|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
1-607 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 1355.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 1 MAQAEVLNLESGAKQVLQETFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLLNGLTVVVSPLISLMKD 80
Cdd:PRK11057 1 MAQAEVLNLESLAKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 81 QVDQLQANGVAAACLNSTQTREQQLEVMTGCRTGQIRLLYIAPERLMLDNFLEHLAHWNPVLLAVDEAHCISQWGHDFRP 160
Cdd:PRK11057 81 QVDQLLANGVAAACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 161 EYAALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYMLMEKFKPLDQLMRYVQEQRGKSGI 240
Cdd:PRK11057 161 EYAALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQLMRYVQEQRGKSGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 241 IYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESY 320
Cdd:PRK11057 241 IYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 321 YQETGRAGRDGLPAEAMLFYDPADMAWLRRCLEEKPQGQLQDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNC 400
Cdd:PRK11057 321 YQETGRAGRDGLPAEAMLFYDPADMAWLRRCLEEKPAGQQQDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 401 DICLDPPKQYDGSTDAQIALSTIGRVNQRFGMGYVVEVIRGANNQRIRDYGHDKLKVYGMGRDKSHEHWVSVIRQLIHLG 480
Cdd:PRK11057 401 DICLDPPKQYDGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 481 LVTQNIAQHSALQLTEAARPVLRGESSLQLAVPRIVALKPKAMQKSFGGNYDRKLFAKLRKLRKSIADESNVPPYVVFND 560
Cdd:PRK11057 481 LVTQNIAQHSALQLTEAARPVLRGEVSLQLAVPRIVALKPRAMQKSFGGNYDRKLFAKLRKLRKSIADEENIPPYVVFND 560
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 162135918 561 ATLIEMAEQMPITASEMLSVNGVGMRKLERFGKPFMALIRAHVDGDD 607
Cdd:PRK11057 561 ATLIEMAEQMPITASEMLSVNGVGQRKLERFGKPFMALIRAHVDGDD 607
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
13-602 |
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: 1037.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 13 AKQVLQETFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLLNGLTVVVSPLISLMKDQVDQLQANGVAA 92
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 93 ACLNSTQTREQQLEVMTGCRTGQIRLLYIAPERLMLDNFLEHLAHWNPVLLAVDEAHCISQWGHDFRPEYAALGQLRQRF 172
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 173 PTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYMLMEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVEDT 252
Cdd:TIGR01389 161 PQVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 253 AARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGL 332
Cdd:TIGR01389 241 AERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 333 PAEAMLFYDPADMAWLRRCLEE-KPQGQLQDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNCDICLDPPKQYD 411
Cdd:TIGR01389 321 PAEAILLYSPADIALLKRRIEQsEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENEVEPCGNCDNCLDPPKSYD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 412 GSTDAQIALSTIGRVNQRFGMGYVVEVIRGANNQRIRDYGHDKLKVYGMGRDKSHEHWVSVIRQLIHLGLVTQNIAQHSA 491
Cdd:TIGR01389 401 ATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEIYIG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 492 LQLTEAARPVLRGESSLQLAVPRIVALKPKAMQKSFGGNYDRKLFAKLRKLRKSIADESNVPPYVVFNDATLIEMAEQMP 571
Cdd:TIGR01389 481 LQLTEAARKVLKNEVEVLLRPFKVVAKEKTRVQKNLSVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAEKRP 560
|
570 580 590
....*....|....*....|....*....|.
gi 162135918 572 ITASEMLSVNGVGMRKLERFGKPFMALIRAH 602
Cdd:TIGR01389 561 ATLNALLKIKGVGQNKLDRYGEAFLEVIREY 591
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
13-479 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 819.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 13 AKQVLQETFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLLNGLTVVVSPLISLMKDQVDQLQANGVAA 92
Cdd:COG0514 5 ALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 93 ACLNSTQTREQQLEVMTGCRTGQIRLLYIAPERLMLDNFLEHLAHWNPVLLAVDEAHCISQWGHDFRPEYAALGQLRQRF 172
Cdd:COG0514 85 AFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGELRERL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 173 PTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYMLMEKF--KPLDQLMRYVQEQRGKSGIIYCNSRAKVE 250
Cdd:COG0514 165 PNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPpdDKLAQLLDFLKEHPGGSGIVYCLSRKKVE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 251 DTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRD 330
Cdd:COG0514 245 ELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 331 GLPAEAMLFYDPADMAWLRRCLEEK-PQGQLQDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNCDICLDPPKQ 409
Cdd:COG0514 325 GLPAEALLLYGPEDVAIQRFFIEQSpPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYFGEELAEPCGNCDNCLGPPET 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 410 YDGSTDAQIALSTIGRVNQRFGMGYVVEVIRGANNQRIRDYGHDKLKVYGMGRDKSHEHWVSVIRQLIHL 479
Cdd:COG0514 405 FDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLLAQ 474
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
15-464 |
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: 802.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 15 QVLQETFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLLNGLTVVVSPLISLMKDQVDQLQANGVAAAC 94
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 95 LNSTQTREQQLEVMTGCRTGQIRLLYIAPERLMLDN-FLEHL-AHWNPVLLAVDEAHCISQWGHDFRPEYAALGQLRQRF 172
Cdd:TIGR00614 81 LNSAQTKEQQLNVLTDLKDGKIKLLYVTPEKISASNrLLQTLeERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 173 PTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYMLMEKF-KPLDQLMRYVQ-EQRGKSGIIYCNSRAKVE 250
Cdd:TIGR00614 161 PNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTpKILEDLLRFIRkEFEGKSGIIYCPSRKKVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 251 DTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRD 330
Cdd:TIGR00614 241 QVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGRD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 331 GLPAEAMLFYDPADMAWLRRCLEEKPQGQLQDIERHKLNAMGAFAEAQTCRRLVLLNYFGE----------GRQEPCGNC 400
Cdd:TIGR00614 321 GLPSECHLFYAPADMNRLRRLLMEEPDGNFRTYKLKLYEMMEYCLNSSTCRRLILLSYFGEkgfnksfcimGTEKCCDNC 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 401 DICLD------PPKQYDGSTDAQIALSTIGRVNQRFGMGYVVEVIRGANNQRIRDYGHDKLKVYGMGRDK 464
Cdd:TIGR00614 401 CKRLDyktkdvTDKVYDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGRGKDE 470
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
8-592 |
8.33e-127 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 401.97 E-value: 8.33e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 8 NLESGAKQVlqetFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLLNGLTVVVSPLISLMKDQV-DQLQ 86
Cdd:PLN03137 447 KLEVNNKKV----FGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQImNLLQ 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 87 ANgVAAACLNSTQTREQQLEVMT--GCRTGQIRLLYIAPERLML-DNFLEHLAHWNP-VLLA---VDEAHCISQWGHDFR 159
Cdd:PLN03137 523 AN-IPAASLSAGMEWAEQLEILQelSSEYSKYKLLYVTPEKVAKsDSLLRHLENLNSrGLLArfvIDEAHCVSQWGHDFR 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 160 PEYAALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYMLMEKFKP-LDQLMRYVQEQR-GK 237
Cdd:PLN03137 602 PDYQGLGILKQKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKKcLEDIDKFIKENHfDE 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 238 SGIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNI 317
Cdd:PLN03137 682 CGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSI 761
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 318 ESYYQETGRAGRDGLPAEAMLFYDPADM---------------AWLRRCLEEKPQGQLQDIERHKLNAMGAFAEAQT-CR 381
Cdd:PLN03137 762 EGYHQECGRAGRDGQRSSCVLYYSYSDYirvkhmisqggveqsPMAMGYNRMASSGRILETNTENLLRMVSYCENEVdCR 841
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 382 RLVLLNYFGEGRQEP-CGN-CDICLDPPK--QYDGSTDAQIALSTIGRVNQRFGMGYVVEVIRGANNQRIRDYGHDKLKV 457
Cdd:PLN03137 842 RFLQLVHFGEKFDSTnCKKtCDNCSSSKSliDKDVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLSL 921
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 458 YGMGRdksHEHWVSVIRQLIHlgLVTQNIAQH------------SALQLTEA-ARPVLRGESSLQLAVPRIV-ALKP--- 520
Cdd:PLN03137 922 HGAGK---HLSKGEASRILHY--LVTEDILAEdvkksdlygsvsSLLKVNESkAYKLFSGGQTIIMRFPSSVkASKPskf 996
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 521 --------------------KAMQKSFGGNYDRKLFAKLRKLRKSIADESN--VPPYVVFNDATLIEMAEQMPITASEML 578
Cdd:PLN03137 997 eatpakgpltsgkqstlpmaTPAQPPVDLNLSAILYTALRKLRTALVKEAGdgVMAYHIFGNATLQQISKRIPRTKEELL 1076
|
650
....*....|....
