLSEHDRDTLLVQPEEIVEMSHMPGD-FFNLYLHQNYIDFFAEVDDLVPASEFLSFADILGGDW 483
Cdd:TIGR00602 388 CKRATLNELDSPRLPSHLSELSRDTLMVGPEEVVEMSHMPGDkTFNLYSHQNYNDFFVEFDDEVKASEFLNFADILSGDW 467

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 484 NTRSLLREYSTSVATRGVMHSNKARGFAHCQGG-SSFRPLHKPQWFLIQKKYRENCLAAKALF--VDFCLPALCLQTQLL 560
Cdd:TIGR00602 468 NTRSLLREYSTSSARRGVMHSNKARGIAHCQGGkSSFRPLHKPQWFLISKKYRENCLAAKALFkvEDFCLPADCLQTQLL 547

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 561 PYLALLTIPMRNKAQISFIQDVGRLPLKRSFGRLKMEALTDRELGLIDPDSGDESPHSGGQPAQEAPGEPAQAAQnadPE 640
Cdd:TIGR00602 548 PYLALDTIPMRNDAQISFIDDLGRLPLKRDFRRLKMEALTDREVGMIDPDSGDEETSFGDDPAVESDSDPSQAAG---PE 624

                         650
                  ....*....|...
gi 1907092987 641 TWSLPLSQNSGSD 653
Cdd:TIGR00602 625 TWSLPDSDNSLSE 637
 
Name Accession Description Interval E-value
rad24 TIGR00602
checkpoint protein rad24; All proteins in this family for which functions are known are ...
 13-653 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: 979.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987  13 TKVTDWVAPAFDDFEANTAITTITASSLTFSNSSHRRKYLPSTLesnrLSARKRGRLSLEQTHGLETSRERLSDNEPWVD 92
Cdd:TIGR00602   1 MDVTDWVKPSFDDFLLSSLISTITKWSLSRPTSSHRRKNSPSTD----IHARKRGFLSLEQDTGLELSSENLDGNEPWVE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987  93 KYKPETQHELAVHKKKIEEVETWLKAQVLEVKPKQggsVLLITGPPGCGKTTTIKILSKELGIQVQEWVNPILPDFQKDD 172
Cdd:TIGR00602  77 KYKPETQHELAVHKKKIEEVETWLKAQVLENAPKR---ILLITGPSGCGKSTTIKILSKELGIQVQEWSNPTLPDFQKND 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 173 YKELLSLESNFSVVpyQSQIAVFNDFLLRATkySKLQMLGDDLTTDKKIILVEELPNQFYRDPNALHEILR-KHVQIGRC 251
Cdd:TIGR00602 154 HKVTLSLESCFSNF--QSQIEVFSEFLLRAT--NKLQMLGDDLMTDKKIILVEDLPNQFYRDTRALHEILRwKYVSIGRC 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 252 PLVFIVSDSVSGDNNQ-RLLFP------RNIQEECSVSNISFNPVAPTIMMKFLNRIVTIEASKNGEKIIVPNKTSLELL 324
Cdd:TIGR00602 230 PLVFIITESLEGDNNQrRLLFPaetimnKEILEEPRVSNISFNPIAPTIMKKFLNRIVTIEAKKNGEKIKVPKKTSVELL 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 325 CQGCSGDIRSAINSLQFSSSKGenSSWSKKKRMSLKSDAAISKSKQKKKHNSTLENQEIQAIGGKDVSLFLFRALGKILY 404
Cdd:TIGR00602 310 CQGCSGDIRSAINSLQFSSSKS--GSLPIKKRMSTKSDAHASKSKIKGKHSSNNENQEIQALGGKDVSLFLFRALGKILY 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 405 CKRAPLTELDSPRLPAHLSEHDRDTLLVQPEEIVEMSHMPGD-FFNLYLHQNYIDFFAEVDDLVPASEFLSFADILGGDW 483
Cdd:TIGR00602 388 CKRATLNELDSPRLPSHLSELSRDTLMVGPEEVVEMSHMPGDkTFNLYSHQNYNDFFVEFDDEVKASEFLNFADILSGDW 467

