|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
39-516 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 784.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 39 DASEALAALHRVFGYEAFRGEQEAVIEHVVAGGDAVVLMPTGGGKSLCYQIPSLVRPGTGVVVSPLIALMQDQVDALRAL 118
Cdd:COG0514 1 LRDDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 119 GVRAGFMNSTQDFDERRMVEAEFLAGELDLLYLAPERLRLGGTLDLLSRGKISVFAIDEAHCVSQWGHDFRPDYLALSLL 198
Cdd:COG0514 81 GIRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 199 GERWPDVPRIALTATATHATHQEITERLNMPAARHFVASFDRPNIQYRIVPK--ADPKKQLLSFLReEHPGDAGIVYCLS 276
Cdd:COG0514 161 RERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKppDDKLAQLLDFLK-EHPGGSGIVYCLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 277 RNSVDKTAEFLSRNGVEAVPYHAGLDAGTRAAHQSRFLREDGLVVVATIAFGMGIDKPDVRFVAHLDLPKSVEGYYQETG 356
Cdd:COG0514 240 RKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 357 RAGRDGLPSTAWMAYGLNDVIQQRKLIQSGEGDEAFRRRAQAHLDSMLALCETAQCRRGQLLAYFGqDPDPSGCGNCDTC 436
Cdd:COG0514 320 RAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYFG-EELAEPCGNCDNC 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 437 LTPPETWDGTVAAQKALSTVVRLqrerGQKFGAVQIVDILLGKRTGKVIQFDHDQLSVFGIGEELTEGEWRGVIRQLLAQ 516
Cdd:COG0514 399 LGPPETFDGTEAAQKALSCVYRT----GQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLLAQ 474
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
47-649 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 residues long. This model represents bacterial proteins with a high degree of similarity in domain architecture and in primary sequence to E. coli RecQ. The model excludes eukaryotic and archaeal proteins with RecQ-like regions, as well as more distantly related bacterial helicases related to RecQ. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273594 [Multi-domain] Cd Length: 591 Bit Score: 753.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 47 LHRVFGYEAFRGEQEAVIEHVVAGGDAVVLMPTGGGKSLCYQIPSLVRPGTGVVVSPLIALMQDQVDALRALGVRAGFMN 126
Cdd:TIGR01389 5 LKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAAAYLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 127 STQDFDERRMVEAEFLAGELDLLYLAPERLRLGGTLDLLSRGKISVFAIDEAHCVSQWGHDFRPDYLALSLLGERWPDVP 206
Cdd:TIGR01389 85 STLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERFPQVP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 207 RIALTATATHATHQEITERLNMPAARHFVASFDRPNIQYRIVPKADPKKQLLSFLReEHPGDAGIVYCLSRNSVDKTAEF 286
Cdd:TIGR01389 165 RIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLK-KHRGQSGIIYASSRKKVEELAER 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 287 LSRNGVEAVPYHAGLDAGTRAAHQSRFLREDGLVVVATIAFGMGIDKPDVRFVAHLDLPKSVEGYYQETGRAGRDGLPST 366
Cdd:TIGR01389 244 LESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDGLPAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 367 AWMAYGLNDVIQQRKLIQSGEGDEAFRRRAQAHLDSMLALCETAQCRRGQLLAYFGQDpDPSGCGNCDTCLTPPETWDGT 446
Cdd:TIGR01389 324 AILLYSPADIALLKRRIEQSEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGEN-EVEPCGNCDNCLDPPKSYDAT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 447 VAAQKALSTVVRLqrerGQKFGAVQIVDILLGKRTGKVIQFDHDQLSVFGIGEELTEGEWRGVIRQLLAQGLLAVEGE-Y 525
Cdd:TIGR01389 403 VEAQKALSCVYRM----GQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEiY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 526 GTLVLTEASGAVLRRERDVPLRkePKKPVTSRSGtsstgsgrgeRKGKAVaAELPEELLpaFEALRAWRAEQAREQGVPA 605
Cdd:TIGR01389 479 IGLQLTEAARKVLKNEVEVLLR--PFKVVAKEKT----------RVQKNL-SVGVDNAL--FEALRELRKEQADEQNVPP 543
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 2542603572 606 YVIFHDATLREIATVWPTSVGELGGISGVGEKKLTTYGEGVLET 649
Cdd:TIGR01389 544 YVIFSDSTLREMAEKRPATLNALLKIKGVGQNKLDRYGEAFLEV 587
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
41-643 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 574.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 41 SEALAA--LHRVFGYEAFRGEQEAVIEHVVAGGDAVVLMPTGGGKSLCYQIPSLVRPGTGVVVSPLIALMQDQVDALRAL 118
Cdd:PRK11057 9 LESLAKqvLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLAN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 119 GVRAGFMNSTQDFDERRMVEAEFLAGELDLLYLAPERLRLGGTLDLLSRGKISVFAIDEAHCVSQWGHDFRPDYLALSLL 198
Cdd:PRK11057 89 GVAAACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 199 GERWPDVPRIALTATATHATHQEITERLNMPAARHFVASFDRPNIQYRIVPKADPKKQLLSFLREEHpGDAGIVYCLSRN 278
Cdd:PRK11057 169 RQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQLMRYVQEQR-GKSGIIYCNSRA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 279 SVDKTAEFLSRNGVEAVPYHAGLDAGTRAAHQSRFLREDGLVVVATIAFGMGIDKPDVRFVAHLDLPKSVEGYYQETGRA 358