gi 162135918 579 SVNGVGMRKLERFG 592
Cdd:PLN03137 1077 EINGLGKAKVSKYG 1090
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
14-209 |
1.15e-112 |
|
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: 334.89 E-value: 1.15e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 14 KQVLQETFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLLNGLTVVVSPLISLMKDQVDQLQANGVAAA 93
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 94 CLNSTQTREQQLEVMTGCRTGQIRLLYIAPERLMLDNFLEHLAHWN----PVLLAVDEAHCISQWGHDFRPEYAALGQLR 169
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLRLGRLR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 162135918 170 QRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFD 209
Cdd:cd17920 161 RALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
15-200 |
1.20e-77 |
|
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: 244.86 E-value: 1.20e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 15 QVLQETFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLLN----GLTVVVSPLISLMKDQVDQLQAnGV 90
Cdd:cd18018 2 KLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRrrgpGLTLVVSPLIALMKDQVDALPR-AI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 91 AAACLNSTQTREQQLEVMTGCRTGQIRLLYIAPERLMLDNFLEHLAHWNPV-LLAVDEAHCISQWGHDFRPEYAALGQ-L 168
Cdd:cd18018 81 KAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTPPIsLLVVDEAHCISEWSHNFRPDYLRLCRvL 160
|
170 180 190
....*....|....*....|....*....|..
gi 162135918 169 RQRFPTLPFMALTATADDTTRQDIVRLLGLND 200
Cdd:cd18018 161 RELLGAPPVLALTATATKRVVEDIASHLGIPE 192
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
13-209 |
1.17e-71 |
|
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: 229.56 E-value: 1.17e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 13 AKQVLQETFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLLNGLTVVVSPLISLMKDQVDQLQANGVAA 92
Cdd:cd18015 6 VKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 93 ACLNSTQTREQQLEVMTGCRTG--QIRLLYIAPERL----MLDNFLE------HLAhwnpvLLAVDEAHCISQWGHDFRP 160
Cdd:cd18015 86 TMLNASSSKEHVKWVHAALTDKnsELKLLYVTPEKIakskRFMSKLEkaynagRLA-----RIAIDEVHCCSQWGHDFRP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 162135918 161 EYAALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFD 209
Cdd:cd18015 161 DYKKLGILKRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
210-340 |
1.30e-71 |
|
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: 226.32 E-value: 1.30e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 210 RPNIRYMLMEKFKP---LDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDD 286
Cdd:cd18794 1 RPNLFYSVRPKDKKdekLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 162135918 287 LQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFY 340
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
17-209 |
4.40e-68 |
|
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: 219.65 E-value: 4.40e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 17 LQETFGYQQFRPGQEEIIDTVL-SGRDCLVVMPTGGGKSLCYQIPALLLNGLTVVVSPLISLMKDQVDQLQANGVAAACL 95
Cdd:cd18017 4 LNEYFGHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 96 NSTQTREqqleVMTGCRTGQIRLLYIAPErlMLDNFLEHLAHWNP--VLLAVDEAHCISQWGHDFRPEYAALGQLRQRFP 173
Cdd:cd18017 84 GSAQSQN----VLDDIKMGKIRVIYVTPE--FVSKGLELLQQLRNgiTLIAIDEAHCVSQWGHDFRSSYRHLGSIRNRLP 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 162135918 174 TLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFD 209
Cdd:cd18017 158 NVPIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
15-209 |
9.50e-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: 198.13 E-value: 9.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 15 QVLQETFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLLNGLTVVVSPLISLMKDQVDQLQANGVAAAC 94
Cdd:cd18016 7 KIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 95 LNSTQTREQQLEVMTGCRTGQ--IRLLYIAPERL----MLDNFLEHLAHWNpvLLA---VDEAHCISQWGHDFRPEYAAL 165
Cdd:cd18016 87 LTGDKTDAEATKIYLQLSKKDpiIKLLYVTPEKIsasnRLISTLENLYERK--LLArfvIDEAHCVSQWGHDFRPDYKRL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 162135918 166 GQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFD 209
Cdd:cd18016 165 NMLRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
14-206 |
4.74e-56 |
|
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: 188.45 E-value: 4.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 14 KQVLQETFGYQQFR-PGQEEIIDTVLSGR-DCLVVMPTGGGKSLCYQIPALLLNGLTVVVSPLISLMKDQVDQLQANGVA 91
Cdd:cd18014 1 RSTLKKVFGHSDFKsPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 92 AACLNSTQTREQQLEVMTGCRTG--QIRLLYIAPERLMLDNF---LEHL-AHWNPVLLAVDEAHCISQWGHDFRPEYAAL 165
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADLESEkpQTKFLYITPEMAATSSFqplLSSLvSRNLLSYLVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 162135918 166 GQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQIS 206
Cdd:cd18014 161 GALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKPVAIFK 201
|
|
| DpdF |
NF041063 |
protein DpdF; |
16-346 |
1.73e-55 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 201.29 E-value: 1.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 16 VLQETFGYQQFR-PGQEEIIDTVLS---GRDCLVVMPTGGGKSLCYQIPALLL---NGLTVVVSPLISLMKDQVDQLQAN 88
Cdd:NF041063 130 FLAEALGFTHYRsPGQREAVRAALLappGSTLIVNLPTGSGKSLVAQAPALLAsrqGGLTLVVVPTVALAIDQERRAREL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 89 GVAAACL----------NSTQTREQqleVMTGCRTGQIRLLYIAPERLM--LDNFLE------HLAHwnpvlLAVDEAHC 150
Cdd:NF041063 210 LRRAGPDlggplawhggLSAEERAA---IRQRIRDGTQRILFTSPESLTgsLRPALFdaaeagLLRY-----LVVDEAHL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 151 ISQWGHDFRPEYAALGQLRQ----------RFPTLpfmALTATADDTTRQDIVRLLGLNDPLIQIS-SFDRPNIRYMLME 219
Cdd:NF041063 282 VDQWGDGFRPEFQLLAGLRRsllrlapsgrPFRTL---LLSATLTESTLDTLETLFGPPGPFIVVSaVQLRPEPAYWVAK 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 220 KFKPLDQLMRYVQEQRG--KSGIIYCNSRAKVEDTAARLQSKGIS-AAAYHAGLENNVRADVQEKFQRDDLQIVVATVAF 296
Cdd:NF041063 359 CDSEEERRERVLEALRHlpRPLILYVTKVEDAEAWLQRLRAAGFRrVALFHGDTPDAERERLIEQWRENELDIVVATSAF 438
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 162135918 297 GMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMA 346
Cdd:NF041063 439 GLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLD 488
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
406-513 |
1.09e-40 |
|
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: 143.45 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 406 PPKQYDGSTDAQIALSTIGRVNQRFGMGYVVEVIRGANNQRIRDYGHDKLKVYGMGRDKSHEHWVSVIRQLIHLGLVTQN 485
Cdd:pfam09382 1 PPETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVD 80
|
90 100
....*....|....*....|....*...
