|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
3-608 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 1345.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 3 VAQAEVLNLESGAKQVLQETFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLLNGLTVVVSPLISLMKD 82
Cdd:PRK11057 1 MAQAEVLNLESLAKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 83 QVDQLQANGVAAACLNSTQTREQQLEVMTGCRTGQIRLLYIAPERLMLDNFLEHLAHWNPVLLAVDEAHCISQWGHDFRP 162
Cdd:PRK11057 81 QVDQLLANGVAAACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 163 EYAALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYMLMEKFKPLDQLMRYVQEQRGKSGI 242
Cdd:PRK11057 161 EYAALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQLMRYVQEQRGKSGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 243 IYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESY 322
Cdd:PRK11057 241 IYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 323 YQETGRAGRDGLPAEAMLFYDPADMAWLRRCLEEKPQGQLQDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNC 402
Cdd:PRK11057 321 YQETGRAGRDGLPAEAMLFYDPADMAWLRRCLEEKPAGQQQDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 403 DICLDPPKQYDGSTDAQIALSTIGRVNQRFGMGYVVEVIRGANNQRIRDYGHDKLKVYGMGRDKSHEHWVSVIRQLIHLG 482
Cdd:PRK11057 401 DICLDPPKQYDGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 483 LVTQNIAQHSALQLTEAARPVL-AESSLQLAVPRIVALKPKAMQKSFGGNYDRKLFAKLRKLRKSIADESNVPPYVVFND 561
Cdd:PRK11057 481 LVTQNIAQHSALQLTEAARPVLrGEVSLQLAVPRIVALKPRAMQKSFGGNYDRKLFAKLRKLRKSIADEENIPPYVVFND 560
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 7428315 562 ATLIEMAEQMPITASEMLSVNGVGMRKLERFGKPFMALIRAHVDGDD 608
Cdd:PRK11057 561 ATLIEMAEQMPITASEMLSVNGVGQRKLERFGKPFMALIRAHVDGDD 607
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
15-603 |
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: 1031.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 15 AKQVLQETFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLLNGLTVVVSPLISLMKDQVDQLQANGVAA 94
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 95 ACLNSTQTREQQLEVMTGCRTGQIRLLYIAPERLMLDNFLEHLAHWNPVLLAVDEAHCISQWGHDFRPEYAALGQLRQRF 174
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 175 PTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYMLMEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVEDT 254
Cdd:TIGR01389 161 PQVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 255 AARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGL 334
Cdd:TIGR01389 241 AERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 335 PAEAMLFYDPADMAWLRRCLEE-KPQGQLQDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNCDICLDPPKQYD 413
Cdd:TIGR01389 321 PAEAILLYSPADIALLKRRIEQsEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENEVEPCGNCDNCLDPPKSYD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 414 GSTDAQIALSTIGRVNQRFGMGYVVEVIRGANNQRIRDYGHDKLKVYGMGRDKSHEHWVSVIRQLIHLGLVTQNIAQHSA 493
Cdd:TIGR01389 401 ATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEIYIG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 494 LQLTEAARPVLA-ESSLQLAVPRIVALKPKAMQKSFGGNYDRKLFAKLRKLRKSIADESNVPPYVVFNDATLIEMAEQMP 572
Cdd:TIGR01389 481 LQLTEAARKVLKnEVEVLLRPFKVVAKEKTRVQKNLSVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAEKRP 560
|
570 580 590
....*....|....*....|....*....|.
gi 7428315 573 ITASEMLSVNGVGMRKLERFGKPFMALIRAH 603
Cdd:TIGR01389 561 ATLNALLKIKGVGQNKLDRYGEAFLEVIREY 591
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
15-481 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 820.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 15 AKQVLQETFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLLNGLTVVVSPLISLMKDQVDQLQANGVAA 94
Cdd:COG0514 5 ALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 95 ACLNSTQTREQQLEVMTGCRTGQIRLLYIAPERLMLDNFLEHLAHWNPVLLAVDEAHCISQWGHDFRPEYAALGQLRQRF 174
Cdd:COG0514 85 AFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGELRERL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 175 PTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYMLMEKF--KPLDQLMRYVQEQRGKSGIIYCNSRAKVE 252
Cdd:COG0514 165 PNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPpdDKLAQLLDFLKEHPGGSGIVYCLSRKKVE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 253 DTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRD 332
Cdd:COG0514 245 ELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 333 GLPAEAMLFYDPADMAWLRRCLEEK-PQGQLQDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNCDICLDPPKQ 411
Cdd:COG0514 325 GLPAEALLLYGPEDVAIQRFFIEQSpPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYFGEELAEPCGNCDNCLGPPET 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 412 YDGSTDAQIALSTIGRVNQRFGMGYVVEVIRGANNQRIRDYGHDKLKVYGMGRDKSHEHWVSVIRQLIHL 481
Cdd:COG0514 405 FDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLLAQ 474
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
17-466 |
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 7428315 17 QVLQETFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLLNGLTVVVSPLISLMKDQVDQLQANGVAAAC 96
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 97 LNSTQTREQQLEVMTGCRTGQIRLLYIAPERLMLDN-FLEHL-AHWNPVLLAVDEAHCISQWGHDFRPEYAALGQLRQRF 174
Cdd:TIGR00614 81 LNSAQTKEQQLNVLTDLKDGKIKLLYVTPEKISASNrLLQTLeERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 175 PTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYMLMEKF-KPLDQLMRYVQ-EQRGKSGIIYCNSRAKVE 252
Cdd:TIGR00614 161 PNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTpKILEDLLRFIRkEFEGKSGIIYCPSRKKVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 253 DTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRD 332
Cdd:TIGR00614 241 QVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGRD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 333 GLPAEAMLFYDPADMAWLRRCLEEKPQGQLQDIERHKLNAMGAFAEAQTCRRLVLLNYFGE----------GRQEPCGNC 402
