|
Name |
Accession |
Description |
Interval |
E-value |
| Sms |
COG1066 |
DNA repair protein RadA/Sms, contains AAA+ ATPase domain [Replication, recombination and ... |
1-513 |
0e+00 |
|
DNA repair protein RadA/Sms, contains AAA+ ATPase domain [Replication, recombination and repair];
Pssm-ID: 440685 [Multi-domain] Cd Length: 453 Bit Score: 582.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 1 MAKTKdEAYECSACGWQVSKWVGQCPNCKEWGTLEKVAIRSSSGKsgstledkiaaraakqrrrsaaatepgarggRRKA 80
Cdd:COG1066 1 MAKTK-TVYVCQECGYESPKWLGRCPECGAWNTLVEEVVAKAKKG-------------------------------RAAS 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 81 SSTSVAAESQRLAQralddeaeerflAETSATDRIPTssseltaitgisaktahavrtGIGELDRVLGSGIVPGSLVLLA 160
Cdd:COG1066 49 GAAGRASKPVPLSE------------VEAEEEPRIST---------------------GIGELDRVLGGGLVPGSVVLIG 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 161 GEPGVGKSTLLLEVAYRCADGDlGPTLYVTGEESVGQVRLRAERTGALSDSLYLSAVSNIEDVIDLTLELSPGLLIVDSV 240
Cdd:COG1066 96 GEPGIGKSTLLLQVAARLAKKG-GKVLYVSGEESASQIKLRAERLGLLSDNLYLLAETDLEAILATIEELKPDLLVIDSI 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 241 QTMR-ADVEGARGGVAQARAVTSALAALAKETGTAIFLVGHVTKDGNVAGPRTMEHLVDVVLNFEGDRHSGLRFLRGLKN 319
Cdd:COG1066 175 QTMYsEELESAPGSVSQVRECAAELIRLAKETGIAVFLVGHVTKEGSIAGPRVLEHMVDTVLYFEGDRHSRYRILRAVKN 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 320 RFGSTDEVGCFEQTAGGIAEVEDPSGLFL-HHRTPTSGTAITVAMDGRRPLLAEVQGLVINTEAHNPRRNVSGLDPRRVP 398
Cdd:COG1066 255 RFGSTNEIGVFEMTEKGLREVSNPSELFLsERDEPVPGSAVTVTMEGTRPLLVEVQALVSPSSFGNPRRTAVGLDSNRLA 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 399 MVAAVLTEHGNFKqLARMEMYVSTVGGMTLSEPAADLAIALALASSMTKQTFQDKTIALGELGLAGEVRRVTDLEWRLKE 478
Cdd:COG1066 335 MLLAVLEKRAGLP-LGDQDVYVNVVGGLKITEPAADLAVALAIASSFRDRPLPPDTVFFGEVGLTGEIRPVSRIEQRLKE 413
|
490 500 510
....*....|....*....|....*....|....*...
gi 1093455227 479 AHRMGFDTAIVPRGAKG---PAGMRLLEAGTVAEAIEL 513
Cdd:COG1066 414 AAKLGFKRAIVPKGNKKklkPKGIEIIGVSTLEEALEA 451
|
|
| sms |
TIGR00416 |
DNA repair protein RadA; The gene protuct codes for a probable ATP-dependent protease involved ... |
1-511 |
3.78e-140 |
|
DNA repair protein RadA; The gene protuct codes for a probable ATP-dependent protease involved in both DNA repair and degradation of proteins, peptides, glycopeptides. Also known as sms. Residues 11-28 of the SEED alignment contain a putative Zn binding domain. Residues 110-117 of the seed contain a putative ATP binding site both documented in Haemophilus (SP:P45266) and in Listeria monocytogenes (SP:Q48761) . for E.coli see ( J. BACTERIOL. 178:5045-5048(1996)). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273067 [Multi-domain] Cd Length: 454 Bit Score: 411.88 E-value: 3.78e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 1 MAKTKdEAYECSACGWQVSKWVGQCPNCKEWGTLEKVAIRSSsgksgstledkiaaraakqrrrsaaatePGARGGRRKA 80
Cdd:TIGR00416 1 MAKAK-SKFVCQHCGADSPKWQGKCPACHAWNTITEERLHRS----------------------------LGAQKNRRNS 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 81 SSTSV--AAESQRLAQraLDDEAEERFLaetsatdriptssseltaitgisaktahavrTGIGELDRVLGSGIVPGSLVL 158
Cdd:TIGR00416 52 GKAGIpqAQKSQTISA--IELEEVPRFS-------------------------------SGFGELDRVLGGGIVPGSLIL 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 159 LAGEPGVGKSTLLLEVAYRCAdGDLGPTLYVTGEESVGQVRLRAERTGALSDSLYLSAVSNIEDVIDLTLELSPGLLIVD 238
Cdd:TIGR00416 99 IGGDPGIGKSTLLLQVACQLA-KNQMKVLYVSGEESLQQIKMRAIRLGLPEPNLYVLSETNWEQICANIEEENPQACVID 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 239 SVQTM-RADVEGARGGVAQARAVTSALAALAKETGTAIFLVGHVTKDGNVAGPRTMEHLVDVVLNFEGDRHSGLRFLRGL 317
Cdd:TIGR00416 178 SIQTLySPDISSAPGSVSQVRECTAELMRLAKTRGIAIFIVGHVTKEGSIAGPKVLEHMVDTVLYFEGDRDSRFRILRSV 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 318 KNRFGSTDEVGCFEQTAGGIAEVEDPSGLFLHHRT-PTSGTAITVAMDGRRPLLAEVQGLVINTEAHNPRRNVSGLDPRR 396
Cdd:TIGR00416 258 KNRFGATNEIGIFEMTEQGLREVLNPSAIFLSRREePMSGSSITVTWEGTRPLLVEIQALVSPTSFANPRRVATGLDQNR 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 397 VPMVAAVLTEHGNFkQLARMEMYVSTVGGMTLSEPAADLAIALALASSMTKQTFQDKTIALGELGLAGEVRRVTDLEWRL 476
Cdd:TIGR00416 338 LALLLAVLEKRLGL-PLADQDVFLNVAGGVKVSEPAADLALLIAIVSSFRDRPLDPDLVFLGEVGLAGEIRPVPSLEERL 416
|
490 500 510
....*....|....*....|....*....|....*...
gi 1093455227 477 KEAHRMGFDTAIVPRGAKG---PAGMRLLEAGTVAEAI 511
Cdd:TIGR00416 417 KEAAKLGFKRAIVPKANSPktaPEGIKVIGVKKVGDAL 454
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
9-340 |
1.10e-127 |
|
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a role in recombination and recombinational repair of DNA damaged by UV radiation, X-rays, and chemical agent and is responsible for the stabilization or processing of branched DNA molecules.
