|
Name |
Accession |
Description |
Interval |
E-value |
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
37-471 |
4.33e-84 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 268.00 E-value: 4.33e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 37 ESDSLLLLKGYAGTGKTSLVGALVKTMAELKQKSILLAPTGRAAKVFSGYAGQKAFTIHKKIYRQkaFSNEPTGFHPADN 116
Cdd:COG0507 138 TTRRVSVLTGGAGTGKTTTLRALLAALEALGLRVALAAPTGKAAKRLSESTGIEARTIHRLLGLR--PDSGRFRHNRDNP 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 117 LHKDTLFIVDEASMIANegldsfvfgtgRLLDDLVQYVYSGeNCRLILMGDVAQLPPVmqtesPALNPETLRGYNLKVQE 196
Cdd:COG0507 216 LTPADLLVVDEASMVDT-----------RLMAALLEALPRA-GARLILVGDPDQLPSV-----GAGAVLRDLIESGTVPV 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 197 ITLTQVVRQSENSGILFNATrlrdALRNGTVEIFPKLRLKGFTDFRKVNGDELIEEISSAYSR--DGIEETMIISRSNKR 274
Cdd:COG0507 279 VELTEVYRQADDSRIIELAH----AIREGDAPEALNARYADVVFVEAEDAEEAAEAIVELYADrpAGGEDIQVLAPTNAG 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 275 ATLYNNGIRNRIL-----------YREEELSSGDRLMIAKNNYFWtagnkemdFIANGEIIQVLRVRRTYElygfrfaDV 343
Cdd:COG0507 355 VDALNQAIREALNpagelerelaeDGELELYVGDRVMFTRNDYDL--------GVFNGDIGTVLSIDEDEG-------RL 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 344 SVRFqdyDLETDVKILLDTLqtaapalpkdlndklfytiledyddvptkagkmkkmkadphynvLQVKYAYAVTCHKAQG 423
Cdd:COG0507 420 TVRF---DGREIVTYDPSEL--------------------------------------------DQLELAYAITVHKSQG 452
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 491852579 424 GQWMNVFLDIGYITEEMLgedFYRWLYTAFTRATHRLYLVNLPEEFEE 471
Cdd:COG0507 453 STFDRVILVLPSEHSPLL---SRELLYTALTRARELLTLVGDRDALAR 497
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
38-174 |
3.88e-34 |
|
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: 125.36 E-value: 3.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 38 SDSLLLLKGYAGTGKTSLVGALVKTMAELKQKSILLAPTGRAAKVFSGYAGQKAFTIHKKIYRQKafsNEPTGFHPADNL 117
Cdd:cd17933 11 RNRVSVLTGGAGTGKTTTLKALLAALEAEGKRVVLAAPTGKAAKRLSESTGIEASTIHRLLGINP---GGGGFYYNEENP 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 491852579 118 HKDTLFIVDEASMIANegldsfvfgtgRLLDDLVQYVYSGenCRLILMGDVAQLPPV 174
Cdd:cd17933 88 LDADLLIVDEASMVDT-----------RLMAALLSAIPAG--ARLILVGDPDQLPSV 131
|
|
| recD_rel |
TIGR01448 |
helicase, putative, RecD/TraA family; This model describes a family similar to RecD, the ... |
38-469 |
1.27e-28 |
|
helicase, putative, RecD/TraA family; This model describes a family similar to RecD, the exodeoxyribonuclease V alpha chain of TIGR01447. Members of this family, however, are not found in a context of RecB and RecC and are longer by about 200 amino acids at the amino end. Chlamydia muridarum has both a member of this family and a RecD. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 273632 [Multi-domain] Cd Length: 720 Bit Score: 119.50 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 38 SDSLLLLKGYAGTGKTSLVGALVKTMAELK--QKSILLAPTGRAAKVFSGYAGQKAFTIHKKIyrQKAFSNEPTGfHPAD 115
