|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
6-477 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 864.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 6 HPAALKVLQEVFGYDSFRGPQQAIIEHVMAGGDALVLMPTGGGKSLCYQIPALLREGTAIVVSPLIALMQDQVAALQQNG 85
Cdd:COG0514 2 RDDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 86 VRAAYLNSSLDYHEAVEVENRLRAGELDLLYVAPERLATARMQVLLEQTKIALFAIDEAHCVSQWGHDFRPEYRQLSHLH 165
Cdd:COG0514 82 IRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGELR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 166 QRFPQVPRIALTATADVPTRGDIMEHLQLQEAALYNSGFDRPNIRYHIAE-NQGNAKEQLLRFIREHhDGEAGIVYCLSR 244
Cdd:COG0514 162 ERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPkPPDDKLAQLLDFLKEH-PGGSGIVYCLSR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 245 RKVEETAAWLERQGLTALPYHAGLPPEQRQHHQTRFLREDGVVVVATIAFGMGIDKPDVRFVAHLNLPKSIEAYYQETGR 324
Cdd:COG0514 241 KKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 325 AGRDGLPADAWMAYGLQDVITLRQMQQDSSAADQQKRIEQQKLDAMLGLCEIISCRRQALLHYFGDHLNSPCGNCDNCLT 404
Cdd:COG0514 321 AGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYFGEELAEPCGNCDNCLG 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316072217 405 PPETWEATVAAQKALSCVYRTEQRFGVTYLVDVLLGKHNERITRFGHDRLSTFGIGKELSANEWKALFRQLIA 477
Cdd:COG0514 401 PPETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLLA 473
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
9-601 |
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: 856.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 9 ALKVLQEVFGYDSFRGPQQAIIEHVMAGGDALVLMPTGGGKSLCYQIPALLREGTAIVVSPLIALMQDQVAALQQNGVRA 88
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 89 AYLNSSLDYHEAVEVENRLRAGELDLLYVAPERLATARMQVLLEQTKIALFAIDEAHCVSQWGHDFRPEYRQLSHLHQRF 168
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 169 PQVPRIALTATADVPTRGDIMEHLQLQEAALYNSGFDRPNIRYHIAENQgNAKEQLLRFIREHhDGEAGIVYCLSRRKVE 248
Cdd:TIGR01389 161 PQVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKN-NKQKFLLDYLKKH-RGQSGIIYASSRKKVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 249 ETAAWLERQGLTALPYHAGLPPEQRQHHQTRFLREDGVVVVATIAFGMGIDKPDVRFVAHLNLPKSIEAYYQETGRAGRD 328
Cdd:TIGR01389 239 ELAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 329 GLPADAWMAYGLQDVITLRQMQQDSSAADQQKRIEQQKLDAMLGLCEIISCRRQALLHYFGDHLNSPCGNCDNCLTPPET 408
Cdd:TIGR01389 319 GLPAEAILLYSPADIALLKRRIEQSEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENEVEPCGNCDNCLDPPKS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 409 WEATVAAQKALSCVYRTEQRFGVTYLVDVLLGKHNERITRFGHDRLSTFGIGKELSANEWKALFRQLIASGYLSVDMEGH 488
Cdd:TIGR01389 399 YDATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEIY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 489 GGIKLTANAKPVLRGEHSLTLRkPSKAKATRRGSKGASATLPHGE-LWEALRQHRRKLAEAQGVPAYVIFHDATLAELVE 567
Cdd:TIGR01389 479 IGLQLTEAARKVLKNEVEVLLR-PFKVVAKEKTRVQKNLSVGVDNaLFEALRELRKEQADEQNVPPYVIFSDSTLREMAE 557
|
570 580 590
....*....|....*....|....*....|....
gi 2316072217 568 QNPQNMEALGAISGIGTRKLADYGEGFLAVILAH 601
Cdd:TIGR01389 558 KRPATLNALLKIKGVGQNKLDRYGEAFLEVIREY 591
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
9-601 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 706.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 9 ALKVLQEVFGYDSFRGPQQAIIEHVMAGGDALVLMPTGGGKSLCYQIPALLREGTAIVVSPLIALMQDQVAALQQNGVRA 88
Cdd:PRK11057 13 AKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 89 AYLNSSLDYHEAVEVENRLRAGELDLLYVAPERLATARMQVLLEQTKIALFAIDEAHCVSQWGHDFRPEYRQLSHLHQRF 168
Cdd:PRK11057 93 ACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQRF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 169 PQVPRIALTATADVPTRGDIMEHLQLQEAALYNSGFDRPNIRYHIAEnQGNAKEQLLRFIREHHdGEAGIVYCLSRRKVE 248
Cdd:PRK11057 173 PTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVE-KFKPLDQLMRYVQEQR-GKSGIIYCNSRAKVE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 249 ETAAWLERQGLTALPYHAGLPPEQRQHHQTRFLREDGVVVVATIAFGMGIDKPDVRFVAHLNLPKSIEAYYQETGRAGRD 328
Cdd:PRK11057 251 DTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRD 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 329 GLPADAWMAYGLQDVITLRQMqQDSSAADQQKRIEQQKLDAMLGLCEIISCRRQALLHYFGDHLNSPCGNCDNCLTPPET 408
Cdd:PRK11057 331 GLPAEAMLFYDPADMAWLRRC-LEEKPAGQQQDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNCDICLDPPKQ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 409 WEATVAAQKALSCVYRTEQRFGVTYLVDVLLGKHNERITRFGHDRLSTFGIGKELSANEWKALFRQLIASGYLSVDMEGH 488
Cdd:PRK11057 410 YDGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLGLVTQNIAQH 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 489 GGIKLTANAKPVLRGEHSLTLRKPSKAKATRRGSKGASATLPHGELWEALRQHRRKLAEAQGVPAYVIFHDATLAELVEQ 568
Cdd:PRK11057 490 SALQLTEAARPVLRGEVSLQLAVPRIVALKPRAMQKSFGGNYDRKLFAKLRKLRKSIADEENIPPYVVFNDATLIEMAEQ 569
|
570 580 590
....*....|....*....|....*....|...