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 484 NTRSLLREYSTSVATRGVMHSNKARGFAHCQGG-SSFRPLHKPQWFLIQKKYRENCLAAKALF--VDFCLPALCLQTQLL 560
Cdd:TIGR00602 468 NTRSLLREYSTSSARRGVMHSNKARGIAHCQGGkSSFRPLHKPQWFLISKKYRENCLAAKALFkvEDFCLPADCLQTQLL 547

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 561 PYLALLTIPMRNKAQISFIQDVGRLPLKRSFGRLKMEALTDRELGLIDPDSGDESPHSGGQPAQEAPGEPAQAAQnadPE 640
Cdd:TIGR00602 548 PYLALDTIPMRNDAQISFIDDLGRLPLKRDFRRLKMEALTDREVGMIDPDSGDEETSFGDDPAVESDSDPSQAAG---PE 624

                         650
                  ....*....|...
gi 1907092987 641 TWSLPLSQNSGSD 653
Cdd:TIGR00602 625 TWSLPDSDNSLSE 637
Rad17 pfam03215
Rad17 P-loop domain;
82-269 1.89e-76

Rad17 P-loop domain;


Pssm-ID: 367398 [Multi-domain]  Cd Length: 186  Bit Score: 242.94  E-value: 1.89e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987  82 ERLSDNEPWVDKYKPETQHELAVHKKKIEEVETWLKAQVLEVKPKqggSVLLITGPPGCGKTTTIKILSKELGIQVQEWV 161
Cdd:pfam03215   1 INDDGGEQWYEKYKPNCLEQLAVHKRKIKDVQEWLDAMFLENAKH---RILLISGPSGCGKSTVIKELSKELGPKYREWS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 162 NPIL---PDFQKDDYKELLSLESNFsvvpyQSQIAVFNDFLLRATKYSKLQMLGDDLTTDKKIILVEELPNQFYRDPNAL 238
Cdd:pfam03215  78 NPTSfrsPPNQVTDFRGDCIVNSRF-----LSQMESFSEFELKGARYLVMQKRGKNAQGNKKLILIEDLPNVFHIDTRRF 152

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1907092987 239 HEILRKHVQIGRC-PLVFIVS--DSVSGDNNQRL 269
Cdd:pfam03215 153 QQVIRQWLYSSEPlPLIICITecEILEGDNNQRK 186
PRK04195 PRK04195
replication factor C large subunit; Provisional
 89-522 2.37e-21

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 97.68  E-value: 2.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987  89 PWVDKYKPETQHELAVHKKKIEEVETWLKAQVLEVKPKqggSVLLItGPPGCGKTTTIKILSKELGIQVQEwVNPilpdf 168
Cdd:PRK04195    3 PWVEKYRPKTLSDVVGNEKAKEQLREWIESWLKGKPKK---ALLLY-GPPGVGKTSLAHALANDYGWEVIE-LNA----- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 169 qkddykellSLESNFSVVpyqSQIAvfndflLRATKYSKLqmlgddLTTDKKIILVEELPNQFYR-DPNALHEILrKHVQ 247
Cdd:PRK04195   73 ---------SDQRTADVI---ERVA------GEAATSGSL------FGARRKLILLDEVDGIHGNeDRGGARAIL-ELIK 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 248 IGRCPLVFIVSDSVSgdnnqrlLFPRNIQEECSVsnISFNPVAPTIMMKFLNRIVtieaskNGEKIIVPNKTsLELLCQG 327
Cdd:PRK04195  128 KAKQPIILTANDPYD-------PSLRELRNACLM--IEFKRLSTRSIVPVLKRIC------RKEGIECDDEA-LKEIAER 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 328 CSGDIRSAINSLQfssskgensswskkkrmslksdaAISKSKQKkkhnstLENQEIQAIGGKDVSLFLFRALGKILYckr 407
Cdd:PRK04195  192 SGGDLRSAINDLQ-----------------------AIAEGYGK------LTLEDVKTLGRRDREESIFDALDAVFK--- 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 408 aplteldsprlpahlSEHDRDTLlvqpEEIVEMSHMPGDFFNlYLHQNYIDFFAEVDDLVPASEFLSFADI-LG-----G 481
Cdd:PRK04195  240 ---------------ARNADQAL----EASYDVDEDPDDLIE-WIDENIPKEYDDPEDIARAYDALSRADIfLGrvkrtQ 299