Cdd:TIGR01448 337 QHKVVILTGGPGTGKTTITRAIIELAEELGglLPVGLAAPTGRAAKRLGEVTGLTASTIHRLL--GYGPDTFRHN-HLED 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 116 NLHKDtLFIVDEASMIaneglDSFvfgtgrLLDDLVQYVYSgeNCRLILMGDVAQLPPVmqteSPALNPETLRGYNLkVQ 195
Cdd:TIGR01448 414 PIDCD-LLIVDESSMM-----DTW------LALSLLAALPD--HARLLLVGDTDQLPSV----GPGQVLKDLILSQA-IP 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 196 EITLTQVVRQSENSGILFNATRLRDAlrngtveifpklRLKGFTDFRKVNGDE------------LIEEISSAYSRDGIE 263
Cdd:TIGR01448 475 VTRLTKVYRQAAGSPIITLAHGILHG------------EAPAWGDFKFLNLTRsepegaarhiplMVEKIVGMARVGGIP 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 264 ETMI------------ISRSNKR-ATLYNNGIRNR--ILYREEELSSGDRLMIAKNNYfwtagNKEmdfIANGEIIQVlr 328
Cdd:TIGR01448 543 GADIqvlapmykgplgIDALNQHlQALLNPYQKGQggIEIAEGEYRKGDRVMQTKNDY-----NNE---IFNGDLGMI-- 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 329 vrrtyelygfrfadVSVRFQDYDLETDVKILLDTlqtaapalpkdlNDKLfYTILEDYDDVPtkagkmkkmkadphynvl 408
Cdd:TIGR01448 613 --------------VKIEGAKQGKKDQVVVDFDG------------NEVE-LTRAELFNLTL------------------ 647
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491852579 409 qvkyAYAVTCHKAQGGQWMNVFLDIGYITEEMLgedfYR-WLYTAFTRATHRLYLVNLPEEF 469
Cdd:TIGR01448 648 ----AYATSIHKSQGSEFPTVILPIHTAHMRML----YRnLLYTALTRAKKRVILVGSAEAF 701
|
|
| AAA_30 |
pfam13604 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
38-228 |
4.52e-25 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B.
Pssm-ID: 433343 [Multi-domain] Cd Length: 191 Bit Score: 101.87 E-value: 4.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 38 SDSLLLLKGYAGTGKTSLVGALVKTMAELKQKSILLAPTGRAAKVFSGYAGQKAFTIHKKIYRQKafsneptgfhPADNL 117
Cdd:pfam13604 17 GDRVAVLVGPAGTGKTTALKALREAWEAAGYRVIGLAPTGRAAKVLGEELGIPADTIAKLLHRLG----------GRAGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 118 HKDTLFIVDEASMIANegldsfvfgtgRLLDDLVQYVySGENCRLILMGDVAQLPPV---------MQTESPAlnpetlr 188
Cdd:pfam13604 87 DPGTLLIVDEAGMVGT-----------RQMARLLKLA-EDAGARVILVGDPRQLPSVeaggafrdlLAAGIGT------- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491852579 189 gynlkvqeITLTQVVRQSEnsgilfnaTRLRDA---LRNGTVE 228
Cdd:pfam13604 148 --------AELTEIVRQRD--------PWQRAAslaLRDGDPA 174
|
|
| PRK13709 |
PRK13709 |
conjugal transfer nickase/helicase TraI; Provisional |
36-181 |
7.80e-10 |
|
conjugal transfer nickase/helicase TraI; Provisional
Pssm-ID: 237478 [Multi-domain] Cd Length: 1747 Bit Score: 61.73 E-value: 7.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 36 EESDSLLLLKGYAGTGKTSLVGALVKTMAELKQKS----ILLAPTGRAAKVFSGyAGQKAFTIHKKIY--RQKAFSNEPT 109
Cdd:PRK13709 981 ESTDRFTVVQGYAGVGKTTQFRAVMSAVNTLPESErprvVGLGPTHRAVGEMRS-AGVDAQTLASFLHdtQLQQRSGETP 1059
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 110 GFhpadnlhKDTLFIVDEASMIANEGLDSFvfgtgrllddlVQYVYSGENcRLILMGDVAQLPPV--------MQTESPA 181
Cdd:PRK13709 1060 DF-------SNTLFLLDESSMVGNTDMARA-----------YALIAAGGG-RAVSSGDTDQLQAIapgqpfrlMQTRSAA 1120
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
37-471 |
