|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
280-664 |
1.17e-135 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 430.33 E-value: 1.17e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 280 TTHDPRHELKRYFGFDDFRTepdgrtLQHDVVLAGMQGKHVLAILATGGGKSLCYQLPALnrfHRNGsLTVIISPLQSLM 359
Cdd:COG0514 1 LRDDALEVLKRVFGYDSFRP------GQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPAL---LLPG-LTLVVSPLIALM 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 360 KDQVDGLLARNVQcAATLNGLLTMPERAEVLEKIQLGDVGILLVSPEQFRNKAFRRAIAQRQVGAWIFDEAHCLSKWGAD 439
Cdd:COG0514 71 KDQVDALRAAGIR-AAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 440 FRPDYLYVSRFIKQFTGdgelAAIGCFTATAKPDVLEDIVlhfkDQLDIT-FERFIGTHERTNLHFEVLPCARAEKRhht 518
Cdd:COG0514 150 FRPDYRRLGELRERLPN----VPVLALTATATPRVRADIA----EQLGLEdPRVFVGSFDRPNLRLEVVPKPPDDKL--- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 519 qALLEDELGRNEGGA-VVFVSSRKGAEELADFLIGHGWACKYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVDKS 597
Cdd:COG0514 219 -AQLLDFLKEHPGGSgIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKP 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553768242 598 DIRLVVHADIPGSLENYLQEAGRAGRDQGEARCVLLYDAQDIENQFGMCEGSKLTLRDIQQILRKLR 664
Cdd:COG0514 298 DVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERAKLD 364
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
288-639 |
2.74e-81 |
|
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are known are 3'-5' DNA-DNA helicases. These proteins are used for recombination, recombinational repair, and possibly maintenance of chromosome stability. 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: 129701 [Multi-domain] Cd Length: 470 Bit Score: 276.27 E-value: 2.74e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 288 LKRYFGFDDFRTepdgrtLQHDVVLAGMQGKHVLAILATGGGKSLCYQLPALnrfhRNGSLTVIISPLQSLMKDQVDGLL 367
Cdd:TIGR00614 3 LKKYFGLSSFRP------VQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPAL----YSDGITLVISPLISLMEDQVLQLQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 368 ARNVQcAATLNGLLTMPERAEVLEKIQLGDVGILLVSPEQF-RNKAFRRAIAQRQVGAWI-FDEAHCLSKWGADFRPDYL 445
Cdd:TIGR00614 73 ALGIP-ATFLNSAQTKEQQLNVLTDLKDGKIKLLYVTPEKIsASNRLLQTLEERKGITLIaVDEAHCISQWGHDFRPDYK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 446 YVSRFIKQFTgdgeLAAIGCFTATAKPDVLEDIV--LHFKDQLditfeRFIGTHERTNLHFEVLPcaraEKRHHTQALLE 523
Cdd:TIGR00614 152 ALGSLKQKFP----NVPVMALTATASPSVREDILrqLNLLNPQ-----IFCTSFDRPNLYYEVRR----KTPKILEDLLR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 524 DELGRNEG-GAVVFVSSRKGAEELADFLIGHGWACKYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVDKSDIRLV 602
Cdd:TIGR00614 219 FIRKEFEGkSGIIYCPSRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFV 298
|
330 340 350
....*....|....*....|....*....|....*..
gi 553768242 603 VHADIPGSLENYLQEAGRAGRDQGEARCVLLYDAQDI 639
Cdd:TIGR00614 299 IHYSLPKSMESYYQESGRAGRDGLPSECHLFYAPADM 335
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
288-485 |
5.33e-68 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 227.91 E-value: 5.33e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 288 LKRYFGFDDFRTepdgrtLQHDVVLAGMQGKHVLAILATGGGKSLCYQLPALNRFHRNGSLTVIISPLQSLMKDQVDGLL 367
Cdd:cd18018 4 LRRVFGHPSFRP------GQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRRRGPGLTLVVSPLIALMKDQVDALP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 368 ARNvqCAATLNGLLTMPERAEVLEKIQLGDVGILLVSPEQFRNKAFRRAIAQR-QVGAWIFDEAHCLSKWGADFRPDYLY 446
Cdd:cd18018 78 RAI--KAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTpPISLLVVDEAHCISEWSHNFRPDYLR 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 553768242 447 VSRFIKQFTGdgeLAAIGCFTATAKPDVLEDIVLHFKDQ 485
Cdd:cd18018 156 LCRVLRELLG---APPVLALTATATKRVVEDIASHLGIP 191
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
288-639 |
1.03e-67 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 241.16 E-value: 1.03e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 288 LKRYFGFDDFRtepDGrtlQHDVVLAGMQGKHVLAILATGGGKSLCYQLPALNRfhrnGSLTVIISPLQSLMKDQVDGLL 367
Cdd:PRK11057 17 LQETFGYQQFR---PG---QQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVL----DGLTLVVSPLISLMKDQVDQLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 368 ARNVQcAATLNGLLTMPERAEVLEKIQLGDVGILLVSPEQFRNKAFRRAIAQRQVGAWIFDEAHCLSKWGADFRPDYLYV 447
Cdd:PRK11057 87 ANGVA-AACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 448 SRFIKQFTGDGELAaigcFTATAKPDVLEDIV--LHFKDQLDitferFIGTHERTNLHFEVLpcaraEKRHHTQAL---L 522
Cdd:PRK11057 166 GQLRQRFPTLPFMA----LTATADDTTRQDIVrlLGLNDPLI-----QISSFDRPNIRYTLV-----EKFKPLDQLmryV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 523 EDELGRNeggAVVFVSSRKGAEELADFLIGHGWACKYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVDKSDIRLV 602
Cdd:PRK11057 232 QEQRGKS---GIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFV 308
|
330 340 350
....*....|....*....|....*....|....*..
gi 553768242 603 VHADIPGSLENYLQEAGRAGRDQGEARCVLLYDAQDI 639
Cdd:PRK11057 309 VHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADM 345
|
|
| DEXQc_UvrD |
cd17932 |
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch ... |
1098-1306 |
6.38e-66 |
|
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. UvrD 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: 350690 [Multi-domain] Cd Length: 189 Bit Score: 221.24 E-value: 6.38e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1098 SAAQRVIVSDDDDvNRLVLAGPGSGKTRVIVHRIAYLLRVRRVPARCIVALTFNRHAANEIKQRLLRLVGP-DAFGVNVM 1176
Cdd:cd17932 1 NPEQREAVTHPDG-PLLVLAGAGSGKTRVLTHRIAYLILEGGVPPERILAVTFTNKAAKEMRERLRKLLGEqLASGVWIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1177 TYHRMAMRLTGtrfergetvEEGRLAQVMSEAVELLEGKRQVegeddlREQLMRGYRYILVDEYQDIDDLQYRLVSALAG 1256
Cdd:cd17932 80 TFHSFALRILR---------RYGDFDDLLLYALELLEENPDV------REKLQSRFRYILVDEYQDTNPLQYELLKLLAG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 553768242 1257 RkaeeegRLCILAVGDDDQNIYAWRDTNNRYIERFREDY-SASTSYLVDNY 1306
Cdd:cd17932 145 D------GKNLFVVGDDDQSIYGFRGADPENILDFEKDFpDAKVIKLEENY 189
|
|
| UvrD |
COG0210 |
Superfamily I DNA or RNA helicase [Replication, recombination and repair]; |
1091-1566 |
1.82e-64 |
|
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
Pssm-ID: 439980 [Multi-domain] Cd Length: 721 Bit Score: 234.44 E-value: 1.82e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1091 RSIVEKLSAAQRVIVSDDDDvNRLVLAGPGSGKTRVIVHRIAYLLRVRRVPARCIVALTFNRHAANEIKQRLLRLVGPDA 1170
Cdd:COG0210 1 SDLLAGLNPEQRAAVEHPEG-PLLVLAGAGSGKTRVLTHRIAYLIAEGGVDPEQILAVTFTNKAAREMRERIEALLGRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1171 FGVNVMTYHRMAMR-----------------------------------LTGTRFERGETV------------------- 1196
Cdd:COG0210 80 RGLWVGTFHSLALRilrrhaellglppnftildgddqlrlikellkelgLDEKRFPPRELLslisraknegltpeelael 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1197 -----EEGRLAQV-------------------MSEAVELLEGkrqvegEDDLREQLMRGYRYILVDEYQDIDDLQYRLVS 1252
Cdd:COG0210 160 laadpEWRAAAELyeayqerlrannaldfddlLLLAVRLLEE------NPEVLEKYQNRFRYILVDEYQDTNPAQYELLR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1253 ALAGRKaeeeGRLCilAVGDDDQNIYAWRDTNNRYIERFREDYS-ASTSYLVDNYRSSACIIEAANSVIGRNPDRL-KQD 1330
Cdd:COG0210 234 LLAGDG----RNLC--VVGDDDQSIYGFRGADPENILRFEKDFPdAKVIKLEQNYRSTQNILDAANAVIANNPGRLgKNL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1331 HPiqidtarrERPKGGD---WESLDPER-----AGWVLRLRVD--AEDD----TRANVQAQAAMAELQRL---------- 1386
Cdd:COG0210 308 WT--------DNGEGEKvrlYVAPDEEEearfvADEIRELHEEgvPLSDiavlYRTNAQSRALEEALRRAgipyrvvggl 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1387 ----------------LTLDPEDWqgcAVLARTHQYLLP---------VQAWCEAHGV---QYCLAADKDSALP---LTA 1435
Cdd:COG0210 380 rfyeraeikdllaylrLLANPDDD---VALLRILNVPRRgigaatlerLREAAREEGIsllEALRDLGELAGLSgraAKA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1436 QRGFVRAVEGLRAITEPVTAAEA-WVPLSETALVPDWYGF--------------FMTAFEQLTAEFGQCPLAAhtLIDWL 1500
Cdd:COG0210 457 LRRFAELLEALRAAAERLPLEELlEALLDESGYEEELREEageeaerrlenleeLVDAAARFEERNPGASLEA--FLEEL 534
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553768242 1501 YDYARELRQQPKQG-LYLGTVHSAKGLEFRHVVVL---DGGWSSQ-----PDTLSDERRLYYVGMTRAEQTLTLC 1566
Cdd:COG0210 535 ALLSDLDAADEDEDaVTLMTLHAAKGLEFPVVFLVgleEGLFPHQrslddEEELEEERRLFYVAITRARERLYLT 609
|
|
| uvrD |
PRK11773 |
DNA-dependent helicase II; Provisional |
1092-1566 |
3.65e-40 |
|
DNA-dependent helicase II; Provisional
Pssm-ID: 236976 [Multi-domain] Cd Length: 721 Bit Score: 160.81 E-value: 3.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1092 SIVEKLSAAQRVIVSDDDDvNRLVLAGPGSGKTRVIVHRIAYLLRVRRVPARCIVALTFNRHAANEIKQRLLRLVGPDAF 1171
Cdd:PRK11773 5 YLLDSLNDKQREAVAAPLG-NMLVLAGAGSGKTRVLVHRIAWLMQVENASPYSIMAVTFTNKAAAEMRHRIEQLLGTSQG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1172 GVNVMTYHRMAMRLTGTR---------FERGETVEEGRLAQVMSEAVELLEGK---RQV---------EG---------- 1220
Cdd:PRK11773 84 GMWVGTFHGLAHRLLRAHwqdanlpqdFQILDSDDQLRLLKRLIKALNLDEKQwppRQAqwyingqkdEGlrpqhiqsyg 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1221 --------------ED--------DLREQLMRGY-----------------RYILVDEYQDIDDLQYRLVSALAGrkaeE 1261
Cdd:PRK11773 164 dpveqtwlkiyqayQEacdraglvDFAELLLRAHelwlnkphilqhyqerfTHILVDEFQDTNAIQYAWIRLLAG----D 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1262 EGRLciLAVGDDDQNIYAWRDTNNRYIERFREDYS-ASTSYLVDNYRSSACIIEAANSVIGRNPDRLKQD--------HP 1332
Cdd:PRK11773 240 TGKV--MIVGDDDQSIYGWRGAQVENIQRFLNDFPgAETIRLEQNYRSTANILKAANALIANNNGRLGKElwtdggdgEP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1333 IQI-------DTAR-------RERPKGGDW-----------------ESLDPER-------------------AGWVLRL 1362
Cdd:PRK11773 318 ISLycafnelDEARfvverikTWQDNGGALsdcailyrsnaqsrvleEALLQAGipyriyggmrfferqeikdALAYLRL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1363 RVDAEDDT---RA-NVQA------------QAAMaelQRLLTLdpedWQGCAVLarTHQYLLPVQAwceAHGVQYCLA-- 1424
Cdd:PRK11773 398 IANRNDDAafeRVvNTPTrgigdrtldvvrQTAR---DRQLTL----WQACRAL--LQEKVLAGRA---ASALQRFIEli 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1425 ---ADKDSALPLTAQRGFVRAVEGLRA----------------ITEPVTAAEAWVPLSETALVPDwygffMTAFeqltae 1485
Cdd:PRK11773 466 dalAQETADMPLHEQTDRVIKDSGLRAmyeqekgekgqarienLEELVTATRQFSYPDEDEDLTP-----LQAF------ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1486 fgqcplAAHTLIDwlydyARELRQQPKQ-GLYLGTVHSAKGLEFRHVV---VLDGGWSSQ-----PDTLSDERRLYYVGM 1556
Cdd:PRK11773 535 ------LSHAALE-----AGEGQADAHEdAVQLMTLHSAKGLEFPLVFivgMEEGLFPSQmsleeGGRLEEERRLAYVGI 603
|
650
....*....|
gi 553768242 1557 TRAEQTLTLC 1566
Cdd:PRK11773 604 TRAMQKLTLT 613
|
|
| UvrD-helicase |
pfam00580 |
UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural ... |
1112-1295 |
6.80e-34 |
|
UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural domains. The Rep family function as dimers. REP helicases catalyze ATP dependent unwinding of double stranded DNA to single stranded DNA. Swiss:P23478, Swiss:P08394 have large insertions near to the carboxy-terminus relative to other members of the family.