gi 2316072217 569 NPQNMEALGAISGIGTRKLADYGEGFLAVILAH 601
Cdd:PRK11057 570 MPITASEMLSVNGVGQRKLERFGKPFMALIRAH 602
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
11-462 |
0e+00 |
|
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: 550.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 11 KVLQEVFGYDSFRGPQQAIIEHVMAGGDALVLMPTGGGKSLCYQIPALLREGTAIVVSPLIALMQDQVAALQQNGVRAAY 90
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 91 LNSSLDYHEAVEVENRLRAGELDLLYVAPERLATAR--MQVLLEQTKIALFAIDEAHCVSQWGHDFRPEYRQLSHLHQRF 168
Cdd:TIGR00614 81 LNSAQTKEQQLNVLTDLKDGKIKLLYVTPEKISASNrlLQTLEERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 169 PQVPRIALTATADVPTRGDIMEHLQLQEAALYNSGFDRPNIRYHIAENQGNAKEQLLRFIREHHDGEAGIVYCLSRRKVE 248
Cdd:TIGR00614 161 PNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTPKILEDLLRFIRKEFEGKSGIIYCPSRKKVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 249 ETAAWLERQGLTALPYHAGLPPEQRQHHQTRFLREDGVVVVATIAFGMGIDKPDVRFVAHLNLPKSIEAYYQETGRAGRD 328
Cdd:TIGR00614 241 QVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGRD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 329 GLPADAWMAYGLQDVITLRQMQQDSSaaDQQKRIEQQKLDAMLGLCEIIS-CRRQALLHYFGD----------HLNSPCG 397
Cdd:TIGR00614 321 GLPSECHLFYAPADMNRLRRLLMEEP--DGNFRTYKLKLYEMMEYCLNSStCRRLILLSYFGEkgfnksfcimGTEKCCD 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2316072217 398 NCDNCL------TPPETWEATVAAQKALSCVYRTEQRFGVTYLVDVLLGKHNERITRFGHDRLSTFGIGKE 462
Cdd:TIGR00614 399 NCCKRLdyktkdVTDKVYDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGRGKD 469
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
14-598 |
4.43e-133 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 418.53 E-value: 4.43e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 14 QEVFGYDSFRGPQQAIIEHVMAGGDALVLMPTGGGKSLCYQIPALLREGTAIVVSPLIALMQDQVAALQQNGVRAAYLNS 93
Cdd:PLN03137 453 KKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSA 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 94 SLDYHEAVEVENRLRAG--ELDLLYVAPERLATA-----RMQVLLEQTKIALFAIDEAHCVSQWGHDFRPEYRQLSHLHQ 166
Cdd:PLN03137 533 GMEWAEQLEILQELSSEysKYKLLYVTPEKVAKSdsllrHLENLNSRGLLARFVIDEAHCVSQWGHDFRPDYQGLGILKQ 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 167 RFPQVPRIALTATADVPTRGDIMEHLQLQEAALYNSGFDRPNIRYHIAENQGNAKEQLLRFIREHHDGEAGIVYCLSRRK 246
Cdd:PLN03137 613 KFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKKCLEDIDKFIKENHFDECGIIYCLSRMD 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 247 VEETAAWLERQGLTALPYHAGLPPEQRQHHQTRFLREDGVVVVATIAFGMGIDKPDVRFVAHLNLPKSIEAYYQETGRAG 326
Cdd:PLN03137 693 CEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAG 772
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 327 RDGLPADAWMAYGLQDVITLRQM------QQDSSAADQQK-----RI---EQQKLDAMLGLCE-IISCRRQALLHYFGDH 391
Cdd:PLN03137 773 RDGQRSSCVLYYSYSDYIRVKHMisqggvEQSPMAMGYNRmassgRIletNTENLLRMVSYCEnEVDCRRFLQLVHFGEK 852
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 392 LNSP-CGN-CDNCLTPPETWE--ATVAAQKALSCVYRTEQRFGVTYLVDVLLGKHNERITRFGHDRLSTFGIGKELSANE 467
Cdd:PLN03137 853 FDSTnCKKtCDNCSSSKSLIDkdVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLSLHGAGKHLSKGE 932
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 468 WKALFRQLIASGYLS-----VDMEGHGGIKLTAN---AKPVLRGEHSLTLRKPSKAKATRRGSKGASA-----------T 528
Cdd:PLN03137 933 ASRILHYLVTEDILAedvkkSDLYGSVSSLLKVNeskAYKLFSGGQTIIMRFPSSVKASKPSKFEATPakgpltsgkqsT 1012
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 529 LP-------------HGELWEALRQHRRKLAE--AQGVPAYVIFHDATLAELVEQNPQNMEALGAISGIGTRKLADYGEG 593
Cdd:PLN03137 1013 LPmatpaqppvdlnlSAILYTALRKLRTALVKeaGDGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKAKVSKYGDR 1092
|
....*
gi 2316072217 594 FLAVI 598
Cdd:PLN03137 1093 LLETI 1097
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
10-205 |
1.73e-107 |
|
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: 321.41 E-value: 1.73e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 10 LKVLQEVFGYDSFRGPQQAIIEHVMAGGDALVLMPTGGGKSLCYQIPALLREGTAIVVSPLIALMQDQVAALQQNGVRAA 89
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 90 YLNSSLDYHEAVEVENRLRAGELDLLYVAPERLATARMQVLL----EQTKIALFAIDEAHCVSQWGHDFRPEYRQLSHLH 165
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLqrlpERKRLALIVVDEAHCVSQWGHDFRPDYLRLGRLR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2316072217 166 QRFPQVPRIALTATADVPTRGDIMEHLQLQEAALYNSGFD 205
Cdd:cd17920 161 RALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
6-205 |
5.61e-73 |
|
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: 232.64 E-value: 5.61e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 6 HPAALKVLQEVFGYDSFRGPQQAIIEHVMAGGDALVLMPTGGGKSLCYQIPALLREGTAIVVSPLIALMQDQVAALQQNG 85
Cdd:cd18015 3 SGKVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 86 VRAAYLNSSLDYHEAVEVENRLRAG--ELDLLYVAPERLA-TARMQVLLEQT----KIALFAIDEAHCVSQWGHDFRPEY 158
Cdd:cd18015 83 ISATMLNASSSKEHVKWVHAALTDKnsELKLLYVTPEKIAkSKRFMSKLEKAynagRLARIAIDEVHCCSQWGHDFRPDY 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2316072217 159 RQLSHLHQRFPQVPRIALTATADVPTRGDIMEHLQLQEAALYNSGFD 205
Cdd:cd18015 163 KKLGILKRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
10-199 |
5.41e-71 |
|
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: 227.14 E-value: 5.41e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 10 LKVLQEVFGYDSFRGPQQAIIEHVMAGGDALVLMPTGGGKSLCYQIPALLRE----GTAIVVSPLIALMQDQVAALQQnG 85
Cdd:cd18018 1 LKLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRrrgpGLTLVVSPLIALMKDQVDALPR-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 86 VRAAYLNSSLDYHEAVEVENRLRAGELDLLYVAPERLATARMQVLLEQTK-IALFAIDEAHCVSQWGHDFRPEYRQLSHL 164
Cdd:cd18018 80 IKAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTPpISLLVVDEAHCISEWSHNFRPDYLRLCRV 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 2316072217 165 HQRFPQVPRI-ALTATADVPTRGDIMEHLQLQEAAL 199