Cdd:PRK11057 248 KVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 359 GRDGLPSTAWMAYGLNDVIQQRKLIQsgEGDEAFRRRAQAH-LDSMLALCETAQCRRGQLLAYFGQDPDPSgCGNCDTCL 437
Cdd:PRK11057 328 GRDGLPAEAMLFYDPADMAWLRRCLE--EKPAGQQQDIERHkLNAMGAFAEAQTCRRLVLLNYFGEGRQEP-CGNCDICL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 438 TPPETWDGTVAAQKALSTVVRLqrerGQKFGAVQIVDILLGKRTGKVIQFDHDQLSVFGIGEELTEGEWRGVIRQLLAQG 517
Cdd:PRK11057 405 DPPKQYDGLEDAQKALSCIYRV----NQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 518 LLAVE-GEYGTLVLTEASGAVLRRERDVPLrKEPKKPVTSRSGTSSTGSGRGERKgkavaaelpeellpAFEALRAWRAE 596
Cdd:PRK11057 481 LVTQNiAQHSALQLTEAARPVLRGEVSLQL-AVPRIVALKPRAMQKSFGGNYDRK--------------LFAKLRKLRKS 545
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 2542603572 597 QAREQGVPAYVIFHDATLREIATVWPTSVGELGGISGVGEKKLTTYG 643
Cdd:PRK11057 546 IADEENIPPYVVFNDATLIEMAEQMPITASEMLSVNGVGQRKLERFG 592
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
47-500 |
1.72e-162 |
|
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: 476.57 E-value: 1.72e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 47 LHRVFGYEAFRGEQEAVIEHVVAGGDAVVLMPTGGGKSLCYQIPSLVRPGTGVVVSPLIALMQDQVDALRALGVRAGFMN 126
Cdd:TIGR00614 3 LKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATFLN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 127 STQDFDERRMVEAEFLAGELDLLYLAPERLRLGGTL--DLLSRGKISVFAIDEAHCVSQWGHDFRPDYLALSLLGERWPD 204
Cdd:TIGR00614 83 SAQTKEQQLNVLTDLKDGKIKLLYVTPEKISASNRLlqTLEERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKFPN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 205 VPRIALTATATHATHQEITERLNMPAARHFVASFDRPNIQYRIVPK-ADPKKQLLSFLREEHPGDAGIVYCLSRNSVDKT 283
Cdd:TIGR00614 163 VPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKtPKILEDLLRFIRKEFEGKSGIIYCPSRKKVEQV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 284 AEFLSRNGVEAVPYHAGLDAGTRAAHQSRFLREDGLVVVATIAFGMGIDKPDVRFVAHLDLPKSVEGYYQETGRAGRDGL 363
Cdd:TIGR00614 243 AAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGRDGL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 364 PSTAWMAYGLNDVIQQRKLIQSgEGDEAFRRRAQAHLDSMLALCETAQCRRGQLLAYFGQ-----DPDPSG----CGNCD 434
Cdd:TIGR00614 323 PSECHLFYAPADMNRLRRLLME-EPDGNFRTYKLKLYEMMEYCLNSSTCRRLILLSYFGEkgfnkSFCIMGtekcCDNCC 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2542603572 435 TCL------TPPETWDGTVAAQKALSTVVRLqrerGQKFGAVQIVDILLGKRTGKVIQFDHDQLSVFGIGEE 500
Cdd:TIGR00614 402 KRLdyktkdVTDKVYDFGPQAQKALSAVGRL----NQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGRGKD 469
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
49-652 |
1.05e-116 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 378.47 E-value: 1.05e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 49 RVFGYEAFRGEQEAVIEHVVAGGDAVVLMPTGGGKSLCYQIPSLVRPGTGVVVSPLIALMQDQVDALRALGVRAGFMNST 128
Cdd:PLN03137 454 KVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSAG 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 129 QDFDERRMVEAEFLAG--ELDLLYLAPERLRLGGTL-----DLLSRGKISVFAIDEAHCVSQWGHDFRPDYLALSLLGER 201
Cdd:PLN03137 534 MEWAEQLEILQELSSEysKYKLLYVTPEKVAKSDSLlrhleNLNSRGLLARFVIDEAHCVSQWGHDFRPDYQGLGILKQK 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 202 WPDVPRIALTATATHATHQEITERLNMPAARHFVASFDRPNIQYRIVPKAdpKKQLL---SFLREEHPGDAGIVYCLSRN 278
Cdd:PLN03137 614 FPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKT--KKCLEdidKFIKENHFDECGIIYCLSRM 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 279 SVDKTAEFLSRNGVEAVPYHAGLDAGTRAAHQSRFLREDGLVVVATIAFGMGIDKPDVRFVAHLDLPKSVEGYYQETGRA 358
Cdd:PLN03137 692 DCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRA 771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 359 GRDGLPSTAWMAYGLNDVIQQRKLIQSGEGDEA-----FRRRAQA---------HLDSMLALCET-AQCRRGQLLAYFGQ 423
Cdd:PLN03137 772 GRDGQRSSCVLYYSYSDYIRVKHMISQGGVEQSpmamgYNRMASSgriletnteNLLRMVSYCENeVDCRRFLQLVHFGE 851
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 424 DPDPSGCGN-CDTCLTPPE--TWDGTVAAQKalstVVRLQRERGQKFGAVQIVDILLGKRTGKVIQFDHDQLSVFGIGEE 500
Cdd:PLN03137 852 KFDSTNCKKtCDNCSSSKSliDKDVTEIARQ----LVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLSLHGAGKH 927
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 501 LTEGEWRGVIRQLLAQGLLA-------VEGEYGTLVLTEASGA----------VLRRERDVPLRKEPKKPVTSRSGTSST 563
Cdd:PLN03137 928 LSKGEASRILHYLVTEDILAedvkksdLYGSVSSLLKVNESKAyklfsggqtiIMRFPSSVKASKPSKFEATPAKGPLTS 1007
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 564 GSGRGERKGKAVAAE----LPEELLPAFEALRAWRAEQAREqGVPAYVIFHDATLREIATVWPTSVGELGGISGVGEKKL 639
Cdd:PLN03137 1008 GKQSTLPMATPAQPPvdlnLSAILYTALRKLRTALVKEAGD-GVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKAKV 1086
|
650
....*....|...