4.33e-84 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 268.00 E-value: 4.33e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 37 ESDSLLLLKGYAGTGKTSLVGALVKTMAELKQKSILLAPTGRAAKVFSGYAGQKAFTIHKKIYRQkaFSNEPTGFHPADN 116
Cdd:COG0507 138 TTRRVSVLTGGAGTGKTTTLRALLAALEALGLRVALAAPTGKAAKRLSESTGIEARTIHRLLGLR--PDSGRFRHNRDNP 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 117 LHKDTLFIVDEASMIANegldsfvfgtgRLLDDLVQYVYSGeNCRLILMGDVAQLPPVmqtesPALNPETLRGYNLKVQE 196
Cdd:COG0507 216 LTPADLLVVDEASMVDT-----------RLMAALLEALPRA-GARLILVGDPDQLPSV-----GAGAVLRDLIESGTVPV 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 197 ITLTQVVRQSENSGILFNATrlrdALRNGTVEIFPKLRLKGFTDFRKVNGDELIEEISSAYSR--DGIEETMIISRSNKR 274
Cdd:COG0507 279 VELTEVYRQADDSRIIELAH----AIREGDAPEALNARYADVVFVEAEDAEEAAEAIVELYADrpAGGEDIQVLAPTNAG 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 275 ATLYNNGIRNRIL-----------YREEELSSGDRLMIAKNNYFWtagnkemdFIANGEIIQVLRVRRTYElygfrfaDV 343
Cdd:COG0507 355 VDALNQAIREALNpagelerelaeDGELELYVGDRVMFTRNDYDL--------GVFNGDIGTVLSIDEDEG-------RL 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 344 SVRFqdyDLETDVKILLDTLqtaapalpkdlndklfytiledyddvptkagkmkkmkadphynvLQVKYAYAVTCHKAQG 423
Cdd:COG0507 420 TVRF---DGREIVTYDPSEL--------------------------------------------DQLELAYAITVHKSQG 452
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 491852579 424 GQWMNVFLDIGYITEEMLgedFYRWLYTAFTRATHRLYLVNLPEEFEE 471
Cdd:COG0507 453 STFDRVILVLPSEHSPLL---SRELLYTALTRARELLTLVGDRDALAR 497
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
38-174 |
3.88e-34 |
|
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: 125.36 E-value: 3.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 38 SDSLLLLKGYAGTGKTSLVGALVKTMAELKQKSILLAPTGRAAKVFSGYAGQKAFTIHKKIYRQKafsNEPTGFHPADNL 117
Cdd:cd17933 11 RNRVSVLTGGAGTGKTTTLKALLAALEAEGKRVVLAAPTGKAAKRLSESTGIEASTIHRLLGINP---GGGGFYYNEENP 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 491852579 118 HKDTLFIVDEASMIANegldsfvfgtgRLLDDLVQYVYSGenCRLILMGDVAQLPPV 174
Cdd:cd17933 88 LDADLLIVDEASMVDT-----------RLMAALLSAIPAG--ARLILVGDPDQLPSV 131
|
|
| recD_rel |
TIGR01448 |
helicase, putative, RecD/TraA family; This model describes a family similar to RecD, the ... |
38-469 |
1.27e-28 |
|
helicase, putative, RecD/TraA family; This model describes a family similar to RecD, the exodeoxyribonuclease V alpha chain of TIGR01447. Members of this family, however, are not found in a context of RecB and RecC and are longer by about 200 amino acids at the amino end. Chlamydia muridarum has both a member of this family and a RecD. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 273632 [Multi-domain] Cd Length: 720 Bit Score: 119.50 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 38 SDSLLLLKGYAGTGKTSLVGALVKTMAELK--QKSILLAPTGRAAKVFSGYAGQKAFTIHKKIyrQKAFSNEPTGfHPAD 115
Cdd:TIGR01448 337 QHKVVILTGGPGTGKTTITRAIIELAEELGglLPVGLAAPTGRAAKRLGEVTGLTASTIHRLL--GYGPDTFRHN-HLED 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 116 NLHKDtLFIVDEASMIaneglDSFvfgtgrLLDDLVQYVYSgeNCRLILMGDVAQLPPVmqteSPALNPETLRGYNLkVQ 195