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1907092987 482 DWntrSLLReYSTSVATRGV--MHSNKARGFAHCQGGSSFRPL 522
Cdd:PRK04195  300 NY---DLWR-YASDLMTAGValAKEKKKRGFTRYQPPSYWRLL 338
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 106-157 1.02e-06

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: 51.45  E-value: 1.02e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907092987 106 KKKIEEVETWLKAQVL---EVKPKQGGSVLLiTGPPGCGKTTTIKILSKELGIQV 157
Cdd:COG0464   166 KEELRELVALPLKRPElreEYGLPPPRGLLL-YGPPGTGKTLLARALAGELGLPL 219
HLD_clamp_RarA cd18139
helical lid domain of recombination factor protein RarA; Recombination factor RarA ...
 291-350 1.20e-06

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: 46.47  E-value: 1.20e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 291 PTIMMKFLNRIVTIEASKNGEKIIVPnKTSLELLCQGCSGDIRSAINSLQFSSSKGENSS 350
Cdd:cd18139     3 EEDLEKLLKRALEDKERGGDRKVTID-DEALELLAEAADGDARSALNLLELAVLSAEEDG 61
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 129-154 4.73e-05

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: 43.90  E-value: 4.73e-05
                           10        20
                   ....*....|....*....|....*.
gi 1907092987  129 GSVLLITGPPGCGKTTTIKILSKELG 154
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELG 27
 
Name Accession Description Interval E-value
rad24 TIGR00602
checkpoint protein rad24; All proteins in this family for which functions are known are ...
 13-653 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: 979.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987  13 TKVTDWVAPAFDDFEANTAITTITASSLTFSNSSHRRKYLPSTLesnrLSARKRGRLSLEQTHGLETSRERLSDNEPWVD 92
Cdd:TIGR00602   1 MDVTDWVKPSFDDFLLSSLISTITKWSLSRPTSSHRRKNSPSTD----IHARKRGFLSLEQDTGLELSSENLDGNEPWVE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987  93 KYKPETQHELAVHKKKIEEVETWLKAQVLEVKPKQggsVLLITGPPGCGKTTTIKILSKELGIQVQEWVNPILPDFQKDD 172
Cdd:TIGR00602  77 KYKPETQHELAVHKKKIEEVETWLKAQVLENAPKR---ILLITGPSGCGKSTTIKILSKELGIQVQEWSNPTLPDFQKND 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 173 YKELLSLESNFSVVpyQSQIAVFNDFLLRATkySKLQMLGDDLTTDKKIILVEELPNQFYRDPNALHEILR-KHVQIGRC 251
Cdd:TIGR00602 154 HKVTLSLESCFSNF--QSQIEVFSEFLLRAT--NKLQMLGDDLMTDKKIILVEDLPNQFYRDTRALHEILRwKYVSIGRC 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 252 PLVFIVSDSVSGDNNQ-RLLFP------RNIQEECSVSNISFNPVAPTIMMKFLNRIVTIEASKNGEKIIVPNKTSLELL 324
Cdd:TIGR00602 230 PLVFIITESLEGDNNQrRLLFPaetimnKEILEEPRVSNISFNPIAPTIMKKFLNRIVTIEAKKNGEKIKVPKKTSVELL 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 325 CQGCSGDIRSAINSLQFSSSKGenSSWSKKKRMSLKSDAAISKSKQKKKHNSTLENQEIQAIGGKDVSLFLFRALGKILY 404
Cdd:TIGR00602 310 CQGCSGDIRSAINSLQFSSSKS--GSLPIKKRMSTKSDAHASKSKIKGKHSSNNENQEIQALGGKDVSLFLFRALGKILY 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 405 CKRAPLTELDSPRLPAHLSEHDRDTLLVQPEEIVEMSHMPGD-FFNLYLHQNYIDFFAEVDDLVPASEFLSFADILGGDW 483
Cdd:TIGR00602 388 CKRATLNELDSPRLPSHLSELSRDTLMVGPEEVVEMSHMPGDkTFNLYSHQNYNDFFVEFDDEVKASEFLNFADILSGDW 467