Cdd:TIGR00614 321 GLPSECHLFYAPADMNRLRRLLMEEPDGNFRTYKLKLYEMMEYCLNSSTCRRLILLSYFGEkgfnksfcimGTEKCCDNC 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 403 DICLD------PPKQYDGSTDAQIALSTIGRVNQRFGMGYVVEVIRGANNQRIRDYGHDKLKVYGMGRDK 466
Cdd:TIGR00614 401 CKRLDyktkdvTDKVYDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGRGKDE 470
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
10-593 |
5.15e-125 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 397.34 E-value: 5.15e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 10 NLESGAKQVlqetFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLLNGLTVVVSPLISLMKDQV-DQLQ 88
Cdd:PLN03137 447 KLEVNNKKV----FGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQImNLLQ 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 89 ANgVAAACLNSTQTREQQLEVMT--GCRTGQIRLLYIAPERLML-DNFLEHLAHWNP-VLLA---VDEAHCISQWGHDFR 161
Cdd:PLN03137 523 AN-IPAASLSAGMEWAEQLEILQelSSEYSKYKLLYVTPEKVAKsDSLLRHLENLNSrGLLArfvIDEAHCVSQWGHDFR 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 162 PEYAALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYMLMEKFKP-LDQLMRYVQEQR-GK 239
Cdd:PLN03137 602 PDYQGLGILKQKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKKcLEDIDKFIKENHfDE 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 240 SGIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNI 319
Cdd:PLN03137 682 CGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSI 761
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 320 ESYYQETGRAGRDGLPAEAMLFYDPADM---------------AWLRRCLEEKPQGQLQDIERHKLNAMGAFAEAQT-CR 383
Cdd:PLN03137 762 EGYHQECGRAGRDGQRSSCVLYYSYSDYirvkhmisqggveqsPMAMGYNRMASSGRILETNTENLLRMVSYCENEVdCR 841
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 384 RLVLLNYFGEGRQEP-CGN-CDICLDPPK--QYDGSTDAQIALSTIGRVNQRFGMGYVVEVIRGANNQRIRDYGHDKLKV 459
Cdd:PLN03137 842 RFLQLVHFGEKFDSTnCKKtCDNCSSSKSliDKDVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLSL 921
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 460 YGMGRdksHEHWVSVIRQLIHlgLVTQNIAQH------------SALQLTEAARPVLAE--SSLQLAVPRIV-ALKP--- 521
Cdd:PLN03137 922 HGAGK---HLSKGEASRILHY--LVTEDILAEdvkksdlygsvsSLLKVNESKAYKLFSggQTIIMRFPSSVkASKPskf 996
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 522 --------------------KAMQKSFGGNYDRKLFAKLRKLRKSIADESN--VPPYVVFNDATLIEMAEQMPITASEML 579
Cdd:PLN03137 997 eatpakgpltsgkqstlpmaTPAQPPVDLNLSAILYTALRKLRTALVKEAGdgVMAYHIFGNATLQQISKRIPRTKEELL 1076
|
650
....*....|....
gi 7428315 580 SVNGVGMRKLERFG 593
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 ... |
16-211 |
1.07e-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: 335.27 E-value: 1.07e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 16 KQVLQETFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLLNGLTVVVSPLISLMKDQVDQLQANGVAAA 95
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 96 CLNSTQTREQQLEVMTGCRTGQIRLLYIAPERLMLDNFLEHLAHWN----PVLLAVDEAHCISQWGHDFRPEYAALGQLR 171
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLRLGRLR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 7428315 172 QRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFD 211
Cdd:cd17920 161 RALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
17-202 |
1.13e-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: 1.13e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 17 QVLQETFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLLN----GLTVVVSPLISLMKDQVDQLQAnGV 92
Cdd:cd18018 2 KLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRrrgpGLTLVVSPLIALMKDQVDALPR-AI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 93 AAACLNSTQTREQQLEVMTGCRTGQIRLLYIAPERLMLDNFLEHLAHWNPV-LLAVDEAHCISQWGHDFRPEYAALGQ-L 170
Cdd:cd18018 81 KAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTPPIsLLVVDEAHCISEWSHNFRPDYLRLCRvL 160
|
170 180 190
....*....|....*....|....*....|..
gi 7428315 171 RQRFPTLPFMALTATADDTTRQDIVRLLGLND 202
Cdd:cd18018 161 RELLGAPPVLALTATATKRVVEDIASHLGIPE 192
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
212-342 |
1.08e-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: 226.71 E-value: 1.08e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 212 RPNIRYMLMEKFKP---LDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDD 288
Cdd:cd18794 1 RPNLFYSVRPKDKKdekLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 7428315 289 LQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFY 342
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
15-211 |
1.20e-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: 1.20e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 15 AKQVLQETFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLLNGLTVVVSPLISLMKDQVDQLQANGVAA 94
Cdd:cd18015 6 VKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 95 ACLNSTQTREQQLEVMTGCRTG--QIRLLYIAPERL----MLDNFLE------HLAhwnpvLLAVDEAHCISQWGHDFRP 162
Cdd:cd18015 86 TMLNASSSKEHVKWVHAALTDKnsELKLLYVTPEKIakskRFMSKLEkaynagRLA-----RIAIDEVHCCSQWGHDFRP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 7428315 163 EYAALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFD 211
Cdd:cd18015 161 DYKKLGILKRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
19-211 |
4.64e-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: 4.64e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 19 LQETFGYQQFRPGQEEIIDTVL-SGRDCLVVMPTGGGKSLCYQIPALLLNGLTVVVSPLISLMKDQVDQLQANGVAAACL 97
Cdd:cd18017 4 LNEYFGHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 98 NSTQTREqqleVMTGCRTGQIRLLYIAPErlMLDNFLEHLAHWNP--VLLAVDEAHCISQWGHDFRPEYAALGQLRQRFP 175
Cdd:cd18017 84 GSAQSQN----VLDDIKMGKIRVIYVTPE--FVSKGLELLQQLRNgiTLIAIDEAHCVSQWGHDFRSSYRHLGSIRNRLP 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 7428315 176 TLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFD 211