gi 162135918 486 IAQHSALQLTEAARPVLRGESSLQLAVP 513
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 ... |
411-502 |
1.51e-37 |
|
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: 134.14 E-value: 1.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 411 DGSTDAQIALSTIGRVNQRFGMGYVVEVIRGANNQRIRDYGHDKLKVYGMGRDKSHEHWVSVIRQLIHLGLVTQNIAQHS 490
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYP 80
|
90
....*....|..
gi 162135918 491 ALQLTEAARPVL 502
Cdd:smart00956 81 YLKLTEKARPVL 92
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
27-190 |
2.71e-29 |
|
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: 113.88 E-value: 2.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 27 RPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPAL-----LLNGL-TVVVSPLISLMKDQVDQLQA----NGVAAACLN 96
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdkLDNGPqALVLAPTRELAEQIYEELKKlgkgLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 97 STQTREQQLEVMTGCrtgqiRLLYIAPERLM----LDNFLEHLAhwnpvLLAVDEAHCISQWGhdFRPEYAA-LGQLRQR 171
Cdd:pfam00270 81 GGDSRKEQLEKLKGP-----DILVGTPGRLLdllqERKLLKNLK-----LLVLDEAHRLLDMG--FGPDLEEiLRRLPKK 148
|
170
....*....|....*....
gi 162135918 172 FPTlpfMALTATADDTTRQ 190
Cdd:pfam00270 149 RQI---LLLSATLPRNLED 164
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
22-368 |
1.19e-27 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 115.63 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 22 GYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALllngltvvvsplislmkDQVDQLQANGVAAACLnsTQTR 101
Cdd:COG0513 21 GYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLL-----------------QRLDPSRPRAPQALIL--APTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 102 E---------QQLEVMTGCRTG----------QIRLLY------IA-PERLM---------LDNfLEHLahwnpVLlavD 146
Cdd:COG0513 82 ElalqvaeelRKLAKYLGLRVAtvyggvsigrQIRALKrgvdivVAtPGRLLdliergaldLSG-VETL-----VL---D 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 147 EAhcisqwghD------FRPE----YAALGQLRQrfpTLPFmalTATADDttrqDIVRLLG--LNDPL-IQIS--SFDRP 211
Cdd:COG0513 153 EA--------DrmldmgFIEDieriLKLLPKERQ---TLLF---SATMPP----EIRKLAKryLKNPVrIEVApeNATAE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 212 NI--RYMLMEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQI 289
Cdd:COG0513 215 TIeqRYYLVDKRDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 290 VVAT-VAfGMGINKPNVRFVVHFDIPRNIESYyq---eTGRAGRDGlpaEAMLFYDPADMAWLRRcLEEKPQgqlQDIER 365
Cdd:COG0513 295 LVATdVA-ARGIDIDDVSHVINYDLPEDPEDYvhrigrTGRAGAEG---TAISLVTPDERRLLRA-IEKLIG---QKIEE 366
|
...
gi 162135918 366 HKL 368
Cdd:COG0513 367 EEL 369
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
19-215 |
2.23e-25 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 103.73 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 19 ETFGYQQFRPGQEEIIDTVLSG-RDCLVVMPTGGGKSLCYQIPALLL-----NGLTVVVSPLISLMKDQVDQLQA----- 87
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKlgpsl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 88 NGVAAACLNSTQTREQQLEVMTGCrtgqIRLLYIAPERL--MLDNFLEHLAHWNpvLLAVDEAHCISQWGhdFRPEYAAL 165
Cdd:smart00487 82 GLKVVGLYGGDSKREQLRKLESGK----TDILVTTPGRLldLLENDKLSLSNVD--LVILDEAHRLLDGG--FGDQLEKL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 162135918 166 gqLRQRFPTLPFMALTATADDTTrQDIVRLLGLNdpLIQISSFDRPNIRY 215
Cdd:smart00487 154 --LKLLPKNVQLLLLSATPPEEI-ENLLELFLND--PVFIDVGFTPLEPI 198
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
529-609 |
6.81e-25 |
|
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: 98.52 E-value: 6.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 529 GNYDRKLFAKLRKLRKSIADESNVPPYVVFNDATLIEMAEQMPITASEMLSVNGVGMRKLERFGKPFMALIRAHVDGDDE 608
Cdd:smart00341 1 RERQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEASDSPSE 80
|
.
gi 162135918 609 E 609
Cdd:smart00341 81 A 81
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
250-331 |
1.66e-24 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 97.28 E-value: 1.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 250 EDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGR 329
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 162135918 330 DG 331
Cdd:smart00490 81 AG 82
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
224-331 |
2.77e-24 |
|
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: 97.67 E-value: 2.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 224 LDQLMRYVQEQRGKSGIIYCNSRAKVEDTAArLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKP 303
Cdd:pfam00271 3 LEALLELLKKERGGKVLIFSQTKKTLEAELL-LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLP 81
|
90 100
....*....|....*....|....*...