Cdd:cd18018 160 LRELLGAPPVlALTATATKRVVEDIASHLGIPESGV 195
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
10-205 |
7.16e-60 |
|
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: 198.51 E-value: 7.16e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 10 LKVLQEVFGYDSFRGPQQAIIEHVMAGGDALVLMPTGGGKSLCYQIPALLREGTAIVVSPLIALMQDQVAALQQNGVRAA 89
Cdd:cd18016 6 MKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPAT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 90 YLNSSLDYHEAVEVENRLRAGE--LDLLYVAPERL-ATAR----MQVLLEQTKIALFAIDEAHCVSQWGHDFRPEYRQLS 162
Cdd:cd18016 86 YLTGDKTDAEATKIYLQLSKKDpiIKLLYVTPEKIsASNRlistLENLYERKLLARFVIDEAHCVSQWGHDFRPDYKRLN 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2316072217 163 HLHQRFPQVPRIALTATADVPTRGDIMEHLQLQEAALYNSGFD 205
Cdd:cd18016 166 MLRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
206-338 |
2.00e-59 |
|
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: 194.35 E-value: 2.00e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 206 RPNIRYHIAENQGNAKE-QLLRFIREHHDGEAGIVYCLSRRKVEETAAWLERQGLTALPYHAGLPPEQRQHHQTRFLRED 284
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKlDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2316072217 285 GVVVVATIAFGMGIDKPDVRFVAHLNLPKSIEAYYQETGRAGRDGLPADAWMAY 338
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
10-196 |
1.02e-55 |
|
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: 187.29 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 10 LKVLQEVFGYDSFRGPQQ--AIIEHVMAGGDALVLMPTGGGKSLCYQIPALLREGTAIVVSPLIALMQDQVAALQQNGVR 87
Cdd:cd18014 1 RSTLKKVFGHSDFKSPLQekATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 88 AAYLNSSLDYHEAVEVENRLRAG--ELDLLYVAPERLATARMQVLLEQ----TKIALFAIDEAHCVSQWGHDFRPEYRQL 161
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADLESEkpQTKFLYITPEMAATSSFQPLLSSlvsrNLLSYLVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190
....*....|....*....|....*....|....*
gi 2316072217 162 SHLHQRFPQVPRIALTATADVPTRGDIMEHLQLQE 196
Cdd:cd18014 161 GALRSRYGHVPWVALTATATPQVQEDIFAQLRLKK 195
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
10-205 |
1.43e-54 |
|
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: 183.82 E-value: 1.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 10 LKVLQEVFGYDSFRGPQQAIIEHVMAGG-DALVLMPTGGGKSLCYQIPALLREGTAIVVSPLIALMQDQVAALQQNGVRA 88
Cdd:cd18017 1 LNALNEYFGHSSFRPVQWKVIRSVLEERrDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 89 AYLNSsldyHEAVEVENRLRAGELDLLYVAPErlATARMQVLLEQ--TKIALFAIDEAHCVSQWGHDFRPEYRQLSHLHQ 166
Cdd:cd18017 81 CFLGS----AQSQNVLDDIKMGKIRVIYVTPE--FVSKGLELLQQlrNGITLIAIDEAHCVSQWGHDFRSSYRHLGSIRN 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 2316072217 167 RFPQVPRIALTATADVPTRGDIMEHLQLQEAALYNSGFD 205
Cdd:cd18017 155 RLPNVPIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| DpdF |
NF041063 |
protein DpdF; |
12-353 |
1.07e-51 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 190.51 E-value: 1.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 12 VLQEVFGYDSFRGP-QQAIIEHVM---AGGDALVLMPTGGGKSLCYQIPALL---REGTAIVVSPLIALMQDQVAALQQN 84
Cdd:NF041063 130 FLAEALGFTHYRSPgQREAVRAALlapPGSTLIVNLPTGSGKSLVAQAPALLasrQGGLTLVVVPTVALAIDQERRAREL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 85 GVRA-AYLNSSLDYH------EAVEVENRLRAGELDLLYVAPERLATARMQVLLEQTK---IALFAIDEAHCVSQWGHDF 154
Cdd:NF041063 210 LRRAgPDLGGPLAWHgglsaeERAAIRQRIRDGTQRILFTSPESLTGSLRPALFDAAEaglLRYLVVDEAHLVDQWGDGF 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 155 RPEYRQLSHLHQRF------PQVPR-IALTATADVPTRgDIMEHL--QLQEAALYNSGFDRPNIRYHIA--ENQGNAKEQ 223
Cdd:NF041063 290 RPEFQLLAGLRRSLlrlapsGRPFRtLLLSATLTESTL-DTLETLfgPPGPFIVVSAVQLRPEPAYWVAkcDSEEERRER 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 224 LLRFIRehHDGEAGIVYCLSRRKVEETAAWLERQGLT--ALpYHAGLPPEQRQHhQTRFLREDGV-VVVATIAFGMGIDK 300
Cdd:NF041063 369 VLEALR--HLPRPLILYVTKVEDAEAWLQRLRAAGFRrvAL-FHGDTPDAERER-LIEQWRENELdIVVATSAFGLGMDK 444
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2316072217 301 PDVRFVAHLNLPKSIEAYYQETGRAGRDGLPADAWMAYGLQDVITLRQMQQDS 353
Cdd:NF041063 445 SDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDIAKSLNRPK 497
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
405-512 |
1.29e-49 |
|
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: 167.33 E-value: 1.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 405 PPETWEATVAAQKALSCVYRTEQRFGVTYLVDVLLGKHNERITRFGHDRLSTFGIGKELSANEWKALFRQLIASGYLSVD 484
Cdd:pfam09382 1 PPETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVD 80
|
90 100
....*....|....*....|....*...
gi 2316072217 485 MEGHGGIKLTANAKPVLRGEHSLTLRKP 512
Cdd:pfam09382 81 IEFYSVLKLTPKAREVLKGEEKVMLRVP 108
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
411-501 |
1.53e-43 |
|
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: 150.32 E-value: 1.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 411 ATVAAQKALSCVYRTEQRFGVTYLVDVLLGKHNERITRFGHDRLSTFGIGKELSANEWKALFRQLIASGYLSVDMEGHGG 490
Cdd:smart00956 2 VTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYPY 81
|
90
....*....|.
gi 2316072217 491 IKLTANAKPVL 501
Cdd:smart00956 82 LKLTEKARPVL 92
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
26-181 |
1.58e-26 |
|
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: 105.79 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 26 QQAIIEHVMAGGDALVLMPTGGGKSLCYQIPAL------LREGTAIVVSPLIALMQDQVAALQQNGvRAAYLNSSLDYHE 99
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLG-KGLGLKVASLLGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 100 AVEVENRLRAGELDLLYVAPERLATarmqvLLEQTK----IALFAIDEAHCVSQWGhdFRPEYRQ-LSHLHqrfPQVPRI 174
Cdd:pfam00270 83 DSRKEQLEKLKGPDILVGTPGRLLD-----LLQERKllknLKLLVLDEAHRLLDMG--FGPDLEEiLRRLP---KKRQIL 152
|
....*..