gi 2542603572 640 TTYGEGVLETLAS 652
Cdd:PLN03137 1087 SKYGDRLLETIES 1099
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
44-239 |
4.05e-88 |
|
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: 274.41 E-value: 4.05e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 44 LAALHRVFGYEAFRGEQEAVIEHVVAGGDAVVLMPTGGGKSLCYQIPSLVRPGTGVVVSPLIALMQDQVDALRALGVRAG 123
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 124 FMNSTQDFDERRMVEAEFLAGELDLLYLAPERLRLGGTLDLLSR----GKISVFAIDEAHCVSQWGHDFRPDYLALSLLG 199
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRlperKRLALIVVDEAHCVSQWGHDFRPDYLRLGRLR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2542603572 200 ERWPDVPRIALTATATHATHQEITERLNMPAARHFVASFD 239
Cdd:cd17920 161 RALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
240-371 |
7.43e-61 |
|
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: 200.13 E-value: 7.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 240 RPNIQYRIVPKADPKKQL--LSFLREEHPGDAGIVYCLSRNSVDKTAEFLSRNGVEAVPYHAGLDAGTRAAHQSRFLRED 317
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLdlLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2542603572 318 GLVVVATIAFGMGIDKPDVRFVAHLDLPKSVEGYYQETGRAGRDGLPSTAWMAY 371
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
41-239 |
4.80e-60 |
|
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: 200.67 E-value: 4.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 41 SEALAALHRVFGYEAFRGEQEAVIEHVVAGGDAVVLMPTGGGKSLCYQIPSLVRPGTGVVVSPLIALMQDQVDALRALGV 120
Cdd:cd18015 4 GKVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 121 RAGFMNSTQDFDERRMVEAEFLAG--ELDLLYLAPERL----RLGGTLD-LLSRGKISVFAIDEAHCVSQWGHDFRPDYL 193
Cdd:cd18015 84 SATMLNASSSKEHVKWVHAALTDKnsELKLLYVTPEKIakskRFMSKLEkAYNAGRLARIAIDEVHCCSQWGHDFRPDYK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2542603572 194 ALSLLGERWPDVPRIALTATATHATHQEITERLNMPAARHFVASFD 239
Cdd:cd18015 164 KLGILKRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
44-195 |
1.51e-58 |
|
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: 196.71 E-value: 1.51e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 44 LAALHRVFGYEAFRGEQEAVIEHVVAGGDAVVLMPTGGGKSLCYQIPSLV----RPGTGVVVSPLIALMQDQVDALRALg 119
Cdd:cd18018 1 LKLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLlrrrGPGLTLVVSPLIALMKDQVDALPRA- 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2542603572 120 VRAGFMNSTQDfDERRMVEAEFL-AGELDLLYLAPERLR-LGGTLDLLSRGKISVFAIDEAHCVSQWGHDFRPDYLAL 195
Cdd:cd18018 80 IKAAALNSSLT-REERRRILEKLrAGEVKILYVSPERLVnESFRELLRQTPPISLLVVDEAHCISEWSHNFRPDYLRL 156
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
42-239 |
1.58e-51 |
|
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: 177.71 E-value: 1.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 42 EALAALHRVFGYEAFRGEQEAVIEHVVAGGDAVVLMPTGGGKSLCYQIPSLVRPGTGVVVSPLIALMQDQVDALRALGVR 121
Cdd:cd18016 4 EMMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 122 AGFMNSTQDFDERRMVEAEFLAGE--LDLLYLAPERL----RLGGTL-DLLSRGKISVFAIDEAHCVSQWGHDFRPDYLA 194
Cdd:cd18016 84 ATYLTGDKTDAEATKIYLQLSKKDpiIKLLYVTPEKIsasnRLISTLeNLYERKLLARFVIDEAHCVSQWGHDFRPDYKR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2542603572 195 LSLLGERWPDVPRIALTATATHATHQEITERLNMPAARHFVASFD 239
Cdd:cd18016 164 LNMLRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
44-208 |
5.45e-48 |
|
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: 168.03 E-value: 5.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 44 LAALHRVFGYEAFRGE-QEAVIEHVVAG-GDAVVLMPTGGGKSLCYQIPSLVRPGTGVVVSPLIALMQDQVDALRALGVR 121
Cdd:cd18014 1 RSTLKKVFGHSDFKSPlQEKATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 122 AGFMNSTQDFDERRMV----EAEflAGELDLLYLAPERLRLGGTLDLLS----RGKISVFAIDEAHCVSQWGHDFRPDYL 193
Cdd:cd18014 81 VDSLNSKLSAQERKRIiadlESE--KPQTKFLYITPEMAATSSFQPLLSslvsRNLLSYLVVDEAHCVSQWGHDFRPDYL 158
|
170
....*....|....*
gi 2542603572 194 ALSLLGERWPDVPRI 208
Cdd:cd18014 159 RLGALRSRYGHVPWV 173
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
44-239 |
2.03e-44 |
|
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: 157.63 E-value: 2.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 44 LAALHRVFGYEAFRGEQEAVIEHVVAGG-DAVVLMPTGGGKSLCYQIPSLVRPGTGVVVSPLIALMQDQVDALRALGVRA 122
Cdd:cd18017 1 LNALNEYFGHSSFRPVQWKVIRSVLEERrDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 123 GFMNSTQdfdeRRMVEAEFLAGELDLLYLAPERLRLGGTLDLLSRGKISVFAIDEAHCVSQWGHDFRPDYLALSLLGERW 202
Cdd:cd18017 81 CFLGSAQ----SQNVLDDIKMGKIRVIYVTPEFVSKGLELLQQLRNGITLIAIDEAHCVSQWGHDFRSSYRHLGSIRNRL 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 2542603572 203 PDVPRIALTATATHATHQEITERLNMPAARHFVASFD 239
Cdd:cd18017 157 PNVPIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
439-549 |
6.71e-39 |
|
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix structure. The RQC domain, found only in RecQ family enzymes, is a high affinity G4 DNA binding domain.