Cdd:TIGR01448 414 PIDCD-LLIVDESSMM-----DTW------LALSLLAALPD--HARLLLVGDTDQLPSV----GPGQVLKDLILSQA-IP 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 196 EITLTQVVRQSENSGILFNATRLRDAlrngtveifpklRLKGFTDFRKVNGDE------------LIEEISSAYSRDGIE 263
Cdd:TIGR01448 475 VTRLTKVYRQAAGSPIITLAHGILHG------------EAPAWGDFKFLNLTRsepegaarhiplMVEKIVGMARVGGIP 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 264 ETMI------------ISRSNKR-ATLYNNGIRNR--ILYREEELSSGDRLMIAKNNYfwtagNKEmdfIANGEIIQVlr 328
Cdd:TIGR01448 543 GADIqvlapmykgplgIDALNQHlQALLNPYQKGQggIEIAEGEYRKGDRVMQTKNDY-----NNE---IFNGDLGMI-- 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 329 vrrtyelygfrfadVSVRFQDYDLETDVKILLDTlqtaapalpkdlNDKLfYTILEDYDDVPtkagkmkkmkadphynvl 408
Cdd:TIGR01448 613 --------------VKIEGAKQGKKDQVVVDFDG------------NEVE-LTRAELFNLTL------------------ 647
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491852579 409 qvkyAYAVTCHKAQGGQWMNVFLDIGYITEEMLgedfYR-WLYTAFTRATHRLYLVNLPEEF 469
Cdd:TIGR01448 648 ----AYATSIHKSQGSEFPTVILPIHTAHMRML----YRnLLYTALTRAKKRVILVGSAEAF 701
|
|
| AAA_30 |
pfam13604 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
38-228 |
4.52e-25 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B.
Pssm-ID: 433343 [Multi-domain] Cd Length: 191 Bit Score: 101.87 E-value: 4.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 38 SDSLLLLKGYAGTGKTSLVGALVKTMAELKQKSILLAPTGRAAKVFSGYAGQKAFTIHKKIYRQKafsneptgfhPADNL 117
Cdd:pfam13604 17 GDRVAVLVGPAGTGKTTALKALREAWEAAGYRVIGLAPTGRAAKVLGEELGIPADTIAKLLHRLG----------GRAGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 118 HKDTLFIVDEASMIANegldsfvfgtgRLLDDLVQYVySGENCRLILMGDVAQLPPV---------MQTESPAlnpetlr 188
Cdd:pfam13604 87 DPGTLLIVDEAGMVGT-----------RQMARLLKLA-EDAGARVILVGDPRQLPSVeaggafrdlLAAGIGT------- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491852579 189 gynlkvqeITLTQVVRQSEnsgilfnaTRLRDA---LRNGTVE 228
Cdd:pfam13604 148 --------AELTEIVRQRD--------PWQRAAslaLRDGDPA 174
|
|
| recD |
TIGR01447 |
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ... |
41-471 |
1.83e-17 |
|
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha subunit, RecD. RecD is part of a RecBCD complex. A related family in the Gram-positive bacteria separates in a phylogenetic tree, has an additional N-terminal extension of about 200 residues, and is not supported as a member of a RecBCD complex by neighboring genes. The related family is consequently described by a different model. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273631 [Multi-domain] Cd Length: 582 Bit Score: 85.20 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 41 LLLLKGYAGTGKTSLV----GALVKTMAELKQKSI-LLAPTGRAA----KVFSGYAGQKAF-------------TIHK-- 96
Cdd:TIGR01447 161 FSLITGGPGTGKTTTVarllLALVKQSPKQGKLRIaLAAPTGKAAarlaESLRKAVKNLAAaealiaalpseavTIHRll 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 97 KIYrqkaFSNEPTGFHPADNLHKDTLfIVDEASMIanegldsfvfgTGRLLDDLVQYVYSGEncRLILMGDVAQLPPV-- 174