Pssm-ID: 395462 [Multi-domain] Cd Length: 267 Bit Score: 132.37 E-value: 6.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1112 NRLVLAGPGSGKTRVIVHRIAYLLRVRRVPARCIVALTFNRHAANEIKQRLLRLVG-PDAFGVNVMTYHRMAMRL----- 1185
Cdd:pfam00580 15 PLLVLAGAGSGKTRVLTERIAYLILEGGIDPEEILAVTFTNKAAREMKERILKLLGkAELSELNISTFHSFCLRIlrkya 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1186 --------------TGTR-------------------------------FERGETVEEG-------RLAQVMSEAVELLE 1213
Cdd:pfam00580 95 nrigllpnfsildeLDQLallkellekdrlnldpkllrklelkeliskaKNRLLSPEELqqgaadpRDKLAAEFYQEYQE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1214 GKRQ----------------VEGEDDLREQLMRGYRYILVDEYQDIDDLQYRLVSALAGRKAEeegrlcILAVGDDDQNI 1277
Cdd:pfam00580 175 RLKEnnaldfddlllltlelLRSDPELLEAYRERFKYILVDEFQDTNPIQYRLLKLLAGGHEN------LFLVGDPDQSI 248
|
250
....*....|....*...
gi 553768242 1278 YAWRDTNNRYIERFREDY 1295
Cdd:pfam00580 249 YGFRGADIENILKFEKDF 266
|
|
| DpdF |
NF041063 |
protein DpdF; |
288-640 |
8.29e-33 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 138.12 E-value: 8.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 288 LKRYFGFDDFRTE------------PDGRTLqhdvvlagmqgkhvLAILATGGGKSLCYQLPALnRFHRNGSLTVIISPL 355
Cdd:NF041063 131 LAEALGFTHYRSPgqreavraallaPPGSTL--------------IVNLPTGSGKSLVAQAPAL-LASRQGGLTLVVVPT 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 356 QSLMKDQ----VDGLLARNVQCAATLN--GLLTMPERAEVLEKIQLGDVGILLVSPEQFR---NKAFRRAIAQRQVGAWI 426
Cdd:NF041063 196 VALAIDQerraRELLRRAGPDLGGPLAwhGGLSAEERAAIRQRIRDGTQRILFTSPESLTgslRPALFDAAEAGLLRYLV 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 427 FDEAHCLSKWGADFRPDYlyvsrfikQftgdgELAAI-----------GCF-----TATAKPDVLEDIVLHFKDQlditf 490
Cdd:NF041063 276 VDEAHLVDQWGDGFRPEF--------Q-----LLAGLrrsllrlapsgRPFrtlllSATLTESTLDTLETLFGPP----- 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 491 ERFI---GTHERTNLHFEVLPCARAEKRhhTQALLE--DELGRNeggAVVFVSSRKGAEELADFLIGHGWA-CKYFHAGL 564
Cdd:NF041063 338 GPFIvvsAVQLRPEPAYWVAKCDSEEER--RERVLEalRHLPRP---LILYVTKVEDAEAWLQRLRAAGFRrVALFHGDT 412
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553768242 565 EPHEKKDIQDAFKSGELKIIVATNAFGMGVDKSDIRLVVHADIPGSLENYLQEAGRAGRDqGEA-RCVLLYDAQDIE 640
Cdd:NF041063 413 PDAERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRD-GKAsLSLLIYTPDDLD 488
|
|
| PRK10919 |
PRK10919 |
ATP-dependent DNA helicase Rep; Provisional |
1114-1324 |
1.71e-27 |
|
ATP-dependent DNA helicase Rep; Provisional
Pssm-ID: 182838 [Multi-domain] Cd Length: 672 Bit Score: 120.72 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1114 LVLAGPGSGKTRVIVHRIAYLLRVRRVPARCIVALTFNRHAANEIKQRLLRLVG-PDAFGVNVMTYHRMAMR-------- 1184
Cdd:PRK10919 19 LVLAGAGSGKTRVITNKIAHLIRGCGYQARHIAAVTFTNKAAREMKERVAQTLGrKEARGLMISTFHTLGLDiikreyaa 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1185 ---------------------LTGTRFERGETVEEGRLAQVM---------SEAVELLEGKRQ----------------- 1217
Cdd:PRK10919 99 lgmksnfslfddtdqlallkeLTEGLIEDDKVLLQQLISTISnwkndlktpAQAAAGAKGERDrifahcyglydahlkac 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1218 -VEGEDDL--------------REQLMRGYRYILVDEYQDIDDLQYRLVSALAGRKAeeegRLCIlaVGDDDQNIYAWRD 1282
Cdd:PRK10919 179 nVLDFDDLillptlllqrneevRERWQNKIRYLLVDEYQDTNTSQYELVKLLVGSRA----RFTV--VGDDDQSIYSWRG 252
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 553768242 1283 TNNRYIERFREDYSA-STSYLVDNYRSSACIIEAANSVIGRNP 1324
Cdd:PRK10919 253 ARPQNLVLLSQDFPAlQVIKLEQNYRSSGRILKAANILIANNP 295
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
544-624 |
4.51e-22 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 91.89 E-value: 4.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 544 EELADFLIGHGWACKYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVDKSDIRLVVHADIPGSLENYLQEAGRAGR 623
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
.
gi 553768242 624 D 624
Cdd:smart00490 81 A 81
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
307-478 |
1.11e-21 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 93.46 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 307 QHDVVLAGMQGKHVLAILATGGGKSLCYQLPALNRFHR--NGSLTVIISPLQSLMKDQVDGLLARNVQCAATLNGLLTMP 384
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKldNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLLGGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 385 ERAEVLEKIQLGDvgILLVSPEQFR-NKAFRRAIaqRQVGAWIFDEAHCLSKWGadFRPDYLYVSRFIKQFTGdgelaaI 463
Cdd:pfam00270 84 SRKEQLEKLKGPD--ILVGTPGRLLdLLQERKLL--KNLKLLVLDEAHRLLDMG--FGPDLEEILRRLPKKRQ------I 151
|
170
....*....|....*
gi 553768242 464 GCFTATAkPDVLEDI 478
Cdd:pfam00270 152 LLLSATL-PRNLEDL 165
|
|
| SF1_C_UvrD |
cd18807 |
C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase ... |
1308-1566 |
2.65e-18 |
|
C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. This family also includes ATP-dependent helicase/nuclease AddA and helicase/nuclease RecBCD subunit RecB, among others. UvrD 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: 350194 [Multi-domain] Cd Length: 150 Bit Score: 83.43 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1308 SSACIIEAANSVIGRNPDRLKqdHPIQIDTARRERPKGgdWESLDPERagwvlrlrvdaeddtranvQAQAAMAELQRLL 1387
Cdd:cd18807 1 STKNILDAANSLIKQNKNRPK--KPLKAGNKSGGPVEL--LLAKDEAD-------------------EAKAIADEIKRLI 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1388 TLDPEDWQGCAVLARTHQYLLPVQAWCEahgvqyclaadkdsalpltaqrgfvraveglraitepvtaaeawvplsetal 1467
Cdd:cd18807 58 ESGPVQYSDIAILVRTNRQARVIEEALR---------------------------------------------------- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1468 vpdwygffmtafeqltaefgqcplaahtlidwlydyarelrqqpkqgLYLGTVHSAKGLEFRHVVVLDGGWSSQP----- 1542
Cdd:cd18807 86 -----------------------------------------------VTLMTIHASKGLEFPVVFIVGLGEGFIPsdasy 118
|
250 260 270
....*....|....*....|....*....|.
gi 553768242 1543 -------DTLSDERRLYYVGMTRAEQTLTLC 1566
Cdd:cd18807 119 haakedeERLEEERRLLYVALTRAKKELYLV 149
|
|
| UvrD_C_2 |
pfam13538 |
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety ... |
1515-1566 |
1.75e-09 |
|
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: 54.89 E-value: 1.75e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 553768242 1515 LYLGTVHSAKGLEFRHVVVLDGGWsSQPDTLSDERRLYYVGMTRAEQTLTLC 1566
Cdd:pfam13538 2 AYALTVHKAQGSEFPAVFLVDPDL-TAHYHSMLRRRLLYTAVTRARKKLVLV 52
|
|
| EXOIII |
smart00479 |
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ... |
10-137 |
2.10e-07 |
|
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other exonucleases;
Pssm-ID: 214685 [Multi-domain] Cd Length: 169 Bit Score: 52.69 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 10 LIFDLEvAPGNADQPDRIFMVGALRPDTGEELE---------RKVD-----------------KDLPSVLDALDSLGQGA 63
Cdd:smart00479 3 VVIDCE-TTGLDPGKDEIIEIAAVDVDGGEIIEvfdtyvkpdRPITdyateihgitpemlddaPTFEEVLEELLEFLRGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 64 SFVlGHNVIDHDLPILKQQAPDL---ALHGLPVIDTLRLSPLAFPQNPYHRL---VKDYKLIRDSLN-SPLTDCRSTLTL 136
Cdd:smart00479 82 ILV-AGNSAHFDLRFLKLEHPRLgikQPPKLPVIDTLKLARATNPGLPKYSLkklAKRLLLEVIQRAhRALDDARATAKL 160
|
.
gi 553768242 137 F 137
Cdd:smart00479 161 F 161
|
|
| PolC |
COG2176 |
DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair]; ... |
11-137 |
9.24e-07 |
|
DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair];
Pssm-ID: 441779 [Multi-domain] Cd Length: 181 Bit Score: 50.91 E-value: 9.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 11 IFDLEVAPGNADQpDRIFMVGALRPDTGEELER-----KVDKDLPS---------------------VLDALDSLGQGAS 64
Cdd:COG2176 12 VFDLETTGLSPKK-DEIIEIGAVKVENGEIVDRfstlvNPGRPIPPfiteltgitdemvadappfeeVLPEFLEFLGDAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 65 FVlGHNViDHDLPILKQQapdLALHGL----PVIDTLRLSPLAFPQNPYHRLvkDYklIRDSLNSPLT-------DCRST 133
Cdd:COG2176 91 LV-AHNA-SFDLGFLNAA---LKRLGLpfdnPVLDTLELARRLLPELKSYKL--DT--LAERLGIPLEdrhralgDAEAT 161
|
....
gi 553768242 134 LTLF 137
Cdd:COG2176 162 AELF 165
|
|
| DEDDh |
cd06127 |
DEDDh 3'-5' exonuclease domain family; DEDDh exonucleases, part of the DnaQ-like (or DEDD) ... |
12-138 |
2.78e-06 |
|
DEDDh 3'-5' exonuclease domain family; DEDDh exonucleases, part of the DnaQ-like (or DEDD) exonuclease superfamily, catalyze the excision of nucleoside monophosphates at the DNA or RNA termini in the 3'-5' direction. These proteins contain four invariant acidic residues in three conserved sequence motifs termed ExoI, ExoII and ExoIII. DEDDh exonucleases are classified as such because of the presence of specific Hx(4)D conserved pattern at the ExoIII motif. The four conserved acidic residues are clustered around the active site and serve as ligands for the two metal ions required for catalysis. Most DEDDh exonucleases are the proofreading subunits (epsilon) or domains of bacterial DNA polymerase III, the main replicating enzyme in bacteria, which functions as the chromosomal replicase. Other members include other DNA and RNA exonucleases such as RNase T, Oligoribonuclease, and RNA exonuclease (REX), among others.