Cdd:cd18017 158 NVPIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
17-211 |
1.03e-59 |
|
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: 1.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 17 QVLQETFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLLNGLTVVVSPLISLMKDQVDQLQANGVAAAC 96
Cdd:cd18016 7 KIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 97 LNSTQTREQQLEVMTGCRTGQ--IRLLYIAPERL----MLDNFLEHLAHWNpvLLA---VDEAHCISQWGHDFRPEYAAL 167
Cdd:cd18016 87 LTGDKTDAEATKIYLQLSKKDpiIKLLYVTPEKIsasnRLISTLENLYERK--LLArfvIDEAHCVSQWGHDFRPDYKRL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 7428315 168 GQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFD 211
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 ... |
16-208 |
4.82e-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: 4.82e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 16 KQVLQETFGYQQFR-PGQEEIIDTVLSGR-DCLVVMPTGGGKSLCYQIPALLLNGLTVVVSPLISLMKDQVDQLQANGVA 93
Cdd:cd18014 1 RSTLKKVFGHSDFKsPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 94 AACLNSTQTREQQLEVMTGCRTG--QIRLLYIAPERLMLDNF---LEHL-AHWNPVLLAVDEAHCISQWGHDFRPEYAAL 167
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADLESEkpQTKFLYITPEMAATSSFqplLSSLvSRNLLSYLVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 7428315 168 GQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQIS 208
Cdd:cd18014 161 GALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKPVAIFK 201
|
|
| DpdF |
NF041063 |
protein DpdF; |
18-348 |
1.34e-55 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 201.68 E-value: 1.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 18 VLQETFGYQQFR-PGQEEIIDTVLS---GRDCLVVMPTGGGKSLCYQIPALLL---NGLTVVVSPLISLMKDQVDQLQAN 90
Cdd:NF041063 130 FLAEALGFTHYRsPGQREAVRAALLappGSTLIVNLPTGSGKSLVAQAPALLAsrqGGLTLVVVPTVALAIDQERRAREL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 91 GVAAACL----------NSTQTREQqleVMTGCRTGQIRLLYIAPERLM--LDNFLE------HLAHwnpvlLAVDEAHC 152
Cdd:NF041063 210 LRRAGPDlggplawhggLSAEERAA---IRQRIRDGTQRILFTSPESLTgsLRPALFdaaeagLLRY-----LVVDEAHL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 153 ISQWGHDFRPEYAALGQLRQ----------RFPTLpfmALTATADDTTRQDIVRLLGLNDPLIQIS-SFDRPNIRYMLME 221
Cdd:NF041063 282 VDQWGDGFRPEFQLLAGLRRsllrlapsgrPFRTL---LLSATLTESTLDTLETLFGPPGPFIVVSaVQLRPEPAYWVAK 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 222 KFKPLDQLMRYVQEQRG--KSGIIYCNSRAKVEDTAARLQSKGIS-AAAYHAGLENNVRADVQEKFQRDDLQIVVATVAF 298
Cdd:NF041063 359 CDSEEERRERVLEALRHlpRPLILYVTKVEDAEAWLQRLRAAGFRrVALFHGDTPDAERERLIEQWRENELDIVVATSAF 438
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 7428315 299 GMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMA 348
Cdd:NF041063 439 GLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLD 488
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
408-514 |
1.26e-37 |
|
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: 134.97 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 408 PPKQYDGSTDAQIALSTIGRVNQRFGMGYVVEVIRGANNQRIRDYGHDKLKVYGMGRDKSHEHWVSVIRQLIHLGLVTQN 487
Cdd:pfam09382 1 PPETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVD 80
|
90 100
....*....|....*....|....*...
gi 7428315 488 IAQHSALQLTEAARPVLA-ESSLQLAVP 514
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 ... |
413-504 |
1.32e-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: 1.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 413 DGSTDAQIALSTIGRVNQRFGMGYVVEVIRGANNQRIRDYGHDKLKVYGMGRDKSHEHWVSVIRQLIHLGLVTQNIAQHS 492
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYP 80
|
90
....*....|..
gi 7428315 493 ALQLTEAARPVL 504
Cdd:smart00956 81 YLKLTEKARPVL 92
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
29-192 |
2.73e-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: 2.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 29 RPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPAL-----LLNGL-TVVVSPLISLMKDQVDQLQA----NGVAAACLN 98
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdkLDNGPqALVLAPTRELAEQIYEELKKlgkgLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 99 STQTREQQLEVMTGCrtgqiRLLYIAPERLM----LDNFLEHLAhwnpvLLAVDEAHCISQWGhdFRPEYAA-LGQLRQR 173
Cdd:pfam00270 81 GGDSRKEQLEKLKGP-----DILVGTPGRLLdllqERKLLKNLK-----LLVLDEAHRLLDMG--FGPDLEEiLRRLPKK 148
|
170
....*....|....*....
gi 7428315 174 FPTlpfMALTATADDTTRQ 192
Cdd:pfam00270 149 RQI---LLLSATLPRNLED 164
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
24-370 |
1.01e-27 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 116.01 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 24 GYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALllngltvvvsplislmkDQVDQLQANGVAAACLnsTQTR 103
Cdd:COG0513 21 GYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLL-----------------QRLDPSRPRAPQALIL--APTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 104 E---------QQLEVMTGCRTG----------QIRLLY------IA-PERLM---------LDNfLEHLahwnpVLlavD 148
Cdd:COG0513 82 ElalqvaeelRKLAKYLGLRVAtvyggvsigrQIRALKrgvdivVAtPGRLLdliergaldLSG-VETL-----VL---D 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 149 EAhcisqwghD------FRPE----YAALGQLRQrfpTLPFmalTATADDttrqDIVRLLG--LNDPL-IQIS--SFDRP 213
Cdd:COG0513 153 EA--------DrmldmgFIEDieriLKLLPKERQ---TLLF---SATMPP----EIRKLAKryLKNPVrIEVApeNATAE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 214 NI--RYMLMEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQI 291
Cdd:COG0513 215 TIeqRYYLVDKRDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 292 VVAT-VAfGMGINKPNVRFVVHFDIPRNIESYyq---eTGRAGRDGlpaEAMLFYDPADMAWLRRcLEEKPQgqlQDIER 367
Cdd:COG0513 295 LVATdVA-ARGIDIDDVSHVINYDLPEDPEDYvhrigrTGRAGAEG---TAISLVTPDERRLLRA-IEKLIG---QKIEE 366
|
...