Pssm-ID: 410866 [Multi-domain] Cd Length: 268 Bit Score: 373.02 E-value: 1.10e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 9 YECSACGWQVSKWVGQCPNCKEWGTLEKVAIRSSSGKSgstledkiaaraakqrrrsaaatepgarggrRKASSTSVAAE 88
Cdd:cd01121 1 YVCQECGYESPKWLGRCPSCGEWNTFVEEVVSASSSAS-------------------------------RRASASPSPSK 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 89 SQRLAQraLDDEAEERFLaetsatdriptssseltaitgisaktahavrTGIGELDRVLGSGIVPGSLVLLAGEPGVGKS 168
Cdd:cd01121 50 PLPLSD--VEAEEEERIS-------------------------------TGIGELDRVLGGGLVPGSVVLIGGDPGIGKS 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 169 TLLLEVAYRCADGDlGPTLYVTGEESVGQVRLRAERTGALSDSLYLSAVSNIEDVIDLTLELSPGLLIVDSVQTMR-ADV 247
Cdd:cd01121 97 TLLLQVAARLAQRG-GKVLYVSGEESLSQIKLRAERLGLGSDNLYLLAETNLEAILAEIEELKPSLVVIDSIQTVYsPEL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 248 EGARGGVAQARAVTSALAALAKETGTAIFLVGHVTKDGNVAGPRTMEHLVDVVLNFEGDRHSGLRFLRGLKNRFGSTDEV 327
Cdd:cd01121 176 TSSPGSVSQVRECAAELLRLAKETGIPVFLVGHVTKDGAIAGPKVLEHMVDTVLYFEGDRGSSYRILRSVKNRFGPTNEI 255
|
330
....*....|...
gi 1093455227 328 GCFEQTAGGIAEV 340
Cdd:cd01121 256 GVFEMTENGLREV 268
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
136-320 |
7.51e-25 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 102.30 E-value: 7.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 136 VRTGIGELDRVLGSGIVPGSLVLLAGEPGVGKSTLLLEVAYR-CADGDlgPTLYVTGEESVGQVRLRAERTG-------- 206
Cdd:COG0467 2 VPTGIPGLDELLGGGLPRGSSTLLSGPPGTGKTTLALQFLAEgLRRGE--KGLYVSFEESPEQLLRRAESLGldleeyie 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 207 --------ALSDSLYLSAVSNIEDVIDLTLELSPGLLIVDSVQTMRAdvegARGGVAQARAVTSALAALAKETGTAIFLV 278
Cdd:COG0467 80 sgllriidLSPEELGLDLEELLARLREAVEEFGAKRVVIDSLSGLLL----ALPDPERLREFLHRLLRYLKKRGVTTLLT 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1093455227 279 GHVTKDGNVAGPRTMEHLVDVVLNFEGDRHSG--LRFLRGLKNR 320
Cdd:COG0467 156 SETGGLEDEATEGGLSYLADGVILLRYVELGGelRRALSVLKMR 199
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
150-403 |
5.82e-17 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 81.87 E-value: 5.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 150 GIVP-GSLVLLAGEPGVGKSTLLLEVAYRCADG-DL-------GPTLYVTGEESVGQVRLRAERTGA------------- 207
Cdd:COG3598 8 GLLPeGGVTLLAGPPGTGKSFLALQLAAAVAAGgPWlgrrvppGKVLYLAAEDDRGELRRRLKALGAdlglpfadldgrl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 208 --LSDSLYLSAVSNIEDVIDLTLELSPGLLIVDSVQTMRADVEGARggvAQARAVTSALAALAKETGTAIFLVGHVTKDG 285
Cdd:COG3598 88 rlLSLAGDLDDTDDLEALERAIEEEGPDLVVIDPLARVFGGDENDA---EEMRAFLNPLDRLAERTGAAVLLVHHTGKGG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 286 nvAGPRTMEHL---------VDVVLNFEGDRHSGLRFLRGLKNRFGSTDEvgcFEQTAGGIAEVEDPSGLFLHHRTPTSG 356
Cdd:COG3598 165 --AGKDSGDRArgssalrgaARSVLVLSREKGEDLRVLTRAKSNYGPEIA---LRWDNGGRLALEEVAALTAGAGEVELK 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1093455227 357 TAITVAMDGRRPLLAEVQGLVINTEAHNPRRNVSGLDPRRVPMVAAV 403
Cdd:COG3598 240 ELVGGVARTGTDSELEEGLLEVPLAEAESAGEDAELAAKAVADEKDA 286
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
136-325 |
6.96e-17 |
|
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410869 [Multi-domain] Cd Length: 222 Bit Score: 79.62 E-value: 6.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 136 VRTGIGELDRVLGSGIVPGSLVLLAGEPGVGKSTLLLEVAYR-CADGDlgPTLYVTGEESVGQVRLRAERTG------AL 208
Cdd:cd01124 1 VKTGIPGLDELLGGGIPKGSVTLLTGGPGTGKTLFGLQFLYAgAKNGE--PGLFFTFEESPERLLRNAKSFGwdfdemED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 209 SDSLYLSAVSNIEDVIDLTLELSPGL-----------LIVDSVQTMRADVEGARggvaQARAVTSALAALAKETGTAIFL 277
Cdd:cd01124 79 EGKLIIVDAPPTEAGRFSLDELLSRIlsiiksfkakrVVIDSLSGLRRAKEDQM----RARRIVIALLNELRAAGVTTIF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1093455227 278 VGHVTKDGN--VAGPRTMEHLVD--VVLNF---EGDRHsglRFLRGLKNRFGSTD 325
Cdd:cd01124 155 TSEMRSFLSseSAGGGDVSFIVDgvILLRYveiEGELR---RTIRVLKMRGTGHD 206
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
151-286 |
4.95e-16 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 76.27 E-value: 4.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 151 IVPGSLVLLAGEPGVGKSTLLLEVAYRCADGDL----------GPTLYVTGEESVGQVRLRAERTGA------------L 208
Cdd:pfam13481 30 LPAGGLGLLAGAPGTGKTTLALDLAAAVATGKPwlggprvpeqGKVLYVSAEGPADELRRRLRAAGAdldlparllflsL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 209 SDSLYL-----------SAVSNIEDVIDLTLElsPGLLIVDSVQ-TMRADVEGARggvaQARAVTSALAALAKETGTAIF 276
Cdd:pfam13481 110 VESLPLffldrggplldADVDALEAALEEVED--PDLVVIDPLArALGGDENSNS----DVGRLVKALDRLARRTGATVL 183
|
170
....*....|
gi 1093455227 277 LVGHVTKDGN 286
Cdd:pfam13481 184 LVHHVGKDGA 193
|
|
| Rubredoxin_2 |
pfam18073 |
Rubredoxin metal binding domain; This is the C-terminal rubredoxin metal binding domain found ... |
9-35 |
3.75e-12 |
|
Rubredoxin metal binding domain; This is the C-terminal rubredoxin metal binding domain found in Interest in lipopolysaccharide (LPS) assembly protein B (LapB). Rubredoxin proteins form small non-heme iron binding sites that use four cysteine residues to coordinate a single metal ion in a tetrahedral environment. Rubredoxins are most commonly found in bacterial systems, but have also been found in eukaryotes. The key features of these rubredoxin-like domains are the extended loops or 'knuckles' and the tetracysteine mode of iron binding. Structural analysis of LapB from Escherichia coli show that the rubredoxin metal binding domain is intimately bound to the TPR motifs and that this association to the TPR motifs is essential to LPS regulation and growth in vivo. Other family members include RadA proteins which play a role in DNA damage repair. In E. coli, a protein known as RadA (or Sms) participates in the recombinational repair of radiation-damaged DNA in a process that uses an undamaged DNA strand in one DNA duplex to fill a DNA strand gap in a homologous sister DNA duplex. RadA carries a zinc finger at the N-terminal domain.