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 484 NTRSLLREYSTSVATRGVMHSNKARGFAHCQGG-SSFRPLHKPQWFLIQKKYRENCLAAKALF--VDFCLPALCLQTQLL 560
Cdd:TIGR00602 468 NTRSLLREYSTSSARRGVMHSNKARGIAHCQGGkSSFRPLHKPQWFLISKKYRENCLAAKALFkvEDFCLPADCLQTQLL 547

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 561 PYLALLTIPMRNKAQISFIQDVGRLPLKRSFGRLKMEALTDRELGLIDPDSGDESPHSGGQPAQEAPGEPAQAAQnadPE 640
Cdd:TIGR00602 548 PYLALDTIPMRNDAQISFIDDLGRLPLKRDFRRLKMEALTDREVGMIDPDSGDEETSFGDDPAVESDSDPSQAAG---PE 624

                         650
                  ....*....|...
gi 1907092987 641 TWSLPLSQNSGSD 653
Cdd:TIGR00602 625 TWSLPDSDNSLSE 637
Rad17 pfam03215
Rad17 P-loop domain;
82-269 1.89e-76

Rad17 P-loop domain;


Pssm-ID: 367398 [Multi-domain]  Cd Length: 186  Bit Score: 242.94  E-value: 1.89e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987  82 ERLSDNEPWVDKYKPETQHELAVHKKKIEEVETWLKAQVLEVKPKqggSVLLITGPPGCGKTTTIKILSKELGIQVQEWV 161
Cdd:pfam03215   1 INDDGGEQWYEKYKPNCLEQLAVHKRKIKDVQEWLDAMFLENAKH---RILLISGPSGCGKSTVIKELSKELGPKYREWS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 162 NPIL---PDFQKDDYKELLSLESNFsvvpyQSQIAVFNDFLLRATKYSKLQMLGDDLTTDKKIILVEELPNQFYRDPNAL 238
Cdd:pfam03215  78 NPTSfrsPPNQVTDFRGDCIVNSRF-----LSQMESFSEFELKGARYLVMQKRGKNAQGNKKLILIEDLPNVFHIDTRRF 152

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1907092987 239 HEILRKHVQIGRC-PLVFIVS--DSVSGDNNQRL 269
Cdd:pfam03215 153 QQVIRQWLYSSEPlPLIICITecEILEGDNNQRK 186
PRK04195 PRK04195
replication factor C large subunit; Provisional
 89-522 2.37e-21

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 97.68  E-value: 2.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987  89 PWVDKYKPETQHELAVHKKKIEEVETWLKAQVLEVKPKqggSVLLItGPPGCGKTTTIKILSKELGIQVQEwVNPilpdf 168
Cdd:PRK04195    3 PWVEKYRPKTLSDVVGNEKAKEQLREWIESWLKGKPKK---ALLLY-GPPGVGKTSLAHALANDYGWEVIE-LNA----- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 169 qkddykellSLESNFSVVpyqSQIAvfndflLRATKYSKLqmlgddLTTDKKIILVEELPNQFYR-DPNALHEILrKHVQ 247
Cdd:PRK04195   73 ---------SDQRTADVI---ERVA------GEAATSGSL------FGARRKLILLDEVDGIHGNeDRGGARAIL-ELIK 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 248 IGRCPLVFIVSDSVSgdnnqrlLFPRNIQEECSVsnISFNPVAPTIMMKFLNRIVtieaskNGEKIIVPNKTsLELLCQG 327
Cdd:PRK04195  128 KAKQPIILTANDPYD-------PSLRELRNACLM--IEFKRLSTRSIVPVLKRIC------RKEGIECDDEA-LKEIAER 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 328 CSGDIRSAINSLQfssskgensswskkkrmslksdaAISKSKQKkkhnstLENQEIQAIGGKDVSLFLFRALGKILYckr 407
Cdd:PRK04195  192 SGGDLRSAINDLQ-----------------------AIAEGYGK------LTLEDVKTLGRRDREESIFDALDAVFK--- 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 408 aplteldsprlpahlSEHDRDTLlvqpEEIVEMSHMPGDFFNlYLHQNYIDFFAEVDDLVPASEFLSFADI-LG-----G 481
Cdd:PRK04195  240 ---------------ARNADQAL----EASYDVDEDPDDLIE-WIDENIPKEYDDPEDIARAYDALSRADIfLGrvkrtQ 299