gi 7428315 368 HKL 370
Cdd:COG0513 367 EEL 369
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
21-217 |
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 7428315 21 ETFGYQQFRPGQEEIIDTVLSG-RDCLVVMPTGGGKSLCYQIPALLL-----NGLTVVVSPLISLMKDQVDQLQA----- 89
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKlgpsl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 90 NGVAAACLNSTQTREQQLEVMTGCrtgqIRLLYIAPERL--MLDNFLEHLAHWNpvLLAVDEAHCISQWGhdFRPEYAAL 167
Cdd:smart00487 82 GLKVVGLYGGDSKREQLRKLESGK----TDILVTTPGRLldLLENDKLSLSNVD--LVILDEAHRLLDGG--FGDQLEKL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 7428315 168 gqLRQRFPTLPFMALTATADDTTrQDIVRLLGLNdpLIQISSFDRPNIRY 217
Cdd:smart00487 154 --LKLLPKNVQLLLLSATPPEEI-ENLLELFLND--PVFIDVGFTPLEPI 198
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
530-610 |
7.45e-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: 98.14 E-value: 7.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 530 GNYDRKLFAKLRKLRKSIADESNVPPYVVFNDATLIEMAEQMPITASEMLSVNGVGMRKLERFGKPFMALIRAHVDGDDE 609
Cdd:smart00341 1 RERQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEASDSPSE 80
|
.
gi 7428315 610 E 610
Cdd:smart00341 81 A 81
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
252-333 |
1.43e-24 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 97.67 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 252 EDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGR 331
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 7428315 332 DG 333
Cdd:smart00490 81 AG 82
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
226-333 |
2.59e-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: 2.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 226 LDQLMRYVQEQRGKSGIIYCNSRAKVEDTAArLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKP 305
Cdd:pfam00271 3 LEALLELLKKERGGKVLIFSQTKKTLEAELL-LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLP 81
|
90 100
....*....|....*....|....*...
gi 7428315 306 NVRFVVHFDIPRNIESYYQETGRAGRDG 333
Cdd:pfam00271 82 DVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
533-600 |
1.89e-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: 1.89e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7428315 533 DRKLFAKLRKLRKSIADESNVPPYVVFNDATLIEMAEQMPITASEMLSVNGVGMRKLERFGKPFMALI 600
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
221-342 |
1.01e-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: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 221 EKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVAT-VAfG 299
Cdd:cd18787 10 EEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATdVA-A 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 7428315 300 MGINKPNVRFVVHFDIPRNIESYYQE---TGRAGRDGlpaEAMLFY 342
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. |
344-406 |
1.74e-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: 76.94 E-value: 1.74e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7428315 344 PADMAWLRRCLEEKP-QGQLQDIERHKLNAMGAFAEAQT-CRRLVLLNYFGE-GRQEPCGNCDICL 406
Cdd:pfam16124 1 YQDVVRLRFLIEQSEaDEERKEVELQKLQAMVAYCENTTdCRRKQLLRYFGEeFDSEPCGNCDNCL 66
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1-350 |
5.39e-17 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 84.18 E-value: 5.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 1 MNVAQAEVLNLesgaKQVLQEtFGYQQFRPGQEEIID-TVLSGRDCLVVMPTGGGKSLCYQIPAL--LLNGLTVV-VSPL 76
Cdd:COG1204 1 MKVAELPLEKV----IEFLKE-RGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILkaLLNGGKALyIVPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 77 ISL----MKDQVDQLQANGVaaaclnstqtreqQLEVMTGCRTGQIRLL-----YIA-PERlmLDNFLEHLAHW-NPV-L 144
Cdd:COG1204 76 RALasekYREFKRDFEELGI-------------KVGVSTGDYDSDDEWLgrydiLVAtPEK--LDSLLRNGPSWlRDVdL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 145 LAVDEAHCIsqwGHDFR-PEY-AALGQLRQRFPTLPFMALTATADDTtrQDIVRLlgLNDPLIqISSFdRP--------- 213
Cdd:COG1204 141 VVVDEAHLI---DDESRgPTLeVLLARLRRLNPEAQIVALSATIGNA--EEIAEW--LDAELV-KSDW-RPvplnegvly 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 214 -NIRYMLMEKFKPLDQLMRYVQ---EQRGKSgIIYCNSRAKVEDTAARLQ------------------------------ 259
Cdd:COG1204 212 dGVLRFDDGSRRSKDPTLALALdllEEGGQV-LVFVSSRRDAESLAKKLAdelkrrltpeereeleelaeellevseeth 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 260 ---------SKGIsaAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPnVRFVVHFDIPRNIES------YYQ 324
Cdd:COG1204 291 tnekladclEKGV--AFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLP-ARRVIIRDTKRGGMVpipvleFKQ 367
|
410 420
....*....|....*....|....*.