Pssm-ID: 176648 [Multi-domain] Cd Length: 159 Bit Score: 48.84 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 12 FDLEVAPGnADQPDRIFMVGALrpdTGEELERKVDKD--LPSVLDALdslgqGASFVLGHNViDHDLPILKQQAPDLALH 89
Cdd:cd06127 35 FETLVNPG-RPIPPEATAIHGI---TDEMLADAPPFEevLPEFLEFL-----GGRVLVAHNA-SFDLRFLNRELRRLGGP 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 553768242 90 GL--PVIDTLRLSPLAFPQNPYHRLvkdYKLIRDSLNSP-------LTDCRSTLTLFN 138
Cdd:cd06127 105 PLpnPWIDTLRLARRLLPGLRSHRL---GLLLAERYGIPlegahraLADALATAELLL 159
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
280-664 |
1.17e-135 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 430.33 E-value: 1.17e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 280 TTHDPRHELKRYFGFDDFRTepdgrtLQHDVVLAGMQGKHVLAILATGGGKSLCYQLPALnrfHRNGsLTVIISPLQSLM 359
Cdd:COG0514 1 LRDDALEVLKRVFGYDSFRP------GQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPAL---LLPG-LTLVVSPLIALM 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 360 KDQVDGLLARNVQcAATLNGLLTMPERAEVLEKIQLGDVGILLVSPEQFRNKAFRRAIAQRQVGAWIFDEAHCLSKWGAD 439
Cdd:COG0514 71 KDQVDALRAAGIR-AAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 440 FRPDYLYVSRFIKQFTGdgelAAIGCFTATAKPDVLEDIVlhfkDQLDIT-FERFIGTHERTNLHFEVLPCARAEKRhht 518
Cdd:COG0514 150 FRPDYRRLGELRERLPN----VPVLALTATATPRVRADIA----EQLGLEdPRVFVGSFDRPNLRLEVVPKPPDDKL--- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 519 qALLEDELGRNEGGA-VVFVSSRKGAEELADFLIGHGWACKYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVDKS 597
Cdd:COG0514 219 -AQLLDFLKEHPGGSgIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKP 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553768242 598 DIRLVVHADIPGSLENYLQEAGRAGRDQGEARCVLLYDAQDIENQFGMCEGSKLTLRDIQQILRKLR 664
Cdd:COG0514 298 DVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERAKLD 364
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
288-639 |
2.74e-81 |
|
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are known are 3'-5' DNA-DNA helicases. These proteins are used for recombination, recombinational repair, and possibly maintenance of chromosome stability. 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: 129701 [Multi-domain] Cd Length: 470 Bit Score: 276.27 E-value: 2.74e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 288 LKRYFGFDDFRTepdgrtLQHDVVLAGMQGKHVLAILATGGGKSLCYQLPALnrfhRNGSLTVIISPLQSLMKDQVDGLL 367
Cdd:TIGR00614 3 LKKYFGLSSFRP------VQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPAL----YSDGITLVISPLISLMEDQVLQLQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 368 ARNVQcAATLNGLLTMPERAEVLEKIQLGDVGILLVSPEQF-RNKAFRRAIAQRQVGAWI-FDEAHCLSKWGADFRPDYL 445
Cdd:TIGR00614 73 ALGIP-ATFLNSAQTKEQQLNVLTDLKDGKIKLLYVTPEKIsASNRLLQTLEERKGITLIaVDEAHCISQWGHDFRPDYK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 446 YVSRFIKQFTgdgeLAAIGCFTATAKPDVLEDIV--LHFKDQLditfeRFIGTHERTNLHFEVLPcaraEKRHHTQALLE 523
Cdd:TIGR00614 152 ALGSLKQKFP----NVPVMALTATASPSVREDILrqLNLLNPQ-----IFCTSFDRPNLYYEVRR----KTPKILEDLLR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 524 DELGRNEG-GAVVFVSSRKGAEELADFLIGHGWACKYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVDKSDIRLV 602
Cdd:TIGR00614 219 FIRKEFEGkSGIIYCPSRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFV 298
|
330 340 350
....*....|....*....|....*....|....*..
gi 553768242 603 VHADIPGSLENYLQEAGRAGRDQGEARCVLLYDAQDI 639
Cdd:TIGR00614 299 IHYSLPKSMESYYQESGRAGRDGLPSECHLFYAPADM 335
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
288-485 |
5.33e-68 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 227.91 E-value: 5.33e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 288 LKRYFGFDDFRTepdgrtLQHDVVLAGMQGKHVLAILATGGGKSLCYQLPALNRFHRNGSLTVIISPLQSLMKDQVDGLL 367
Cdd:cd18018 4 LRRVFGHPSFRP------GQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRRRGPGLTLVVSPLIALMKDQVDALP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 368 ARNvqCAATLNGLLTMPERAEVLEKIQLGDVGILLVSPEQFRNKAFRRAIAQR-QVGAWIFDEAHCLSKWGADFRPDYLY 446
Cdd:cd18018 78 RAI--KAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTpPISLLVVDEAHCISEWSHNFRPDYLR 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 553768242 447 VSRFIKQFTGdgeLAAIGCFTATAKPDVLEDIVLHFKDQ 485
Cdd:cd18018 156 LCRVLRELLG---APPVLALTATATKRVVEDIASHLGIP 191
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
288-639 |
1.03e-67 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 241.16 E-value: 1.03e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 288 LKRYFGFDDFRtepDGrtlQHDVVLAGMQGKHVLAILATGGGKSLCYQLPALNRfhrnGSLTVIISPLQSLMKDQVDGLL 367
Cdd:PRK11057 17 LQETFGYQQFR---PG---QQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVL----DGLTLVVSPLISLMKDQVDQLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 368 ARNVQcAATLNGLLTMPERAEVLEKIQLGDVGILLVSPEQFRNKAFRRAIAQRQVGAWIFDEAHCLSKWGADFRPDYLYV 447
Cdd:PRK11057 87 ANGVA-AACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 448 SRFIKQFTGDGELAaigcFTATAKPDVLEDIV--LHFKDQLDitferFIGTHERTNLHFEVLpcaraEKRHHTQAL---L 522
Cdd:PRK11057 166 GQLRQRFPTLPFMA----LTATADDTTRQDIVrlLGLNDPLI-----QISSFDRPNIRYTLV-----EKFKPLDQLmryV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 523 EDELGRNeggAVVFVSSRKGAEELADFLIGHGWACKYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVDKSDIRLV 602
Cdd:PRK11057 232 QEQRGKS---GIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFV 308
|
330 340 350
....*....|....*....|....*....|....*..
gi 553768242 603 VHADIPGSLENYLQEAGRAGRDQGEARCVLLYDAQDI 639
Cdd:PRK11057 309 VHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADM 345
|
|
| DEXQc_UvrD |
cd17932 |
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch ... |
1098-1306 |
6.38e-66 |
|
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. UvrD 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: 350690 [Multi-domain] Cd Length: 189 Bit Score: 221.24 E-value: 6.38e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1098 SAAQRVIVSDDDDvNRLVLAGPGSGKTRVIVHRIAYLLRVRRVPARCIVALTFNRHAANEIKQRLLRLVGP-DAFGVNVM 1176
Cdd:cd17932 1 NPEQREAVTHPDG-PLLVLAGAGSGKTRVLTHRIAYLILEGGVPPERILAVTFTNKAAKEMRERLRKLLGEqLASGVWIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1177 TYHRMAMRLTGtrfergetvEEGRLAQVMSEAVELLEGKRQVegeddlREQLMRGYRYILVDEYQDIDDLQYRLVSALAG 1256
Cdd:cd17932 80 TFHSFALRILR---------RYGDFDDLLLYALELLEENPDV------REKLQSRFRYILVDEYQDTNPLQYELLKLLAG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 553768242 1257 RkaeeegRLCILAVGDDDQNIYAWRDTNNRYIERFREDY-SASTSYLVDNY 1306
Cdd:cd17932 145 D------GKNLFVVGDDDQSIYGFRGADPENILDFEKDFpDAKVIKLEENY 189
|
|
| UvrD |
COG0210 |
Superfamily I DNA or RNA helicase [Replication, recombination and repair]; |
1091-1566 |
1.82e-64 |
|
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
Pssm-ID: 439980 [Multi-domain] Cd Length: 721 Bit Score: 234.44 E-value: 1.82e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1091 RSIVEKLSAAQRVIVSDDDDvNRLVLAGPGSGKTRVIVHRIAYLLRVRRVPARCIVALTFNRHAANEIKQRLLRLVGPDA 1170
Cdd:COG0210 1 SDLLAGLNPEQRAAVEHPEG-PLLVLAGAGSGKTRVLTHRIAYLIAEGGVDPEQILAVTFTNKAAREMRERIEALLGRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1171 FGVNVMTYHRMAMR-----------------------------------LTGTRFERGETV------------------- 1196
Cdd:COG0210 80 RGLWVGTFHSLALRilrrhaellglppnftildgddqlrlikellkelgLDEKRFPPRELLslisraknegltpeelael 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1197 -----EEGRLAQV-------------------MSEAVELLEGkrqvegEDDLREQLMRGYRYILVDEYQDIDDLQYRLVS 1252
Cdd:COG0210 160 laadpEWRAAAELyeayqerlrannaldfddlLLLAVRLLEE------NPEVLEKYQNRFRYILVDEYQDTNPAQYELLR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1253 ALAGRKaeeeGRLCilAVGDDDQNIYAWRDTNNRYIERFREDYS-ASTSYLVDNYRSSACIIEAANSVIGRNPDRL-KQD 1330
Cdd:COG0210 234 LLAGDG----RNLC--VVGDDDQSIYGFRGADPENILRFEKDFPdAKVIKLEQNYRSTQNILDAANAVIANNPGRLgKNL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1331 HPiqidtarrERPKGGD---WESLDPER-----AGWVLRLRVD--AEDD----TRANVQAQAAMAELQRL---------- 1386
Cdd:COG0210 308 WT--------DNGEGEKvrlYVAPDEEEearfvADEIRELHEEgvPLSDiavlYRTNAQSRALEEALRRAgipyrvvggl 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1387 ----------------LTLDPEDWqgcAVLARTHQYLLP---------VQAWCEAHGV---QYCLAADKDSALP---LTA 1435
Cdd:COG0210 380 rfyeraeikdllaylrLLANPDDD---VALLRILNVPRRgigaatlerLREAAREEGIsllEALRDLGELAGLSgraAKA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1436 QRGFVRAVEGLRAITEPVTAAEA-WVPLSETALVPDWYGF--------------FMTAFEQLTAEFGQCPLAAhtLIDWL 1500
Cdd:COG0210 457 LRRFAELLEALRAAAERLPLEELlEALLDESGYEEELREEageeaerrlenleeLVDAAARFEERNPGASLEA--FLEEL 534
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553768242 1501 YDYARELRQQPKQG-LYLGTVHSAKGLEFRHVVVL---DGGWSSQ-----PDTLSDERRLYYVGMTRAEQTLTLC 1566
Cdd:COG0210 535 ALLSDLDAADEDEDaVTLMTLHAAKGLEFPVVFLVgleEGLFPHQrslddEEELEEERRLFYVAITRARERLYLT 609
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
285-484 |
1.94e-63 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 214.71 E-value: 1.94e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 285 RHELKRYFGFDDFRTepdgrtLQHDVVLAGMQGKHVLAILATGGGKSLCYQLPALnrfHRNGsLTVIISPLQSLMKDQVD 364
Cdd:cd17920 1 EQILKEVFGYDEFRP------GQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPAL---LLDG-VTLVVSPLISLMQDQVD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 365 GLLARNVQCAAtLNGLLTMPERAEVLEKIQLGDVGILLVSPEQFRNKAFRRAIAQRQVGAWI----FDEAHCLSKWGADF 440
Cdd:cd17920 71 RLQQLGIRAAA-LNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPERKRLalivVDEAHCVSQWGHDF 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 553768242 441 RPDYLYVSRFIKQFTGdgelAAIGCFTATAKPDVLEDIV--LHFKD 484
Cdd:cd17920 150 RPDYLRLGRLRRALPG----VPILALTATATPEVREDILkrLGLRN 191
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
289-638 |
6.04e-50 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 195.11 E-value: 6.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 289 KRYFGFDDFRtePDgrtlQHDVVLAGMQGKHVLAILATGGGKSLCYQLPALnrfhRNGSLTVIISPLQSLMKDQVDGLLA 368
Cdd:PLN03137 453 KKVFGNHSFR--PN----QREIINATMSGYDVFVLMPTGGGKSLTYQLPAL----ICPGITLVISPLVSLIQDQIMNLLQ 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 369 RNVQcAATLNGLLTMPERAEVLEKI--QLGDVGILLVSPEQF-RNKAFRRAI----AQRQVGAWIFDEAHCLSKWGADFR 441