Pssm-ID: 462780 [Multi-domain] Cd Length: 108 Bit Score: 139.21 E-value: 6.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 439 PPETWDGTVAAQKALSTVVRLqrerGQKFGAVQIVDILLGKRTGKVIQFDHDQLSVFGIGEELTEGEWRGVIRQLLAQGL 518
Cdd:pfam09382 1 PPETVDVTEEAQKILSCVYRT----GQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGY 76
|
90 100 110
....*....|....*....|....*....|..
gi 2542603572 519 LAVEGE-YGTLVLTEASGAVLRRERDVPLRKE 549
Cdd:pfam09382 77 LEVDIEfYSVLKLTPKAREVLKGEEKVMLRVP 108
|
|
| DpdF |
NF041063 |
protein DpdF; |
46-383 |
3.83e-38 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 151.99 E-value: 3.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 46 ALHRVFGYEAFR--GEQEAVieHVV----AGGDAVVLMPTGGGKSLCYQIPSLVRPGTG---VVVSPLIALMQDQVDALR 116
Cdd:NF041063 130 FLAEALGFTHYRspGQREAV--RAAllapPGSTLIVNLPTGSGKSLVAQAPALLASRQGgltLVVVPTVALAIDQERRAR 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 117 ALGVRAGFMNST-------QDFDERRMVEAEFLAGELDLLYLAPERL--RLGGTL-DLLSRGKISVFAIDEAHCVSQWGH 186
Cdd:NF041063 208 ELLRRAGPDLGGplawhggLSAEERAAIRQRIRDGTQRILFTSPESLtgSLRPALfDAAEAGLLRYLVVDEAHLVDQWGD 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 187 DFRPDYLALSLLGERWPDVPrialtatathathqeiterlnmPAARHFV------------------------------A 236
Cdd:NF041063 288 GFRPEFQLLAGLRRSLLRLA----------------------PSGRPFRtlllsatltestldtletlfgppgpfivvsA 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 237 SFDRPNIQYRIVPKADPK------KQLLSFLreehPGDAgIVYCLSRNSVDKTAEFLSRNGVEAVpyhAGLDAGTRAAHQ 310
Cdd:NF041063 346 VQLRPEPAYWVAKCDSEEerrervLEALRHL----PRPL-ILYVTKVEDAEAWLQRLRAAGFRRV---ALFHGDTPDAER 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 311 SRFL---REDGL-VVVATIAFGMGIDKPDVRFVAHLDLPKSVEGYYQETGRAGRDGLPSTAWMAYGLNDV-----IQQRK 381
Cdd:NF041063 418 ERLIeqwRENELdIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLdiaksLNRPK 497
|
..
gi 2542603572 382 LI 383
Cdd:NF041063 498 LI 499
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
444-538 |
6.61e-35 |
|
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix structure; The RQC domain, found only in RecQ family enzymes, is a high affinity G4 DNA binding domain.
Pssm-ID: 214936 [Multi-domain] Cd Length: 92 Bit Score: 127.59 E-value: 6.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 444 DGTVAAQKALSTVVRLqrerGQKFGAVQIVDILLGKRTGKVIQFDHDQLSVFGIGEELTEGEWRGVIRQLLAQGLLAVEG 523
Cdd:smart00956 1 DVTEEAQKLLSCVYRT----GQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDG 76
|
90
....*....|....*.
gi 2542603572 524 E-YGTLVLTEASGAVL 538
Cdd:smart00956 77 GrYPYLKLTEKARPVL 92
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
375-437 |
9.09e-24 |
|
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ.
Pssm-ID: 465031 [Multi-domain] Cd Length: 66 Bit Score: 95.05 E-value: 9.09e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2542603572 375 DVIQQRKLIQSGEGDEAFRRRAQAHLDSMLALCE-TAQCRRGQLLAYFGQDPDPSGCGNCDTCL 437
Cdd:pfam16124 3 DVVRLRFLIEQSEADEERKEVELQKLQAMVAYCEnTTDCRRKQLLRYFGEEFDSEPCGNCDNCL 66
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
60-195 |
1.53e-22 |
|
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: 95.00 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 60 QEAVIEHVVAGGDAVVLMPTGGGKSLCYQIPSLVR------PGTGVVVSPLIALMQDQVDALRALGVRAGFMNSTQDFDE 133
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAldkldnGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLLGGD 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2542603572 134 RRMVEAEFLAGeLDLLYLAPERLrlggtLDLLSR----GKISVFAIDEAHCVSQWGhdFRPDYLAL 195
Cdd:pfam00270 84 SRKEQLEKLKG-PDILVGTPGRL-----LDLLQErkllKNLKLLVLDEAHRLLDMG--FGPDLEEI 141
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
587-650 |
4.59e-21 |
|
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic acid binding. Mutations in the HRDC domain cause human disease. It is interesting to note that the RecQ helicase in Deinococcus radiodurans has three tandem HRDC domains.