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1907092987 482 DWntrSLLReYSTSVATRGV--MHSNKARGFAHCQGGSSFRPL 522
Cdd:PRK04195  300 NY---DLWR-YASDLMTAGValAKEKKKRGFTRYQPPSYWRLL 338
rfc PRK00440
replication factor C small subunit; Reviewed
 88-348 7.36e-08

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 54.88  E-value: 7.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987  88 EPWVDKYKPETQHELAVHKKKIEEVETWLKAQVLevkPKqggsvLLITGPPGCGKTTTIKILSKEL-Giqvqewvnpilp 166
Cdd:PRK00440    5 EIWVEKYRPRTLDEIVGQEEIVERLKSYVKEKNM---PH-----LLFAGPPGTGKTTAALALARELyG------------ 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 167 dfqkDDYKELLsLESNFSvvpYQSQIAVFNDfllRATKYSKLQMLGDdltTDKKIILVEELPNQFYRDPNALHEILRKHV 246
Cdd:PRK00440   65 ----EDWRENF-LELNAS---DERGIDVIRN---KIKEFARTAPVGG---APFKIIFLDEADNLTSDAQQALRRTMEMYS 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 247 QIGRcplvFIVSDSVSgdnnQRLLFPrnIQEECSVsnISFNPVAPTIMMKFLNRIvtieASKNGEKIivpNKTSLELLCQ 326
Cdd:PRK00440  131 QNTR----FILSCNYS----SKIIDP--IQSRCAV--FRFSPLKKEAVAERLRYI----AENEGIEI---TDDALEAIYY 191

                         250       260
                  ....*....|....*....|..
gi 1907092987 327 GCSGDIRSAINSLQFSSSKGEN 348
Cdd:PRK00440  192 VSEGDMRKAINALQAAAATGKE 213
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 106-157 1.02e-06

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: 51.45  E-value: 1.02e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907092987 106 KKKIEEVETWLKAQVL---EVKPKQGGSVLLiTGPPGCGKTTTIKILSKELGIQV 157
Cdd:COG0464   166 KEELRELVALPLKRPElreEYGLPPPRGLLL-YGPPGTGKTLLARALAGELGLPL 219
HLD_clamp_RarA cd18139
helical lid domain of recombination factor protein RarA; Recombination factor RarA ...
 291-350 1.20e-06

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: 46.47  E-value: 1.20e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 291 PTIMMKFLNRIVTIEASKNGEKIIVPnKTSLELLCQGCSGDIRSAINSLQFSSSKGENSS 350
Cdd:cd18139     3 EEDLEKLLKRALEDKERGGDRKVTID-DEALELLAEAADGDARSALNLLELAVLSAEEDG 61
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 132-157 1.78e-05

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: 44.89  E-value: 1.78e-05
                          10        20
                  ....*....|....*....|....*.
gi 1907092987 132 LLITGPPGCGKTTTIKILSKELGIQV 157
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPF 26
dNK pfam01712
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2. ...
 134-171 4.46e-05