Cdd:TIGR01447 241 GIK----PDTKRFRHHERNPLPLDVL-VVDEASMV-----------DLPLMAKLLKALPPNT--KLILLGDKNQLPSVea 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 175 ---------MQTESPALNPETLRGYNLKVQEITLTQVV------RQSENSGI--LFNATRLRDALRngtveIFPKLRLKG 237
Cdd:TIGR01447 303 gavlgdlceLASIGKSILYALCKKINSKTRNPLSDNVCflktshRFGKDSGIgqLAKAINSGDIEA-----VLNNLRSGQ 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 238 FTDFRKVNGDE-LIEEISSAY--SRDGIEETMIISRSNKRATLYNN---------------GIRNRI---LYR------E 290
Cdd:TIGR01447 378 LIEFEFLNSKEdAIERLKNLYvkYRTFLQKLAALSDAKEILETFDRlrlltalrdgpfgvlGLNRRIeqeLQEkyfdpdE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 291 EELSSGDRLMIAKNNYFWTagnkemdfIANGEIIQVLRVrrtyelygfRFADVSVRFQDYDLETDVkilldtlqtaapaL 370
Cdd:TIGR01447 458 EGWYIGRPIMVTENDYTLG--------LFNGDIGVLLRD---------PDGILTVWFHFADGSKAV-------------L 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 371 PKDLNdklfytiledyddvptkagkmkkmkadphynvlQVKYAYAVTCHKAQGGQWMNVFLDIGYITEEMLGEDFyrwLY 450
Cdd:TIGR01447 508 PSRLP---------------------------------NYETAFAMTVHKSQGSEFDHVILILPNGNSPVLTREL---LY 551
|
490 500
....*....|....*....|.
gi 491852579 451 TAFTRATHRLYLVNLPEEFEE 471
Cdd:TIGR01447 552 TGITRAKDQLSVWSDKETLNA 572
|
|
| UvrD_C_2 |
pfam13538 |
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety ... |
412-463 |
2.22e-17 |
|
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety of helicase enzymes. This domain has a AAA-like structural fold.
Pssm-ID: 463913 [Multi-domain] Cd Length: 52 Bit Score: 75.69 E-value: 2.22e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 491852579 412 YAYAVTCHKAQGGQWMNVFLDIGYITEEMLGEDFYRWLYTAFTRATHRLYLV 463
Cdd:pfam13538 1 LAYALTVHKAQGSEFPAVFLVDPDLTAHYHSMLRRRLLYTAVTRARKKLVLV 52
|
|
| AAA_19 |
pfam13245 |
AAA domain; |
40-174 |
6.37e-16 |
|
AAA domain;
Pssm-ID: 433059 [Multi-domain] Cd Length: 136 Bit Score: 74.18 E-value: 6.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 40 SLLLLKGYAGTGKTSLVGALVKTMAELKQKS---ILLAPTGRAAKVFSGYAGQKAFTIHKKIyrqkafsneptGFHP--A 114
Cdd:pfam13245 12 KVVLLTGGPGTGKTTTIRHIVALLVALGGVSfpiLLAAPTGRAAKRLSERTGLPASTIHRLL-----------GFDDleA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491852579 115 DNLHKDT-------LFIVDEASMianegLDsfVFGTGRLLDDLVqyvysgENCRLILMGDVAQLPPV 174
Cdd:pfam13245 81 GGFLRDEeepldgdLLIVDEFSM-----VD--LPLAYRLLKALP------DGAQLLLVGDPDQLPSV 134
|
|
| SF1_C_RecD |
cd18809 |
C-terminal helicase domain of RecD family helicases; RecD is a member of the RecBCD (EC 3.1.11. ... |
413-463 |
2.86e-11 |
|
C-terminal helicase domain of RecD family helicases; 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 family helicases are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350196 [Multi-domain] Cd Length: 80 Bit Score: 59.11 E-value: 2.86e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 491852579 413 AYAVTCHKAQGGQWMNVFLDIGYITEEMlgedFYRWLYTAFTRATHRLYLV 463
Cdd:cd18809 33 AYAMTIHKSQGSEFDRVIVVLPTSHPML----SRGLLYTALTRARKLLTLV 79
|
|
| PRK13709 |
PRK13709 |
conjugal transfer nickase/helicase TraI; Provisional |
36-181 |
7.80e-10 |
|