Pssm-ID: 425755 [Multi-domain] Cd Length: 68 Bit Score: 87.21 E-value: 4.59e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2542603572 587 FEALRAWRAEQAREQGVPAYVIFHDATLREIATVWPTSVGELGGISGVGEKKLTTYGEGVLETL 650
Cdd:pfam00570 5 LKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
281-362 |
1.13e-19 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 83.80 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 281 DKTAEFLSRNGVEAVPYHAGLDAGTRAAHQSRFLREDGLVVVATIAFGMGIDKPDVRFVAHLDLPKSVEGYYQETGRAGR 360
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 2542603572 361 DG 362
Cdd:smart00490 81 AG 82
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
254-362 |
4.51e-19 |
|
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: 83.03 E-value: 4.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 254 KKQLLSFLREEHPGDAGIVYCLSRNSVDKTaEFLSRNGVEAVPYHAGLDAGTRAAHQSRFLREDGLVVVATIAFGMGIDK 333
Cdd:pfam00271 2 KLEALLELLKKERGGKVLIFSQTKKTLEAE-LLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*....
gi 2542603572 334 PDVRFVAHLDLPKSVEGYYQETGRAGRDG 362
Cdd:pfam00271 81 PDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
51-208 |
2.96e-18 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 83.70 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 51 FGYEAFRGEQEAVIEHVVAG-GDAVVLMPTGGGKSLCYQIPSL-----VRPGTGVVVSPLIALMQDQVDALRALGVRAGF 124
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALealkrGKGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 125 MNST-QDFDERRMVEAEFLAGELDLLYLAPERLRLGGTLDLLSRGKISVFAIDEAHCVSQWGhdFRPDYLAlsLLGERWP 203
Cdd:smart00487 84 KVVGlYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEK--LLKLLPK 159
|
....*
gi 2542603572 204 DVPRI 208
Cdd:smart00487 160 NVQLL 164
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
245-363 |
6.10e-17 |
|
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: 77.55 E-value: 6.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 245 YRIVPKADPKKQLLSFLREEHPGDAGIVYCLSRNSVDKTAEFLSRNGVEAVPYHAGLDAGTRAAHQSRFLREDGLVVVAT 324
Cdd:cd18787 5 YVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVAT 84
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2542603572 325 IAFGMGIDKPDVRFVAHLDLPKSVEGYyq---eTGRAGRDGL 363
Cdd:cd18787 85 DVAARGLDIPGVDHVINYDLPRDAEDYvhrigrTGRAGRKGT 126
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
580-651 |
5.42e-13 |
|
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the HRDC domain cause human disease.
Pssm-ID: 128635 [Multi-domain] Cd Length: 81 Bit Score: 64.63 E-value: 5.42e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2542603572 580 PEELLPAFEALRAWRAEQAREQGVPAYVIFHDATLREIATVWPTSVGELGGISGVGEKKLTTYGEGVLETLA 651
Cdd:smart00341 1 RERQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQ 72
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
60-363 |
1.10e-12 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 70.56 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 60 QEAVIEHVVAGGDAVVLMPTGGGKSLCYQIPSL----------VRpgtGVVVSP---LIAlmqdQV-DALRALGVRAGFm 125
Cdd:COG0513 29 QAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLqrldpsrpraPQ---ALILAPtreLAL----QVaEELRKLAKYLGL- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 126 NST-----QDFDErrmvEAEFLAGELDLLYLAPERLrlggtLDLLSRGKIS-----VFAIDEAhcvsqwghD------FR 189
Cdd:COG0513 101 RVAtvyggVSIGR----QIRALKRGVDIVVATPGRL-----LDLIERGALDlsgveTLVLDEA--------DrmldmgFI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 190 PD--YLALSLLGER--------WPdvPRIaltatathathQEITER-LNMPAaRHFVA--SFDRPNIQYRI--VPKADpK 254
Cdd:COG0513 164 EDieRILKLLPKERqtllfsatMP--PEI-----------RKLAKRyLKNPV-RIEVApeNATAETIEQRYylVDKRD-K 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 255 KQLLSFLREEHPGDAGIVYCLSRNSVDKTAEFLSRNGVEAVPYHAGLDAGTRAAHQSRFLREDGLVVVAT-IAfGMGIDK 333
Cdd:COG0513 229 LELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATdVA-ARGIDI 307
|
330 340 350
....*....|....*....|....*....|....