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: 45.00  E-value: 4.46e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1907092987 134 ITGPPGCGKTTTIKILSKELGIQ-----VQEWVNPILPDFQKD 171
Cdd:pfam01712   3 IEGNIGAGKSTLTKILSKRLGFKvfeepVDRWTNPYLDKFYKD 45
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 129-154 4.73e-05

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: 43.90  E-value: 4.73e-05
                           10        20
                   ....*....|....*....|....*.
gi 1907092987  129 GSVLLITGPPGCGKTTTIKILSKELG 154
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELG 27
PLN03025 PLN03025
replication factor C subunit; Provisional
 89-153 6.80e-05

replication factor C subunit; Provisional


Pssm-ID: 178596 [Multi-domain]  Cd Length: 319  Bit Score: 45.49  E-value: 6.80e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907092987  89 PWVDKYKPETQHELAVHKKKIEevetwlKAQVLevkpKQGGSV--LLITGPPGCGKTTTIKILSKEL 153
Cdd:PLN03025    2 PWVEKYRPTKLDDIVGNEDAVS------RLQVI----ARDGNMpnLILSGPPGTGKTTSILALAHEL 58
HLD_clamp_RFC cd18140
helical lid domain of replication factor C subunit; Replication factor C (RFC) is five-protein ...
 311-348 7.38e-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: 40.98  E-value: 7.38e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1907092987 311 EKIIVPNKtSLELLCQGCSGDIRSAINSLQFSSSKGEN 348
Cdd:cd18140    17 EGVKIDEE-ALEAIAEKSEGDMRKAINDLQAAAAGGGV 53
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 129-199 1.08e-04

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: 43.56  E-value: 1.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907092987 129 GSVLLITGPPGCGKTTTIKILSKELGiqVQEWVNPILPdfqKDDYKELLSLESnfsvVPYQSQIAVFNDFL 199
Cdd:COG4088     4 PMLLILTGPPGSGKTTFAKALAQRLY--AEGIAVALLH---SDDFRRFLVNES----FPKETYEEVVEDVR 65
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 116-154 1.37e-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: 42.52  E-value: 1.37e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907092987 116 LKAQVLEVKPKQGGSVLLITGPPGCGKTTTIKILSKELG 154
Cdd:cd00009     6 AIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELF 44
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 106-157 1.48e-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: 42.66  E-value: 1.48e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907092987 106 KKKIEEV--ETWLKAQVLEVKPKQGGSVLLItGPPGCGKTTTIKILSKELGIQV 157
Cdd:cd19481     2 KASLREAveAPRRGSRLRRYGLGLPKGILLY-GPPGTGKTLLAKALAGELGLPL 54
AAA_18 pfam13238
AAA domain;
133-155 3.62e-04

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 40.87  E-value: 3.62e-04
                          10        20
                  ....*....|....*....|...
gi 1907092987 133 LITGPPGCGKTTTIKILSKELGI 155
Cdd:pfam13238   2 LITGTPGVGKTTLAKELSKRLGF 24
Dck COG1428
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
134-171 5.38e-04

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 41.70  E-value: 5.38e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1907092987 134 ITGPPGCGKTTTIKILSKELGIQ-----VQEwvNPILPDFQKD 171
Cdd:COG1428     8 VEGNIGAGKTTLARLLAEHLGAElllepVED--NPFLEDFYED 48
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 46-154 6.66e-04

ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 42.30  E-value: 6.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987  46 SHRRKYLPSTLESNRLSARKrgrlsLEQTHGLETSRERLSDNEPWVDKYKPE-TQHELAVHKKKIEE----VETWLK-AQ 119
Cdd:COG1222    28 ELALLLQPVKALELLEEAPA-----LLLNDANLTQKRLGTPRGTAVPAESPDvTFDDIGGLDEQIEEireaVELPLKnPE 102

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907092987 120 VLE---VKPKQGgsVLLiTGPPGCGKTTTIKILSKELG 154
Cdd:COG1222   103 LFRkygIEPPKG--VLL-YGPPGTGKTLLAKAVAGELG 137
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
106-155 7.18e-04