conjugal transfer nickase/helicase TraI; Provisional
Pssm-ID: 237478 [Multi-domain] Cd Length: 1747 Bit Score: 61.73 E-value: 7.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 36 EESDSLLLLKGYAGTGKTSLVGALVKTMAELKQKS----ILLAPTGRAAKVFSGyAGQKAFTIHKKIY--RQKAFSNEPT 109
Cdd:PRK13709 981 ESTDRFTVVQGYAGVGKTTQFRAVMSAVNTLPESErprvVGLGPTHRAVGEMRS-AGVDAQTLASFLHdtQLQQRSGETP 1059
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 110 GFhpadnlhKDTLFIVDEASMIANEGLDSFvfgtgrllddlVQYVYSGENcRLILMGDVAQLPPV--------MQTESPA 181
Cdd:PRK13709 1060 DF-------SNTLFLLDESSMVGNTDMARA-----------YALIAAGGG-RAVSSGDTDQLQAIapgqpfrlMQTRSAA 1120
|
|
| TraI_TIGR |
TIGR02760 |
conjugative transfer relaxase protein TraI; This protein is a component of the relaxosome ... |
36-221 |
2.07e-08 |
|
conjugative transfer relaxase protein TraI; This protein is a component of the relaxosome complex. In the process of conjugative plasmid transfer the realaxosome binds to the plasmid at the oriT (origin of transfer) site. The relaxase protein TraI mediates the single-strand nicking and ATP-dependent unwinding (relaxation, helicase activity) of the plasmid molecule. These two activities reside in separate domains of the protein.
Pssm-ID: 274285 [Multi-domain] Cd Length: 1960 Bit Score: 56.84 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 36 EESDSLLLLKGYAGTGKTSLVGALVKTMAEL----KQKSILLAPTGRAAKVFSGyAGQKAFTIHKKIYRQKAFSNEPTGF 111
Cdd:TIGR02760 1033 STKDRFVAVQGLAGVGKTTMLESRYKPVLQAfeseQLQVIGLAPTHEAVGELKS-AGVQAQTLDSFLTDISLYRNSGGDF 1111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 112 hpadnlhKDTLFIVDEASMIANEGLDSFVfgtgrlldDLVQYVYSgencRLILMGDVAQLppvmQTESPALnPETLRGYN 191
Cdd:TIGR02760 1112 -------RNTLFILDESSMVSNFQLTHAT--------ELVQKSGS----RAVSLGDIAQL----QSLAAGK-PFELAITF 1167
|
170 180 190
....*....|....*....|....*....|
gi 491852579 192 LKVQEITLTQVVRQSensgilfNATRLRDA 221
Cdd:TIGR02760 1168 DIIDTAIMKEIVRQN-------NSAELKAA 1190
|
|
| DEXSc_Pif1_like |
cd18037 |
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like ... |
46-204 |
3.75e-08 |
|
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like helicases involved in maintaining genome stability through unwinding double-stranded DNAs (dsDNAs), DNA/RNA hybrids, and G quadruplex (G4) structures. The members of Pif1 helicase subfamily studied so far all appear to contribute to telomere maintenance. Pif1 is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350795 [Multi-domain] Cd Length: 183 Bit Score: 53.02 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 46 GYAGTGKTSLVGALVKTMAELKQKSILLAPTGRAA--------------KVFSGYAGQKAFTIHKKIYRQKAFsneptgf 111
Cdd:cd18037 19 GSAGTGKSYLLRRIIRALPSRPKRVAVTASTGIAAcniggttlhsfagiGLGSEPAEDLLERVKRSPYLVQRW------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 112 hpadnLHKDTLfIVDEASMIANEGLDSfvfgtgrlLDDLVQYVYsGEN-----CRLILMGDVAQLPPVMQT------ESP 180
Cdd:cd18037 92 -----RKCDVL-IIDEISMLDADLFDK--------LDRVAREVR-GSDkpfggIQLILCGDFLQLPPVTKNserqafFFR 156
|
170 180
....*....|....*....|....*..