gi 162135918 304 NVRFVVHFDIPRNIESYYQETGRAGRDG 331
Cdd:pfam00271 82 DVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
532-599 |
2.00e-22 |
|
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: 91.06 E-value: 2.00e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162135918 532 DRKLFAKLRKLRKSIADESNVPPYVVFNDATLIEMAEQMPITASEMLSVNGVGMRKLERFGKPFMALI 599
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
219-340 |
1.03e-19 |
|
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: 85.25 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 219 EKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVAT-VAfG 297
Cdd:cd18787 10 EEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATdVA-A 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 162135918 298 MGINKPNVRFVVHFDIPRNIESYYQE---TGRAGRDGlpaEAMLFY 340
Cdd:cd18787 89 RGLDIPGVDHVINYDLPRDAEDYVHRigrTGRAGRKG---TAITFV 131
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
342-404 |
1.91e-17 |
|
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: 76.56 E-value: 1.91e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162135918 342 PADMAWLRRCLEEKP-QGQLQDIERHKLNAMGAFAEAQT-CRRLVLLNYFGE-GRQEPCGNCDICL 404
Cdd:pfam16124 1 YQDVVRLRFLIEQSEaDEERKEVELQKLQAMVAYCENTTdCRRKQLLRYFGEeFDSEPCGNCDNCL 66
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
19-348 |
9.36e-17 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 83.41 E-value: 9.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 19 ETFGYQQFRPGQEEIID-TVLSGRDCLVVMPTGGGKSLCYQIPAL--LLNGLTVV-VSPLISL----MKDQVDQLQANGV 90
Cdd:COG1204 16 KERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILkaLLNGGKALyIVPLRALasekYREFKRDFEELGI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 91 aaaclnstqtreqQLEVMTGCRTGQIRLL-----YIA-PERLmlDNFLEHLAHW-NPV-LLAVDEAHCIsqwGHDFR-PE 161
Cdd:COG1204 96 -------------KVGVSTGDYDSDDEWLgrydiLVAtPEKL--DSLLRNGPSWlRDVdLVVVDEAHLI---DDESRgPT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 162 Y-AALGQLRQRFPTLPFMALTATADDTtrQDIVRLLglNDPLIqISSFdRP----------NIRYMLMEKFKPLDQLMRY 230
Cdd:COG1204 158 LeVLLARLRRLNPEAQIVALSATIGNA--EEIAEWL--DAELV-KSDW-RPvplnegvlydGVLRFDDGSRRSKDPTLAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 231 VQ---EQRGKSgIIYCNSRAKVEDTAARLQ---------------------------------------SKGIsaAAYHA 268
Cdd:COG1204 232 ALdllEEGGQV-LVFVSSRRDAESLAKKLAdelkrrltpeereeleelaeellevseethtnekladclEKGV--AFHHA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 269 GLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPnVRFVVHFDIPRNIES------YYQETGRAGRDGlpaeamlfYDP 342
Cdd:COG1204 309 GLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLP-ARRVIIRDTKRGGMVpipvleFKQMAGRAGRPG--------YDP 379
|
....*.
gi 162135918 343 ADMAWL 348
Cdd:COG1204 380 YGEAIL 385
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
27-327 |
5.25e-16 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 81.22 E-value: 5.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 27 RPGQEEIIDTVLS-----GRDCLVVMPTGGGKSL----CYQipALLLNGLTVVVSPLISLMKDQVDQLQANGVAAACLNS 97
Cdd:COG1061 82 RPYQQEALEALLAalergGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEELRRFLGDPLAGGG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 98 TQTREQQLEVMTgcrtgqIRLLYIapeRLMLDNFLEHlahwnPVLLAVDEAHcisqwgHDFRPEYAalgQLRQRFPTLPF 177
Cdd:COG1061 160 KKDSDAPITVAT------YQSLAR---RAHLDELGDR-----FGLVIIDEAH------HAGAPSYR---RILEAFPAAYR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 178 MALTAT--ADDTTRQDIVRLLGL-----------------------NDPL-------IQISSFDRPNIRYMLMEKFKPLD 225
Cdd:COG1061 217 LGLTATpfRSDGREILLFLFDGIvyeyslkeaiedgylappeyygiRVDLtderaeyDALSERLREALAADAERKDKILR 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 226 QLMRyvQEQRGKSGIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNV 305
Cdd:COG1061 297 ELLR--EHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRL 374
|
330 340
....*....|....*....|....*
gi 162135918 306 RFVVHFdipRNIES---YYQETGRA 327
Cdd:COG1061 375 DVAILL---RPTGSpreFIQRLGRG 396
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
22-349 |
2.05e-15 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 79.51 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 22 GYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPalLLNGL--------TVVVSPLISLMKdQVDQL------QA 87
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLP--LLHNLdpelkapqILVLAPTRELAV-QVAEAmtdfskHM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 88 NGVAAACLNSTQTREQQLEVMtgcRTGQiRLLYIAPERLmldnfLEHLAHWNPVL-----LAVDEAHCISQWGHDFRPEy 162
Cdd:PRK11634 102 RGVNVVALYGGQRYDVQLRAL---RQGP-QIVVGTPGRL-----LDHLKRGTLDLsklsgLVLDEADEMLRMGFIEDVE- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 163 AALGQLRQRFPTLPFmalTATADDTTRQDIVRLLglNDPL---IQISSFDRPNIR--YMLMEKFKPLDQLMRYVQEQRGK 237
Cdd:PRK11634 172 TIMAQIPEGHQTALF---SATMPEAIRRITRRFM--KEPQevrIQSSVTTRPDISqsYWTVWGMRKNEALVRFLEAEDFD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 238 SGIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNI 317
Cdd:PRK11634 247 AAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDS 326
|
330 340 350
....*....|....*....|....*....|..
gi 162135918 318 ESYYQETGRAGRDGLPAEAMLFYDPADMAWLR 349
Cdd:PRK11634 327 ESYVHRIGRTGRAGRAGRALLFVENRERRLLR 358
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
30-344 |
5.11e-15 |
|
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: 78.34 E-value: 5.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 30 QEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPAL--LLNGLT---VVVSPLISLMKDQVDQLQA------NGVAAACLN-- 96
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLeaLLEDPGataLYLYPTKALARDQLRRLRElaealgLGVRVATYDgd 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 97 -STQTREQQLEvmtgcrTGQIRLlyIAPErlMLD-NFLEHLAHWNPVL-----LAVDEAHcisqwghdfrpEY------- 162
Cdd:COG1205 141 tPPEERRWIRE------HPDIVL--TNPD--MLHyGLLPHHTRWARFFrnlryVVIDEAH-----------TYrgvfgsh 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 163 -AALgqLR--QRF-------PTlpFMALTATA-------------------DDTTRQDIVRLLGLNDPLIqissfDRPNI 213
Cdd:COG1205 200 vANV--LRrlRRIcrhygsdPQ--FILASATIgnpaehaerltgrpvtvvdEDGSPRGERTFVLWNPPLV-----DDGIR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 214 RYMLMEKfkpLDQLMRYVQeqRGKSGIIYCNSRAKVEDTAARLQSK------GISAAAYHAGLENNVRADVQEKFQRDDL 287
Cdd:COG1205 271 RSALAEA---ARLLADLVR--EGLRTLVFTRSRRGAELLARYARRAlrepdlADRVAAYRAGYLPEERREIERGLRSGEL 345
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 162135918 288 QIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAML--FYDPAD 344
Cdd:COG1205 346 LGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLvaGDDPLD 404
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
5-366 |
3.76e-14 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 74.48 E-value: 3.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 5 EVLNLEsgaKQVLQETFGYQQFRPG--QEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLLNGLTVVVSPLISL--MKD 80
Cdd:PTZ00424 31 DALKLN---EDLLRGIYSYGFEKPSaiQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILapTRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 81 QVDQLQANGVAA---------ACLNSTQTREQQLEVMTGcrtgqIRLLYIAPERL--MLDNflEHLAHWNPVLLAVDEAH 149
Cdd:PTZ00424 108 LAQQIQKVVLALgdylkvrchACVGGTVVRDDINKLKAG-----VHMVVGTPGRVydMIDK--RHLRVDDLKLFILDEAD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 150 CISQWGhdFRpeyaalGQLRQRFPTLPFMALTATADDTTRQDIVRLLG--LNDP---LIQISSFDRPNIR--YMLMEKFK 222
Cdd:PTZ00424 181 EMLSRG--FK------GQIYDVFKKLPPDVQVALFSATMPNEILELTTkfMRDPkriLVKKDELTLEGIRqfYVAVEKEE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 223 -PLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGIN 301
Cdd:PTZ00424 253 wKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGID 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162135918 302 KPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAwlrrcleekpqgQLQDIERH 366
Cdd:PTZ00424 333 VQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIE------------QLKEIERH 385
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
201-332 |
9.61e-14 |
|
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: 69.12 E-value: 9.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 201 PLIQ-ISSFDRPNIRYMLMEKFKPLDQLMRYV---QEQRGKSGIIYCNSRAKVEDTAARLqsKGIsaAAYHAGLENNVRA 276
Cdd:cd18795 4 PLEEyVLGFNGLGIKLRVDVMNKFDSDIIVLLkieTVSEGKPVLVFCSSRKECEKTAKDL--AGI--AFHHAGLTREDRE 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162135918 277 DVQEKFQRDDLQIVVATVAFGMGINKPNVRFVV----HFDIPRNIE----SYYQETGRAGRDGL 332
Cdd:cd18795 80 LVEELFREGLIKVLVATSTLAAGVNLPARTVIIkgtqRYDGKGYRElsplEYLQMIGRAGRPGF 143
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
240-340 |
4.87e-13 |
|
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: 64.65 E-value: 4.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 240 IIYCNSRAKVEDTAARLQskgisaaayhaglennvradvqekfqrddlqIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319
Cdd:cd18785 7 IVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSAAS 55
|
90 100
....*....|....*....|..