gi 2316072217 175 ALTATAD 181
Cdd:pfam00270 153 LLSATLP 159
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
340-403 |
1.26e-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: 96.98 E-value: 1.26e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2316072217 340 LQDVITLRQMQQDSSAADQQKRIEQQKLDAMLGLCE-IISCRRQALLHYFGDHLNS-PCGNCDNCL 403
Cdd:pfam16124 1 YQDVVRLRFLIEQSEADEERKEVELQKLQAMVAYCEnTTDCRRKQLLRYFGEEFDSePCGNCDNCL 66
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
15-185 |
6.89e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 99.49 E-value: 6.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 15 EVFGYDSFRGPQQAIIEHVMAG-GDALVLMPTGGGKSLCYQIPALLR-----EGTAIVVSPLIALMQDQVAALQQ----N 84
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKlgpsL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 85 GVRAAYLNSSLDYHEAVEvenRLRAGELDLLYVAPERLATARMQVLLEQTKIALFAIDEAHCVSQWGhdFRPEYRQLshL 164
Cdd:smart00487 82 GLKVVGLYGGDSKREQLR---KLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKL--L 154
|
170 180
....*....|....*....|.
gi 2316072217 165 HQRFPQVPRIALTATADVPTR 185
Cdd:smart00487 155 KLLPKNVQLLLLSATPPEEIE 175
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
248-329 |
5.76e-21 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 87.27 E-value: 5.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 248 EETAAWLERQGLTALPYHAGLPPEQRQHHQTRFLREDGVVVVATIAFGMGIDKPDVRFVAHLNLPKSIEAYYQETGRAGR 327
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 2316072217 328 DG 329
Cdd:smart00490 81 AG 82
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
222-329 |
3.64e-20 |
|
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: 85.73 E-value: 3.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 222 EQLLRFIREHHDGEAgIVYCLSRRKVEETAAwLERQGLTALPYHAGLPPEQRQHHQTRFLREDGVVVVATIAFGMGIDKP 301
Cdd:pfam00271 4 EALLELLKKERGGKV-LIFSQTKKTLEAELL-LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLP 81
|
90 100
....*....|....*....|....*...
gi 2316072217 302 DVRFVAHLNLPKSIEAYYQETGRAGRDG 329
Cdd:pfam00271 82 DVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
531-598 |
8.13e-20 |
|
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: 83.35 E-value: 8.13e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2316072217 531 HGELWEALRQHRRKLAEAQGVPAYVIFHDATLAELVEQNPQNMEALGAISGIGTRKLADYGEGFLAVI 598
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
36-179 |
5.35e-19 |
|
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: 83.99 E-value: 5.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 36 GGDALVLMPTGGGKSLCYQIPALLR----EGTAIVVSPLIALMQDQVAALQQ---NGVRAAYLNSSLDYHEavevENRLR 108
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLllkkGKKVLVLVPTKALALQTAERLRElfgPGIRVAVLVGGSSAEE----REKNK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316072217 109 AGELDLLYVAPERLATARMQ-VLLEQTKIALFAIDEAHCVSQWGHDFRPEYrqLSHLHQRFPQVPRIALTAT 179
Cdd:cd00046 77 LGDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALILD--LAVRKAGLKNAQVILLSAT 146
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
26-329 |
1.50e-17 |
|
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: 86.43 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 26 QQAIIEHVMAGGDALVLMPTGGGKSLCYQIPALL-----REGTAIVVSPLIALMQDQVAALQQ------NGVRAAylnss 94
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEalledPGATALYLYPTKALARDQLRRLRElaealgLGVRVA----- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 95 lDYHEAVEVENRLRAGE--------LDLLYVAperlatarmqVLLEQTKIALF-------AIDEAHcvsqwghdfrpEYR 159
Cdd:COG1205 136 -TYDGDTPPEERRWIREhpdivltnPDMLHYG----------LLPHHTRWARFfrnlryvVIDEAH-----------TYR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 160 QL--SHLH------QRF-------PQVprIALTATADVPTrgdimEHLQ------------------LQEAALYNSGFDR 206
Cdd:COG1205 194 GVfgSHVAnvlrrlRRIcrhygsdPQF--ILASATIGNPA-----EHAErltgrpvtvvdedgsprgERTFVLWNPPLVD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 207 PNIR-YHIAEnqgnAKEQLLRFIREHHdgeAGIVYCLSRRKVEETAAWLERQ------GLTALPYHAGLPPEQRQHHQTR 279
Cdd:COG1205 267 DGIRrSALAE----AARLLADLVREGL---RTLVFTRSRRGAELLARYARRAlrepdlADRVAAYRAGYLPEERREIERG 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2316072217 280 FLREDGVVVVATIAFGMGIDKPDVRFVAHLNLPKSIEAYYQETGRAGRDG 329
Cdd:COG1205 340 LRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRG 389
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
23-325 |
1.44e-15 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 80.07 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 23 RGPQQAIIEHVMA-----GGDALVLMPTGGGKSL----CYQipALLREGTAIVVSPLIALMQDQVAALQQngvraaYLNS 93
Cdd:COG1061 82 RPYQQEALEALLAalergGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEELRR------FLGD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 94 SLDYHEAVEVENRLrageldllYVAPerLATARMQVLLEQTK--IALFAIDEAHcvsqwgHDFRPEYRQLShlhQRFPQV 171
Cdd:COG1061 154 PLAGGGKKDSDAPI--------TVAT--YQSLARRAHLDELGdrFGLVIIDEAH------HAGAPSYRRIL---EAFPAA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 172 PRIALTATadvPTRGDIME-----------HLQLQEAA-----------LYNSGFDRPNIRY---------HIAENQGNA 220
Cdd:COG1061 215 YRLGLTAT---PFRSDGREillflfdgivyEYSLKEAIedgylappeyyGIRVDLTDERAEYdalserlreALAADAERK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 221 KEQLLRFIREHHDGEAGIVYCLSRRKVEETAAWLERQGLTALPYHAGLPPEQRQHHQTRFLREDGVVVVATIAFGMGIDK 300
Cdd:COG1061 292 DKILRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDV 371
|
330 340
....*....|....*....|....*
gi 2316072217 301 PDVRFVAHLNLPKSIEAYYQETGRA 325
Cdd:COG1061 372 PRLDVAILLRPTGSPREFIQRLGRG 396
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
221-330 |
7.79e-15 |
|
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: 71.38 E-value: 7.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 221 KEQLLRFIREHHDGEAGIVYCLSRRKVEETAAWLERQGLTALPYHAGLPPEQRQHHQTRFLREDGVVVVATIAFGMGIDK 300
Cdd:cd18787 14 KLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAARGLDI 93
|
90 100 110
....*....|....*....|....*....|...