Pssm-ID: 436248 [Multi-domain] Cd Length: 28 Bit Score: 60.25 E-value: 3.75e-12
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
153-304 |
7.76e-12 |
|
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: 63.16 E-value: 7.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 153 PGSLVLLAGEPGVGKSTLLLEVAyRCADGDLGPTLYVTGEESVGQVRLRAERTGALSDSLYLSAVSNIEDVIDLTLELSP 232
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALA-RELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKP 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093455227 233 GLLIVDSVQTMRADVEGARggvAQARAVTSALAALAKETGTAIFLVGHVTKDgnvAGPRTMEHLVDVVLNFE 304
Cdd:smart00382 80 DVLILDEITSLLDAEQEAL---LLLLEELRLLLLLKSEKNLTVILTTNDEKD---LGPALLRRRFDRRIVLL 145
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
136-337 |
3.95e-11 |
|
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and eukaryotes. More than one copy is sometimes found in each protein. This family includes KaiC, which is one of the Kai proteins among which direct protein-protein association may be a critical process in the generation of circadian rhythms in cyanobacteria.
Pssm-ID: 429095 [Multi-domain] Cd Length: 231 Bit Score: 63.03 E-value: 3.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 136 VRTGIGELDRVLGSGIVPGSLVLLAGEPGVGKSTLLLEVAYRCADGDLGPTLYVTGEESVGQVRLRAERTG--------- 206
Cdd:pfam06745 1 VKTGIPGLDEILKGGFPEGRVVLITGGPGTGKTIFGLQFLYNGALKYGEPGVFVTLEEPPEDLRENARSFGwdlekleee 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 207 -------ALSDSLYLSAVSNIEDVIDLTLEL-------SPGLLIVDSVQTMradveGARGGVAQARAVTSALAALAKETG 272
Cdd:pfam06745 81 gklaiidASTSGIGIAEVEDRFDLEELIERLreaireiGAKRVVIDSITTL-----FYLLKPAVAREILRRLKRVLKGLG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093455227 273 -TAIFLVGHVTKDGNVAGPRTMEHLVD--VVLNFEGDRHSGLRFLRGLKNRFGSTD-EVGCFEQTAGGI 337
Cdd:pfam06745 156 vTAIFTSEKPSGEGGIGGYGVEEFIVDgvIRLDLKEIEEERVRTIEIVKMRGTPHSmKRYPFEITDNGI 224
|
|
| DnaB_C |
pfam03796 |
DnaB-like helicase C terminal domain; The hexameric helicase DnaB unwinds the DNA duplex at ... |
136-270 |
6.11e-11 |
|
DnaB-like helicase C terminal domain; The hexameric helicase DnaB unwinds the DNA duplex at the Escherichia coli chromosome replication fork. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerization of the N-terminal domain has been observed and may occur during the enzymatic cycle. This C-terminal domain contains an ATP-binding site and is therefore probably the site of ATP hydrolysis.
Pssm-ID: 427509 [Multi-domain] Cd Length: 254 Bit Score: 62.82 E-value: 6.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 136 VRTGIGELDRVLgSGIVPGSLVLLAGEPGVGKSTLLLEVAYRCADGDLGPTLYV----TGEE-------SVGQVRLRAER 204
Cdd:pfam03796 2 LPTGFTDLDRLT-GGLQPGDLIIIAARPSMGKTAFALNIARNAAVKHKKPVAIFslemSAEQlvmrllaSEAGVDSQKLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 205 TGALSDS----LYlSAVSNIED---VIDLTLELSP----------------GLLIVDSVQTMRAdveGARGG--VAQARA 259
Cdd:pfam03796 81 TGQLTDEdwekLA-KAAGRLSEaplYIDDTPGLSIaeirakarrlkrehglGLIVIDYLQLMSG---GSRGEnrQQEISE 156
|
170
....*....|.
gi 1093455227 260 VTSALAALAKE 270
Cdd:pfam03796 157 ISRSLKALAKE 167
|
|
| DnaB_C |
cd00984 |
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase ... |
135-278 |
6.25e-11 |
|
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase DnaB unwinds the DNA duplex at the chromosome replication fork. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerization of the N-terminal domain has been observed and may occur during the enzymatic cycle. This C-terminal domain contains an ATP-binding site and is therefore probably the site of ATP hydrolysis.
Pssm-ID: 410864 [Multi-domain] Cd Length: 256 Bit Score: 62.91 E-value: 6.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 135 AVRTGIGELDRVLGsGIVPGSLVLLAGEPGVGKSTLLLEVAYRCADGDLGPTLYVTGEES-----------VGQVRLRAE 203
Cdd:cd00984 1 GLPTGFTDLDKLTG-GLQPGDLIIIAARPSMGKTAFALNIAENIALDEGLPVLFFSLEMSaeqlaerllssESGVSLSKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 204 RTGALSD---SLYLSAVSNIED---VID----LTLE-------------LSPGLLIVDSVQTMRADvEGARGGVAQARAV 260
Cdd:cd00984 80 RTGRLDDedwERLTAAMGELSElplYIDdtpgLTVDeirakarrlkrehGGLGLIVIDYLQLIRGS-KRAENRQQEVAEI 158
|
170
....*....|....*...
gi 1093455227 261 TSALAALAKETGTAIFLV 278
Cdd:cd00984 159 SRSLKALAKELNVPVIAL 176
|
|
| RepA_RSF1010_like |
cd01125 |
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family ... |
154-286 |
7.94e-10 |
|
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family includes the homo-hexameric replicative helicase RepA encoded by plasmid RSF1010. RSF1010 is found in most Gram-negative bacteria and some Gram-positive bacteria . The RepA protein of Plasmid RSF1010 is a 5'-3' DNA helicase which can utilize ATP, dATP, GTP and dGTP (and CTP and dCTP to a lesser extent).