gi 2542603572 334 PDVRFVAHLDLPKSVEgYYQ----ETGRAGRDGL 363
Cdd:COG0513 308 DDVSHVINYDLPEDPE-DYVhrigRTGRAGAEGT 340
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
70-208 |
2.45e-12 |
|
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: 65.12 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 70 GGDAVVLMPTGGGKSLCYQIP----SLVRPGTGVVVSPLIALMQDQVDALRAL---GVRAGFMNSTQDFDERRmveaEFL 142
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAalllLLKKGKKVLVLVPTKALALQTAERLRELfgpGIRVAVLVGGSSAEERE----KNK 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2542603572 143 AGELDLLYLAPERL-RLGGTLDLLSRGKISVFAIDEAHCVSQWGHDFRPDYLALSLLGErwPDVPRI 208
Cdd:cd00046 77 LGDADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGL--KNAQVI 141
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
60-367 |
6.18e-12 |
|
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: 69.09 E-value: 6.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 60 QEAVIEHVVAGGDAVVLMPTGGGKSLCYQIPSL-----VRPGTGVVVSPLIALMQDQVDALRAL------GVRAGFMNST 128
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLealleDPGATALYLYPTKALARDQLRRLRELaealglGVRVATYDGD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 129 QDFDERRMV--EAEFLAGELDLLYLAperLRLGGTL--DLLSRGKISVfaIDEAHC--------VSQ-----------WG 185
Cdd:COG1205 141 TPPEERRWIreHPDIVLTNPDMLHYG---LLPHHTRwaRFFRNLRYVV--IDEAHTyrgvfgshVANvlrrlrricrhYG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 186 HDFR----------PDYLALSLLGErwpDVprialtatathathQEITERLNMPAARHFVasFDRPNIQYRIVPK---AD 252
Cdd:COG1205 216 SDPQfilasatignPAEHAERLTGR---PV--------------TVVDEDGSPRGERTFV--LWNPPLVDDGIRRsalAE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 253 PKKQLLSFLREEHPgdaGIVYCLSRNSVDKTAEFLSRNGVEAV------PYHAGLDAGTRAAHQSRFLREDGLVVVATIA 326
Cdd:COG1205 277 AARLLADLVREGLR---TLVFTRSRRGAELLARYARRALREPDladrvaAYRAGYLPEERREIERGLRSGELLGVVSTNA 353
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2542603572 327 FGMGIDkpdvrfVAHLDL------PKSVEGYYQETGRAGRDGLPSTA 367
Cdd:COG1205 354 LELGID------IGGLDAvvlagyPGTRASFWQQAGRAGRRGQDSLV 394
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
60-179 |
5.75e-10 |
|
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: 5.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 60 QEAVIEHVVAGGDAVVLMPTGGGKSLCYQIPSLVR----PG-TGVVVSPLIALMQDQVDALRALGVR--AGFMNSTQDFD 132
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEAllrdPGsRALYLYPTKALAQDQLRSLRELLEQlgLGIRVATYDGD 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2542603572 133 ERRMVEAEFLAGELDLLYLAPERLRLG------GTLDLLSRGKISVfaIDEAH 179
Cdd:cd17923 85 TPREERRAIIRNPPRILLTNPDMLHYAllphhdRWARFLRNLRYVV--LDEAH 135
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
271-369 |
1.66e-09 |
|
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: 56.88 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 271 IVYCLSRNSVDKTAEFLSRNGVEAVP-------YHAGLDAGTRAAHQSRFLREDGLVVVATIAFGMGIDKPDVRFVAHLD 343
Cdd:cd18797 39 IVFCRSRKLAELLLRYLKARLVEEGPlaskvasYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|....*.
gi 2542603572 344 LPKSVEGYYQETGRAGRDGLPSTAWM 369
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDSLVIL 144
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
52-367 |
3.35e-09 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 59.80 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 52 GYEAFRGEQEAVIEHVVAGGDAVVLMPTGGGKSLCYQIP-----SLVRPG--------TGVVVSP---LIALMQDQVDAL 115
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPiisrcCTIRSGhpseqrnpLAMVLTPtreLCVQVEDQAKVL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 116 -------RALGVRAGFMnSTQDFDERRMVEaeflageldLLYLAPERLrlggtLDLLSR-----GKISVFAIDEAHCVSQ 183
Cdd:PLN00206 220 gkglpfkTALVVGGDAM-PQQLYRIQQGVE---------LIVGTPGRL-----IDLLSKhdielDNVSVLVLDEVDCMLE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 184 WGhdFRPD----YLALSLlgerwPDVprialtATATHATHQEITERLNMPAARHFVASFDRPNIQYRIVPK-------AD 252
Cdd:PLN00206 285 RG--FRDQvmqiFQALSQ-----PQV------LLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQlaiwvetKQ 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 253 PKKQLLSFLR-EEHPGDAGIVYCLSRNSVDKTAEFLSR-NGVEAVPYHAGLDAGTRAAHQSRFLREDGLVVVATIAFGMG 330
Cdd:PLN00206 352 KKQKLFDILKsKQHFKPPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRG 431
|
330 340 350
....*....|....*....|....*....|....*..