gi 2316072217 301 PDVRFVAHLNLPKSIEAYYQ---ETGRAGRDGL 330
Cdd:cd18787 94 PGVDHVINYDLPRDAEDYVHrigRTGRAGRKGT 126
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
6-330 |
2.29e-14 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 75.57 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 6 HPAALKVLQEVfGYDSfrgP---QQAIIEHVMAGGDALVLMPTGGGKSLCYQIPAL--LREGT-----AIVVSP---LIa 72
Cdd:COG0513 10 SPPLLKALAEL-GYTT---PtpiQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLqrLDPSRprapqALILAPtreLA- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 73 lMQ--DQVAALQQN-GVRAAYLNSSLDYHEAVEvenRLRAGeLDLLyVA-PERLATarmqvLLEQTKIALFAI-----DE 143
Cdd:COG0513 85 -LQvaEELRKLAKYlGLRVATVYGGVSIGRQIR---ALKRG-VDIV-VAtPGRLLD-----LIERGALDLSGVetlvlDE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 144 AhcvsqwghD------FRPEYRQ-LSHLhqrfPQVPRIAL-TATADVPTR---GDIMEHLQLQEAAlyNSGFDRPNIRYH 212
Cdd:COG0513 154 A--------DrmldmgFIEDIERiLKLL----PKERQTLLfSATMPPEIRklaKRYLKNPVRIEVA--PENATAETIEQR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 213 IAENQGNAKEQLLRFIREHHDGEAGIVYCLSRRKVEETAAWLERQGLTALPYHAGLPPEQRQHHQTRFLREDGVVVVAT- 291
Cdd:COG0513 220 YYLVDKRDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATd 299
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2316072217 292 IAfGMGIDKPDVRFVAHLNLPKSIEAYyq---eTGRAGRDGL 330
Cdd:COG0513 300 VA-ARGIDIDDVSHVINYDLPEDPEDYvhrigrTGRAGAEGT 340
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
533-603 |
4.59e-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: 4.59e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2316072217 533 ELWEALRQHRRKLAEAQGVPAYVIFHDATLAELVEQNPQNMEALGAISGIGTRKLADYGEGFLAVILAHQK 603
Cdd:smart00341 6 RLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEASD 76
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
15-334 |
1.28e-11 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 67.12 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 15 EVFGYDSFRGPQQAIIEHVMAGGDALVLMPTGGGKSLCYQIPALLREGT-------------AIVVSP---LIALMQDQv 78
Cdd:PLN00206 137 ETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTirsghpseqrnplAMVLTPtreLCVQVEDQ- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 79 aalqqngvrAAYLNSSLDYHEAVEVEN--------RLRAGeLDLLYVAPERLATARMQVLLEQTKIALFAIDEAHCVSQW 150
Cdd:PLN00206 216 ---------AKVLGKGLPFKTALVVGGdampqqlyRIQQG-VELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLER 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 151 GhdFRPEYRQLSH-LHQrfPQVpriaLTATADVPTRGDIMEHLQLQEAALYNSGF-DRPNIRYH---IAENQGNAKEQLL 225
Cdd:PLN00206 286 G--FRDQVMQIFQaLSQ--PQV----LLFSATVSPEVEKFASSLAKDIILISIGNpNRPNKAVKqlaIWVETKQKKQKLF 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 226 RFIR-EHHDGEAGIVYCLSRRKVEETA-AWLERQGLTALPYHAGLPPEQRQHHQTRFLREDGVVVVATIAFGMGIDKPDV 303
Cdd:PLN00206 358 DILKsKQHFKPPAVVFVSSRLGADLLAnAITVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRV 437
|
330 340 350
....*....|....*....|....*....|.
gi 2316072217 304 RFVAHLNLPKSIEAYYQETGRAGRDGLPADA 334
Cdd:PLN00206 438 RQVIIFDMPNTIKEYIHQIGRASRMGEKGTA 468
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
7-329 |
2.44e-11 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 66.12 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 7 PAALKVLQEVfGYDSFRGPQQAIIEHVMAGGDALVLMPTGGGKSLCYQIPALL--------REGTA--IVVSPLIAL-MQ 75
Cdd:PRK11192 10 ESLLEALQDK-GYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQhlldfprrKSGPPriLILTPTRELaMQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 76 --DQVAALQQN----------GVraAYLNssldyHEAVEVENrlrageLDLLYVAPERLatarMQVLLEQ----TKIALF 139
Cdd:PRK11192 89 vaDQARELAKHthldiatitgGV--AYMN-----HAEVFSEN------QDIVVATPGRL----LQYIKEEnfdcRAVETL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 140 AIDEAHCVSQWGhdfrpeyrqlshlhqrFPQ-VPRIAL-----------TATADVPTRGDIMEHLqLQEAALYN---SGF 204
Cdd:PRK11192 152 ILDEADRMLDMG----------------FAQdIETIAAetrwrkqtllfSATLEGDAVQDFAERL-LNDPVEVEaepSRR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 205 DRPNIR--YHIAENQgNAKEQLLRFIREHHDGEAGIVYCLSRRKVEETAAWLERQGLTALPYHAGLPPEQRQHHQTRFlr 282
Cdd:PRK11192 215 ERKKIHqwYYRADDL-EHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRL-- 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2316072217 283 EDGVV--VVATIAFGMGIDKPDVRFVAHLNLPKSIEAYYQE---TGRAGRDG 329
Cdd:PRK11192 292 TDGRVnvLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRigrTGRAGRKG 343
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
238-332 |
5.30e-10 |
|
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: 58.04 E-value: 5.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 238 IVYCLSRRKVEETAAWLeRQGLTALP--------YHAGLPPEQRQHHQTRFLREDGVVVVATIAFGMGIDKPDVRFVAHL 309
Cdd:cd18797 39 IVFCRSRKLAELLLRYL-KARLVEEGplaskvasYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLA 117
|
90 100
....*....|....*....|...
gi 2316072217 310 NLPKSIEAYYQETGRAGRDGLPA 332
Cdd:cd18797 118 GYPGSLASLWQQAGRAGRRGKDS 140
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
17-330 |
1.49e-09 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 60.68 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 17 FGYDSFRGPQQAIIE-HVMAGGDALVLMPTGGGKSLCYQIP---ALLREGTAIVVSPLIAL----MQDQVAALQQNGVRA 88
Cdd:COG1204 18 RGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAilkALLNGGKALYIVPLRALasekYREFKRDFEELGIKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 89 AYlnSSLDYheaveVENRLRAGELDLLYVAPErlataRMQVLLEQ-----TKIALFAIDEAHCVsqwGHDFR-PEYRQ-L 161
Cdd:COG1204 98 GV--STGDY-----DSDDEWLGRYDILVATPE-----KLDSLLRNgpswlRDVDLVVVDEAHLI---DDESRgPTLEVlL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 162 SHLHQRFPQVPRIALTATadVPTRGDIMEHLqlqEAALYNSGFdRPNIRY---------HIAENQGNAKEQLLRFIREH- 231
Cdd:COG1204 163 ARLRRLNPEAQIVALSAT--IGNAEEIAEWL---DAELVKSDW-RPVPLNegvlydgvlRFDDGSRRSKDPTLALALDLl 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 232 HDGEAGIVYCLSRRKVEETAAWL-----------ERQGLTALPY--------------------------HAGLPPEQRQ 274
Cdd:COG1204 237 EEGGQVLVFVSSRRDAESLAKKLadelkrrltpeEREELEELAEellevseethtnekladclekgvafhHAGLPSELRR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 275 hhqtrfLREDGV------VVVAT--IAFGmgidkpdvrfvahLNLP-----------------KSIEaYYQETGRAGRDG 329
Cdd:COG1204 317 ------LVEDAFreglikVLVATptLAAG-------------VNLParrviirdtkrggmvpiPVLE-FKQMAGRAGRPG 376
|
.