Pssm-ID: 410870 Cd Length: 238 Bit Score: 59.32 E-value: 7.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 154 GSLVLLAGEPGVGKSTLLLEVAYRCADGDL---------GPTLYVTGEESVGQV--RLRA-------ERTGALS----DS 211
Cdd:cd01125 1 GTLGMLVGPPGSGKSFLALDLAVAVATGRDwlgerrvkqGRVVYLAAEDPRDGLrrRLKAigahlgdEDAALAEnlviEN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093455227 212 LY---LSAVSNIEDVIDLTLEL-SPGLLIVDSVQtmRADVEGARGGVAQARAVTSALAALAKETGTAIFLVGHVTKDGN 286
Cdd:cd01125 81 LRgkpVSIDAEAPELERIIEELeGVRLIIIDTLA--RVLHGGDENDAADMGAFVAGLDRIARETGAAVLLVHHTGKDAA 157
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
136-232 |
2.49e-09 |
|
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410896 [Multi-domain] Cd Length: 225 Bit Score: 57.74 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 136 VRTGIGELDRVLGSGIVPGSLVLLAGEPGVGKSTLLLE-VAYRCADGdlGPTLYVTGEESVGQVRLRAERTGALSDSLY- 213
Cdd:cd19488 1 ISTGIPGLDDILRGGLPPRRLYLVEGAPGTGKTTLALQfLLEGAANG--ETGLYITLSETEQELRAVALSHGWSLDGIHi 78
|
90 100
....*....|....*....|.
gi 1093455227 214 --LSAVSNIEDVIDLTLELSP 232
Cdd:cd19488 79 feLSPSESALDAAQQYTILHP 99
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
138-337 |
1.39e-08 |
|
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional homologue to the bacterial RecA. The precise function of RadB is unclear.
Pssm-ID: 410882 [Multi-domain] Cd Length: 216 Bit Score: 55.01 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 138 TGIGELDRVLGSGIVPGSLVLLAGEPGVGKSTLLLEVAYRCADGDLGpTLYVTGE----ESVGQVrlRAERTGALSDSLY 213
Cdd:cd01394 3 TGSKSLDSLLGGGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKK-VVYIDTEglspERFQQI--AGERFESIASNII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 214 L----------SAVSNIEDVIDltlELSPGLLIVDSVQTM-RADVEGARGGVAQARAVTSALAALAKETGTAIFLVGHV- 281
Cdd:cd01394 80 VfepysfdeqgVAIQEAEKLLK---SDKVDLVVVDSATALyRLELGDDSEANRELSRQMSKLLSIARKYDIPVVITNQVy 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 282 --TKDGNVA--GPRTMEHLVDVVLNFEGDRhSGLRFLRGLKNRFGSTDEVGCFEQTAGGI 337
Cdd:cd01394 157 sdIDDDRLKpvGGTLLEHWSKAIIRLEKSP-PGLRRATLEKHRSRPEGQSAGFRITDRGI 215
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
136-270 |
1.01e-07 |
|
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410895 [Multi-domain] Cd Length: 219 Bit Score: 52.69 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 136 VRTGIGELDRVLGSGIVPGSLVLLAGEPGVGKSTLLLEVAYRCADGDLGPTLYVTgEESVGQVRLRAERTG----ALSDS 211
Cdd:cd19487 1 VSSGVPELDELLGGGLERGTSTLLIGPAGVGKSTLALQFAKAAAARGERSVLFSF-DESIGTLFERSEALGidlrAMVEK 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1093455227 212 LYLSavsnIEDVIdlTLELSPGllivDSVQTMRADVEGARGGVAQARAVTSALAALAKE 270
Cdd:cd19487 80 GLLS----IEQID--PAELSPG----EFAQRVRTSVEQEDARVVVIDSLNGYLNAMPDE 128
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
106-284 |
1.04e-07 |
|
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ATPase RecA protein.
Pssm-ID: 462471 [Multi-domain] Cd Length: 255 Bit Score: 53.07 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 106 LAETSATDrIPTSSSELTAITgisaktahavrTGIGELDRVLGSGIVPGSLVLLAGEPGVGKSTLLLEVAYRCA-----D 180
Cdd:pfam08423 1 MGFTTATE-LHQRRSELIQIT-----------TGSKELDKLLGGGIETGSITEIFGEFRTGKTQLCHTLCVTCQlplemG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 181 GDLGPTLYVTGEESVGQVRLR--AERTG-----ALSDSLYLSAVsNIEDVIDLTLELSP-------GLLIVDSVQTM-RA 245
Cdd:pfam08423 69 GGEGKALYIDTEGTFRPERLVaiAERYGldpedVLDNVAYARAY-NSEHQMQLLQQAAAmmsesrfALLIVDSATALyRT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1093455227 246 DVEGaRGGVA----QARAVTSALAALAKETGTAIFLVGHVTKD 284
Cdd:pfam08423 148 DFSG-RGELAerqqHLAKFLRTLQRLADEFGVAVVITNQVVAQ 189
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
136-284 |
1.16e-07 |
|
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic proteins RAD51, RAD55/57 and the meiosis-specific protein DMC1, and the archaeal protein RadA. They are closely related to the bacterial RecA group. Rad51 proteins catalyze a similar recombination reaction as RecA, using ATP-dependent DNA binding activity and a DNA-dependent ATPase. However, this reaction is less efficient and requires accessory proteins such as RAD55/57 .
Pssm-ID: 410868 [Multi-domain] Cd Length: 234 Bit Score: 52.92 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 136 VRTGIGELDRVLGSGIVPGSLVLLAGEPGVGKSTLLLEVAYRC-----ADGDLGPTLYVTGEESVGQVRLR--AERTG-- 206
Cdd:cd01123 1 ITTGSKELDKLLGGGIETGSITEMFGEFRTGKTQLCHTLAVTCqlpidRGGGEGKAIYIDTEGTFRPERLRaiAQRFGld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 207 ---ALSDSLYLSAVSN------IEDVIDLTLELSPGLLIVDSVQTM-RADVEGaRGGVAQARA----VTSALAALAKETG 272
Cdd:cd01123 81 pddVLDNVAYARAFNSdhqtqlLDQAAAMMVESRFKLLIVDSATALyRTDYSG-RGELSARQMhlakFLRMLQRLADEFG 159
|
170
....*....|..