gi 7428315 325 ETGRAGRDGlpaeamlfYDPADMAWL 350
Cdd:COG1204 368 MAGRAGRPG--------YDPYGEAIL 385
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
29-329 |
4.66e-16 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 81.61 E-value: 4.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 29 RPGQEEIIDTVLS-----GRDCLVVMPTGGGKSL----CYQipALLLNGLTVVVSPLISLMKDQVDQLQANGVAAACLNS 99
Cdd:COG1061 82 RPYQQEALEALLAalergGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEELRRFLGDPLAGGG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 100 TQTREQQLEVMTgcrtgqIRLLYIapeRLMLDNFLEHlahwnPVLLAVDEAHcisqwgHDFRPEYAalgQLRQRFPTLPF 179
Cdd:COG1061 160 KKDSDAPITVAT------YQSLAR---RAHLDELGDR-----FGLVIIDEAH------HAGAPSYR---RILEAFPAAYR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 180 MALTAT--ADDTTRQDIVRLLGL-----------------------NDPL-------IQISSFDRPNIRYMLMEKFKPLD 227
Cdd:COG1061 217 LGLTATpfRSDGREILLFLFDGIvyeyslkeaiedgylappeyygiRVDLtderaeyDALSERLREALAADAERKDKILR 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 228 QLMRyvQEQRGKSGIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNV 307
Cdd:COG1061 297 ELLR--EHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRL 374
|
330 340
....*....|....*....|....*
gi 7428315 308 RFVVHFdipRNIES---YYQETGRA 329
Cdd:COG1061 375 DVAILL---RPTGSpreFIQRLGRG 396
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
24-351 |
2.25e-15 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 79.51 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 24 GYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPalLLNGL--------TVVVSPLISLMKdQVDQL------QA 89
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLP--LLHNLdpelkapqILVLAPTRELAV-QVAEAmtdfskHM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 90 NGVAAACLNSTQTREQQLEVMtgcRTGQiRLLYIAPERLmldnfLEHLAHWNPVL-----LAVDEAHCISQWGHDFRPEy 164
Cdd:PRK11634 102 RGVNVVALYGGQRYDVQLRAL---RQGP-QIVVGTPGRL-----LDHLKRGTLDLsklsgLVLDEADEMLRMGFIEDVE- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 165 AALGQLRQRFPTLPFmalTATADDTTRQDIVRLLglNDPL---IQISSFDRPNIR--YMLMEKFKPLDQLMRYVQEQRGK 239
Cdd:PRK11634 172 TIMAQIPEGHQTALF---SATMPEAIRRITRRFM--KEPQevrIQSSVTTRPDISqsYWTVWGMRKNEALVRFLEAEDFD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 240 SGIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNI 319
Cdd:PRK11634 247 AAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDS 326
|
330 340 350
....*....|....*....|....*....|..
gi 7428315 320 ESYYQETGRAGRDGLPAEAMLFYDPADMAWLR 351
Cdd:PRK11634 327 ESYVHRIGRTGRAGRAGRALLFVENRERRLLR 358
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
32-346 |
4.43e-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: 78.72 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 32 QEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPAL--LLNGLT---VVVSPLISLMKDQVDQLQA------NGVAAACLN-- 98
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLeaLLEDPGataLYLYPTKALARDQLRRLRElaealgLGVRVATYDgd 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 99 -STQTREQQLEvmtgcrTGQIRLlyIAPErlMLD-NFLEHLAHWNPVL-----LAVDEAHcisqwghdfrpEY------- 164
Cdd:COG1205 141 tPPEERRWIRE------HPDIVL--TNPD--MLHyGLLPHHTRWARFFrnlryVVIDEAH-----------TYrgvfgsh 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 165 -AALgqLR--QRF-------PTlpFMALTATA-------------------DDTTRQDIVRLLGLNDPLIqissfDRPNI 215
Cdd:COG1205 200 vANV--LRrlRRIcrhygsdPQ--FILASATIgnpaehaerltgrpvtvvdEDGSPRGERTFVLWNPPLV-----DDGIR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 216 RYMLMEKfkpLDQLMRYVQeqRGKSGIIYCNSRAKVEDTAARLQSK------GISAAAYHAGLENNVRADVQEKFQRDDL 289
Cdd:COG1205 271 RSALAEA---ARLLADLVR--EGLRTLVFTRSRRGAELLARYARRAlrepdlADRVAAYRAGYLPEERREIERGLRSGEL 345
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 7428315 290 QIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAML--FYDPAD 346
Cdd:COG1205 346 LGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLvaGDDPLD 404
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
7-368 |
3.84e-14 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 74.48 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 7 EVLNLEsgaKQVLQETFGYQQFRPG--QEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLLNGLTVVVSPLISL--MKD 82
Cdd:PTZ00424 31 DALKLN---EDLLRGIYSYGFEKPSaiQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILapTRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 83 QVDQLQANGVAA---------ACLNSTQTREQQLEVMTGcrtgqIRLLYIAPERL--MLDNflEHLAHWNPVLLAVDEAH 151
Cdd:PTZ00424 108 LAQQIQKVVLALgdylkvrchACVGGTVVRDDINKLKAG-----VHMVVGTPGRVydMIDK--RHLRVDDLKLFILDEAD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 152 CISQWGhdFRpeyaalGQLRQRFPTLPFMALTATADDTTRQDIVRLLG--LNDP---LIQISSFDRPNIR--YMLMEKFK 224
Cdd:PTZ00424 181 EMLSRG--FK------GQIYDVFKKLPPDVQVALFSATMPNEILELTTkfMRDPkriLVKKDELTLEGIRqfYVAVEKEE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 225 -PLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGIN 303
Cdd:PTZ00424 253 wKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGID 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7428315 304 KPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAwlrrcleekpqgQLQDIERH 368
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 ... |
203-334 |
8.57e-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: 8.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 203 PLIQ-ISSFDRPNIRYMLMEKFKPLDQLMRYV---QEQRGKSGIIYCNSRAKVEDTAARLqsKGIsaAAYHAGLENNVRA 278
Cdd:cd18795 4 PLEEyVLGFNGLGIKLRVDVMNKFDSDIIVLLkieTVSEGKPVLVFCSSRKECEKTAKDL--AGI--AFHHAGLTREDRE 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7428315 279 DVQEKFQRDDLQIVVATVAFGMGINKPNVRFVV----HFDIPRNIE----SYYQETGRAGRDGL 334
Cdd:cd18795 80 LVEELFREGLIKVLVATSTLAAGVNLPARTVIIkgtqRYDGKGYRElsplEYLQMIGRAGRPGF 143
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
242-342 |
4.60e-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: 4.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 242 IIYCNSRAKVEDTAARLQskgisaaayhaglennvradvqekfqrddlqIVVATVAFGMGINKPNVRFVVHFDIPRNIES 321
Cdd:cd18785 7 IVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSAAS 55
|
90 100
....*....|....*....|..