Cdd:PLN03137 523 ANIP-AASLSAGMEWAEQLEILQELssEYSKYKLLYVTPEKVaKSDSLLRHLenlnSRGLLARFVIDEAHCVSQWGHDFR 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 442 PDYLYVSRFIKQFTGDGELAaigcFTATAKPDVLEDIVLHFKDQLDITFERfigTHERTNLHFEVLPcaraekrhHTQAL 521
Cdd:PLN03137 602 PDYQGLGILKQKFPNIPVLA----LTATATASVKEDVVQALGLVNCVVFRQ---SFNRPNLWYSVVP--------KTKKC 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 522 LED------ELGRNEGGaVVFVSSRKGAEELADFLIGHGWACKYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVD 595
Cdd:PLN03137 667 LEDidkfikENHFDECG-IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGIN 745
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 553768242 596 KSDIRLVVHADIPGSLENYLQEAGRAGRDQGEARCVLLYDAQD 638
Cdd:PLN03137 746 KPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYSD 788
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
499-634 |
2.79e-42 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350181 [Multi-domain] Cd Length: 134 Bit Score: 151.21 E-value: 2.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 499 RTNLHFEVLPcaraeKRHHTQALLEDELGR---NEGGAVVFVSSRKGAEELADFLIGHGWACKYFHAGLEPHEKKDIQDA 575
Cdd:cd18794 1 RPNLFYSVRP-----KDKKDEKLDLLKRIKvehLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRK 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 553768242 576 FKSGELKIIVATNAFGMGVDKSDIRLVVHADIPGSLENYLQEAGRAGRDQGEARCVLLY 634
Cdd:cd18794 76 WLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| uvrD |
PRK11773 |
DNA-dependent helicase II; Provisional |
1092-1566 |
3.65e-40 |
|
DNA-dependent helicase II; Provisional
Pssm-ID: 236976 [Multi-domain] Cd Length: 721 Bit Score: 160.81 E-value: 3.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1092 SIVEKLSAAQRVIVSDDDDvNRLVLAGPGSGKTRVIVHRIAYLLRVRRVPARCIVALTFNRHAANEIKQRLLRLVGPDAF 1171
Cdd:PRK11773 5 YLLDSLNDKQREAVAAPLG-NMLVLAGAGSGKTRVLVHRIAWLMQVENASPYSIMAVTFTNKAAAEMRHRIEQLLGTSQG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1172 GVNVMTYHRMAMRLTGTR---------FERGETVEEGRLAQVMSEAVELLEGK---RQV---------EG---------- 1220
Cdd:PRK11773 84 GMWVGTFHGLAHRLLRAHwqdanlpqdFQILDSDDQLRLLKRLIKALNLDEKQwppRQAqwyingqkdEGlrpqhiqsyg 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1221 --------------ED--------DLREQLMRGY-----------------RYILVDEYQDIDDLQYRLVSALAGrkaeE 1261
Cdd:PRK11773 164 dpveqtwlkiyqayQEacdraglvDFAELLLRAHelwlnkphilqhyqerfTHILVDEFQDTNAIQYAWIRLLAG----D 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1262 EGRLciLAVGDDDQNIYAWRDTNNRYIERFREDYS-ASTSYLVDNYRSSACIIEAANSVIGRNPDRLKQD--------HP 1332
Cdd:PRK11773 240 TGKV--MIVGDDDQSIYGWRGAQVENIQRFLNDFPgAETIRLEQNYRSTANILKAANALIANNNGRLGKElwtdggdgEP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1333 IQI-------DTAR-------RERPKGGDW-----------------ESLDPER-------------------AGWVLRL 1362
Cdd:PRK11773 318 ISLycafnelDEARfvverikTWQDNGGALsdcailyrsnaqsrvleEALLQAGipyriyggmrfferqeikdALAYLRL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1363 RVDAEDDT---RA-NVQA------------QAAMaelQRLLTLdpedWQGCAVLarTHQYLLPVQAwceAHGVQYCLA-- 1424
Cdd:PRK11773 398 IANRNDDAafeRVvNTPTrgigdrtldvvrQTAR---DRQLTL----WQACRAL--LQEKVLAGRA---ASALQRFIEli 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1425 ---ADKDSALPLTAQRGFVRAVEGLRA----------------ITEPVTAAEAWVPLSETALVPDwygffMTAFeqltae 1485
Cdd:PRK11773 466 dalAQETADMPLHEQTDRVIKDSGLRAmyeqekgekgqarienLEELVTATRQFSYPDEDEDLTP-----LQAF------ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1486 fgqcplAAHTLIDwlydyARELRQQPKQ-GLYLGTVHSAKGLEFRHVV---VLDGGWSSQ-----PDTLSDERRLYYVGM 1556
Cdd:PRK11773 535 ------LSHAALE-----AGEGQADAHEdAVQLMTLHSAKGLEFPLVFivgMEEGLFPSQmsleeGGRLEEERRLAYVGI 603
|
650
....*....|
gi 553768242 1557 TRAEQTLTLC 1566
Cdd:PRK11773 604 TRAMQKLTLT 613
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
288-483 |
6.99e-39 |
|
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350772 [Multi-domain] Cd Length: 205 Bit Score: 144.54 E-value: 6.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 288 LKRYFGFDDFRTEpdgrtLQHDVVLAGMQGKH-VLAILATGGGKSLCYQLPALnrfhRNGSLTVIISPLQSLMKDQVDGL 366
Cdd:cd18014 4 LKKVFGHSDFKSP-----LQEKATMAVVKGNKdVFVCMPTGAGKSLCYQLPAL----LAKGITIVISPLIALIQDQVDHL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 367 LARNVQCAaTLNGLLTMPERAEVLEKIQ--LGDVGILLVSPEQFRNKAFRRAIA---QRQVGAWI-FDEAHCLSKWGADF 440
Cdd:cd18014 75 KTLKIRVD-SLNSKLSAQERKRIIADLEseKPQTKFLYITPEMAATSSFQPLLSslvSRNLLSYLvVDEAHCVSQWGHDF 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 553768242 441 RPDYLYVSRFIKQFtgdGELAAIGcFTATAKPDVLEDI--VLHFK 483
Cdd:cd18014 154 RPDYLRLGALRSRY---GHVPWVA-LTATATPQVQEDIfaQLRLK 194
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
288-478 |
1.32e-34 |
|
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350773 [Multi-domain] Cd Length: 209 Bit Score: 132.10 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 288 LKRYFGFDDFRTepdgrtLQHDVVLAGMQGKHVLAILATGGGKSLCYQLPALNRfhrnGSLTVIISPLQSLMKDQVDGLL 367
Cdd:cd18015 10 LKNVFKLEKFRP------LQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCS----DGFTLVVSPLISLMEDQLMALK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 368 ARNVQcAATLNGLLTMPERAEVLEKIQLGDVG--ILLVSPEQ------FRNKaFRRAIAQRQVGAWIFDEAHCLSKWGAD 439
Cdd:cd18015 80 KLGIS-ATMLNASSSKEHVKWVHAALTDKNSElkLLYVTPEKiakskrFMSK-LEKAYNAGRLARIAIDEVHCCSQWGHD 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 553768242 440 FRPDYLYVSRFIKQFTGdgelAAIGCFTATAKPDVLEDI 478
Cdd:cd18015 158 FRPDYKKLGILKRQFPN----VPILGLTATATSKVLKDV 192
|
|
| UvrD-helicase |
pfam00580 |
UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural ... |
1112-1295 |
6.80e-34 |
|
UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural domains. The Rep family function as dimers. REP helicases catalyze ATP dependent unwinding of double stranded DNA to single stranded DNA. Swiss:P23478, Swiss:P08394 have large insertions near to the carboxy-terminus relative to other members of the family.
Pssm-ID: 395462 [Multi-domain] Cd Length: 267 Bit Score: 132.37 E-value: 6.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1112 NRLVLAGPGSGKTRVIVHRIAYLLRVRRVPARCIVALTFNRHAANEIKQRLLRLVG-PDAFGVNVMTYHRMAMRL----- 1185
Cdd:pfam00580 15 PLLVLAGAGSGKTRVLTERIAYLILEGGIDPEEILAVTFTNKAAREMKERILKLLGkAELSELNISTFHSFCLRIlrkya 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1186 --------------TGTR-------------------------------FERGETVEEG-------RLAQVMSEAVELLE 1213
Cdd:pfam00580 95 nrigllpnfsildeLDQLallkellekdrlnldpkllrklelkeliskaKNRLLSPEELqqgaadpRDKLAAEFYQEYQE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1214 GKRQ----------------VEGEDDLREQLMRGYRYILVDEYQDIDDLQYRLVSALAGRKAEeegrlcILAVGDDDQNI 1277
Cdd:pfam00580 175 RLKEnnaldfddlllltlelLRSDPELLEAYRERFKYILVDEFQDTNPIQYRLLKLLAGGHEN------LFLVGDPDQSI 248
|
250
....*....|....*...
gi 553768242 1278 YAWRDTNNRYIERFREDY 1295
Cdd:pfam00580 249 YGFRGADIENILKFEKDF 266
|
|
| DpdF |
NF041063 |
protein DpdF; |
288-640 |
8.29e-33 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 138.12 E-value: 8.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 288 LKRYFGFDDFRTE------------PDGRTLqhdvvlagmqgkhvLAILATGGGKSLCYQLPALnRFHRNGSLTVIISPL 355
Cdd:NF041063 131 LAEALGFTHYRSPgqreavraallaPPGSTL--------------IVNLPTGSGKSLVAQAPAL-LASRQGGLTLVVVPT 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 356 QSLMKDQ----VDGLLARNVQCAATLN--GLLTMPERAEVLEKIQLGDVGILLVSPEQFR---NKAFRRAIAQRQVGAWI 426
Cdd:NF041063 196 VALAIDQerraRELLRRAGPDLGGPLAwhGGLSAEERAAIRQRIRDGTQRILFTSPESLTgslRPALFDAAEAGLLRYLV 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 427 FDEAHCLSKWGADFRPDYlyvsrfikQftgdgELAAI-----------GCF-----TATAKPDVLEDIVLHFKDQlditf 490
Cdd:NF041063 276 VDEAHLVDQWGDGFRPEF--------Q-----LLAGLrrsllrlapsgRPFrtlllSATLTESTLDTLETLFGPP----- 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 491 ERFI---GTHERTNLHFEVLPCARAEKRhhTQALLE--DELGRNeggAVVFVSSRKGAEELADFLIGHGWA-CKYFHAGL 564
Cdd:NF041063 338 GPFIvvsAVQLRPEPAYWVAKCDSEEER--RERVLEalRHLPRP---LILYVTKVEDAEAWLQRLRAAGFRrVALFHGDT 412
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553768242 565 EPHEKKDIQDAFKSGELKIIVATNAFGMGVDKSDIRLVVHADIPGSLENYLQEAGRAGRDqGEA-RCVLLYDAQDIE 640
Cdd:NF041063 413 PDAERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRD-GKAsLSLLIYTPDDLD 488
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
286-483 |
3.00e-32 |
|
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations in RecQ2 cause Bloom syndrome.
Pssm-ID: 350774 [Multi-domain] Cd Length: 208 Bit Score: 125.32 E-value: 3.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 286 HELKRYFGFDDFRTEpdgrtlQHDVVLAGMQGKHVLAILATGGGKSLCYQLPALnrfhRNGSLTVIISPLQSLMKDQVDG 365
Cdd:cd18016 7 KIFHKKFGLHQFRTN------QLEAINAALLGEDCFVLMPTGGGKSLCYQLPAC----VSPGVTVVISPLRSLIVDQVQK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 366 LLARNVqCAATLNGLLTMPERAEVLEKIQLGD--VGILLVSPEQFR-----NKAFRRAIAQRQVGAWIFDEAHCLSKWGA 438
Cdd:cd18016 77 LTSLDI-PATYLTGDKTDAEATKIYLQLSKKDpiIKLLYVTPEKISasnrlISTLENLYERKLLARFVIDEAHCVSQWGH 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 553768242 439 DFRPDYLYVSRFIKQFTGDGELAaigcFTATAKPDVLEDIVLHFK 483
Cdd:cd18016 156 DFRPDYKRLNMLRQKFPSVPMMA----LTATATPRVQKDILNQLK 196
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
288-479 |
9.66e-32 |
|
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ATP-dependent helicase or WRN) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Werner's syndrome.
Pssm-ID: 350775 [Multi-domain] Cd Length: 193 Bit Score: 123.35 E-value: 9.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 288 LKRYFGFDDFRTepdgrtLQHDVVLAGMQ-GKHVLAILATGGGKSLCYQLPALNRfhrnGSLTVIISPLQSLMKDQVDGL 366
Cdd:cd18017 4 LNEYFGHSSFRP------VQWKVIRSVLEeRRDNLVVMATGYGKSLCYQYPSVLL----NSLTLVISPLISLMEDQVLQL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 367 LARNVQCAatlngLLTMPERAEVLEKIQLGDVGILLVSPEQ-FRNKAFRRAIAqRQVGAWIFDEAHCLSKWGADFRPDYL 445
Cdd:cd18017 74 VMSNIPAC-----FLGSAQSQNVLDDIKMGKIRVIYVTPEFvSKGLELLQQLR-NGITLIAIDEAHCVSQWGHDFRSSYR 147
|
170 180 190
....*....|....*....|....*....|....