Predicted ATPase, AAA+ superfamily [General function prediction only];


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 41.79  E-value: 7.18e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907092987 106 KKKIEEV-ETWLKAQVLE---VKPKQGgsvLLITGPPGCGKTTTIKILSKELGI 155
Cdd:COG1223    11 KKKLKLIiKELRRRENLRkfgLWPPRK---ILFYGPPGTGKTMLAEALAGELKL 61
Fap7 COG1936
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
131-157 8.70e-04

Broad-specificity NMP kinase [Nucleotide transport and metabolism];


Pssm-ID: 441539 [Multi-domain]  Cd Length: 173  Bit Score: 40.57  E-value: 8.70e-04
                          10        20
                  ....*....|....*....|....*..
gi 1907092987 131 VLLITGPPGCGKTTTIKILSKELGIQV 157
Cdd:COG1936     2 RIAITGTPGTGKTTVAKLLAERLGLEV 28
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 101-155 8.85e-04

first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 40.47  E-value: 8.85e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907092987 101 ELAVHKKKIEEVetwlkAQVLEVKPKQGgsvLLITGPPGCGKTTTIKILSKELGI 155
Cdd:cd19518    14 ELLIHPILPPEY-----FQHLGVEPPRG---VLLHGPPGCGKTMLANAIAGELKV 60
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 110-157 1.24e-03

first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 39.97  E-value: 1.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907092987 110 EEVETWLK----AQVLEVKPKQGgsvLLITGPPGCGKTTTIKILSKELGIQV 157
Cdd:cd19503    14 ELIELPLKypelFRALGLKPPRG---VLLHGPPGTGKTLLARAVANEAGANF 62
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 121-187 1.24e-03

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 39.94  E-value: 1.24e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907092987 121 LEVKPkqgGSVLLITGPPGCGKTTTIKILSKELgiqvqewvNP----ILPDFQKDDYKELLSLESNFSVVP 187
Cdd:pfam00005   6 LTLNP---GEILALVGPNGAGKSTLLKLIAGLL--------SPtegtILLDGQDLTDDERKSLRKEIGYVF 65
AAA_19 pfam13245
AAA domain;
116-165 2.16e-03

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 38.74  E-value: 2.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907092987 116 LKAQVLEVKPKqggsVLLITGPPGCGKTTTIKILSKELgIQVQEWVNPIL 165
Cdd:pfam13245   2 REAVRTALPSK----VVLLTGGPGTGKTTTIRHIVALL-VALGGVSFPIL 46
AAA_28 pfam13521
AAA domain;
134-157 2.19e-03

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 39.55  E-value: 2.19e-03
                          10        20
                  ....*....|....*....|....
gi 1907092987 134 ITGPPGCGKTTTIKILSKELGIQV 157
Cdd:pfam13521   4 ITGGPSTGKTTLAEALAARFGYPV 27
PRK04182 PRK04182
cytidylate kinase; Provisional
 134-155 2.52e-03

cytidylate kinase; Provisional


Pssm-ID: 235244 [Multi-domain]  Cd Length: 180  Bit Score: 39.40  E-value: 2.52e-03
                          10        20
                  ....*....|....*....|..
gi 1907092987 134 ITGPPGCGKTTTIKILSKELGI 155
Cdd:PRK04182    5 ISGPPGSGKTTVARLLAEKLGL 26
AAA_17 pfam13207
AAA domain;
135-157 2.62e-03