gi 7428315 322 YYQETGRAGRDG-LPAEAMLFY 342
Cdd:cd18785 56 YIQRVGRAGRGGkDEGEVILFV 77
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
42-185 |
1.40e-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: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 42 GRDCLVVMPTGGGKSLCYQIPALLLN----GLTVVVSPLISLMKDQ---VDQLQANGVAAACLNSTQTREQQLEVmtgcR 114
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLlkkgKKVLVLVPTKALALQTaerLRELFGPGIRVAVLVGGSSAEEREKN----K 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7428315 115 TGQIRLLYIAPERLmLDNFLEHLAHWNP--VLLAVDEAHCISQWGHDFRPEYAALgqLRQRFPTLPFMALTAT 185
Cdd:cd00046 77 LGDADIIIATPDML-LNLLLREDRLFLKdlKLIIVDEAHALLIDSRGALILDLAV--RKAGLKNAQVILLSAT 146
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
21-341 |
3.21e-12 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 69.05 E-value: 3.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 21 ETFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLL-------------NGLTVVVSP---LISLMKDQV 84
Cdd:PLN00206 137 ETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRcctirsghpseqrNPLAMVLTPtreLCVQVEDQA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 85 dQLQANGV--AAACLNSTQTREQQLEvmtgcRTGQ-IRLLYIAPERLmLDNFLEHLAHWNPV-LLAVDEAHCISQWGhdF 160
Cdd:PLN00206 217 -KVLGKGLpfKTALVVGGDAMPQQLY-----RIQQgVELIVGTPGRL-IDLLSKHDIELDNVsVLVLDEVDCMLERG--F 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 161 RPEyaaLGQLRQRFPTLPFMALTATaddtTRQDIVRL---LGLNDPLIQISSFDRPNirymlmekfKPLDQLMRYVQEQR 237
Cdd:PLN00206 288 RDQ---VMQIFQALSQPQVLLFSAT----VSPEVEKFassLAKDIILISIGNPNRPN---------KAVKQLAIWVETKQ 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 238 GKS---------------GIIYCNSRAKVEDTA-ARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMG 301
Cdd:PLN00206 352 KKQklfdilkskqhfkppAVVFVSSRLGADLLAnAITVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRG 431
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 7428315 302 INKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLF 341
Cdd:PLN00206 432 VDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVF 471
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
242-340 |
3.36e-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: 3.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 242 IIYCNSRAKVE----DTAARLQSKGISA---AAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFD 314
Cdd:cd18797 39 IVFCRSRKLAElllrYLKARLVEEGPLAskvASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|....*.
gi 7428315 315 IPRNIESYYQETGRAGRDGLPAEAML 340
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDSLVIL 144
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
237-331 |
1.50e-10 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 64.14 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 237 RGKSgIIYCNSRAKVEDTAARLqskGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRfvVHFDIP 316
Cdd:COG1202 427 RGQT-IIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQ--VIFDSL 500
|
90 100
....*....|....*....|.
gi 7428315 317 R------NIESYYQETGRAGR 331
Cdd:COG1202 501 AmgiewlSVQEFHQMLGRAGR 521
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
24-333 |
3.73e-10 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 62.27 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 24 GYQqfRPG--QEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPAL--LLN------GLT--VVVSP---LISLMKDQVDQLQ 88
Cdd:PRK11192 20 GYT--RPTaiQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALqhLLDfprrksGPPriLILTPtreLAMQVADQARELA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 89 AN----------GVA----AACLNSTQtreqQLEVMTgcrTGqiRLL-YIAPErlmldNFLEHLAHWnpvlLAVDEAHCI 153
Cdd:PRK11192 98 KHthldiatitgGVAymnhAEVFSENQ----DIVVAT---PG--RLLqYIKEE-----NFDCRAVET----LILDEADRM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 154 SQWGhdFRPEYAAL-GQLRQRFPTLPFmalTATADDTTRQDIVRLLgLNDPlIQI----SSFDRPNIR--YML---ME-K 222
Cdd:PRK11192 160 LDMG--FAQDIETIaAETRWRKQTLLF---SATLEGDAVQDFAERL-LNDP-VEVeaepSRRERKKIHqwYYRaddLEhK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 223 FKPLDQLMRyvQEQRGKSgIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVAT-VAfGMG 301
Cdd:PRK11192 233 TALLCHLLK--QPEVTRS-IVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATdVA-ARG 308
|
330 340 350
....*....|....*....|....*....|....*
gi 7428315 302 INKPNVRFVVHFDIPRNIESYYQE---TGRAGRDG 333
Cdd:PRK11192 309 IDIDDVSHVINFDMPRSADTYLHRigrTGRAGRKG 343
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
40-344 |
1.09e-09 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 61.33 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 40 LSGRDCLVVMPTGGGKSLCYQIPA--------LLLNG---LTVVVSPLISLMkDQVDQlQANGVAA-------ACLNSTQ 101
Cdd:PTZ00110 165 LSGRDMIGIAETGSGKTLAFLLPAivhinaqpLLRYGdgpIVLVLAPTRELA-EQIRE-QCNKFGAsskirntVAYGGVP 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 102 TREQQLEVMTGcrtgqIRLLYIAPERLMldNFLE-HLAHWNPV-LLAVDEAHCISQWGhdFRPEYAAL-GQLRQRFPTLP 178
Cdd:PTZ00110 243 KRGQIYALRRG-----VEILIACPGRLI--DFLEsNVTNLRRVtYLVLDEADRMLDMG--FEPQIRKIvSQIRPDRQTLM 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 179 FMA-----LTATADDTTRQDIVRllglndplIQISSFDRP---NIRYMLM-----EKFKPLDQLMRYVQEQRGKSgIIYC 245
Cdd:PTZ00110 314 WSAtwpkeVQSLARDLCKEEPVH--------VNVGSLDLTachNIKQEVFvveehEKRGKLKMLLQRIMRDGDKI-LIFV 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 246 NSRaKVEDTAAR-LQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQ 324
Cdd:PTZ00110 385 ETK-KGADFLTKeLRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVH 463
|
330 340
....*....|....*....|
gi 7428315 325 ETGRAGRDGLPAEAMLFYDP 344
Cdd:PTZ00110 464 RIGRTGRAGAKGASYTFLTP 483
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
237-331 |
1.70e-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: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 237 RGKSGIIYCNSRAKVEDTAARL------QSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFV 310
Cdd:cd18796 37 RHKSTLVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLV 116
|
90 100
....*....|....*....|.