gi 1093455227 273 TAIFLVGHVTKD 284
Cdd:cd01123 160 VAVVVTNQVVAQ 171
|
|
| PRK07773 |
PRK07773 |
replicative DNA helicase; Validated |
113-270 |
1.78e-07 |
|
replicative DNA helicase; Validated
Pssm-ID: 236093 [Multi-domain] Cd Length: 886 Bit Score: 53.99 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 113 DRIPTSSSELTAITGisaktahaVRTGIGELDRVLGsGIVPGSLVLLAGEPGVGKSTLLLEVAYRCADGDLGPTLYVTGE 192
Cdd:PRK07773 185 DEIDAIASSGGLARG--------VPTGFTELDAMTN-GLHPGQLIIVAARPSMGKTTFGLDFARNCAIRHRLAVAIFSLE 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 193 ESVGQVRLR---AE--------RTGALSDSLY------LSAVSN----IEDVIDLTL------------ELSPGLLIVDS 239
Cdd:PRK07773 256 MSKEQLVMRllsAEakiklsdmRSGRMSDDDWtrlaraMGEISEapifIDDTPNLTVmeirakarrlrqEANLGLIVVDY 335
|
170 180 190
....*....|....*....|....*....|....
gi 1093455227 240 VQTMradvEGARGG---VAQARAVTSALAALAKE 270
Cdd:PRK07773 336 LQLM----TSGKKYenrQQEVSEISRHLKLLAKE 365
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
113-284 |
2.13e-07 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 52.69 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 113 DRIPTSSSELTAITGISAKTAHAVR-------TGIGELDRVLGSGIVPGSLVLLAGEPGVGKSTLLLEVAYRCA-----D 180
Cdd:PTZ00035 70 EKIKEAASKLVPMGFISATEYLEARkniiritTGSTQLDKLLGGGIETGSITELFGEFRTGKTQLCHTLCVTCQlpieqG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 181 GDLGPTLYVTGE-----ESVGQVrlrAERTG-----ALSDSLYLSAvSNIEDVIDLTLELSP-------GLLIVDSVQTM 243
Cdd:PTZ00035 150 GGEGKVLYIDTEgtfrpERIVQI---AERFGldpedVLDNIAYARA-YNHEHQMQLLSQAAAkmaeerfALLIVDSATAL 225
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1093455227 244 -RADVEGaRGGVAqARA-----VTSALAALAKETGTAIFLVGHVTKD 284
Cdd:PTZ00035 226 fRVDYSG-RGELA-ERQqhlgkFLRALQKLADEFNVAVVITNQVMAD 270
|
|
| DnaB |
COG0305 |
Replicative DNA helicase [Replication, recombination and repair]; |
89-275 |
4.25e-07 |
|
Replicative DNA helicase [Replication, recombination and repair];
Pssm-ID: 440074 [Multi-domain] Cd Length: 429 Bit Score: 52.39 E-value: 4.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 89 SQRLAQRALD---------DEAEERF--LAETSAT--------------DRIPTSSSELTAITGISaktahavrTGIGEL 143
Cdd:COG0305 110 GTEIVELAYDededvdellDEAEQKIfeIAEKRSSkgfvsisdilkealERIEELYKNGGGITGVP--------TGFTDL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 144 DRVLGsGIVPGSLVLLAGEPGVGKSTLLLEVAYRCADGDLGPTLYV----TGEE-------SVGQVRLRAERTGALSDS- 211
Cdd:COG0305 182 DKLTG-GLQPGDLIILAARPSMGKTAFALNIARNAAIKEGKPVAIFslemSAEQlvmrllsSEARIDSSKLRTGKLSDEd 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 212 --LYLSAVSNIEDV---IDLTLELSP----------------GLLIVDSVQTMRADveGARGGVAQARA-VTSALAALAK 269
Cdd:COG0305 261 weRLSSAAGELSEApiyIDDTPGLTIaeirakarrlkrehglGLIVIDYLQLMSGS--GRSENRQQEISeISRSLKALAK 338
|
....*.
gi 1093455227 270 ETGTAI 275
Cdd:COG0305 339 ELNVPV 344
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
138-341 |
6.17e-07 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 50.25 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 138 TGIGELDRVLGSGIVPGSLVLLAGEPGVGKSTLLLEVAYRCADGDlGPTLYV-TgeESVGQVRLRA---ERTGALSDSLY 213
Cdd:PRK09361 7 TGCKMLDELLGGGFERGTITQIYGPPGSGKTNICLQLAVEAAKNG-KKVIYIdT--EGLSPERFKQiagEDFEELLSNII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 214 LSAVSNIED---VIDLTLELSP---GLLIVDSVQTM-RADVEGARGGVAQARAVT---SALAALAKETGTAIFLVGHVTK 283
Cdd:PRK09361 84 IFEPSSFEEqseAIRKAEKLAKenvGLIVLDSATSLyRLELEDEEDNSKLNRELGrqlTHLLKLARKHDLAVVITNQVYS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093455227 284 DGNV-----AGPRTMEHLVDVVLNFEGDRhSGLRFLRGLKNRFGSTDEVGCFEQTAGGIAEVE 341
Cdd:PRK09361 164 DIDSdglrpLGGHTLEHWSKTILRLEKFR-NGKRRATLEKHRSRPEGESAEFRITDRGIEIID 225
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
143-282 |
1.56e-06 |
|
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells 3) recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. XRCC3, together with the other RAD51 paralogs, RAD51B, RAD51C, RAD51D, and XRCC2, helps recruit RAD51 to the break site.
Pssm-ID: 410899 [Multi-domain] Cd Length: 250 Bit Score: 49.60 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 143 LDRVLGSGIVPGSLVLLAGEPGVGKSTLLLEVAYRC-----ADGDLGPTLYVTGEESVGQVRLR-----------AERTG 206
Cdd:cd19491 1 LDELLGGGIPVGGITEIAGESGAGKTQLCLQLALTVqlpreLGGLGGGAVYICTESSFPSKRLQqlasslpkryhLEKAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 207 ALSDSLYLSAVSNIEDVIDL-------TLELSP-GLLIVDSVQTM-RADVEGARGGVAQaRA-----VTSALAALAKETG 272
Cdd:cd19491 81 NFLDNIFVEHVADLETLEHClnyqlpaLLERGPiRLVVIDSIAALfRSEFDTSRSDLVE-RAkylrrLADHLKRLADKYN 159
|
170
....*....|
gi 1093455227 273 TAIFLVGHVT 282
Cdd:cd19491 160 LAVVVVNQVT 169
|
|
| RecA-like_Gp4D_helicase |
cd19483 |
RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase; This family includes the ... |
157-322 |
3.52e-06 |
|
RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase; This family includes the RecA-like domain of the Gp4D fragment of the Gene4 helicase-primase (Gp4) from bacteriophage T7. Gp4D (residues 241-566) is the minimal fragment of the Gp4 that forms hexameric rings, it contains the helicase domain and the linker connecting the helicase and primase domains. Helicases are ring-shaped oligomeric enzymes that unwind DNA at the replication fork; they couple NTP hydrolysis to the unwinding of nucleic acid duplexes into their component strands. This family belongs to the RecA-like NTPase superfamily 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: 410891 [Multi-domain] Cd Length: 231 Bit Score: 48.34 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 157 VLLAGEPGVGKSTLLLEVAYRCADGDLGPTLYVTGEESVGQVRLR-----AERTGAL---------------------SD 210
Cdd:cd19483 1 VTIGAGSGIGKSTIVRELAYHLITEHGEKVGIISLEESVEETAKGlagkhLGKPEPLelprdditeeeeddafdnelgSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 211 SLYL------SAVSNIEDVIDlTLELSPG--LLIVDSVQTMRADVEGARGGVAQARAVTsALAALAKETGTAIFLVGHVT 282
Cdd:cd19483 81 RFFLydhfgsLDWDNLKEKIR-YMVKVLGckVIVLDHLTILVSGLDSSDERKELDEIMT-ELAALVKELGVTIILVSHLR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 283 KDGNVAGP--------------RTMEHLVDVVLNFEGDRHS------GLRFLRGLKNRFG 322
Cdd:cd19483 159 RPGGGKGHeeggevsesdlrgsSAIAQLSDYVIGLERNKQAddpverNTTRVRVLKNRFT 218
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
144-319 |
1.74e-05 |
|
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51B, together with the other RAD51 paralogs, RAD51C, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site.