gi 2542603572 331 IDKPDVRFVAHLDLPKSVEGYYQETGRAGRDGLPSTA 367
Cdd:PLN00206 432 VDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTA 468
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
320-362 |
2.73e-08 |
|
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: 51.17 E-value: 2.73e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2542603572 320 VVVATIAFGMGIDKPDVRFVAHLDLPKSVEGYYQETGRAGRDG 362
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGG 67
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
57-358 |
1.07e-07 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 55.03 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 57 RGEQEAVIEHVVA-----GGDAVVLMPTGGGKSL----CYQipSLVRPGTGVVVSPLIALMQDQVDALRAlgvragFMNS 127
Cdd:COG1061 82 RPYQQEALEALLAalergGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEELRR------FLGD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 128 TQDFDERRMVEAEFLAGELDLLYLAPERLRLGGTLDLLsrgkisvfAIDEAHcvsqwgH-----------DFRPDY-LAL 195
Cdd:COG1061 154 PLAGGGKKDSDAPITVATYQSLARRAHLDELGDRFGLV--------IIDEAH------HagapsyrrileAFPAAYrLGL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 196 S---------------------------LLGERW---PDVPRIALTATATHATHQEITERLNmpaarhfvasfdrpniqY 245
Cdd:COG1061 220 TatpfrsdgreillflfdgivyeyslkeAIEDGYlapPEYYGIRVDLTDERAEYDALSERLR-----------------E 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 246 RIVPKADPKKQLLSFLREEHPGD-AGIVYCLSRNSVDKTAEFLSRNGVEAVPYHAGLDAGTRAAHQSRFlREDGLVVVAT 324
Cdd:COG1061 283 ALAADAERKDKILRELLREHPDDrKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAF-RDGELRILVT 361
|
330 340 350
....*....|....*....|....*....|....*
gi 2542603572 325 IA-FGMGIDKPDVRFVAHLDLPKSVEGYYQETGRA 358
Cdd:COG1061 362 VDvLNEGVDVPRLDVAILLRPTGSPREFIQRLGRG 396
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
576-671 |
4.42e-07 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 52.57 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 576 AAELPEELLPAFEALRAWRAEQAREQGVPAYVIFHDATLREIATVWPTSVGELGGISGVGEKKLTTYGEGVLETLA-SLG 654
Cdd:COG0349 202 AWKLNPRQLAVLRELAAWREREARKRDVPRNRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAVAeALA 281
|
90
....*....|....*..
gi 2542603572 655 GPTGSAPAGDPSPAGDP 671
Cdd:COG0349 282 LPEEELPEPPRRLPLSP 298
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
51-179 |
5.12e-06 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 49.51 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 51 FGYEAFRGEQEAVIEHVVAGGDAVVL-MPTGGGKSLCYQIP---SLVRPGTGVVVSPLIAL----MQDQVDALRALGVRA 122
Cdd:COG1204 18 RGIEELYPPQAEALEAGLLEGKNLVVsAPTASGKTLIAELAilkALLNGGKALYIVPLRALasekYREFKRDFEELGIKV 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2542603572 123 GFmnSTQDFDERrmveaEFLAGELDLLYLAPERLRLggtldLLSRG-----KISVFAIDEAH 179
Cdd:COG1204 98 GV--STGDYDSD-----DEWLGRYDILVATPEKLDS-----LLRNGpswlrDVDLVVVDEAH 147
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
245-385 |
1.05e-05 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 48.28 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 245 YRIVPKADPKKQLLSFLREEHPGDAGIVYCLSRNSVDKTAEFLSRNGVEAVPYHAGLDAGTRAAHQSRFLREDGLVVVAT 324
Cdd:PTZ00424 245 YVAVEKEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITT 324
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2542603572 325 IAFGMGIDKPDVRFVAHLDLPKSVEGYYQETGRAGRDGLPSTAwMAYGLNDVIQQRKLIQS 385
Cdd:PTZ00424 325 DLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVA-INFVTPDDIEQLKEIER 384
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
36-362 |
4.64e-05 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 46.77 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 36 LGADASEALAALhrvfGYEAFRGEQEAVIEHVVAGGDAVVLMPTGGGKSLCYQIPSL------VRPGTGVVVSPLIAL-- 107
Cdd:PRK11634 13 LKAPILEALNDL----GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLhnldpeLKAPQILVLAPTRELav 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 108 -----MQDQVDALRALGVRAgfMNSTQDFDerrmVEAEFLAGELDLLYLAPERLrlggtLDLLSRG-----KISVFAIDE 177
Cdd:PRK11634 89 qvaeaMTDFSKHMRGVNVVA--LYGGQRYD----VQLRALRQGPQIVVGTPGRL-----LDHLKRGtldlsKLSGLVLDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 178 AHCVSQWG--HDFR------PDYLALSLLGERWPDVPRialtatathathqEITER-LNMPAARHFVASF-DRPNIQ--Y 245
Cdd:PRK11634 158 ADEMLRMGfiEDVEtimaqiPEGHQTALFSATMPEAIR-------------RITRRfMKEPQEVRIQSSVtTRPDISqsY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 246 RIVPKADPKKQLLSFLREEHpGDAGIVYCLSRNSVDKTAEFLSRNGVEAVPYHAGLDAGTRAAHQSRFlrEDGL--VVVA 323
Cdd:PRK11634 225 WTVWGMRKNEALVRFLEAED-FDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERL--KDGRldILIA 301
|
330 340 350
....*....|....*....|....*....|....*....
gi 2542603572 324 TIAFGMGIDKPDVRFVAHLDLPKSVEGYYQETGRAGRDG 362
Cdd:PRK11634 302 TDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAG 340
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
61-182 |
1.00e-04 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type 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: 350786 [Multi-domain] Cd Length: 177 Bit Score: 43.48 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 61 EAVIEHVVAGGDAVVLMPTGGGKSLCYQ---IPSLVRPGTGVVVSPLIALMQDQVD---ALRALGVRAGFmnSTQDFDER 134
Cdd:cd18028 8 EAVRAGLLKGENLLISIPTASGKTLIAEmamVNTLLEGGKALYLVPLRALASEKYEefkKLEEIGLKVGI--STGDYDED 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2542603572 135 rmveAEFLaGELDLLYLAPERlrlggtLDLLSRGK------ISVFAIDEAHCVS 182
Cdd:cd18028 86 ----DEWL-GDYDIIVATYEK------FDSLLRHSpswlrdVGVVVVDEIHLIS 128
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
257-367 |
1.17e-04 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 45.32 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 257 LLSFLREEHPGDAgIVYCLSRNSVDKTAEFLSRNGVEAVPYHAGLDAGTRAAHQSRFLREDGLVVVATIAFGMGIDKPDV 336
Cdd:PRK11192 236 LCHLLKQPEVTRS-IVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDV 314
|
90 100 110
....*....|....*....|....*....|.