gi 162135918 320 YYQETGRAGRDG-LPAEAMLFY 340
Cdd:cd18785 56 YIQRVGRAGRGGkDEGEVILFV 77
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
40-183 |
1.36e-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: 65.50 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 40 GRDCLVVMPTGGGKSLCYQIPALLLN----GLTVVVSPLISLMKDQ---VDQLQANGVAAACLNSTQTREQQLEVmtgcR 112
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLlkkgKKVLVLVPTKALALQTaerLRELFGPGIRVAVLVGGSSAEEREKN----K 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162135918 113 TGQIRLLYIAPERLmLDNFLEHLAHWNP--VLLAVDEAHCISQWGHDFRPEYAALgqLRQRFPTLPFMALTAT 183
Cdd:cd00046 77 LGDADIIIATPDML-LNLLLREDRLFLKdlKLIIVDEAHALLIDSRGALILDLAV--RKAGLKNAQVILLSAT 146
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
240-338 |
3.65e-12 |
|
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: 64.20 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 240 IIYCNSRAKVE----DTAARLQSKGISA---AAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFD 312
Cdd:cd18797 39 IVFCRSRKLAElllrYLKARLVEEGPLAskvASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|....*.
gi 162135918 313 IPRNIESYYQETGRAGRDGLPAEAML 338
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDSLVIL 144
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
19-339 |
3.68e-12 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 69.05 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 19 ETFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLL-------------NGLTVVVSP---LISLMKDQV 82
Cdd:PLN00206 137 ETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRcctirsghpseqrNPLAMVLTPtreLCVQVEDQA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 83 dQLQANGV--AAACLNSTQTREQQLEvmtgcRTGQ-IRLLYIAPERLmLDNFLEHLAHWNPV-LLAVDEAHCISQWGhdF 158
Cdd:PLN00206 217 -KVLGKGLpfKTALVVGGDAMPQQLY-----RIQQgVELIVGTPGRL-IDLLSKHDIELDNVsVLVLDEVDCMLERG--F 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 159 RPEyaaLGQLRQRFPTLPFMALTATaddtTRQDIVRL---LGLNDPLIQISSFDRPNirymlmekfKPLDQLMRYVQEQR 235
Cdd:PLN00206 288 RDQ---VMQIFQALSQPQVLLFSAT----VSPEVEKFassLAKDIILISIGNPNRPN---------KAVKQLAIWVETKQ 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 236 GKS---------------GIIYCNSRAKVEDTA-ARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMG 299
Cdd:PLN00206 352 KKQklfdilkskqhfkppAVVFVSSRLGADLLAnAITVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRG 431
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 162135918 300 INKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLF 339
Cdd:PLN00206 432 VDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVF 471
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
235-329 |
1.61e-10 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 64.14 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 235 RGKSgIIYCNSRAKVEDTAARLqskGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRfvVHFDIP 314
Cdd:COG1202 427 RGQT-IIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQ--VIFDSL 500
|
90 100
....*....|....*....|.
gi 162135918 315 R------NIESYYQETGRAGR 329
Cdd:COG1202 501 AmgiewlSVQEFHQMLGRAGR 521
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
22-331 |
4.10e-10 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 62.27 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 22 GYQqfRPG--QEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPAL--LLN------GLT--VVVSP---LISLMKDQVDQLQ 86
Cdd:PRK11192 20 GYT--RPTaiQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALqhLLDfprrksGPPriLILTPtreLAMQVADQARELA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 87 AN----------GVA----AACLNSTQtreqQLEVMTgcrTGqiRLL-YIAPErlmldNFLEHLAHWnpvlLAVDEAHCI 151
Cdd:PRK11192 98 KHthldiatitgGVAymnhAEVFSENQ----DIVVAT---PG--RLLqYIKEE-----NFDCRAVET----LILDEADRM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 152 SQWGhdFRPEYAAL-GQLRQRFPTLPFmalTATADDTTRQDIVRLLgLNDPlIQI----SSFDRPNIR--YML---ME-K 220
Cdd:PRK11192 160 LDMG--FAQDIETIaAETRWRKQTLLF---SATLEGDAVQDFAERL-LNDP-VEVeaepSRRERKKIHqwYYRaddLEhK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 221 FKPLDQLMRyvQEQRGKSgIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVAT-VAfGMG 299
Cdd:PRK11192 233 TALLCHLLK--QPEVTRS-IVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATdVA-ARG 308
|
330 340 350
....*....|....*....|....*....|....*
gi 162135918 300 INKPNVRFVVHFDIPRNIESYYQE---TGRAGRDG 331
Cdd:PRK11192 309 IDIDDVSHVINFDMPRSADTYLHRigrTGRAGRKG 343
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
38-342 |
1.10e-09 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 61.33 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 38 LSGRDCLVVMPTGGGKSLCYQIPA--------LLLNG---LTVVVSPLISLMkDQVDQlQANGVAA-------ACLNSTQ 99
Cdd:PTZ00110 165 LSGRDMIGIAETGSGKTLAFLLPAivhinaqpLLRYGdgpIVLVLAPTRELA-EQIRE-QCNKFGAsskirntVAYGGVP 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 100 TREQQLEVMTGcrtgqIRLLYIAPERLMldNFLE-HLAHWNPV-LLAVDEAHCISQWGhdFRPEYAAL-GQLRQRFPTLP 176
Cdd:PTZ00110 243 KRGQIYALRRG-----VEILIACPGRLI--DFLEsNVTNLRRVtYLVLDEADRMLDMG--FEPQIRKIvSQIRPDRQTLM 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 177 FMA-----LTATADDTTRQDIVRllglndplIQISSFDRP---NIRYMLM-----EKFKPLDQLMRYVQEQRGKSgIIYC 243
Cdd:PTZ00110 314 WSAtwpkeVQSLARDLCKEEPVH--------VNVGSLDLTachNIKQEVFvveehEKRGKLKMLLQRIMRDGDKI-LIFV 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 244 NSRaKVEDTAAR-LQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQ 322
Cdd:PTZ00110 385 ETK-KGADFLTKeLRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVH 463
|
330 340
....*....|....*....|
gi 162135918 323 ETGRAGRDGLPAEAMLFYDP 342
Cdd:PTZ00110 464 RIGRTGRAGAKGASYTFLTP 483
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
235-329 |
1.77e-09 |
|
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: 56.50 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 235 RGKSGIIYCNSRAKVEDTAARL------QSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFV 308
Cdd:cd18796 37 RHKSTLVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLV 116
|
90 100
....*....|....*....|.