Pssm-ID: 410901 [Multi-domain] Cd Length: 222 Bit Score: 46.16 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 144 DRVLGSGIVPGSLVLLAGEPGVGKSTLLLEVAYRCA-----DGDLGPTLYVTGEESVGQVRLRA---------------- 202
Cdd:cd19493 1 DTALAGGLPLGAITEITGASGSGKTQFALTLASSAAmparkGGLDGGVLYIDTESKFSAERLAEiaearfpeafsgfmee 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 203 -ERTGALSDSLYLSAVSNIEDVIDLTLELSP-------GLLIVDSVQTM-RADVEGARGGVAQAR----AVTSALAALAK 269
Cdd:cd19493 81 nERAEEMLKRVAVVRVTTLAQLLERLPNLEEhilssgvRLVVIDSIAALvRREFGGSDGEVTERHnalaREASSLKRLAE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 270 ETGTAIFLVGHVTKDGNVAGP----------RTMEHLVDVVLNFEGDRHSGLRFLRGLKN 319
Cdd:cd19493 161 EFRIAVLVTNQATTHFGDAGDgssgvtaalgDAWAHAVNTRLRLERCLLQLRRVLEIVKS 220
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
136-282 |
2.32e-05 |
|
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51 is recruited to the break site with the help of its paralogs, RAD51D, RAD51B, RAD51C, XRCC3, and XRCC2, where it forms long helical polymers which wrap around the ssDNA tail at the break which leads to pairing and strand invasion.
Pssm-ID: 410921 [Multi-domain] Cd Length: 235 Bit Score: 45.77 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 136 VRTGIGELDRVLGSGIVPGSLVLLAGEPGVGKSTLLLEVAYRCA-----DGDLGPTLYVTGEESVGQVRLR--AERTGaL 208
Cdd:cd19513 1 ITTGSKELDKLLGGGIETGSITELFGEFRTGKTQLCHTLAVTCQlpidqGGGEGKALYIDTEGTFRPERLLaiAERYG-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 209 SDSLYLSAVS-----NIEDVIDLTLELSP-------GLLIVDSVQTM-RADVEGaRGGVAqARAVTSA-----LAALAKE 270
Cdd:cd19513 80 NGEDVLDNVAyarayNTDHQMQLLIQASAmmaesryALLIVDSATALyRTDYSG-RGELS-ARQMHLAkflrmLQRLADE 157
|
170
....*....|..
gi 1093455227 271 TGTAIFLVGHVT 282
Cdd:cd19513 158 FGVAVVITNQVV 169
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
113-293 |
2.84e-05 |
|
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein involved in DNA homologous recombination and repair. It is similar in sequence the exclusively meiotic recombinase DMC1 (TIGR02238), to archaeal families RadA (TIGR02236) and RadB (TIGR02237), and to bacterial RecA (TIGR02012).
Pssm-ID: 274048 [Multi-domain] Cd Length: 316 Bit Score: 46.26 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 113 DRIPTSSSELTAITGISAKTAHAVR-------TGIGELDRVLGSGIVPGSLVLLAGEPGVGKSTLLLEVAYRCA-----D 180
Cdd:TIGR02239 48 DKILAEAAKLVPMGFTTATEFHQRRqeviqltTGSKELDKLLGGGIETGSITEIFGEFRTGKTQLCHTLAVTCQlpidqG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 181 GDLGPTLYVTGEESVGQVRLR--AERTGaLSDSLYLSAVS-----NIEDVIDLTLELSP-------GLLIVDSVQTM-RA 245
Cdd:TIGR02239 128 GGEGKALYIDTEGTFRPERLLaiAERYG-LNPEDVLDNVAyarayNTDHQLQLLQQAAAmmsesrfALLIVDSATALyRT 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1093455227 246 DVEGaRGGVAqARAVTSA-----LAALAKETGTAIFLVGHVTkdGNVAGPRTM 293
Cdd:TIGR02239 207 DFSG-RGELS-ARQMHLArflrsLQRLADEFGVAVVITNQVV--AQVDGAGSM 255
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
115-240 |
3.05e-05 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 46.41 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 115 IPTSSSELTaitgisaKTAHAVR--TGIGELDRVLGSGIVPGSLVLLAGEPGVGKSTLLLEVAYR-CADGDlgPTLYVTG 191
Cdd:PRK09302 239 LPLTAMRLT-------QRSSNERisSGVPDLDEMLGGGFFRGSIILVSGATGTGKTLLASKFAEAaCRRGE--RCLLFAF 309
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093455227 192 EESVGQ-VR---------LRAERTGALS-DSLYlSAVSNIED----VIDLTLELSPGLLIVDSV 240
Cdd:PRK09302 310 EESRAQlIRnarswgidlEKMEEKGLLKiICAR-PESYGLEDhliiIKREIEEFKPSRVAIDPL 372
|
|
| PRK04328 |
PRK04328 |
hypothetical protein; Provisional |
136-310 |
4.74e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235281 Cd Length: 249 Bit Score: 45.07 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 136 VRTGIGELDRVLGSGIVPGSLVLLAGEPGVGKSTLLLEVAYRCADGDlGPTLYVTGEESVGQVRL----------RAERT 205
Cdd:PRK04328 5 VKTGIPGMDEILYGGIPERNVVLLSGGPGTGKSIFSQQFLWNGLQMG-EPGVYVALEEHPVQVRRnmrqfgwdvrKYEEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 206 G--ALSDSL------------YLsaVSNIEDVIDLTLELSPGL-------LIVDSVQTMRADVEG-ARGGVAQARAVTSA 263
Cdd:PRK04328 84 GkfAIVDAFtggigsaakrekYV--VKDPDDVRELIDVLRQAIkdigakrVVIDSVSTLYLTKPAmARSIVMQLKRVLSG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1093455227 264 LaalaketGTAIFLVGHVTKDGNVAGPRTMEHLVDVVLNFEGDRHSG 310
Cdd:PRK04328 162 L-------GCTAIFVSQVSVGERGFGGPGVEHAVDGIIRLDLDEIDG 201
|
|
| PRK05748 |
PRK05748 |
replicative DNA helicase; Provisional |
109-270 |
5.23e-05 |
|
replicative DNA helicase; Provisional
Pssm-ID: 180232 [Multi-domain] Cd Length: 448 Bit Score: 45.72 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 109 TSATDRIPTSSSELTAITGISaktahavrTGIGELDRVLgSGIVPGSLVLLAGEPGVGKSTLLLEVAYRCADgDLGPTLY 188
Cdd:PRK05748 167 VKAYDRIEMLHNQTGDITGIP--------TGFTDLDKMT-SGLQPNDLIIVAARPSVGKTAFALNIAQNVAT-KTDKNVA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 189 V----TGEESVGQVRLRAE--------RTGALSD---SLYLSAVSNIEDV---IDLTLELSP-----------------G 233
Cdd:PRK05748 237 IfsleMGAESLVMRMLCAEgnidaqrlRTGQLTDddwPKLTIAMGSLSDApiyIDDTPGIKVteirarcrrlaqehgglG 316
|
170 180 190
....*....|....*....|....*....|....*..