gi 553768242 446 YVSRfIKQFTGDGELAAIgcfTATAKPDVLEDIV 479
Cdd:cd18017 148 HLGS-IRNRLPNVPIVAL---TATATPSVRDDII 177
|
|
| PRK10919 |
PRK10919 |
ATP-dependent DNA helicase Rep; Provisional |
1114-1324 |
1.71e-27 |
|
ATP-dependent DNA helicase Rep; Provisional
Pssm-ID: 182838 [Multi-domain] Cd Length: 672 Bit Score: 120.72 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1114 LVLAGPGSGKTRVIVHRIAYLLRVRRVPARCIVALTFNRHAANEIKQRLLRLVG-PDAFGVNVMTYHRMAMR-------- 1184
Cdd:PRK10919 19 LVLAGAGSGKTRVITNKIAHLIRGCGYQARHIAAVTFTNKAAREMKERVAQTLGrKEARGLMISTFHTLGLDiikreyaa 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1185 ---------------------LTGTRFERGETVEEGRLAQVM---------SEAVELLEGKRQ----------------- 1217
Cdd:PRK10919 99 lgmksnfslfddtdqlallkeLTEGLIEDDKVLLQQLISTISnwkndlktpAQAAAGAKGERDrifahcyglydahlkac 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1218 -VEGEDDL--------------REQLMRGYRYILVDEYQDIDDLQYRLVSALAGRKAeeegRLCIlaVGDDDQNIYAWRD 1282
Cdd:PRK10919 179 nVLDFDDLillptlllqrneevRERWQNKIRYLLVDEYQDTNTSQYELVKLLVGSRA----RFTV--VGDDDQSIYSWRG 252
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 553768242 1283 TNNRYIERFREDYSA-STSYLVDNYRSSACIIEAANSVIGRNP 1324
Cdd:PRK10919 253 ARPQNLVLLSQDFPAlQVIKLEQNYRSSGRILKAANILIANNP 295
|
|
| RecB |
COG1074 |
3#-5# helicase subunit RecB of the DNA repair enzyme RecBCD (exonuclease V) [Replication, ... |
1099-1566 |
5.09e-26 |
|
3#-5# helicase subunit RecB of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440692 [Multi-domain] Cd Length: 866 Bit Score: 116.60 E-value: 5.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1099 AAQRVIVSDDDDVNRLVLAGPGSGKTRVIVHRIAYLLRVRRVPARCIVALTFNRHAANEIKQRLLR-----LVGPDAF-- 1171
Cdd:COG1074 7 TDAQRRALDPLGGSVLVEASAGSGKTYTLVARYLRLLLERGLDPEEILVVTFTRAAAAEMRERIRErlaeaADLEDPDle 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1172 -----------------GVNVMTYHRMAMRL-------TGTRFE-----------RGETVEE------------------ 1198
Cdd:COG1074 87 elararrrlaralenldRAAISTIHSFCQRLlrefafeAGLDPNfellddaeallLEEAVDDllreayapldalalarll 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1199 ------------------------------------------------------------------GRLAQVMSEAVELL 1212
Cdd:COG1074 167 dafgrdddsleelllalyklrsrpdwleelaeldealealreallkakealaalrealaaaaapllAALLRLLAAVLARY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1213 EGKRQVEGE-------------------DDLREQLMRGYRYILVDEYQDIDDLQYRLVSALAGRKAEEEGRLCIlaVGDD 1273
Cdd:COG1074 247 ERRKRERGLldfddllhralrllrdedaPWVAERLRERYRHILVDEFQDTSPLQWEILRRLAGEALADGRTLFL--VGDP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1274 DQNIYAWRDTN----NRYIERFREDYSASTSYLVDNYRSSACIIEAANSVIGRNPDRlkQDHPIQIDTARRERPkgGDWE 1349
Cdd:COG1074 325 KQSIYRFRGADpelfLEARRALEGRVDGERLTLTTNFRSTPEVVDAVNALFAQLMGA--GFGEIPYEPVEALRP--GAYP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1350 SLDperagWVLRLRVDAEDDTRANVQAQAAMAELQRLLT-----------LDPEDwqgCAVLARTHQYLLPVQAWCEAHG 1418
Cdd:COG1074 401 AVE-----LWPLEPDDVSEEDAREREARAVAARIRRLLAegttvegggrpVRPGD---IAVLVRTRSEAAAIARALKAAG 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1419 V-----------------------QYCLAADKDSAL------P-----------LTAQRGFVRAVEGLRAITEPVTAAEA 1458
Cdd:COG1074 473 IpvaasdrlslfespevrdllallRALLNPEDDLALaavlrsPlfglsdedlaaLAADRKGESLWEALRAYERLARALER 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1459 WVPLSETAL---VPDWYGFFMTAFE----QLTAEFGQCPLAAHTLIDWLYDYARELRQQPKQGLY--------------- 1516
Cdd:COG1074 553 LRALRELARrlgLAELLERLLEETGllerLLALPGGERRLANLLHLDELLQLALEYEQTGGPGLAgflrwlerliedggd 632
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553768242 1517 --------------LGTVHSAKGLEFRHVVVLDGGWSSQPDTLSDERRLYYVGMTRAEQTLTLC 1566
Cdd:COG1074 633 eekrrlesdadavrIMTIHKSKGLEFPVVFLPALRERARAEELAEELRLLYVALTRARDRLVLS 696
|
|
| AAA_19 |
pfam13245 |
AAA domain; |
1114-1281 |
2.31e-23 |
|
AAA domain;
Pssm-ID: 433059 [Multi-domain] Cd Length: 136 Bit Score: 97.29 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1114 LVLAGPGSGKTRVIVHRIAYLLRVRRVPARcIVALTFNRHAANEIKQRLlrlvgpdafGVNVMTYHRMamrltgtrferg 1193
Cdd:pfam13245 15 LLTGGPGTGKTTTIRHIVALLVALGGVSFP-ILLAAPTGRAAKRLSERT---------GLPASTIHRL------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1194 etVEEGRLaqvmsEAVELLEGkrqveGEDDLREQLmrgyryILVDEYQDID-DLQYRLVSALAGRKaeeegrlCILAVGD 1272
Cdd:pfam13245 73 --LGFDDL-----EAGGFLRD-----EEEPLDGDL------LIVDEFSMVDlPLAYRLLKALPDGA-------QLLLVGD 127
|
....*....
gi 553768242 1273 DDQNIYAWR 1281
Cdd:pfam13245 128 PDQLPSVGP 136
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
315-633 |
1.15e-22 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 105.69 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 315 MQGKHVLAILATGGGKSLCYQLPALNRFHRNGSLTVI-ISPLQSLMKDQVDGLLARNVQC-----AATLNGLLTMPERAE 388
Cdd:COG1205 69 RAGKNVVIATPTASGKSLAYLLPVLEALLEDPGATALyLYPTKALARDQLRRLRELAEALglgvrVATYDGDTPPEERRW 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 389 VLEKiqlGDV----------GILLVSPeQFRnKAFRRAiaqRQVgawIFDEAHCLS-------------------KWGAD 439
Cdd:COG1205 149 IREH---PDIvltnpdmlhyGLLPHHT-RWA-RFFRNL---RYV---VIDEAHTYRgvfgshvanvlrrlrricrHYGSD 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 440 FrpdylyvsrfikQFtgdgelaaIGCfTAT-AKPDVLedivlhfkdqlditFERFIG------------THERTNLHFE- 505
Cdd:COG1205 218 P------------QF--------ILA-SATiGNPAEH--------------AERLTGrpvtvvdedgspRGERTFVLWNp 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 506 --VLPCARAEKRHHTQALLEDeLGRNEGGAVVFVSSRKGAEELADFLIGHGWACKY------FHAGLEPHEKKDIQDAFK 577
Cdd:COG1205 263 plVDDGIRRSALAEAARLLAD-LVREGLRTLVFTRSRRGAELLARYARRALREPDLadrvaaYRAGYLPEERREIERGLR 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 553768242 578 SGELKIIVATNAFGMGVDKSDIRLVVHADIPGSLENYLQEAGRAGRDQGEARCVLL 633
Cdd:COG1205 342 SGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLV 397
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
544-624 |
4.51e-22 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 91.89 E-value: 4.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 544 EELADFLIGHGWACKYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVDKSDIRLVVHADIPGSLENYLQEAGRAGR 623
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
.
gi 553768242 624 D 624
Cdd:smart00490 81 A 81
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
307-478 |
1.11e-21 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 93.46 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 307 QHDVVLAGMQGKHVLAILATGGGKSLCYQLPALNRFHR--NGSLTVIISPLQSLMKDQVDGLLARNVQCAATLNGLLTMP 384
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKldNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLLGGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 385 ERAEVLEKIQLGDvgILLVSPEQFR-NKAFRRAIaqRQVGAWIFDEAHCLSKWGadFRPDYLYVSRFIKQFTGdgelaaI 463
Cdd:pfam00270 84 SRKEQLEKLKGPD--ILVGTPGRLLdLLQERKLL--KNLKLLVLDEAHRLLDMG--FGPDLEEILRRLPKKRQ------I 151
|
170
....*....|....*
gi 553768242 464 GCFTATAkPDVLEDI 478
Cdd:pfam00270 152 LLLSATL-PRNLEDL 165
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
520-623 |
2.02e-21 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 90.73 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 520 ALLEDELGRNEGG-AVVFVSSRKGAEelADFLIG-HGWACKYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVDKS 597
Cdd:pfam00271 4 EALLELLKKERGGkVLIFSQTKKTLE--AELLLEkEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLP 81
|
90 100
....*....|....*....|....*.
gi 553768242 598 DIRLVVHADIPGSLENYLQEAGRAGR 623
Cdd:pfam00271 82 DVDLVINYDLPWNPASYIQRIGRAGR 107
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
513-623 |
1.02e-20 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, 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: 350174 [Multi-domain] Cd Length: 131 Bit Score: 89.49 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 513 EKRHHTQALLEDELGRNEGG-AVVFVSSRKGAEELADFLIGHGWACKYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFG 591
Cdd:cd18787 9 EEEEKKLLLLLLLLEKLKPGkAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAA 88
|
90 100 110
....*....|....*....|....*....|..
gi 553768242 592 MGVDKSDIRLVVHADIPGSLENYLQEAGRAGR 623
Cdd:cd18787 89 RGLDIPGVDHVINYDLPRDAEDYVHRIGRTGR 120
|
|
| SF1_C_UvrD |
cd18807 |
C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase ... |
1308-1566 |
2.65e-18 |
|
C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. This family also includes ATP-dependent helicase/nuclease AddA and helicase/nuclease RecBCD subunit RecB, among others. UvrD 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: 350194 [Multi-domain] Cd Length: 150 Bit Score: 83.43 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1308 SSACIIEAANSVIGRNPDRLKqdHPIQIDTARRERPKGgdWESLDPERagwvlrlrvdaeddtranvQAQAAMAELQRLL 1387
Cdd:cd18807 1 STKNILDAANSLIKQNKNRPK--KPLKAGNKSGGPVEL--LLAKDEAD-------------------EAKAIADEIKRLI 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1388 TLDPEDWQGCAVLARTHQYLLPVQAWCEahgvqyclaadkdsalpltaqrgfvraveglraitepvtaaeawvplsetal 1467
Cdd:cd18807 58 ESGPVQYSDIAILVRTNRQARVIEEALR---------------------------------------------------- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1468 vpdwygffmtafeqltaefgqcplaahtlidwlydyarelrqqpkqgLYLGTVHSAKGLEFRHVVVLDGGWSSQP----- 1542
Cdd:cd18807 86 -----------------------------------------------VTLMTIHASKGLEFPVVFIVGLGEGFIPsdasy 118
|
250 260 270
....*....|....*....|....*....|.
gi 553768242 1543 -------DTLSDERRLYYVGMTRAEQTLTLC 1566
Cdd:cd18807 119 haakedeERLEEERRLLYVALTRAKKELYLV 149
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
535-633 |
5.59e-18 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350184 [Multi-domain] Cd Length: 146 Bit Score: 82.30 E-value: 5.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 535 VFVSSRKGAEELADFL---IGHGWACKY----FHAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVDKSDIRLVVHADI 607
Cdd:cd18797 40 VFCRSRKLAELLLRYLkarLVEEGPLASkvasYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAGY 119
|
90 100
....*....|....*....|....*.
gi 553768242 608 PGSLENYLQEAGRAGRDQGEARCVLL 633
Cdd:cd18797 120 PGSLASLWQQAGRAGRRGKDSLVILV 145
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
520-628 |
6.50e-18 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350182 [Multi-domain] Cd Length: 154 Bit Score: 82.22 E-value: 6.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 520 ALLEDELGRNEGGAVVFVSSRKGAEELADFLIGhgwaCKYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVD---- 595
Cdd:cd18795 33 VLLKIETVSEGKPVLVFCSSRKECEKTAKDLAG----IAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpar 108
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 553768242 596 ----KSDIRLVV--HADIPGSleNYLQEAGRAGR----DQGEA 628
Cdd:cd18795 109 tviiKGTQRYDGkgYRELSPL--EYLQMIGRAGRpgfdTRGEA 149
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
315-671 |
1.03e-17 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 87.90 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 315 MQGKHVLAILATGGGKSLCYQLPALNRFHRNGSLTV---IISP-----------LQSL----------------MKDQVD 364
Cdd:COG0513 37 LAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPqalILAPtrelalqvaeeLRKLakylglrvatvyggvsIGRQIR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 365 gLLARNVQCA-ATlnglltmPERaeVLE-----KIQLGDVGILlvspeqfrnkafrraiaqrqvgawIFDEAhclskwga 438
Cdd:COG0513 117 -ALKRGVDIVvAT-------PGR--LLDliergALDLSGVETL------------------------VLDEA-------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 439 D------FRPDylyVSRFIKQFTGDGELAaigCFTATAKPDVLEDIVLHFKDQLDITFERFIGTHERTNLHFevLPCARA 512
Cdd:COG0513 155 DrmldmgFIED---IERILKLLPKERQTL---LFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRY--YLVDKR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 513 EKRHHTQALLEDElgrNEGGAVVFVSSRKGAEELADFLIGHGWACKYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFGM 592
Cdd:COG0513 227 DKLELLRRLLRDE---DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAAR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 593 GVDKSDIRLVVHADIPGSLENYLQEAG---RAGRDqGEArcVLLYDAQDienqfgmcegskltLRDIQQILRKLRKESER 669
Cdd:COG0513 304 GIDIDDVSHVINYDLPEDPEDYVHRIGrtgRAGAE-GTA--ISLVTPDE--------------RRLLRAIEKLIGQKIEE 366
|
..