gi 7428315 311 VHFDIPRNIESYYQETGRAGR 331
Cdd:cd18796 117 IQIGSPKSVARLLQRLGRSGH 137
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
7-331 |
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 7428315 7 EVLNLESGAKQVLQETfGYQQFRPGQEEIIDT-VLSGRDCLVVMPTGGGKSLCYQIPAL--LLN--GLTVVVSPLISLMK 81
Cdd:PRK00254 4 DELRVDERIKRVLKER-GIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVnkLLRegGKAVYLVPLKALAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 82 DQVDQLQ-----ANGVAAACLNSTQTREQqlevmtgcrTGQIRLLYIAPERLmlDNFLEHLAHW--NPVLLAVDEAHCIS 154
Cdd:PRK00254 83 EKYREFKdweklGLRVAMTTGDYDSTDEW---------LGKYDIIIATAEKF--DSLLRHGSSWikDVKLVVADEIHLIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 155 QWGHDFRPEYAaLGQLRQRFPTLPFMALTATADDTTRQdivrllgLNDPLIqISSFDRPNIRYML------------MEK 222
Cdd:PRK00254 152 SYDRGATLEMI-LTHMLGRAQILGLSATVGNAEELAEW-------LNAELV-VSDWRPVKLRKGVfyqgflfwedgkIER 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 223 FKPLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLqSKGIS----------------------------------AAAY 268
Cdd:PRK00254 223 FPNSWESLVYDAVKKGKGALVFVNTRRSAEKEALEL-AKKIKrfltkpelralkeladsleenptneklkkalrggVAFH 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7428315 269 HAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVH----------FDIPrnIESYYQETGRAGR 331
Cdd:PRK00254 302 HAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRdtkrysnfgwEDIP--VLEIQQMMGRAGR 372
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
495-610 |
6.99e-08 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 54.88 E-value: 6.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 495 QLTEAARPVLAESSLQ-LAVPRIVALKPKAMQKSFGGNY--DRKLFAKLRKL---RKSIADESNVPPYVVFNDATLIEMA 568
Cdd:COG0349 165 ELEREGRLEWAEEECArLLDPATYREDPEEAWLRLKGAWklNPRQLAVLRELaawREREARKRDVPRNRVLKDEALLELA 244
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 7428315 569 EQMPITASEMLSVNGVGMRKLERFGKPFMALIRAHVDGDDEE 610
Cdd:COG0349 245 RRQPKSLEELARLRGLSPGEIRRHGEELLAAVAEALALPEEE 286
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
215-333 |
1.20e-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: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 215 IRYMLMEKFKPLDQLMRYVQEQRGKSgIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDD--LQIV 292
Cdd:cd18793 5 IEEVVSGKLEALLELLEELREPGEKV-LIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFL 83
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 7428315 293 VATVAFGMGINKPNVRFVVHFDIPRN--IESyyQETGRAGRDG 333
Cdd:cd18793 84 LSTKAGGVGLNLTAANRVILYDPWWNpaVEE--QAIDRAHRIG 124
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
229-341 |
2.79e-07 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 53.42 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 229 LMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVR 308
Cdd:PRK04537 248 LLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVK 327
|
90 100 110
....*....|....*....|....*....|...
gi 7428315 309 FVVHFDIPRNIESYYQETGRAGRDGLPAEAMLF 341
Cdd:PRK04537 328 YVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
228-333 |
3.27e-06 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 50.27 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 228 QLMRYVQEQRGKSgIIYCNSRAKVEDTAARLQS---------------------------KGIsaAAYHAGLENNVRADV 280
Cdd:PRK01172 227 SLIKETVNDGGQV-LVFVSSRKNAEDYAEMLIQhfpefndfkvssennnvyddslnemlpHGV--AFHHAGLSNEQRRFI 303
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7428315 281 QEKFQRDDLQIVVATVAFGMGINKPnVRFVVHFDIPR----------NIEsYYQETGRAGRDG 333
Cdd:PRK01172 304 EEMFRNRYIKVIVATPTLAAGVNLP-ARLVIVRDITRygnggirylsNME-IKQMIGRAGRPG 364
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
221-333 |
3.72e-06 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 49.91 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 221 EKFKPLDQLMRyvqEQRGKSGIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGM 300
Cdd:PRK01297 321 DKYKLLYNLVT---QNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGR 397
|
90 100 110
....*....|....*....|....*....|...