gi 2316072217 330 L 330
Cdd:COG1204 377 Y 377
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
26-81 |
7.06e-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: 55.67 E-value: 7.06e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2316072217 26 QQAIIEHVMAGGDALVLMPTGGGKSLCYQIP---ALLRE--GTAIVVSPLIALMQDQVAAL 81
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPileALLRDpgSRALYLYPTKALAQDQLRSL 65
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
287-329 |
5.05e-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: 50.40 E-value: 5.05e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2316072217 287 VVVATIAFGMGIDKPDVRFVAHLNLPKSIEAYYQETGRAGRDG 329
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGG 67
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
168-327 |
3.97e-07 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 53.36 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 168 FPQVPRIALTATADVPtrGDIMEHLQLqEAALYNsgfDRP-NIRYHIAENQGNAKEQLL-RFIREHHD-----GEAG--I 238
Cdd:COG1202 358 CPGAQWIYLSATVGNP--EELAKKLGA-KLVEYE---ERPvPLERHLTFADGREKIRIInKLVKREFDtksskGYRGqtI 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 239 VYCLSRRKVEETAAWLerqGLTALPYHAGLPPEQRQHHQTRFLREDGVVVVATIAFGMGIDKP--DVRFVAhlnLPKSIE 316
Cdd:COG1202 432 IFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPasQVIFDS---LAMGIE 505
|
170
....*....|....*.
gi 2316072217 317 -----AYYQETGRAGR 327
Cdd:COG1202 506 wlsvqEFHQMLGRAGR 521
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
25-181 |
4.73e-07 |
|
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: 50.34 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 25 PQQAIIEHVMAGGDALVL-MPTGGGKSLC--YQIPALLRE--GTAIVVSPLIALMqDQVAA-----LQQNGVRAAYLNSS 94
Cdd:cd17921 5 IQREALRALYLSGDSVLVsAPTSSGKTLIaeLAILRALATsgGKAVYIAPTRALV-NQKEAdlrerFGPLGKNVGLLTGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 95 ldyheavEVENRLRAGELDLLYVAPERL--ATARMQVLLEQtKIALFAIDEAHCVSQwghdfrPEY-----RQLSHLHQR 167
Cdd:cd17921 84 -------PSVNKLLLAEADILVATPEKLdlLLRNGGERLIQ-DVRLVVVDEAHLIGD------GERgvvleLLLSRLLRI 149
|
170
....*....|....
gi 2316072217 168 FPQVPRIALTATAD 181
Cdd:cd17921 150 NKNARFVGLSATLP 163
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
11-351 |
9.14e-07 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 51.37 E-value: 9.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 11 KVLQEVFGYdSFRGP---QQAIIEHVMAGGDALVLMPTGGGKSLCYQIPALLREGTAIVVSPLIALMQDQVAALQQNGVR 87
Cdd:PTZ00424 38 DLLRGIYSY-GFEKPsaiQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELAQQIQKVV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 88 AA---YLNssLDYHEAV------EVENRLRAGeLDLLYVAPERLATARMQVLLEQTKIALFAIDEAHCVSQWGhdFRPey 158
Cdd:PTZ00424 117 LAlgdYLK--VRCHACVggtvvrDDINKLKAG-VHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRG--FKG-- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 159 rQLSHLHQRFPQVPRIALTaTADVPTrgDIME----------HLQLQEAALYNSGfdrpnIR-YHIAENQGNAKEQLLRF 227
Cdd:PTZ00424 190 -QIYDVFKKLPPDVQVALF-SATMPN--EILElttkfmrdpkRILVKKDELTLEG-----IRqFYVAVEKEEWKFDTLCD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 228 IREHHDGEAGIVYCLSRRKVEETAAWLERQGLTALPYHAGLPPEQRQHHQTRFLREDGVVVVATIAFGMGIDKPDVRFVA 307
Cdd:PTZ00424 261 LYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVI 340
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2316072217 308 HLNLPKSIEAYYQETGRAGRDGLPADAWMAYGLQDVITLRQMQQ 351
Cdd:PTZ00424 341 NYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIER 384
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
18-329 |
1.01e-06 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 51.77 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 18 GYDSFRGPQQAIIEHVMAGGDALVLMPTGGGKSLCYQIPAL------LREGTAIVVSPLIALMQdQVA------ALQQNG 85
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLhnldpeLKAPQILVLAPTRELAV-QVAeamtdfSKHMRG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 86 VRAAYLNSSLDYheavEVENR-LRAGElDLLYVAPERLATARMQVLLEQTKIALFAIDEAHCVSQWGHdfrpeyrqLSHL 164
Cdd:PRK11634 104 VNVVALYGGQRY----DVQLRaLRQGP-QIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGF--------IEDV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 165 HQRFPQVPRIALTA--TADVP------TRGDIMEHlqlQEAALYNSGFDRPNIRYHIAENQGNAK-EQLLRFIrEHHDGE 235
Cdd:PRK11634 171 ETIMAQIPEGHQTAlfSATMPeairriTRRFMKEP---QEVRIQSSVTTRPDISQSYWTVWGMRKnEALVRFL-EAEDFD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 236 AGIVYCLSRRKVEETAAWLERQGLTALPYHAGLppEQRQHHQTRFLREDGV--VVVATIAFGMGIDKPDVRFVAHLNLPK 313
Cdd:PRK11634 247 AAIIFVRTKNATLEVAEALERNGYNSAALNGDM--NQALREQTLERLKDGRldILIATDVAARGLDVERISLVVNYDIPM 324
|
330
....*....|....*.
gi 2316072217 314 SIEAYYQETGRAGRDG 329
Cdd:PRK11634 325 DSESYVHRIGRTGRAG 340
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
6-329 |
7.75e-06 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 48.76 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 6 HPAALKVLQEVfGYDSFRGPQQAIIEHVMAGGDALVLMPTGGGKSLCYQIPAL-------------LREGTAIVVSP--- 69
Cdd:PRK01297 95 APELMHAIHDL-GFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIInqllqtpppkeryMGEPRALIIAPtre 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 70 -LIALMQDQVAALQQNGVRAAYLNSSLDYHEAVEvenRLRAGELDLLYVAPERLA--TARMQVLLEQtkIALFAIDEAHC 146
Cdd:PRK01297 174 lVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLK---QLEARFCDILVATPGRLLdfNQRGEVHLDM--VEVMVLDEADR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 147 VSQWGhdFRPEYRQLshLHQRFPQVPRIAL----TATADV-------PTRGDIMEHLQLQEAAlynsgfdrPNIRYHIAE 215
Cdd:PRK01297 249 MLDMG--FIPQVRQI--IRQTPRKEERQTLlfsaTFTDDVmnlakqwTTDPAIVEIEPENVAS--------DTVEQHVYA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 216 NQGNAKEQLLRFIREHHDGEAGIVYCLSRRKVEETAAWLERQGLTAlpyhAGLPPEQRQHHQTRFL---REDGV-VVVAT 291
Cdd:PRK01297 317 VAGSDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINA----AQLSGDVPQHKRIKTLegfREGKIrVLVAT 392
|
330 340 350
....*....|....*....|....*....|....*...