gi 491852579 181 ALNP---ETLRGYNLKVQEITLTQVVR 204
Cdd:cd18037 157 GDQQfcfEAKSWERCIFLTVELTKVFR 183
|
|
| DEXXQc_Upf1-like |
cd17934 |
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ... |
41-205 |
5.96e-06 |
|
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), coronavirus Nsp13, and similar proteins. They belong to 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: 438708 [Multi-domain] Cd Length: 121 Bit Score: 45.30 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 41 LLLLKGYAGTGKTSLVGALVKT-MAELKQKSILLAptgraakvfsgyagqkaftihkkiyrqkAFSNEPTgfhpaDNLhk 119
Cdd:cd17934 1 ISLIQGPPGTGKTTTIAAIVLQlLKGLRGKRVLVT----------------------------AQSNVAV-----DNV-- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 120 DTLfIVDEASMIaNEGldsfvfgtgrlldDLVQYVYSGEncRLILMGDVAQLPPVMQTESPALNPETLRGYNLKVQEITL 199
Cdd:cd17934 46 DVV-IIDEASQI-TEP-------------ELLIALIRAK--KVVLVGDPKQLPPVVQEDHAALLGLSFILSLLLLFRLLL 108
|
....*.
gi 491852579 200 TQVVRQ 205
Cdd:cd17934 109 PGSPKV 114
|
|
| PIF1 |
pfam05970 |
PIF1-like helicase; This family includes homologs of the PIF1 helicase, which inhibits ... |
46-286 |
8.20e-06 |
|
PIF1-like helicase; This family includes homologs of the PIF1 helicase, which inhibits telomerase activity and is cell cycle regulated. This family includes a large number of largely uncharacterized plant proteins. This family includes a P-loop motif that is involved in nucleotide binding.
Pssm-ID: 428699 [Multi-domain] Cd Length: 361 Bit Score: 47.76 E-value: 8.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 46 GYAGTGKTSLVGALVKTMAELKQKSILLAPTGRAAKVFSGyaGQkafTIHK--KIYRQKA-FS--NEPTGFHPADNLHKD 120
Cdd:pfam05970 28 GYGGTGKTFLWKAIITSLRSEGKIVLAVASSGVAALLLPG--GR---TAHSrfGIPLDIDeLStcKIKRGSKLAELLEKT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 121 TLFIVDEASMIANEGLDSFVFGTGRLLDDLVQYVYSGENcrLILMGDVAQLPPVMQ--TESPALNPETLRGYNLK-VQEI 197
Cdd:pfam05970 103 SLIVWDEAPMTHRHCFEALDRTLRDILSETDDKPFGGKT--VVLGGDFRQILPVIPkgSRPEIVNASITNSYLWKhVKVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 198 TLTQVVRQSENSGILFNATRLRD------ALRNGTV--EIFPKLRLKGFTDFRKVNGDELIEEISSAYSRDGIEETMIIS 269
Cdd:pfam05970 181 ELTKNMRLLADSLDQTEAKELQDfsdwllAIGDGKIndENEREQLIDIPIDILLNTGGDPIEAIVSEVYPDILQNSTDPN 260
|
250
....*....|....*...
gi 491852579 270 RSNKRATLY-NNGIRNRI 286
Cdd:pfam05970 261 YLEERAILCpTNEDVDEI 278
|
|
| TraI_TIGR |
TIGR02760 |
conjugative transfer relaxase protein TraI; This protein is a component of the relaxosome ... |
39-172 |
1.40e-05 |
|
conjugative transfer relaxase protein TraI; This protein is a component of the relaxosome complex. In the process of conjugative plasmid transfer the realaxosome binds to the plasmid at the oriT (origin of transfer) site. The relaxase protein TraI mediates the single-strand nicking and ATP-dependent unwinding (relaxation, helicase activity) of the plasmid molecule. These two activities reside in separate domains of the protein.