gi 1093455227 234 LLIVDSVQTMRADVEGARGGVAQARAVTSALAALAKE 270
Cdd:PRK05748 317 LILIDYLQLIQGSGRSGENRQQEVSEISRSLKALAKE 353
|
|
| FlaH |
COG2874 |
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility]; |
136-190 |
5.80e-05 |
|
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility];
Pssm-ID: 442121 Cd Length: 230 Bit Score: 44.44 E-value: 5.80e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1093455227 136 VRTGIGELDRVLGSGIVPGSLVLLAGEPGVGKSTLLLEVAYRCADGDLGPTLYVT 190
Cdd:COG2874 3 ISTGNDELDKRLGGGIPLGSLVLIEGENGTGKSVLSQQFAYGALENGLSVTYIST 57
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
153-250 |
6.33e-05 |
|
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: 43.29 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 153 PGSLVLLAGEPGVGKSTLLLEVAYRCADGDlGPTLYVTGEESVGQVRLRAERTgalsdslylsaVSNIEDVIDLTLELSP 232
Cdd:cd00009 18 PPKNLLLYGPPGTGKTTLARAIANELFRPG-APFLYLNASDLLEGLVVAELFG-----------HFLVRLLFELAEKAKP 85
|
90
....*....|....*...
gi 1093455227 233 GLLIVDSVQTMRADVEGA 250
Cdd:cd00009 86 GVLFIDEIDSLSRGAQNA 103
|
|
| KaiC_arch |
cd19486 |
KaiC family protein; uncharacterized subfamily similar to Pyrococcus horikoshii PH0284; KaiC ... |
136-310 |
8.58e-05 |
|
KaiC family protein; uncharacterized subfamily similar to Pyrococcus horikoshii PH0284; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410894 Cd Length: 230 Bit Score: 44.00 E-value: 8.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 136 VRTGIGELDRVLGSGIVPGSLVLLAGEPGVGKSTLLLEVAYR-CADGDlgPTLYVTGEESVGQVRLRAERTG-------- 206
Cdd:cd19486 1 VKTGIPGMDEILHGGIPERNVVLLSGGPGTGKSIFSQQFLWNgLKEGE--PGVFVALEEHPVQVRRNMEQFGwdvreyer 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 207 ----ALSDSL------------YLsaVSNIEDVIDLTLELSPGL-------LIVDSVQTMRADVEG-ARGGVAQARAVTS 262
Cdd:cd19486 79 egkfAIVDAFtggigeaaerekYV--VKDPDDVRELIDVLRQAIrdigakrVVIDSVTTLYITKPAmARRIVMQLKRVLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1093455227 263 ALAAlaketgTAIFLVGHVTKDGNVAGPrTMEHLVDVVLNFEGDRHSG 310
Cdd:cd19486 157 GLGC------TSIFVSQVSVGERGFGGP-GVEHAVDGIIRLDLDEVDG 197
|
|
| PRK06067 |
PRK06067 |
flagellar accessory protein FlaH; Validated |
138-190 |
1.24e-04 |
|
flagellar accessory protein FlaH; Validated
Pssm-ID: 180381 Cd Length: 234 Bit Score: 43.42 E-value: 1.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1093455227 138 TGIGELDRVLGSGIVPGSLVLLAGEPGVGKSTLLLEVAYRCADGDLGPTLYVT 190
Cdd:PRK06067 9 TGNEELDRKLGGGIPFPSLILIEGDHGTGKSVLSQQFVYGALKQGKKVYVITT 61
|
|
| ChlI |
pfam13541 |
Subunit ChlI of Mg-chelatase; |
449-492 |
7.38e-04 |
|
Subunit ChlI of Mg-chelatase;
Pssm-ID: 433293 [Multi-domain] Cd Length: 121 Bit Score: 39.35 E-value: 7.38e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1093455227 449 TFQDKTIALGELGLAGEVRRVTDLEWRLKEAHRMGFDTAIVPRG 492
Cdd:pfam13541 77 PVLEETIFLGELSLDGSLRPVRGALPIALAARKHGFRGLIVPKE 120
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
156-189 |
1.32e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 41.71 E-value: 1.32e-03
10 20 30
....*....|....*....|....*....|....
gi 1093455227 156 LVLLaGEPGVGKSTLLLEVAYRCADGDLGPTLYV 189
Cdd:COG5635 183 LLIL-GEPGSGKTTLLRYLALELAERYLDAEDPI 215
|
|
| RecA-like_superfamily |
cd01120 |
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ... |
157-293 |
1.65e-03 |
|
RecA-like_NTPases; RecA-like NTPases. This superfamily 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: 410865 [Multi-domain] Cd Length: 119 Bit Score: 38.64 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 157 VLLAGEPGVGKSTLLLEVAYRCADGDlGPTLYVTgeesvgqvrlraertgALSDSLYLsavsniedVIDLTLELSPGLLI 236
Cdd:cd01120 1 ILITGPPGSGKTTLLLQFAEQALLSD-EPVIFIS----------------FLDTILEA--------IEDLIEEKKLDIII 55
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1093455227 237 VDSVQTMRADVEGARGGvAQARAVTSALAAlAKETGTAIFLVGHVTKDGNVAGPRTM 293
Cdd:cd01120 56 IDSLSSLARASQGDRSS-ELLEDLAKLLRA-ARNTGITVIATIHSDKFDIDRGGSSN 110
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
136-284 |
1.70e-03 |
|
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in meiosis. It assembles at the sites of programmed DNA double-strand breaks and carries out a search for allelic DNA sequences located on homologous chromatids. It forms octameric rings.