gi 2316072217 292 IAFGMGIDKPDVRFVAHLNLPKSIEAYYQETGRAGRDG 329
Cdd:PRK01297 393 DVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAG 430
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
226-327 |
2.25e-05 |
|
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: 44.56 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 226 RFIREHHDGEAGIVYCLSRRKVEETAAWL------ERQGLTALPYHAGLPPEQRQHHQTRFLREDGVVVVATIAFGMGID 299
Cdd:cd18796 30 EVIFLLERHKSTLVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGID 109
|
90 100
....*....|....*....|....*...
gi 2316072217 300 KPDVRFVAHLNLPKSIEAYYQETGRAGR 327
Cdd:cd18796 110 IGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
6-334 |
5.52e-05 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 46.10 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 6 HPAALKVLQEVfGYdSFRGPQQAIIEHV-MAGGDALVLMPTGGGKSLCYQI---------PALL----REGTAIVVSPL- 70
Cdd:PRK04537 17 HPALLAGLESA-GF-TRCTPIQALTLPVaLPGGDVAGQAQTGTGKTLAFLVavmnrllsrPALAdrkpEDPRALILAPTr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 71 ---IALMQDQVAALQQNGVRAAYLNSSLDYHEAVEVenrLRAGeLDLLYVAPERLATARMQ---VLLEQTKIALfaIDEA 144
Cdd:PRK04537 95 elaIQIHKDAVKFGADLGLRFALVYGGVDYDKQREL---LQQG-VDVIIATPGRLIDYVKQhkvVSLHACEICV--LDEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 145 HCVSQWGHdfrpeYRQLSHLHQRFPQ-VPRIALTATADVPTRGDIM--EHL-QLQEAALYNSGFDRPNIRYHIAENQGNA 220
Cdd:PRK04537 169 DRMFDLGF-----IKDIRFLLRRMPErGTRQTLLFSATLSHRVLELayEHMnEPEKLVVETETITAARVRQRIYFPADEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 221 KEQLLRFIREHHDGEAGIVYCLSRRKVEETAAWLERQGLTALPYHAGLPPEQRQHHQTRFLREDGVVVVATIAFGMGIDK 300
Cdd:PRK04537 244 KQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHI 323
|
330 340 350
....*....|....*....|....*....|....
gi 2316072217 301 PDVRFVAHLNLPKSIEAYYQETGRAGRDGLPADA 334
Cdd:PRK04537 324 DGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDA 357
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
25-202 |
1.10e-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: 43.09 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 25 PQQAIIEHVMAGGDALVL-MPTGGGKSLCYQ---IPALLREGTAIVVSPLIALMQDQV---AALQQNGVRAAYlnSSLDY 97
Cdd:cd18028 5 PQAEAVRAGLLKGENLLIsIPTASGKTLIAEmamVNTLLEGGKALYLVPLRALASEKYeefKKLEEIGLKVGI--STGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 98 HEAVEvenrlRAGELDLLYVAPERLATarmqvLLEQTK-----IALFAIDEAHCVSQWGHDFRPEYrQLSHLHQRFPQVP 172
Cdd:cd18028 83 DEDDE-----WLGDYDIIVATYEKFDS-----LLRHSPswlrdVGVVVVDEIHLISDEERGPTLES-IVARLRRLNPNTQ 151
|
170 180 190
....*....|....*....|....*....|
gi 2316072217 173 RIALTATadVPTRGDIMEHLqlqEAALYNS 202
Cdd:cd18028 152 IIGLSAT--IGNPDELAEWL---NAELVES 176
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
22-179 |
1.46e-04 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part 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: 350684 [Multi-domain] Cd Length: 146 Bit Score: 42.29 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 22 FRGPQQ----AIIEHVmAGGDALVLMPTGGGKSLC-YQIPALLREGTAIVVSPLIALMQDQVAALQQngvraAYLNSSLd 96
Cdd:cd17926 1 LRPYQEealeAWLAHK-NNRRGILVLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFED-----FLGDSSI- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 97 yheaveveNRLRAGELDLLYVAPERLATarMQVL---LEQTKI-----ALFAIDEAHCVSQwghdfrpeyRQLSHLHQRF 168
Cdd:cd17926 74 --------GLIGGGKKKDFDDANVVVAT--YQSLsnlAEEEKDlfdqfGLLIVDEAHHLPA---------KTFSEILKEL 134
|
170
....*....|.
gi 2316072217 169 PQVPRIALTAT 179
Cdd:cd17926 135 NAKYRLGLTAT 145
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
215-329 |
1.59e-04 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 44.76 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 215 ENQGNAKEQLLRFIRehhDGEAGIVYCLSRRKVEETAAWLERQGLTALPYHAGLPPEQRQHHQTRFLREDGVVVVATIAF 294
Cdd:PTZ00110 361 EKRGKLKMLLQRIMR---DGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVA 437
|
90 100 110
....*....|....*....|....*....|....*
gi 2316072217 295 GMGIDKPDVRFVAHLNLPKSIEAYYQETGRAGRDG 329
Cdd:PTZ00110 438 SRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAG 472
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
238-330 |
2.57e-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: 41.77 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 238 IVYCLSRRKVEETAAWLerQGLTAlpYHAGLPPEQRQhhqtrfLREDG------VVVVATIAFGMGIDKPdvrfvAHLNL 311
Cdd:cd18795 47 LVFCSSRKECEKTAKDL--AGIAF--HHAGLTREDRE------LVEELfregliKVLVATSTLAAGVNLP-----ARTVI 111
|
90 100 110
....*....|....*....|....*....|..
gi 2316072217 312 PKSIEA-------------YYQETGRAGRDGL 330
Cdd:cd18795 112 IKGTQRydgkgyrelspleYLQMIGRAGRPGF 143
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
239-333 |
6.42e-04 |
|
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene encodes a DNA and RNA helicase, which is localized in mitochondria and is a subunit of the degradosome complex involved in regulation of RNA surveillance and turnover. SUV3 exhibits DNA and RNA-dependent ATPase, DNA and RNA-binding and DNA and RNA unwinding activities. SUV3 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: 350192 [Multi-domain] Cd Length: 135 Bit Score: 40.23 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 239 VYCLSRRKVEETAAWLERQ-GL-TALPYhAGLPPEQRQHHQTRFLREDGV--VVVATIAFGMG------------IDKPD 302
Cdd:cd18805 22 VVAFSRKDIFSLKREIEKRtGLkCAVIY-GALPPETRRQQARLFNDPESGydVLVASDAIGMGlnlnirrvifssLSKFD 100
|
90 100 110
....*....|....*....|....*....|.