gi 162135918 309 VHFDIPRNIESYYQETGRAGR 329
Cdd:cd18796 117 IQIGSPKSVARLLQRLGRSGH 137
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
5-329 |
1.15e-08 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 58.29 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 5 EVLNLESGAKQVLQETfGYQQFRPGQEEIIDT-VLSGRDCLVVMPTGGGKSLCYQIPAL--LLN--GLTVVVSPLISLMK 79
Cdd:PRK00254 4 DELRVDERIKRVLKER-GIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVnkLLRegGKAVYLVPLKALAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 80 DQVDQLQ-----ANGVAAACLNSTQTREQqlevmtgcrTGQIRLLYIAPERLmlDNFLEHLAHW--NPVLLAVDEAHCIS 152
Cdd:PRK00254 83 EKYREFKdweklGLRVAMTTGDYDSTDEW---------LGKYDIIIATAEKF--DSLLRHGSSWikDVKLVVADEIHLIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 153 QWGHDFRPEYAaLGQLRQRFPTLPFMALTATADDTTRQdivrllgLNDPLIqISSFDRPNIRYML------------MEK 220
Cdd:PRK00254 152 SYDRGATLEMI-LTHMLGRAQILGLSATVGNAEELAEW-------LNAELV-VSDWRPVKLRKGVfyqgflfwedgkIER 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 221 FKPLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLqSKGIS----------------------------------AAAY 266
Cdd:PRK00254 223 FPNSWESLVYDAVKKGKGALVFVNTRRSAEKEALEL-AKKIKrfltkpelralkeladsleenptneklkkalrggVAFH 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162135918 267 HAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVH----------FDIPrnIESYYQETGRAGR 329
Cdd:PRK00254 302 HAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRdtkrysnfgwEDIP--VLEIQQMMGRAGR 372
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
213-331 |
1.21e-07 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. 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: 350180 [Multi-domain] Cd Length: 135 Bit Score: 50.94 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 213 IRYMLMEKFKPLDQLMRYVQEQRGKSgIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDD--LQIV 290
Cdd:cd18793 5 IEEVVSGKLEALLELLEELREPGEKV-LIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFL 83
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 162135918 291 VATVAFGMGINKPNVRFVVHFDIPRN--IESyyQETGRAGRDG 331
Cdd:cd18793 84 LSTKAGGVGLNLTAANRVILYDPWWNpaVEE--QAIDRAHRIG 124
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
510-609 |
2.03e-07 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 53.34 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 510 LAVPRIVALKPKAMQKSFGGNY--DRKLFAKLRKL---RKSIADESNVPPYVVFNDATLIEMAEQMPITASEMLSVNGVG 584
Cdd:COG0349 182 LLDPATYREDPEEAWLRLKGAWklNPRQLAVLRELaawREREARKRDVPRNRVLKDEALLELARRQPKSLEELARLRGLS 261
|
90 100
....*....|....*....|....*
gi 162135918 585 MRKLERFGKPFMALIRAHVDGDDEE 609
Cdd:COG0349 262 PGEIRRHGEELLAAVAEALALPEEE 286
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
227-339 |
2.96e-07 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 53.42 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 227 LMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVR 306
Cdd:PRK04537 248 LLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVK 327
|
90 100 110
....*....|....*....|....*....|...
gi 162135918 307 FVVHFDIPRNIESYYQETGRAGRDGLPAEAMLF 339
Cdd:PRK04537 328 YVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
226-331 |
3.09e-06 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 50.27 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 226 QLMRYVQEQRGKSgIIYCNSRAKVEDTAARLQS---------------------------KGIsaAAYHAGLENNVRADV 278
Cdd:PRK01172 227 SLIKETVNDGGQV-LVFVSSRKNAEDYAEMLIQhfpefndfkvssennnvyddslnemlpHGV--AFHHAGLSNEQRRFI 303
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162135918 279 QEKFQRDDLQIVVATVAFGMGINKPnVRFVVHFDIPR----------NIEsYYQETGRAGRDG 331
Cdd:PRK01172 304 EEMFRNRYIKVIVATPTLAAGVNLP-ARLVIVRDITRygnggirylsNME-IKQMIGRAGRPG 364
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
219-331 |
3.87e-06 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 49.53 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 219 EKFKPLDQLMRyvqEQRGKSGIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGM 298
Cdd:PRK01297 321 DKYKLLYNLVT---QNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGR 397
|
90 100 110
....*....|....*....|....*....|...