gi 553768242 670 RK 671
Cdd:COG0513 367 EE 368
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
318-492 |
4.40e-17 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 81.38 E-value: 4.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 318 KHVLAILATGGGKSLCYQLPALNRFHRNGSL-TVIISPLQSLMKDQVDGLLARNVQCAATLNGLLTMPERAEVLEKIQLG 396
Cdd:smart00487 25 RDVILAAPTGSGKTLAALLPALEALKRGKGGrVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 397 DVGILLVSPEQFRNKAFRRAIAQRQVGAWIFDEAHCLSKWGadFRPDYLYVSRFIKQFtgdgelAAIGCFTATAKPDVLE 476
Cdd:smart00487 105 KTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKLLKLLPKN------VQLLLLSATPPEEIEN 176
|
170
....*....|....*.
gi 553768242 477 DIVLHFKDQLDITFER 492
Cdd:smart00487 177 LLELFLNDPVFIDVGF 192
|
|
| COG3972 |
COG3972 |
Superfamily I DNA and RNA helicases [Replication, recombination and repair]; |
1021-1559 |
2.46e-16 |
|
Superfamily I DNA and RNA helicases [Replication, recombination and repair];
Pssm-ID: 443172 [Multi-domain] Cd Length: 565 Bit Score: 84.50 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1021 DDYQRLDEHYREKRIQVHVMReYAEVALGSMREARDLVKHYFTLAKQEFIRRY----FAGREEVLKLATSEESWRSIVEK 1096
Cdd:COG3972 81 QVVLDGVRALFEVLLQVDRES-VRNLTEDHLRSLRLLAASRRDFLFALLLPEIppapFVQALRLLNLVSLEDFFLPLIAV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1097 LSAAQRVIVSDDDDVNRLVLAGPGSGKTRVIVHRIAYLLRvrRVPARCIVALTFNRHAANEIKQRLLR-----LVGPDAF 1171
Cdd:COG3972 160 LDLQQERIARSIPDGPQRIRGVAGSGKTVLLAAKAAYLAL--KHPGWRILVTCFNRSLADHLRDLIPRflrrfSNGEPED 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1172 GVNVMTYHRMAMRL---TGTRFERGETVEEGrlaqvMSEAVELLEgkRQVEGEDDLREqlmrgYRYILVDEYQDIDDLQY 1248
Cdd:COG3972 238 NVKLIVFHAWGGKLlkqYGIPPLTFSQPNEA-----FDEACKALL--EAIQGEIIPPI-----YDAILIDEAQDFEPEFL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1249 RLVSALAgrkAEEEGRLCILavGDDDQNIYAWRDTNNRYIERFREDysasTSYLVDNYRSSACIIEAANSvIGRNPDRLK 1328
Cdd:COG3972 306 RLLYQLL---KPPKKRLIWA--YDEAQNIYGRKIPSAGGIPAGIGR----DTILKKNYRNTRPILTFAHA-FGMGLLRPP 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1329 QdhPIQIDTARRERPKGGDWESL--DPERAGW---VLRLRvdaEDDTRANvQAQAAMAELQRLLT---LDPEDwqgCAVL 1400
Cdd:COG3972 376 G--LLQGDAEDYEVERPGDKVTLirPPEPAGRkgpLPEFK---KYDDRAE-ELEAIAEEIKKNLRdegLRPSD---IAVI 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1401 ArthqyllpvqawceahgvqyclaadkdsALPLTAQRGFVRAVEGLRAITEPVTAAeaWVPLSETalvpdwygFFMTafe 1480
Cdd:COG3972 447 Y----------------------------LGNNEAKELGDRLAAALERQGIDSYIA--GARSDPN--------FFWK--- 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 553768242 1481 qltaefgqcplaahtlidwlydyarelrqqpKQGLYLGTVHSAKGLEFRHVVVLDGGWSSQPDTLSDERRLYYVGMTRA 1559
Cdd:COG3972 486 -------------------------------DGGVTISTIHRAKGLEAPVVIIVGLDQLAKGESLERLRNLLYVAMTRA 533
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
306-623 |
1.56e-14 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 78.68 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 306 LQHDVVLAGMQGKHVLAILATGGGKSLCYQLPALNR---FHRNGS------LTVIISPLQSL---MKDQVDgLLARNVQC 373
Cdd:PLN00206 147 IQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRcctIRSGHPseqrnpLAMVLTPTRELcvqVEDQAK-VLGKGLPF 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 374 -AATLNGLLTMPERaevLEKIQLGdVGILLVSPEQFRNKAFRRAIAQRQVGAWIFDEAHCLSKWGadFRPDYLYVSRFIK 452
Cdd:PLN00206 226 kTALVVGGDAMPQQ---LYRIQQG-VELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERG--FRDQVMQIFQALS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 453 QftgdgelAAIGCFTATAKPDVLEDIVLHFKDQLDITferfIGTHERTNLHFEVLpCARAEKRHHTQALLEDELGRN--E 530
Cdd:PLN00206 300 Q-------PQVLLFSATVSPEVEKFASSLAKDIILIS----IGNPNRPNKAVKQL-AIWVETKQKKQKLFDILKSKQhfK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 531 GGAVVFVSSRKGAEELADFL-IGHGWACKYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVDKSDIRLVVHADIPG 609
Cdd:PLN00206 368 PPAVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPN 447
|
330
....*....|....
gi 553768242 610 SLENYLQEAGRAGR 623
Cdd:PLN00206 448 TIKEYIHQIGRASR 461
|
|
| helD |
PRK11054 |
DNA helicase IV; Provisional |
1101-1330 |
3.06e-14 |
|
DNA helicase IV; Provisional
Pssm-ID: 182930 [Multi-domain] Cd Length: 684 Bit Score: 78.07 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1101 QRVIVSDDDDVnrLVLAGPGSGKTRVIVHRIAYLLRVRRVPARCIVALTFNRHAANEIKQRLLRLVGPDafGVNVMTYHR 1180
Cdd:PRK11054 202 ARAVVNGEDSL--LVLAGAGSGKTSVLVARAGWLLARGQAQPEQILLLAFGRQAAEEMDERIRERLGTE--DITARTFHA 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1181 MAMRL-----------------------------------TGTRFER---------------GETVEEGRLAQVMSEAVE 1210
Cdd:PRK11054 278 LALHIiqqgskkvpvisklendskarhalliaewrkqcseKKAQAKGwrqwlteelqwdvpeGNFWDDEKLQRRLASRLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1211 LLEG---------KRQVEGEDD-----------------------LREQ---------------LMRG-----YRYILVD 1238
Cdd:PRK11054 358 RWVSlmrmhggsqAEMIAQAPEevrdlfqkrlklmapllkawkkaLKAEnavdfsglihqavnyLEKGrfispWKHILVD 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1239 EYQDIDDLQYRLVSALagrkAEEEGRLCILAVGDDDQNIYAWRDTNNRYIERFREDYSASTSYLVD-NYRSSACIIEAAN 1317
Cdd:PRK11054 438 EFQDISPQRAALLAAL----RKQNSQTTLFAVGDDWQAIYRFSGADLSLTTAFHERFGEGDRCHLDtTYRFNSRIGEVAN 513
|
330
....*....|...
gi 553768242 1318 SVIGRNPDRLKQD 1330
Cdd:PRK11054 514 RFIQQNPHQLKKP 526
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
317-469 |
3.40e-14 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 71.67 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 317 GKHVLAILATGGGKSLCYQLPALNRFHRNGSLTVIISPLQSLMKDQ---VDGLLARNVQCAAtLNGLLTMPERaevlEKI 393
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKKGKKVLVLVPTKALALQTaerLRELFGPGIRVAV-LVGGSSAEER----EKN 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553768242 394 QLGDVGILLVSPEQFRNKAFR-RAIAQRQVGAWIFDEAHCLSKWGADFRPDYLYVSRFIKqftgdGELAAIGCfTAT 469
Cdd:cd00046 76 KLGDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGL-----KNAQVILL-SAT 146
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
317-761 |
3.76e-12 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 71.21 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 317 GKHVLAILATGGGKSLCyQLPALNRFHRNGSlTVIISPLQSLMKdqvdgllarnvQCAATLNGLLTMPERAEVLEKIqlg 396
Cdd:COG1061 100 GGRGLVVAPTGTGKTVL-ALALAAELLRGKR-VLVLVPRRELLE-----------QWAEELRRFLGDPLAGGGKKDS--- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 397 DVGILLVSPEQFRNKAFRRAIAQRqVGAWIFDEAHCLskwGAD-FRpdylyvsRFIKQFTGDGELAaigcFTATakPDvl 475
Cdd:COG1061 164 DAPITVATYQSLARRAHLDELGDR-FGLVIIDEAHHA---GAPsYR-------RILEAFPAAYRLG----LTAT--PF-- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 476 edivlhFKDQLDITFERFIG-THERT-----------NLHFEVLPCARAEKRHHTQAL---LEDELGRNEGGA------- 533
Cdd:COG1061 225 ------RSDGREILLFLFDGiVYEYSlkeaiedgylaPPEYYGIRVDLTDERAEYDALserLREALAADAERKdkilrel 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 534 ----------VVFVSSRKGAEELADFLIGHGWACKYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVDKSDIRLVV 603
Cdd:COG1061 299 lrehpddrktLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 604 HADIPGSLENYLQEAGRAGRDQGEARCVLLYD------------AQDIENQFGMCEGSKLTLRDIQQILRKLRKESERRK 671
Cdd:COG1061 379 LLRPTGSPREFIQRLGRGLRPAPGKEDALVYDfvgndvpvleelAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVK 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 672 GGKVVITAGEVLMDEQVETSFEAGERDAETKVVTAVAWLERGQFLRREENQTQIFPASLKLSKEEADKRLANAKLPARRL 751
Cdd:COG1061 459 GELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLEL 538
|
490
....*....|
gi 553768242 752 EEFKAILSFL 761
Cdd:COG1061 539 LELLAALLRL 548
|
|
| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
1114-1295 |
1.42e-11 |
|
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. Their helicase core is surrounded by C and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains or domains engaged in protein-protein interactions. SF1 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: 438706 [Multi-domain] Cd Length: 121 Bit Score: 63.27 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1114 LVLAGPGSGKTRVIVHRIAYLLRVRRVPARCIVALTFNRHAANEIkqrllrlvgpdafgvnvmtyhrmamrltgtrferg 1193
Cdd:cd17914 3 LIQGPPGTGKTRVLVKIVAALMQNKNGEPGRILLVTPTNKAAAQL----------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1194 etveegrlaqvmseavellegkrqvegeddlreqlmrgyRYILVDEYQDIDDLQYRLVSALAGRkaeeEGRLCIlaVGDD 1273
Cdd:cd17914 48 ---------------------------------------DNILVDEAAQILEPETSRLIDLALD----QGRVIL--VGDH 82
|
170 180
....*....|....*....|....*..
gi 553768242 1274 DQNIYAWR-----DTNNRYIERFREDY 1295
Cdd:cd17914 83 DQLGPVWRgavlaKICNEQSLFTRLVR 109
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
532-634 |
1.01e-10 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The 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: 350172 [Multi-domain] Cd Length: 77 Bit Score: 59.25 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 532 GAVVFVSSRKGAEELADflighgwackyfhaglephekkdiqdafksgELKIIVATNAFGMGVDKSDIRLVVHADIPGSL 611
Cdd:cd18785 5 KIIVFTNSIEHAEEIAS-------------------------------SLEILVATNVLGEGIDVPSLDTVIFFDPPSSA 53
|
90 100
....*....|....*....|....
gi 553768242 612 ENYLQEAGRAGRD-QGEARCVLLY 634
Cdd:cd18785 54 ASYIQRVGRAGRGgKDEGEVILFV 77
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
513-623 |
2.39e-10 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 65.18 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 513 EKRHHTQALLEdELGRNEGGAVVFVSSRKGAEELADFLIGHGWACKYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFGM 592
Cdd:PTZ00110 361 EKRGKLKMLLQ-RIMRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASR 439
|
90 100 110
....*....|....*....|....*....|.