Pssm-ID: 274285 [Multi-domain] Cd Length: 1960 Bit Score: 47.98 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 39 DSLLLLKGYAGTGKTSLVGALVKtMAELKQKSI-LLAPTGRAAKVFSGYAGQKAFTI---HKKIYRQKAFSNEPTGFHPA 114
Cdd:TIGR02760 446 KRFIIINGFGGTGSTEIAQLLLH-LASEQGYEIqIITAGSLSAQELRQKIPRLASTFitwVKNLFNDDQDHTVQGLLDKS 524
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 491852579 115 DNLHKDTLFIVDEASMIANEGLDSFVFGTGRllddlvqyvysgENCRLILMGDVAQLP 172
Cdd:TIGR02760 525 SPFSNKDIFVVDEANKLSNNELLKLIDKAEQ------------HNSKLILLNDSAQRQ 570
|
|
| PRK14712 |
PRK14712 |
conjugal transfer nickase/helicase TraI; Provisional |
36-284 |
6.30e-05 |
|
conjugal transfer nickase/helicase TraI; Provisional
Pssm-ID: 237796 [Multi-domain] Cd Length: 1623 Bit Score: 45.62 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 36 EESDSLLLLKGYAGTGKTSLVGALVKTMAELKQ----KSILLAPTGRAAKVFSGyAGQKAFT----IHKKIYRQKafSNE 107
Cdd:PRK14712 849 ETSDRFTVVQGYAGVGKTTQFRAVMSAVNMLPEserpRVVGLGPTHRAVGEMRS-AGVDAQTlasfLHDTQLQQR--SGE 925
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 108 PTGFhpadnlhKDTLFIVDEASMIANEGLDS----FVFGTGRLL----DDLVQYVYSGENCRL---------ILMGD-VA 169
Cdd:PRK14712 926 TPDF-------SNTLFLLDESSMVGNTDMARayalIAAGGGRAVasgdTDQLQAIAPGQPFRLqqtrsaadvVIMKEiVR 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 170 QLPPVMQTESPALNPETLRGYNlKVQEITLTQVVRQSENSGILFNATRLRDALRNGTVEIFPKLRLKG--FTDFRKVNGD 247
Cdd:PRK14712 999 QTPELREAVYSLINRDVERALS-GLERVKPSQVPRLEGAWAPEHSVTEFSHSQEAKLAEAQQKAMLKGeaFPDVPMTLYE 1077
|
250 260 270
....*....|....*....|....*....|....*..
gi 491852579 248 ELIEEIsSAYSRDGIEETMIISRSNKRATLYNNGIRN 284
Cdd:PRK14712 1078 AIVRDY-TGRTPEAREQTLIVTHLNEDRRVLNSMIHD 1113
|
|
| DEXXQc_DNA2 |
cd18041 |
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ... |
38-176 |
8.74e-04 |
|
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5-3 helicase, and endonuclease activities, and is involved in DNA replication and DNA repair in the nucleus and mitochondrion. It is involved in Okazaki fragment processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. It is also involved in 5-end resection of DNA during double-strand break (DSB) repair; it is recruited by BLM and mediates the cleavage of 5-ssDNA, while the 3-ssDNA cleavage is prevented by the presence of RPA. DNA2 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: 350799 [Multi-domain] Cd Length: 203 Bit Score: 40.68 E-value: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 38 SDSLLLLKGYAGTGKTSLVGALVKTMAELKqKSILLAPTGRAA--KVFSGYAGQK--------AFTIHKKIyRQKAFSNE 107
Cdd:cd18041 16 AKDYALILGMPGTGKTTTIAALVRILVALG-KSVLLTSYTHSAvdNILLKLKKFGvnflrlgrLKKIHPDV-QEFTLEAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491852579 108 PTGFHPADNLHK----------------DTLF--------IVDEASMIanegLDSFVFGTGRLLDdlvqyvysgencRLI 163
Cdd:cd18041 94 LKSCKSVEELESkyesvsvvattclginHPIFrrrtfdycIVDEASQI----TLPICLGPLRLAK------------KFV 157
|
170
....*....|...
gi 491852579 164 LMGDVAQLPPVMQ 176
Cdd:cd18041 158 LVGDHYQLPPLVK 170
|
|
| |