gi 2316072217 303 VRFVAHLnlpkSIEAYYQETGRAGRDGLPAD 333
Cdd:cd18805 101 GNEMRPL----SPSEVKQIAGRAGRFGSHFP 127
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
18-327 |
7.19e-04 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 42.49 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 18 GYDSFRGPQQAIIEHVMAGGDALVLMPTGGGKSLCYQIPALLREGTAIV-------VSPLIALMQDQVAALQQNGVR--A 88
Cdd:PRK10590 20 GYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPhakgrrpVRALILTPTRELAAQIGENVRdyS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 89 AYLN-SSLDYHEAVEVEN---RLRAGeLDLLYVAPERLATARMQVLLEQTKIALFAIDEAHCVSQWG--HDFRpeyRQLS 162
Cdd:PRK10590 100 KYLNiRSLVVFGGVSINPqmmKLRGG-VDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGfiHDIR---RVLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 163 HLHQRfPQVPRIALTATADVPTRGDIMEHLQLQ-EAALYNSGFDRpnIRYHIAENQGNAKEQLLRFIREHHDGEAGIVYC 241
Cdd:PRK10590 176 KLPAK-RQNLLFSATFSDDIKALAEKLLHNPLEiEVARRNTASEQ--VTQHVHFVDKKRKRELLSQMIGKGNWQQVLVFT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 242 LSRRKVEETAAWLERQGLTALPYHAglppEQRQHHQTRFL---REDGV-VVVATIAFGMGIDKPDVRFVAHLNLPKSIEA 317
Cdd:PRK10590 253 RTKHGANHLAEQLNKDGIRSAAIHG----NKSQGARTRALadfKSGDIrVLVATDIAARGLDIEELPHVVNYELPNVPED 328
|
330
....*....|
gi 2316072217 318 YYQETGRAGR 327
Cdd:PRK10590 329 YVHRIGRTGR 338
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
11-69 |
7.41e-04 |
|
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350707 [Multi-domain] Cd Length: 214 Bit Score: 41.42 E-value: 7.41e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2316072217 11 KVLQEVFGYDSFRGPQQAIIEHVMAGGDALVLMPTGGGKSLCYQIPALLR-----------EGT-AIVVSP 69
Cdd:cd17949 3 SHLKSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRllsleprvdrsDGTlALVLVP 73
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
36-179 |
8.37e-04 |
|
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: 40.26 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 36 GGDALVLMPTGGGKSLCYQIPALLR------EGTAIV-VSPLIALMQDQVAALQqngvraAYLNSSLDYheaVEVE---- 104
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSladepeKGVQVLyISPLKALINDQERRLE------EPLDEIDLE---IPVAvrhg 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 105 -------NRLRAGELDLLYVAPERLAtarmqVLLEQTKIA-LFA------IDEAHCV--SQWGHDFRPEYRQLSHLHQRf 168
Cdd:cd17922 72 dtsqsekAKQLKNPPGILITTPESLE-----LLLVNKKLReLFAglryvvVDEIHALlgSKRGVQLELLLERLRKLTGR- 145
|
170
....*....|.
gi 2316072217 169 pQVPRIALTAT 179
Cdd:cd17922 146 -PLRRIGLSAT 155
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
542-598 |
9.91e-04 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 41.78 E-value: 9.91e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2316072217 542 RRKLAEAQGVPAYVIFHDATLAELVEQNPQNMEALGAISGIGTRKLADYGEGFLAVI 598
Cdd:COG0349 220 REREARKRDVPRNRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAV 276
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
26-73 |
2.01e-03 |
|
DEAD-box helicase domain of 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 39.73 E-value: 2.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2316072217 26 QQAIIEHVMAGGDALVLMPTGGGKSLCYQIPAL--LREGTAIVVSPLIAL 73
Cdd:cd00268 17 QAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILekLLPEPKKKGRGPQAL 66
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
81-115 |
2.52e-03 |
|
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: 39.15 E-value: 2.52e-03
10 20 30
....*....|....*....|....*....|....*
gi 2316072217 81 LQQNGVRAAYLNSSLDYHEAVEVENRLRAGELDLL 115
Cdd:cd18790 47 LQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVL 81
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
10-81 |
2.85e-03 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350718 [Multi-domain] Cd Length: 202 Bit Score: 39.48 E-value: 2.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316072217 10 LKVLQEvFGYDSFRGPQQAIIEHVMAGGDALVLMPTGGGKSLCYQIPALlregtAIVVSPLIALMQDQVAAL 81
Cdd:cd17960 2 LDVVAE-LGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVL-----EILLKRKANLKKGQVGAL 67
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
21-199 |
3.20e-03 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex 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. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part 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: 350685 [Multi-domain] Cd Length: 201 Bit Score: 39.34 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 21 SFRGPQQAIIEHVMAGGDALVLMPTGGGKS-----LC----YQIPAlLREGTAIVVSPLIALMQDQVAALQQNGVRAAYL 91
Cdd:cd17927 2 KPRNYQLELAQPALKGKNTIICLPTGSGKTfvavlICehhlKKFPA-GRKGKVVFLANKVPLVEQQKEVFRKHFERPGYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 92 NSSLDYHEAVEVENRLRAGELDLLYVAPERLATARMQ-VLLEQTKIALFAIDEAHCVSQWGhdfrpEYRQLSHLH----- 165
Cdd:cd17927 81 VTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSgTIVSLSDFSLLVFDECHNTTKNH-----PYNEIMFRYldqkl 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2316072217 166 ---QRFPQVprIALTAT---ADVPTRGDIMEHLQLQEAAL 199
Cdd:cd17927 156 gssGPLPQI--LGLTASpgvGGAKNTEEALEHICKLCANL 193
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
44-207 |
5.13e-03 |
|
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.
Pssm-ID: 350784 [Multi-domain] Cd Length: 202 Bit Score: 38.74 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 44 PTGGGKSLCYQI----PALLREGTAIVVSPLIALMQDQVAALQQngvraayLNSSLDYHeaveVEN---------RLRAG 110
Cdd:cd18026 41 PTSGGKTLVAEIlmlkRLLERRKKALFVLPYVSIVQEKVDALSP-------LFEELGFR----VEGyagnkgrspPKRRK 109
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316072217 111 ELDLLYVAPERlATARMQVLLEQTK---IALFAIDEAHCVSQwghdfrpEYR---------QLSHLHQRFPQVprIALTA 178
Cdd:cd18026 110 SLSVAVCTIEK-ANSLVNSLIEEGRldeLGLVVVDELHMLGD-------GHRgallellltKLLYAAQKNIQI--VGMSA 179
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170 180
....*....|....*....|....*....
gi 2316072217 179 TadVPTRGDIMEHLQlqeAALYNSGFdRP 207
Cdd:cd18026 180 T--LPNLEELASWLR---AELYTTNF-RP 202
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