gi 553768242 593 GVDKSDIRLVVHADIPGSLENYLQEAGRAGR 623
Cdd:PTZ00110 440 GLDVKDVKYVINFDFPNQIEDYVHRIGRTGR 470
|
|
| HelD |
COG3973 |
DNA helicase IV [Replication, recombination and repair]; |
1211-1566 |
2.83e-10 |
|
DNA helicase IV [Replication, recombination and repair];
Pssm-ID: 443173 [Multi-domain] Cd Length: 699 Bit Score: 65.27 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1211 LLEGKRQVEGEDDLREqlmrgYRYILVDEYQDIDDLQYRLVsalagrkaeeeGRLCILA----VGDDDQNIYAWRDTNN- 1285
Cdd:COG3973 454 LDELAELLGGPDRTWT-----YGHVVVDEAQDLSPMQWRVL-----------KRRFPSAsftiVGDLAQAIHPYRGAESw 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1286 -RYIERFREDYSASTSyLVDNYRSSACIIEAANSVIGRNPDRLKQDHPIqidtarrerpkggdwesldpERAGWVLRL-R 1363
Cdd:COG3973 518 eEVLEPLGGDRARLVE-LTKSYRSTAEIMEFANRVLRAAGPDLPPPESV--------------------RRHGEPPRVvR 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1364 VDAEDDtranvQAQAAMAELQRLLTldpEDWQGCAVLARTHQYLLPVQAWceahgvqycLAADKDSALPLTAQRGFvraV 1443
Cdd:COG3973 577 VPSEAE-----LAAAVVEAVRELLA---EGEGTIAVICKTAREAEALYAA---------LKAGLPVTLIDDESEEL---E 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1444 EGLRAItepvtaaeawvplsetalvpdwygffmtafeqltaefgqcplaahtlidwlydyarelrqqpkqglylgTVHSA 1523
Cdd:COG3973 637 AGVVVL---------------------------------------------------------------------PAYLA 647
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 553768242 1524 KGLEFRHVVVLDggwssqPDTLSDE----RRLYYVGMTRAEQTLTLC 1566
Cdd:COG3973 648 KGLEFDAVVVVD------PDEIVYEsprgRRLLYVALTRATHRLTVL 688
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
535-628 |
7.35e-10 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350183 [Multi-domain] Cd Length: 150 Bit Score: 59.20 E-value: 7.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 535 VFVSSRKGAEELADFL----IGHGWACKYF--HAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVDKSDIRLVVHADIP 608
Cdd:cd18796 43 VFTNTRSQAERLAQRLrelcPDRVPPDFIAlhHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSP 122
|
90 100
....*....|....*....|
gi 553768242 609 GSLENYLQEAGRAGRDQGEA 628
Cdd:cd18796 123 KSVARLLQRLGRSGHRPGAA 142
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
307-431 |
1.56e-09 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 59.14 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 307 QHDVVLAGMQGKHVLAILATGGGKSLCYQLPALNRF-HRNGSLTVIISPLQSLMKDQVDGLLARNVQC-----AATLNGL 380
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALlRDPGSRALYLYPTKALAQDQLRSLRELLEQLglgirVATYDGD 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 553768242 381 LTMPERaevlEKIQLGDVGILLVSPEQ-----FRNKAFRRaiaqRQVGAW---IFDEAH 431
Cdd:cd17923 85 TPREER----RAIIRNPPRILLTNPDMlhyalLPHHDRWA----RFLRNLryvVLDEAH 135
|
|
| UvrD_C_2 |
pfam13538 |
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety ... |
1515-1566 |
1.75e-09 |
|
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: 54.89 E-value: 1.75e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 553768242 1515 LYLGTVHSAKGLEFRHVVVLDGGWsSQPDTLSDERRLYYVGMTRAEQTLTLC 1566
Cdd:pfam13538 2 AYALTVHKAQGSEFPAVFLVDPDL-TAHYHSMLRRRLLYTAVTRARKKLVLV 52
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
518-721 |
2.74e-08 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 58.37 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 518 TQALLEDELgRNEGGAVVFVSSRKGAEELADFL---------------------------------------IGHGWAck 558
Cdd:COG1204 228 TLALALDLL-EEGGQVLVFVSSRRDAESLAKKLadelkrrltpeereeleelaeellevseethtnekladcLEKGVA-- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 559 YFHAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVDK-------SDIRLVVHADIPgSLEnYLQEAGRAGR----DQGE 627
Cdd:COG1204 305 FHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLparrviiRDTKRGGMVPIP-VLE-FKQMAGRAGRpgydPYGE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 628 ARCVL--LYDAQDIENQFgmcegsklTLRDIQQILRKLRKESERRKggKVV--ITAGEVLMDEQVETSFE-------AGE 696
Cdd:COG1204 383 AILVAksSDEADELFERY--------ILGEPEPIRSKLANESALRT--HLLalIASGFANSREELLDFLEntfyayqYDK 452
|
250 260
....*....|....*....|....*
gi 553768242 697 RDAETKVVTAVAWLERGQFLRREEN 721
Cdd:COG1204 453 GDLEEVVDDALEFLLENGFIEEDGD 477
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
522-595 |
7.59e-08 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 57.59 E-value: 7.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 522 LEDELGRNE----------GGAVVFVSSRKGAEELADFLighGWACKYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFG 591
Cdd:COG1202 409 IINKLVKREfdtksskgyrGQTIIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALA 485
|
....
gi 553768242 592 MGVD 595
Cdd:COG1202 486 AGVD 489
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
533-623 |
1.03e-07 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 56.37 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 533 AVVFVSSRKGAEELADFLIGHGWACKYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVDKSDIRLVVHADIPGSLE 612
Cdd:PTZ00424 270 AIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPE 349
|
90
....*....|.
gi 553768242 613 NYLQEAGRAGR 623
Cdd:PTZ00424 350 NYIHRIGRSGR 360
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
547-633 |
1.48e-07 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350189 [Multi-domain] Cd Length: 142 Bit Score: 52.21 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 547 ADFLIGHGWACKYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVDKSDIRLVVHADIPGSLENYLQEAGRAGRDQg 626
Cdd:cd18802 57 CGFLIGRGNSSQRKRSLMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN- 135
|
....*..
gi 553768242 627 eARCVLL 633
Cdd:cd18802 136 -SKYILM 141
|
|
| EXOIII |
smart00479 |
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ... |
10-137 |
2.10e-07 |
|
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other exonucleases;
Pssm-ID: 214685 [Multi-domain] Cd Length: 169 Bit Score: 52.69 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 10 LIFDLEvAPGNADQPDRIFMVGALRPDTGEELE---------RKVD-----------------KDLPSVLDALDSLGQGA 63
Cdd:smart00479 3 VVIDCE-TTGLDPGKDEIIEIAAVDVDGGEIIEvfdtyvkpdRPITdyateihgitpemlddaPTFEEVLEELLEFLRGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 64 SFVlGHNVIDHDLPILKQQAPDL---ALHGLPVIDTLRLSPLAFPQNPYHRL---VKDYKLIRDSLN-SPLTDCRSTLTL 136
Cdd:smart00479 82 ILV-AGNSAHFDLRFLKLEHPRLgikQPPKLPVIDTLKLARATNPGLPKYSLkklAKRLLLEVIQRAhRALDDARATAKL 160
|
.
gi 553768242 137 F 137
Cdd:smart00479 161 F 161
|
|
| PRK13909 |
PRK13909 |
RecB-like helicase; |
1232-1605 |
2.10e-07 |
|
RecB-like helicase;
Pssm-ID: 237554 [Multi-domain] Cd Length: 910 Bit Score: 56.13 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1232 YRYILVDEYQDIDDLQYRLVSALAGRKAEEEGRLCI---LAVGDDDQNIYAWRDTNNRYIERFREDYSASTSYLVDNYRS 1308
Cdd:PRK13909 329 ISHILIDEFQDTSVLQYKILLPLIDEIKSGEGQKKFrsfFYVGDVKQSIYRFRGGKKELFDKVSKDFKQKVDNLDTNYRS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1309 SACIIEAANSVIGRNPDRLKQDHPIQIDTarrerpkggdwesldperAGWVLRLRVDAEDDTRanvqAQAAMAELQRLLT 1388
Cdd:PRK13909 409 APLIVDFVNEVFKKKYKNYKTQYAEQHKS------------------GGYVEVVEVADESEEL----LEQLLQEIQFLLE 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1389 L--DPEDwqgCAVLARTHQYLLPVQAWCEAhgvQYCLAADKDSALPLTAQRgFVRAV-EGLRA---------------IT 1450
Cdd:PRK13909 467 KgiDPDD---IAILCWTNDDALEIKEFLQE---QFGIKAVTESSAKLINQP-EVKALiEALKYclfgeeiykhnvlklLG 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1451 EPVTAAEAWVPLSETALVPDWYgffmtafeqLTAEFGQCPLAAHTLI----------DWLYDYAR---ELRQQPKQGLYL 1517
Cdd:PRK13909 540 KEPDKIPSFLPKEESVAEFVKK---------LIEELKLYDENLLKFLelasgyedieEFLFKLEPcdkEIASEESKGVQI 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1518 GTVHSAKGLEFRHVVVLD--GGWSSQPDTL--------------------------------------SDERRLYYVGMT 1557
Cdd:PRK13909 611 MTVHKSKGLEFEHVIVCDrlGKPNSDSSNLlfeydgielwqiyyrikgrenfdkdyaralekekalkyEEEINVLYVAFT 690
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 553768242 1558 RAEQTLTLCEFPGGNPFVR---NLTQEVIGKRFVGEPIPELEKRYLQLSLK 1605
Cdd:PRK13909 691 RAKNSLIVVKKDESSGSMFeilDLKPLERGEIEIKEPKISPKKESLITSVK 741
|
|
| UvrD_C |
pfam13361 |
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety ... |
1519-1565 |
3.80e-07 |
|
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: 433145 [Multi-domain] Cd Length: 377 Bit Score: 54.33 E-value: 3.80e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 553768242 1519 TVHSAKGLEFRHVVVL---DGGWSSQ-----PDTLSDERRLYYVGMTRAEQTLTL 1565
Cdd:pfam13361 318 TIHQAKGLEFDTVFLAgleEGIFPSYrsikdEGNLEEERRLFYVAITRAKKRLYI 372
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
529-623 |
5.00e-07 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 54.50 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 529 NEGG-AVVFVSSRKGAEELADFL---------------------------IGHGWAckYFHAGLEPHEKKDIQDAFKSGE 580
Cdd:PRK01172 234 NDGGqVLVFVSSRKNAEDYAEMLiqhfpefndfkvssennnvyddslnemLPHGVA--FHHAGLSNEQRRFIEEMFRNRY 311
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 553768242 581 LKIIVATNAFGMGVDKSdIRLVVHADIP--GSL-ENYL------QEAGRAGR 623
Cdd:PRK01172 312 IKVIVATPTLAAGVNLP-ARLVIVRDITryGNGgIRYLsnmeikQMIGRAGR 362
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
561-634 |
8.39e-07 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 54.16 E-value: 8.39e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553768242 561 HAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVDKSDIRLVVHADIPGSLENYLQEAGRAGRDQGEARCVLLY 634
Cdd:PRK09751 308 HGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGHQVGGVSKGLFF 381
|
|
| PolC |
COG2176 |
DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair]; ... |
11-137 |
9.24e-07 |
|
DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair];
Pssm-ID: 441779 [Multi-domain] Cd Length: 181 Bit Score: 50.91 E-value: 9.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 11 IFDLEVAPGNADQpDRIFMVGALRPDTGEELER-----KVDKDLPS---------------------VLDALDSLGQGAS 64
Cdd:COG2176 12 VFDLETTGLSPKK-DEIIEIGAVKVENGEIVDRfstlvNPGRPIPPfiteltgitdemvadappfeeVLPEFLEFLGDAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 65 FVlGHNViDHDLPILKQQapdLALHGL----PVIDTLRLSPLAFPQNPYHRLvkDYklIRDSLNSPLT-------DCRST 133
Cdd:COG2176 91 LV-AHNA-SFDLGFLNAA---LKRLGLpfdnPVLDTLELARRLLPELKSYKL--DT--LAERLGIPLEdrhralgDAEAT 161
|
....
gi 553768242 134 LTLF 137
Cdd:COG2176 162 AELF 165
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
521-702 |
1.24e-06 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 53.34 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 521 LLEDELGRNEGGAV-VFVSSRKGAEELADFLIGH--------GWACKYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFG 591
Cdd:PRK13766 355 IVKEQLGKNPDSRIiVFTQYRDTAEKIVDLLEKEgikavrfvGQASKDGDKGMSQKEQIEILDKFRAGEFNVLVSTSVAE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 592 MGVDKSDIRLVV-HADIPgSLENYLQEAGRAGRdQGEARCVLLY--DAQDiENQF--------GMcegsKLTLRDIQQIL 660
Cdd:PRK13766 435 EGLDIPSVDLVIfYEPVP-SEIRSIQRKGRTGR-QEEGRVVVLIakGTRD-EAYYwssrrkekKM----KEELKNLKGIL 507
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 553768242 661 RKLRKESERRKGGKVVITAGEVLMDEQVETSFEAGERDAETK 702
Cdd:PRK13766 508 NKKLQELDEEQKGEEEEKDEQLSLDDFVKSKGKEEEEEEEKE 549
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
466-628 |
1.85e-06 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 52.65 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 466 FTATAKPDVLEDIVLHFKD--QLDITFERFIGTHERTNLHFEvlpcARAEKrhhtQALLEDELGRNEGG-AVVFVSSRKG 542
Cdd:PRK04537 198 FSATLSHRVLELAYEHMNEpeKLVVETETITAARVRQRIYFP----ADEEK----QTLLLGLLSRSEGArTMVFVNTKAF 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 543 AEELADFLIGHGWACKYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVDKSDIRLVVHADIPGSLENYLQEAGRAG 622
Cdd:PRK04537 270 VERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTA 349
|
....*...
gi 553768242 623 R--DQGEA 628
Cdd:PRK04537 350 RlgEEGDA 357
|
|
| DEDDh |
cd06127 |
DEDDh 3'-5' exonuclease domain family; DEDDh exonucleases, part of the DnaQ-like (or DEDD) ... |
12-138 |
2.78e-06 |
|
DEDDh 3'-5' exonuclease domain family; DEDDh exonucleases, part of the DnaQ-like (or DEDD) exonuclease superfamily, catalyze the excision of nucleoside monophosphates at the DNA or RNA termini in the 3'-5' direction. These proteins contain four invariant acidic residues in three conserved sequence motifs termed ExoI, ExoII and ExoIII. DEDDh exonucleases are classified as such because of the presence of specific Hx(4)D conserved pattern at the ExoIII motif. The four conserved acidic residues are clustered around the active site and serve as ligands for the two metal ions required for catalysis. Most DEDDh exonucleases are the proofreading subunits (epsilon) or domains of bacterial DNA polymerase III, the main replicating enzyme in bacteria, which functions as the chromosomal replicase. Other members include other DNA and RNA exonucleases such as RNase T, Oligoribonuclease, and RNA exonuclease (REX), among others.