gi 162135918 299 GINKPNVRFVVHFDIPRNIESYYQETGRAGRDG 331
Cdd:PRK01297 398 GIHIDGISHVINFTLPEDPDDYVHRIGRTGRAG 430
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
22-365 |
4.19e-06 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 49.42 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 22 GYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLLngltvvvsplisLMKDQVDQLQANGVAAACLnsTQTR 101
Cdd:PRK10590 20 GYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQH------------LITRQPHAKGRRPVRALIL--TPTR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 102 EQQLEV---------------------------MTGCRTGqIRLLYIAPERLmLDnflehLAHWNPV------LLAVDEA 148
Cdd:PRK10590 86 ELAAQIgenvrdyskylnirslvvfggvsinpqMMKLRGG-VDVLVATPGRL-LD-----LEHQNAVkldqveILVLDEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 149 HCISQWG--HDFRPEYAALGQLRQRfptlpfMALTATADDTTRQDIVRLLglNDPL-IQI----SSFDRPNIRYMLMEKF 221
Cdd:PRK10590 159 DRMLDMGfiHDIRRVLAKLPAKRQN------LLFSATFSDDIKALAEKLL--HNPLeIEVarrnTASEQVTQHVHFVDKK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 222 KPLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGIN 301
Cdd:PRK10590 231 RKRELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLD 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162135918 302 KPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYdpadmawlrrCLEEkpQGQLQDIER 365
Cdd:PRK10590 311 IEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLV----------CVDE--HKLLRDIEK 362
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
30-149 |
5.15e-06 |
|
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: 47.19 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 30 QEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPAL--LL---NGLTVVVSPLISLMKDQVDQLQA------NGVAAACLN-S 97
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILeaLLrdpGSRALYLYPTKALAQDQLRSLRElleqlgLGIRVATYDgD 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162135918 98 TQTREqqlevmtgcRTGQIRllyiAPERLMLDNF--LEHL-----AHWNPVL-----LAVDEAH 149
Cdd:cd17923 85 TPREE---------RRAIIR----NPPRILLTNPdmLHYAllphhDRWARFLrnlryVVLDEAH 135
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
255-332 |
5.90e-06 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 49.55 E-value: 5.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 255 RLQSKGIsaAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPnVRFVV-----------HFDI-PRnieSYYQ 322
Cdd:COG4581 296 RLLRRGI--AVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMP-ARTVVftklskfdgerHRPLtAR---EFHQ 369
|
90
....*....|
gi 162135918 323 ETGRAGRDGL 332
Cdd:COG4581 370 IAGRAGRRGI 379
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
224-329 |
8.61e-06 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 48.68 E-value: 8.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 224 LDQLMRYVQE--QRGKSGIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDD--LQIVVATVAFGMG 299
Cdd:COG0553 535 LEALLELLEEllAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEG 614
|
90 100 110
....*....|....*....|....*....|
gi 162135918 300 INKPNVRFVVHFDIPRNIESYYQETGRAGR 329
Cdd:COG0553 615 LNLTAADHVIHYDLWWNPAVEEQAIDRAHR 644
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
26-183 |
1.20e-05 |
|
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: 45.37 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 26 FRPGQEEIIDTVL---SGRDCLVVMPTGGGKSLC-YQIPALLLNGLTVVVSPLISLMKDQVDQL-QANGVAAACL---NS 97
Cdd:cd17926 1 LRPYQEEALEAWLahkNNRRGILVLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFeDFLGDSSIGLiggGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 98 TQTREQQLEVMTgcrTGQIRLLYIAPERLMLDNFLehlahwnpvLLAVDEAHCIS--QWGHdfrpeyaalgqLRQRFPTL 175
Cdd:cd17926 81 KKDFDDANVVVA---TYQSLSNLAEEEKDLFDQFG---------LLIVDEAHHLPakTFSE-----------ILKELNAK 137
|
....*...
gi 162135918 176 PFMALTAT 183
Cdd:cd17926 138 YRLGLTAT 145
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
12-72 |
3.61e-05 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 46.84 E-value: 3.61e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162135918 12 GAKQVLQETFGYQQFRPGQ----EEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLL---NGLTVVVS 72
Cdd:COG1199 1 ADDGLLALAFPGFEPRPGQremaEAVARALAEGRHLLIEAGTGTGKTLAYLVPALLAareTGKKVVIS 68
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
40-149 |
4.24e-05 |
|
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: 44.11 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 40 GRDCLVVMPTGGGKSLCYQIPALL------LNGLTVV-VSPLISLMKDQVDQLQangvaAAClnstqtREQQLEVMTGCR 112
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSsladepEKGVQVLyISPLKALINDQERRLE-----EPL------DEIDLEIPVAVR 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 162135918 113 TG---------QIR----LLYIAPERL--MLDNflEHLAHwnpvLLA------VDEAH 149
Cdd:cd17922 70 HGdtsqsekakQLKnppgILITTPESLelLLVN--KKLRE----LFAglryvvVDEIH 121
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
236-329 |
6.32e-05 |
|
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350185 [Multi-domain] Cd Length: 174 Bit Score: 43.83 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 236 GKSGIIYCNS---RAKVEDTAARLQSKGISAAAYHAGLENNVradvqEKFQRDDLQIVVATVAF-GM---GINKPN-VRF 307
Cdd:cd18798 24 GDGGLIFVSIdygKEYAEELKEFLERHGIKAELALSSTEKNL-----EKFEEGEIDVLIGVASYyGVlvrGIDLPErIKY 98
|
90 100
....*....|....*....|..
gi 162135918 308 VVHFDIPrnIESYYQETGRAGR 329
Cdd:cd18798 99 AIFYGVP--VTTYIQASGRTSR 118
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
215-331 |
1.24e-04 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 42.58 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 215 YMLMEK-FKPLDQLMRYVQEQRGKSGIIYCNSRAKV----------EDTAARLQSK-----GISAAAYHAGLENNVRADV 278
Cdd:cd18802 3 IVVIPKlQKLIEILREYFPKTPDFRGIIFVERRATAvvlsrllkehPSTLAFIRCGfligrGNSSQRKRSLMTQRKQKET 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 162135918 279 QEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDG 331
Cdd:cd18802 83 LDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN 135
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
237-329 |
1.69e-04 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins 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: 350186 [Multi-domain] Cd Length: 116 Bit Score: 41.39 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 237 KSGIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRAD-VQEKFQRDDLQIVVA-TVA-FGMGINKPNVRFVVhFDi 313
Cdd:cd18799 7 IKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDeALILLFFGELKPPILvTVDlLTTGVDIPEVDNVV-FL- 84
|
90
....*....|....*....
gi 162135918 314 pRNIES---YYQETGRAGR 329
Cdd:cd18799 85 -RPTESrtlFLQMLGRGLR 102
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
22-62 |
1.81e-04 |
|
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: 42.81 E-value: 1.81e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 162135918 22 GYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPAL 62
Cdd:cd00268 9 GFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPIL 49
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
25-183 |
2.38e-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: 42.32 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 25 QFRPGQEEIIDT-VLSGRDCLVVMPTGGGKSLCYQ---IPALLLNGLTVVVSPLISLmkdqvdqlqangvAAACLNSTQT 100
Cdd:cd18028 1 ELYPPQAEAVRAgLLKGENLLISIPTASGKTLIAEmamVNTLLEGGKALYLVPLRAL-------------ASEKYEEFKK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 101 REqQLEVMTGCRTGQIRllyIAPERLM-----------LDNFLEHLAHW-NPV-LLAVDEAHCISQWGHDFRPEyAALGQ 167
Cdd:cd18028 68 LE-EIGLKVGISTGDYD---EDDEWLGdydiivatyekFDSLLRHSPSWlRDVgVVVVDEIHLISDEERGPTLE-SIVAR 142
|
170
....*....|....*.
gi 162135918 168 LRQRFPTLPFMALTAT 183
Cdd:cd18028 143 LRRLNPNTQIIGLSAT 158
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
240-331 |
2.96e-04 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 43.42 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 240 IIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319
Cdd:PRK04837 259 IIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCED 338
|
90
....*....|..
gi 162135918 320 YYQETGRAGRDG 331
Cdd:PRK04837 339 YVHRIGRTGRAG 350
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
30-183 |
5.26e-04 |
|
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an IFN-inducible cytoplasmic helicase that plays a role in RIG-I-mediated type I interferon (IFN) nuclease-mediated viral RNA degradation. DDX60 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: 350783 [Multi-domain] Cd Length: 192 Bit Score: 41.58 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 30 QEEIIDTVLSGRDCLVVMPTGGGKSLC--YQIPALLL---NGLTVVVSPLISLmkdqVDQLQANGVA---------AACL 95
Cdd:cd18025 6 QRELLDIVDRRESALIVAPTSSGKTFIsyYCMEKVLResdDGVVVYVAPTKAL----VNQVVAEVYArfskkyppsGKSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 96 NSTQTREQQLEVMTGCrtgQIrlLYIAPERLMLDNFLEHLAHWNPVLLAV--DEAHCISQWGHdfrpeyaalGQLRQRFP 173
Cdd:cd18025 82 WGVFTRDYRHNNPMNC---QV--LITVPECLEILLLSPHNASWVPRIKYVifDEIHSIGQSED---------GAVWEQLL 147
|
170
....*....|...