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 38.76  E-value: 2.62e-03
                          10        20
                  ....*....|....*....|...
gi 1907092987 135 TGPPGCGKTTTIKILSKELGIQV 157
Cdd:pfam13207   1 TGVPGSGKTTQLKKLAEKLGFPH 23
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 116-150 2.65e-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: 39.15  E-value: 2.65e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1907092987 116 LKAQVLEVKPkqgGSVLLITGPPGCGKTTTIKILS 150
Cdd:cd00267    15 LDNVSLTLKA---GEIVALVGPNGSGKSTLLRAIA 46
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 127-154 3.37e-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: 39.77  E-value: 3.37e-03
                          10        20
                  ....*....|....*....|....*...
gi 1907092987 127 QGGSVLLITGPPGCGKTTTIKILSKELG 154
Cdd:COG3267    41 QGGGFVVLTGEVGTGKTTLLRRLLERLP 68
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
 128-153 4.57e-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: 38.30  E-value: 4.57e-03
                          10        20
                  ....*....|....*....|....*.
gi 1907092987 128 GGSVLLITGPPGCGKTTTIKILSKEL 153
Cdd:cd17933    11 RNRVSVLTGGAGTGKTTTLKALLAAL 36
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
 134-156 5.47e-03

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 37.85  E-value: 5.47e-03
                          10        20
                  ....*....|....*....|...
gi 1907092987 134 ITGPPGCGKTTTIKILSKELGIQ 156
Cdd:cd02020     4 IDGPAGSGKSTVAKLLAKKLGLP 26
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 116-150 5.75e-03

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 38.29  E-value: 5.75e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1907092987 116 LKAQVLEVKPkqgGSVLLITGPPGCGKTTTIKILS 150
Cdd:cd03223    17 LKDLSFEIKP---GDRLLITGPSGTGKSSLFRALA 48
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 118-259 6.58e-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: 37.87  E-value: 6.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 118 AQVLEVKPKQGGSVLLITGPPGCGKTTTIKILSKELGIQVQEWVNPILPDFQKddYKELLSLESNFSVVPYqsqiavfnd 197
Cdd:pfam13191  13 LDALDRVRSGRPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLP--YSPLLEALTREGLLRQ--------- 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907092987 198 fLLRATKYSKLQMLGDDLTTdkkiiLVEELPNQFYRDPNALHEILRKHVQIGRC---PLVFIVSD 259
Cdd:pfam13191  82 -LLDELESSLLEAWRAALLE-----ALAPVPELPGDLAERLLDLLLRLLDLLARgerPLVLVLDD 140
AAA_22 pfam13401
AAA domain;
126-156 7.61e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 37.32  E-value: 7.61e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1907092987 126 KQGGSVLLITGPPGCGKTTTIKILSKELGIQ 156
Cdd:pfam13401   2 RFGAGILVLTGESGTGKTTLLRRLLEQLPEV 32
44 PHA02544
clamp loader, small subunit; Provisional
 90-157 7.81e-03

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 38.82  E-value: 7.81e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907092987  90 WVDKYKPETQHE--LAVHKKKIeevetwLKAQVlevkpKQGG--SVLLITGPPGCGKTTTIKILSKELGIQV 157
Cdd:PHA02544   11 WEQKYRPSTIDEciLPAADKET------FKSIV-----KKGRipNMLLHSPSPGTGKTTVAKALCNEVGAEV 71
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 132-160 8.56e-03

MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 38.61  E-value: 8.56e-03
                          10        20
                  ....*....|....*....|....*....
gi 1907092987 132 LLITGPPGCGKTTTIKILSKELGIQVQEW 160
Cdd:COG0714    34 LLLEGVPGVGKTTLAKALARALGLPFIRI 62
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 127-276 8.60e-03

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 38.54  E-value: 8.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092987 127 QGGSVLLITGPPGCGKTTTIKILSKELGIQVQEwvnpILpdFQKDDYKElLSLESNFSVVPYQSQI-AVFNDfllraTKY 205
Cdd:PRK10247   31 RAGEFKLITGPSGCGKSTLLKIVASLISPTSGT----LL--FEGEDIST-LKPEIYRQQVSYCAQTpTLFGD-----TVY 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907092987 206 SKL----QMLGDdlTTDKKIILVE----ELPNqfyrdpnalhEILRKHVqigrcplvfivsDSVSGDNNQRLLFPRNIQ 276
Cdd:PRK10247   99 DNLifpwQIRNQ--QPDPAIFLDDlerfALPD----------TILTKNI------------AELSGGEKQRISLIRNLQ 153
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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