Pssm-ID: 410922 [Multi-domain] Cd Length: 236 Bit Score: 40.03 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 136 VRTGIGELDRVLGSGIVPGSLVLLAGEPGVGKSTLLLEVAYRC-----ADGDLGPTLYVTGEESVGQVRLR--AERTG-- 206
Cdd:cd19514 1 ISTGSTELDKLLGGGIESMSITEVFGEFRTGKTQLSHTLCVTAqlpgsMGGGGGKVAYIDTEGTFRPDRIRpiAERFGvd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 207 ---ALSDSLYLSAVsNIEDVIDLTLELSP--------GLLIVDSVQTM-RADVEGaRGGVAQARA----VTSALAALAKE 270
Cdd:cd19514 81 hdaVLDNILYARAY-TSEHQMELLDYVAAkfheeavfRLLIIDSIMALfRVDFSG-RGELAERQQklaqMLSRLQKISEE 158
|
170
....*....|....
gi 1093455227 271 TGTAIFLVGHVTKD 284
Cdd:cd19514 159 YNVAVFITNQVTAD 172
|
|
| KaiC_C |
cd19484 |
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most ... |
136-240 |
1.72e-03 |
|
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410892 [Multi-domain] Cd Length: 218 Bit Score: 40.00 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 136 VRTGIGELDRVL-GSGIVPGSLVLLAGEPGVGKSTLLLE-VAYRCADGDlgPTLYVTGEESVGQV-R---------LRAE 203
Cdd:cd19484 1 ISTGIPRLDAMLgGGGFFRGSSILVSGATGTGKTLLAASfADAACRRGE--RCLYFAFEESPAQLiRnaksigidlEQME 78
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1093455227 204 RTGALSDSLYLSAVSNIED----VIDLTLELSPGLLIVDSV 240
Cdd:cd19484 79 RKGLLKIICARPELYGLEDhliiIKSEINEFKPSRVIVDPL 119
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
149-192 |
1.90e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.98 E-value: 1.90e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1093455227 149 SGIV-PGSLVLLAGEPGVGKSTLLLEVAyrcadGDLGPTLYVTGE 192
Cdd:PLN03140 185 SGIIkPSRMTLLLGPPSSGKTTLLLALA-----GKLDPSLKVSGE 224
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
142-279 |
2.46e-03 |
|
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: 38.80 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 142 ELDRVLGSGIVPGSLVLLAGEPGVGKSTLLlevayRCADGDLG-PTLYVTGEESVGQVRLRAERtgalsdslylsavsNI 220
Cdd:cd19481 14 RGSRLRRYGLGLPKGILLYGPPGTGKTLLA-----KALAGELGlPLIVVKLSSLLSKYVGESEK--------------NL 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 221 EDVIDLTLELSPGLLIVDSVQTMRADVEGARGGVAQARAVTSALAAL-AKETGTAIFLVG 279
Cdd:cd19481 75 RKIFERARRLAPCILFIDEIDAIGRKRDSSGESGELRRVLNQLLTELdGVNSRSKVLVIA 134
|
|
| PRK08533 |
PRK08533 |
flagellar accessory protein FlaH; Reviewed |
142-176 |
3.46e-03 |
|
flagellar accessory protein FlaH; Reviewed
Pssm-ID: 181459 Cd Length: 230 Bit Score: 39.28 E-value: 3.46e-03
10 20 30
....*....|....*....|....*....|....*
gi 1093455227 142 ELDRVLGSGIVPGSLVLLAGEPGVGKSTLLLEVAY 176
Cdd:PRK08533 12 ELHKRLGGGIPAGSLILIEGDESTGKSILSQRLAY 46
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
154-282 |
6.17e-03 |
|
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA repair, and the induction of the SOS response. RecA couples ATP hydrolysis to DNA strand exchange. While prokaryotes have a single RecA protein, eukaryotes have multiple RecA homologs such as Rad51, DMC1 and Rad55/57. Archaea have the RecA-like homologs RadA and RadB.
Pssm-ID: 410881 [Multi-domain] Cd Length: 185 Bit Score: 38.10 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 154 GSLVLLAGEPGVGKSTLLLEVAYRCAdGDLGPTLYVTGEESVGQVRLRA---------ERTGALSDSLYLSAVSNIEDVI 224
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANAL-LLGGGVVWIDTEGAFPPSRLVQileaspsseLELAEALSRLLYFRPPDTLAHL 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093455227 225 DLTLELSP--------GLLIVDSVQTM--RADVEGARGGVAQARA------VTSALAALAKETGTAIFLVGHVT 282
Cdd:cd01393 80 LALDSLPEslfpppntSLVVVDSVSALfrKAFPRGGDGDSSSSLRarllsqLARALQKLAAQFNLAVVVTNQVT 153
|
|
| PRK08506 |
PRK08506 |
replicative DNA helicase; Provisional |
138-238 |
6.25e-03 |
|
replicative DNA helicase; Provisional
Pssm-ID: 236278 [Multi-domain] Cd Length: 472 Bit Score: 39.22 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 138 TGIGELDRvLGSGIVPGSLVLLAGEPGVGKSTLLLEVAYRCADGDLGPTLYvTGEESVGQVRLRAE-----------RTG 206
Cdd:PRK08506 177 TGFVELNK-MTKGFNKGDLIIIAARPSMGKTTLCLNMALKALNQDKGVAFF-SLEMPAEQLMLRMLsaktsiplqnlRTG 254
|
90 100 110
....*....|....*....|....*....|..
gi 1093455227 207 ALSDSLYlsavSNIEDVIDltlELSPGLLIVD 238
Cdd:PRK08506 255 DLDDDEW----ERLSDACD---ELSKKKLFVY 279
|
|
| Rad51C |
cd19492 |
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
154-282 |
7.05e-03 |
|
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51C, together with the other RAD51 paralogs, RAD51B, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site. Additionally, RAD51C acts as a mediator in the early steps of DNA damage signaling.
Pssm-ID: 410900 [Multi-domain] Cd Length: 172 Bit Score: 37.59 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455227 154 GSLVLLAGEPGVGKSTLLLEVAY-----RCADGDLGPTLYVTGEESVGQVRLR----AERTgALSDSL--YLSAVSNIed 222
Cdd:cd19492 1 GKITEICGVPGVGKTQLCMQLAVnvqipKCFGGLAGEAIYIDTEGSFNIHYFRvhdyVELL-ALINSLpkFLEDHPKV-- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093455227 223 vidltlelspGLLIVDSV-QTMRADVEGArggVAQARAVTSA---LAALAKETGTAIFLVGHVT 282
Cdd:cd19492 78 ----------KLIVVDSIaFPFRHDFDDL---AQRTRLLNGLaqlLHSLARQHNLAVVLTNQVT 128
|
|
| |