Pssm-ID: 176648 [Multi-domain] Cd Length: 159 Bit Score: 48.84 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 12 FDLEVAPGnADQPDRIFMVGALrpdTGEELERKVDKD--LPSVLDALdslgqGASFVLGHNViDHDLPILKQQAPDLALH 89
Cdd:cd06127 35 FETLVNPG-RPIPPEATAIHGI---TDEMLADAPPFEevLPEFLEFL-----GGRVLVAHNA-SFDLRFLNRELRRLGGP 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 553768242 90 GL--PVIDTLRLSPLAFPQNPYHRLvkdYKLIRDSLNSP-------LTDCRSTLTLFN 138
Cdd:cd06127 105 PLpnPWIDTLRLARRLLPGLRSHRL---GLLLAERYGIPlegahraLADALATAELLL 159
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
533-661 |
2.91e-06 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 52.16 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 533 AVVFVSSRKGAEELADFLIGHGWACKYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVDKSDIRLVVHADIPGSLE 612
Cdd:PRK11634 248 AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSE 327
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 553768242 613 NYLQEAGRAGRdQGEARCVLLYdaqdIENQfgmcegSKLTLRDIQQILR 661
Cdd:PRK11634 328 SYVHRIGRTGR-AGRAGRALLF----VENR------ERRLLRNIERTMK 365
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
317-438 |
3.11e-06 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from 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: 350680 [Multi-domain] Cd Length: 166 Bit Score: 49.12 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 317 GKHVLAILATGGGKSLCYQLPALNRFHRNG--SLTVI-ISPLQSLMKDQvdgllARNVQCAATLNGL----------LTM 383
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPekGVQVLyISPLKALINDQ-----ERRLEEPLDEIDLeipvavrhgdTSQ 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553768242 384 PERAEVLEKIQlgdvGILLVSPEQFR----NKAFRRAIAqrQVGAWIFDEAHCL--SKWGA 438
Cdd:cd17922 76 SEKAKQLKNPP----GILITTPESLElllvNKKLRELFA--GLRYVVVDEIHALlgSKRGV 130
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
528-634 |
7.41e-06 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350177 [Multi-domain] Cd Length: 171 Bit Score: 48.01 E-value: 7.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 528 RNEGgAVVFVSSRKGAEELADFLIGHGWACKYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVDKSDIRLV--VHA 605
Cdd:cd18790 26 RGER-VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVaiLDA 104
|
90 100 110
....*....|....*....|....*....|...
gi 553768242 606 DIPGSLENY---LQEAGRAGRD-QGEarcVLLY 634
Cdd:cd18790 105 DKEGFLRSEtslIQTIGRAARNvNGK---VILY 134
|
|
| SF1_C |
cd18786 |
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ... |
1509-1565 |
1.27e-05 |
|
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Similar to SF2 helicases, they do not form toroidal, predominantly hexameric structures like SF3-6. SF1 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The 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: 350173 [Multi-domain] Cd Length: 89 Bit Score: 45.12 E-value: 1.27e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 553768242 1509 QQPKQGLYLGTVHSAKGLEFRHVVVLDggwssqPDTLSDERRLYYVGMTRAEQTLTL 1565
Cdd:cd18786 37 EFDLQLVGAITIDSSQGLTFDVVTLYL------PTANSLTPRRLYVALTRARKRLVI 87
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
543-635 |
2.15e-05 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350198 [Multi-domain] Cd Length: 159 Bit Score: 46.57 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 543 AEELADFLIGHgWACKYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVD--KSDIRLVVHADIPGsLENYLQEAGR 620
Cdd:cd18811 51 YEYLKERFRPE-LNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDvpNATVMVIEDAERFG-LSQLHQLRGR 128
|
90
....*....|....*
gi 553768242 621 AGRDQGEARCVLLYD 635
Cdd:cd18811 129 VGRGDHQSYCLLVYK 143
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
532-623 |
3.36e-05 |
|
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350185 [Multi-domain] Cd Length: 174 Bit Score: 46.14 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 532 GAVVFVSSRKG---AEELADFLIGHGWACKYFHAGlephEKKDIQDaFKSGELKIIVATNAF-GMGVDKSD----IRLVV 603
Cdd:cd18798 26 GGLIFVSIDYGkeyAEELKEFLERHGIKAELALSS----TEKNLEK-FEEGEIDVLIGVASYyGVLVRGIDlperIKYAI 100
|
90 100
....*....|....*....|
gi 553768242 604 HADIPgsLENYLQEAGRAGR 623
Cdd:cd18798 101 FYGVP--VTTYIQASGRTSR 118
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
513-638 |
6.61e-05 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 47.64 E-value: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 513 EKRHHTQALLEDELgrNEGGA-VVFVSSRKGAE-----------------------ELADFL---------------IGH 553
Cdd:PRK02362 227 PSKDDTLNLVLDTL--EEGGQcLVFVSSRRNAEgfakraasalkktltaaeraelaELAEEIrevsdtetskdladcVAK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 554 GWAckYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVDKSDIRLVVH-----------ADIPgSLEnYLQEAGRAG 622
Cdd:PRK02362 305 GAA--FHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRdyrrydggagmQPIP-VLE-YHQMAGRAG 380
|
170 180
....*....|....*....|
gi 553768242 623 RDQ----GEArcVLLYDAQD 638
Cdd:PRK02362 381 RPGldpyGEA--VLLAKSYD 398
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
521-662 |
1.04e-04 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 46.73 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 521 LLEDELGRNEGGAV-VFVSSRKGAEELADFLIGHGWACKYFHAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVDKSDI 599
Cdd:PRK10590 235 LLSQMIGKGNWQQVlVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEEL 314
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553768242 600 RLVVHADIPGSLENYLQEAGRAGRDQ--GEARCVLLYDAQdienqfgmcegsKLtLRDIQQILRK 662
Cdd:PRK10590 315 PHVVNYELPNVPEDYVHRIGRTGRAAatGEALSLVCVDEH------------KL-LRDIEKLLKK 366
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
1519-1566 |
1.04e-04 |
|
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: 46.89 E-value: 1.04e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 553768242 1519 TVHSAKGLEFRHVVVLDGGWSSQPDTlsdeRRLYYVGMTRAEQTLTLC 1566
Cdd:COG0507 446 TVHKSQGSTFDRVILVLPSEHSPLLS----RELLYTALTRARELLTLV 489
|
|
| recB |
PRK10876 |
exonuclease V subunit beta; Provisional |
1217-1317 |
1.19e-04 |
|
exonuclease V subunit beta; Provisional
Pssm-ID: 236784 [Multi-domain] Cd Length: 1181 Bit Score: 47.27 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 1217 QVEGEDDLREQLMRGYRYILVDEYQDIDDLQYRLVSALAGRKAEEEgrlcILAVGDDDQNIYAWRDTN-NRYIeRFREDY 1295
Cdd:PRK10876 363 QSEGGEALAAAIRTRYPVAMIDEFQDTDPQQYRIFRRIYRHQPETA----LLLIGDPKQAIYAFRGADiFTYM-KARSEV 437
|
90 100
....*....|....*....|...
gi 553768242 1296 SAstSYLVD-NYRSSACIIEAAN 1317
Cdd:PRK10876 438 SA--HYTLDtNWRSAPGMVNSVN 458
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
522-633 |
1.39e-04 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350188 [Multi-domain] Cd Length: 143 Bit Score: 43.88 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 522 LEDELGRNEGGAVVFVSSRKGAEELADFL------------IGHgwACKYFHAGLEPHEKKDIQDAFKSGELKIIVATNA 589
Cdd:cd18801 22 FKKKQEGSDTRVIIFSEFRDSAEEIVNFLskirpgiratrfIGQ--ASGKSSKGMSQKEQKEVIEQFRKGGYNVLVATSI 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 553768242 590 FGMGVDKSDIRLVVHADIPGSLENYLQEAGRAGRDQGeARCVLL 633
Cdd:cd18801 100 GEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGRKRQ-GRVVVL 142
|
|
| SF1_C_RecD |
cd18809 |
C-terminal helicase domain of RecD family helicases; RecD is a member of the RecBCD (EC 3.1.11. ... |
1519-1565 |
5.94e-04 |
|
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: 40.24 E-value: 5.94e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 553768242 1519 TVHSAKGLEFRHVVVLdggWSSQPDTLSdeRRLYYVGMTRAEQTLTL 1565
Cdd:cd18809 37 TIHKSQGSEFDRVIVV---LPTSHPMLS--RGLLYTALTRARKLLTL 78
|
|
| DEAD-like_helicase_N |
cd17912 |
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ... |
1112-1158 |
9.45e-04 |
|
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase superfamily is a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. The N-terminal domain contains the ATP-binding region.
Pssm-ID: 350670 [Multi-domain] Cd Length: 81 Bit Score: 39.81 E-value: 9.45e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 553768242 1112 NRLVLAGPGSGKTRVIVHRIAYLLrvrrVPARCIVALTFNRHAANEI 1158
Cdd:cd17912 1 NILHLGPTGSGKTLVAIQKIASAM----SSGKSVLVVTPTKLLAHEI 43
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
326-472 |
1.10e-03 |
|
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350780 [Multi-domain] Cd Length: 189 Bit Score: 41.98 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 326 TGGGKSLCYQLPALNRFHRN-GSLTVIISPLQSLMKDQVDGLLARnvqcaatlnglLTMPERAEVLE--------KIQLG 396
Cdd:cd18022 26 TGSGKTIAAELAMFRAFNKYpGSKVVYIAPLKALVRERVDDWKKR-----------FEEKLGKKVVEltgdvtpdMKALA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 397 DVGILLVSPEQF----RNKAFRRAIaqRQVGAWIFDEAHCLskwGADFRPDY-LYVSR--FIKQFTGdGELAAIGCFTAT 469
Cdd:cd18022 95 DADIIITTPEKWdgisRSWQTREYV--QQVSLIIIDEIHLL---GSDRGPVLeVIVSRmnYISSQTE-KPVRLVGLSTAL 168
|
...
gi 553768242 470 AKP 472
Cdd:cd18022 169 ANA 171
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
504-623 |
1.15e-03 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 43.77 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 504 FEVLPCARAEKRHHtqALLEDELGRNEGGAVVFVSSRKGAEELA--------------------------DFLIGHGWAC 557
Cdd:COG4581 217 FRVNPELLRPPSRH--EVIEELDRGGLLPAIVFIFSRRGCDEAAqqllsarlttkeeraeireaidefaeDFSVLFGKTL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 558 KYF--------HAGLEPHEKKDIQDAFKSGELKIIVATNAFGMGVDKSdIRLVV-----------HADIPGSLenYLQEA 618
Cdd:COG4581 295 SRLlrrgiavhHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMP-ARTVVftklskfdgerHRPLTARE--FHQIA 371
|
....*
gi 553768242 619 GRAGR 623
Cdd:COG4581 372 GRAGR 376
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
532-628 |
1.35e-03 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 43.65 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 532 GAVVFVSSRKGAE-----------------------ELADFL------------IGHGWAckYFHAGLEPHEKKDIQDAF 576
Cdd:PRK00254 240 GALVFVNTRRSAEkealelakkikrfltkpelralkELADSLeenptneklkkaLRGGVA--FHHAGLGRTERVLIEDAF 317
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 553768242 577 KSGELKIIVATNAFGMGVDKSDIRLVVH----------ADIPgSLEnYLQEAGRAGRDQ----GEA 628
Cdd:PRK00254 318 REGLIKVITATPTLSAGINLPAFRVIIRdtkrysnfgwEDIP-VLE-IQQMMGRAGRPKydevGEA 381
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
307-434 |
1.48e-03 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 41.48 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 307 QHDVVLAGMQ-GKHVLAILATGGGKSLCYQLPALNRFHRNGSLTVIISPLQSLMkDQVDGLLARNVQCAATLNGLLTmpe 385
Cdd:cd17921 6 QREALRALYLsGDSVLVSAPTSSGKTLIAELAILRALATSGGKAVYIAPTRALV-NQKEADLRERFGPLGKNVGLLT--- 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 553768242 386 RAEVLEKIQLGDVGILLVSPEQFRNKAFRRAIAQ-RQVGAWIFDEAHCLS 434
Cdd:cd17921 82 GDPSVNKLLLAEADILVATPEKLDLLLRNGGERLiQDVRLVVVDEAHLIG 131
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
520-658 |
2.23e-03 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350179 [Multi-domain] Cd Length: 160 Bit Score: 40.71 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553768242 520 ALLEDELGRneGGAVVFVSSR---------KGAEELADFLIGH--GWACKYFHAGLEPHEKKDIQDAFKSGELKIIVATN 588
Cdd:cd18792 17 EAIERELAR--GGQVYYVYPRieesekldlKSIEALAEELKELvpEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTT 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 553768242 589 AFGMGVD--KSDIRLVVHADIPGsLENYLQEAGRAGRDQGEARCVLLYdaqdiENQFGMCEGSKLTLRDIQQ 658
Cdd:cd18792 95 VIEVGIDvpNANTMIIEDADRFG-LSQLHQLRGRVGRGKHQSYCYLLY-----PDPKKLTETAKKRLRAIAE 160
|
|
| |