gi 162135918 174 TL---PFMALTAT 183
Cdd:cd18025 148 LLipcPFLALSAT 160
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
224-340 |
6.09e-04 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 42.99 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 224 LDQLMRYvqeqrgKSGIIYCNSRAKVEDTAARL---------QSKGISAAA------------------------YHAGL 270
Cdd:PRK09751 238 LDEVLRH------RSTIVFTNSRGLAEKLTARLnelyaarlqRSPSIAVDAahfestsgatsnrvqssdvfiarsHHGSV 311
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 271 ENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFY 340
Cdd:PRK09751 312 SKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGHQVGGVSKGLFF 381
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
26-200 |
6.69e-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: 41.09 E-value: 6.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 26 FRPGQEEIIDTV-LSGRDCLVVMPTGGGKSLC--YQIPALLL--NGLTVVVSPLISLMKDQVDQLQ-----ANGVAAAC- 94
Cdd:cd17921 2 LNPIQREALRALyLSGDSVLVSAPTSSGKTLIaeLAILRALAtsGGKAVYIAPTRALVNQKEADLRerfgpLGKNVGLLt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 95 ----LNSTQTREQQLEVMTgcrtgqirllyiaPERL--MLDNfLEHLAHWNPVLLAVDEAHCISQwghdfrPEYAALGQ- 167
Cdd:cd17921 82 gdpsVNKLLLAEADILVAT-------------PEKLdlLLRN-GGERLIQDVRLVVVDEAHLIGD------GERGVVLEl 141
|
170 180 190
....*....|....*....|....*....|....*..
gi 162135918 168 ----LRQRFPTLPFMALTATADDTtrQDIVRLLGLND 200
Cdd:cd17921 142 llsrLLRINKNARFVGLSATLPNA--EDLAEWLGVED 176
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
225-328 |
7.24e-04 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 42.57 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 225 DQLMRYVQEQRgkSGIIYCNSRAKVEDTAARLQSK-----GISA-AAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGM 298
Cdd:PRK13767 275 ETLHELIKEHR--TTLIFTNTRSGAERVLYNLRKRfpeeyDEDNiGAHHSSLSREVRLEVEEKLKRGELKVVVSSTSLEL 352
|
90 100 110
....*....|....*....|....*....|
gi 162135918 299 GINKPNVRFVVHFDIPRNIESYYQETGRAG 328
Cdd:PRK13767 353 GIDIGYIDLVVLLGSPKSVSRLLQRIGRAG 382
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
19-63 |
7.97e-04 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 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: 350715 [Multi-domain] Cd Length: 198 Bit Score: 41.04 E-value: 7.97e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 162135918 19 ETFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALL 63
Cdd:cd17957 6 EESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQ 50
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
14-148 |
9.27e-04 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It 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: 350714 [Multi-domain] Cd Length: 231 Bit Score: 41.08 E-value: 9.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 14 KQVLQEtFGYQQFRPGQEEIIDTVLSG---------RDCLVVMPTGGGKSLCYQIP---ALL------LNGLTVV-VSPL 74
Cdd:cd17956 2 LKNLQN-NGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPivqALSkrvvprLRALIVVpTKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 75 ISLMKDQVDQLQANGV--AAACLNSTQTREQQLEVMTGCRTGQ---IRLLYIAPERLM--LDN---F-LEHLAhwnpvLL 143
Cdd:cd17956 81 VQQVYKVFESLCKGTGlkVVSLSGQKSFKKEQKLLLVDTSGRYlsrVDILVATPGRLVdhLNStpgFtLKHLR-----FL 155
|
....*
gi 162135918 144 AVDEA 148
Cdd:cd17956 156 VIDEA 160
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
22-110 |
9.81e-04 |
|
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members 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: 350716 [Multi-domain] Cd Length: 197 Bit Score: 40.91 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 22 GYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALL-----------LNGLTV-VVSP---LISLMKDQVDQLQ 86
Cdd:cd17958 9 GFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIhldlqpipreqRNGPGVlVLTPtreLALQIEAECSKYS 88
|
90 100
....*....|....*....|....
gi 162135918 87 ANGVAAACLNSTQTREQQLEVMTG 110
Cdd:cd17958 89 YKGLKSVCVYGGGNRNEQIEDLSK 112
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
14-73 |
1.62e-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: 40.25 E-value: 1.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162135918 14 KQVLQEtFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPAL--LLNGLT---------VVVSP 73
Cdd:cd17960 2 LDVVAE-LGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLeiLLKRKAnlkkgqvgaLIISP 71
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
263-338 |
1.78e-03 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 41.48 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 263 AAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVV----HFD-----IPRNIESYYQETGRAGRDGL- 332
Cdd:PRK02362 306 AAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIrdyrRYDggagmQPIPVLEYHQMAGRAGRPGLd 385
|
....*..
gi 162135918 333 P-AEAML 338
Cdd:PRK02362 386 PyGEAVL 392
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
22-62 |
1.95e-03 |
|
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, 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: 350698 [Multi-domain] Cd Length: 201 Bit Score: 39.97 E-value: 1.95e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 162135918 22 GYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPAL 62
Cdd:cd17940 18 GFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPIL 58
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
15-62 |
6.09e-03 |
|
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 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: 350711 [Multi-domain] Cd Length: 222 Bit Score: 38.51 E-value: 6.09e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 162135918 15 QVLQEtFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPAL 62
Cdd:cd17953 25 DLIKK-LGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMF 71
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
25-149 |
7.00e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 37.65 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135918 25 QFRPGQEEIIDTVLSGRDC-----LVVMPTGGGKSLCY-QIPALLLNGL----TVVVSPLISLMKDQVDQLQANGVAAAC 94
Cdd:pfam04851 3 ELRPYQIEAIENLLESIKNgqkrgLIVMATGSGKTLTAaKLIARLFKKGpikkVLFLVPRKDLLEQALEEFKKFLPNYVE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162135918 95 LNstqtreqqlEVMTGCR----TGQIRLLYIAPERLM--LDNFLEHLAHWNPVLLAVDEAH 149
Cdd:pfam04851 83 IG---------EIISGDKkdesVDDNKIVVTTIQSLYkaLELASLELLPDFFDVIIIDEAH 134
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
22-62 |
9.51e-03 |
|
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor 3B-Associated 125 kDa Protein, RHELP, or RNAHP) is an NTPase with a preference for ATP, the hydrolysis of which is enhanced by various RNA substrates. It acts as a non-processive RNA helicase with protein displacement and RNA annealing activities. DDX42 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: 350710 [Multi-domain] Cd Length: 197 Bit Score: 37.78 E-value: 9.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 162135918 22 GYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPAL 62
Cdd:cd17952 9 EYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPML 49
|
|
| |