gi 2542603572 337 RFVAHLDLPKSVEGYYQETGRAGRDGLPSTA 367
Cdd:PRK11192 315 SHVINFDMPRSADTYLHRIGRTGRAGRKGTA 345
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
60-183 |
2.78e-04 |
|
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: 42.25 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 60 QEAVIEHVVAGGDAVVL-MPTGGGKSLC--YQIPSLVRPGTGVVV--SPLIAL----MQDQVDALRALGVRAGFMnsTQD 130
Cdd:cd17921 6 QREALRALYLSGDSVLVsAPTSSGKTLIaeLAILRALATSGGKAVyiAPTRALvnqkEADLRERFGPLGKNVGLL--TGD 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2542603572 131 FDERRmveaeFLAGELDLLYLAPERLRLggtldLLSRG------KISVFAIDEAHCVSQ 183
Cdd:cd17921 84 PSVNK-----LLLAEADILVATPEKLDL-----LLRNGgerliqDVRLVVVDEAHLIGD 132
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
68-362 |
3.33e-04 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 43.99 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 68 VAGGDAVVLMPTGGGKSLCYQIPSLV--------RPGTGVVVSPLiALMQDQVDALRALGVR-------------AGFMN 126
Cdd:PTZ00110 165 LSGRDMIGIAETGSGKTLAFLLPAIVhinaqpllRYGDGPIVLVL-APTRELAEQIREQCNKfgasskirntvayGGVPK 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 127 STQDFDERRMVEaeflageldLLYLAPERLrlggtLDLLSRG-----KISVFAIDEA-------------HCVSQwghdF 188
Cdd:PTZ00110 244 RGQIYALRRGVE---------ILIACPGRL-----IDFLESNvtnlrRVTYLVLDEAdrmldmgfepqirKIVSQ----I 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 189 RPDYLALsLLGERWPdvprialtatathATHQEITERLNMPAARHF-VASFDRP---NI-QY-RIVPKADPKKQLLSFLR 262
Cdd:PTZ00110 306 RPDRQTL-MWSATWP-------------KEVQSLARDLCKEEPVHVnVGSLDLTachNIkQEvFVVEEHEKRGKLKMLLQ 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 263 E-EHPGDAGIVYCLSRnsvdKTAEFLSR----NGVEAVPYHAGLDAGTRAAHQSRFLREDGLVVVATIAFGMGIDKPDVR 337
Cdd:PTZ00110 372 RiMRDGDKILIFVETK----KGADFLTKelrlDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVK 447
|
330 340
....*....|....*....|....*
gi 2542603572 338 FVAHLDLPKSVEGYYQETGRAGRDG 362
Cdd:PTZ00110 448 YVINFDFPNQIEDYVHRIGRTGRAG 472
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
271-360 |
6.28e-04 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 42.96 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 271 IVYCLSRNSVDKTAEFLsrnGVEAVPYHAGLDAGTRAAHQSRFLREDGLVVVATIAFGMGIDKP--DVRF------VAHL 342
Cdd:COG1202 431 IIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPasQVIFdslamgIEWL 507
|
90
....*....|....*...
gi 2542603572 343 dlpkSVEGYYQETGRAGR 360
Cdd:COG1202 508 ----SVQEFHQMLGRAGR 521
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
271-363 |
7.45e-04 |
|
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: 40.61 E-value: 7.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 271 IVYCLSRNSVDKTAEFLSrnGVEAvpYHAGLdagtraahqSRFLRE-------DGL--VVVATIAFGMGIDKPdvrfvAH 341
Cdd:cd18795 47 LVFCSSRKECEKTAKDLA--GIAF--HHAGL---------TREDRElveelfrEGLikVLVATSTLAAGVNLP-----AR 108
|
90 100 110
....*....|....*....|....*....|....*..
gi 2542603572 342 L---------------DLPKSVegYYQETGRAGRDGL 363
Cdd:cd18795 109 TviikgtqrydgkgyrELSPLE--YLQMIGRAGRPGF 143
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
254-360 |
8.76e-04 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 42.49 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 254 KKQLLSFLREEHPGDAGIVYCLSRNSVDKTAEFLSRNGVEAVPYHAGLDAGTRAAHQSRFLREDGLVVVATIAFGMGIDK 333
Cdd:PRK10590 232 KRELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDI 311
|
90 100
....*....|....*....|....*..
gi 2542603572 334 PDVRFVAHLDLPKSVEGYYQETGRAGR 360
Cdd:PRK10590 312 EELPHVVNYELPNVPEDYVHRIGRTGR 338
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
292-360 |
2.17e-03 |
|
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: 39.17 E-value: 2.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542603572 292 VEAVPYHAG-LDAGTRAAHQSRFLREDGLVVVATIAFGMGIDKPDVRFVAHLDLPKSVEGYYQETGRAGR 360
Cdd:cd18796 68 PDFIALHHGsLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
70-118 |
7.57e-03 |
|
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: 37.95 E-value: 7.57e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2542603572 70 GGDAVVLMPTGGGKSLCYQIPSLVR------PGTGVV-VSPLIALMQDQVDALRAL 118
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSladepeKGVQVLyISPLKALINDQERRLEEP 56
|
|
| |