gi 7428315 301 GINKPNVRFVVHFDIPRNIESYYQETGRAGRDG 333
Cdd:PRK01297 398 GIHIDGISHVINFTLPEDPDDYVHRIGRTGRAG 430
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
24-367 |
4.02e-06 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 49.42 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 24 GYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLLngltvvvsplisLMKDQVDQLQANGVAAACLnsTQTR 103
Cdd:PRK10590 20 GYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQH------------LITRQPHAKGRRPVRALIL--TPTR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 104 EQQLEV---------------------------MTGCRTGqIRLLYIAPERLmLDnflehLAHWNPV------LLAVDEA 150
Cdd:PRK10590 86 ELAAQIgenvrdyskylnirslvvfggvsinpqMMKLRGG-VDVLVATPGRL-LD-----LEHQNAVkldqveILVLDEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 151 HCISQWG--HDFRPEYAALGQLRQRfptlpfMALTATADDTTRQDIVRLLglNDPL-IQI----SSFDRPNIRYMLMEKF 223
Cdd:PRK10590 159 DRMLDMGfiHDIRRVLAKLPAKRQN------LLFSATFSDDIKALAEKLL--HNPLeIEVarrnTASEQVTQHVHFVDKK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 224 KPLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGIN 303
Cdd:PRK10590 231 RKRELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLD 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7428315 304 KPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYdpadmawlrrCLEEkpQGQLQDIER 367
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 ... |
32-151 |
5.02e-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: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 32 QEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPAL--LL---NGLTVVVSPLISLMKDQVDQLQA------NGVAAACLN-S 99
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILeaLLrdpGSRALYLYPTKALAQDQLRSLRElleqlgLGIRVATYDgD 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7428315 100 TQTREqqlevmtgcRTGQIRllyiAPERLMLDNF--LEHL-----AHWNPVL-----LAVDEAH 151
Cdd:cd17923 85 TPREE---------RRAIIR----NPPRILLTNPdmLHYAllphhDRWARFLrnlryVVLDEAH 135
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
257-334 |
5.87e-06 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 49.55 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 257 RLQSKGIsaAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPnVRFVV-----------HFDI-PRnieSYYQ 324
Cdd:COG4581 296 RLLRRGI--AVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMP-ARTVVftklskfdgerHRPLtAR---EFHQ 369
|
90
....*....|
gi 7428315 325 ETGRAGRDGL 334
Cdd:COG4581 370 IAGRAGRRGI 379
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
226-331 |
8.86e-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: 8.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 226 LDQLMRYVQE--QRGKSGIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDD--LQIVVATVAFGMG 301
Cdd:COG0553 535 LEALLELLEEllAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEG 614
|
90 100 110
....*....|....*....|....*....|
gi 7428315 302 INKPNVRFVVHFDIPRNIESYYQETGRAGR 331
Cdd:COG0553 615 LNLTAADHVIHYDLWWNPAVEEQAIDRAHR 644
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
28-185 |
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 7428315 28 FRPGQEEIIDTVL---SGRDCLVVMPTGGGKSLC-YQIPALLLNGLTVVVSPLISLMKDQVDQL-QANGVAAACL---NS 99
Cdd:cd17926 1 LRPYQEEALEAWLahkNNRRGILVLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFeDFLGDSSIGLiggGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 100 TQTREQQLEVMTgcrTGQIRLLYIAPERLMLDNFLehlahwnpvLLAVDEAHCIS--QWGHdfrpeyaalgqLRQRFPTL 177
Cdd:cd17926 81 KKDFDDANVVVA---TYQSLSNLAEEEKDLFDQFG---------LLIVDEAHHLPakTFSE-----------ILKELNAK 137
|
....*...
gi 7428315 178 PFMALTAT 185
Cdd:cd17926 138 YRLGLTAT 145
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
14-74 |
3.50e-05 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 46.84 E-value: 3.50e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7428315 14 GAKQVLQETFGYQQFRPGQ----EEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLL---NGLTVVVS 74
Cdd:COG1199 1 ADDGLLALAFPGFEPRPGQremaEAVARALAEGRHLLIEAGTGTGKTLAYLVPALLAareTGKKVVIS 68
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
42-151 |
4.01e-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: 44.50 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 42 GRDCLVVMPTGGGKSLCYQIPALL------LNGLTVV-VSPLISLMKDQVDQLQangvaAAClnstqtREQQLEVMTGCR 114
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSsladepEKGVQVLyISPLKALINDQERRLE-----EPL------DEIDLEIPVAVR 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 7428315 115 TG---------QIR----LLYIAPERL--MLDNflEHLAHwnpvLLA------VDEAH 151
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 ... |
238-331 |
6.33e-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: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 238 GKSGIIYCNS---RAKVEDTAARLQSKGISAAAYHAGLENNVradvqEKFQRDDLQIVVATVAF-GM---GINKPN-VRF 309
Cdd:cd18798 24 GDGGLIFVSIdygKEYAEELKEFLERHGIKAELALSSTEKNL-----EKFEEGEIDVLIGVASYyGVlvrGIDLPErIKY 98
|
90 100
....*....|....*....|..
gi 7428315 310 VVHFDIPrnIESYYQETGRAGR 331
Cdd:cd18798 99 AIFYGVP--VTTYIQASGRTSR 118
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
217-333 |
1.21e-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: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 217 YMLMEK-FKPLDQLMRYVQEQRGKSGIIYCNSRAKV----------EDTAARLQSK-----GISAAAYHAGLENNVRADV 280
Cdd:cd18802 3 IVVIPKlQKLIEILREYFPKTPDFRGIIFVERRATAvvlsrllkehPSTLAFIRCGfligrGNSSQRKRSLMTQRKQKET 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 7428315 281 QEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDG 333
Cdd:cd18802 83 LDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN 135
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
239-331 |
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 7428315 239 KSGIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRAD-VQEKFQRDDLQIVVA-TVA-FGMGINKPNVRFVVhFDi 315
Cdd:cd18799 7 IKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDeALILLFFGELKPPILvTVDlLTTGVDIPEVDNVV-FL- 84
|
90
....*....|....*....
gi 7428315 316 pRNIES---YYQETGRAGR 331
Cdd:cd18799 85 -RPTESrtlFLQMLGRGLR 102
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
24-64 |
1.84e-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: 1.84e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 7428315 24 GYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPAL 64
Cdd:cd00268 9 GFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPIL 49
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
27-185 |
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 7428315 27 QFRPGQEEIIDT-VLSGRDCLVVMPTGGGKSLCYQ---IPALLLNGLTVVVSPLISLmkdqvdqlqangvAAACLNSTQT 102
Cdd:cd18028 1 ELYPPQAEAVRAgLLKGENLLISIPTASGKTLIAEmamVNTLLEGGKALYLVPLRAL-------------ASEKYEEFKK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 103 REqQLEVMTGCRTGQIRllyIAPERLM-----------LDNFLEHLAHW-NPV-LLAVDEAHCISQWGHDFRPEyAALGQ 169
Cdd:cd18028 68 LE-EIGLKVGISTGDYD---EDDEWLGdydiivatyekFDSLLRHSPSWlRDVgVVVVDEIHLISDEERGPTLE-SIVAR 142
|
170
....*....|....*.
gi 7428315 170 LRQRFPTLPFMALTAT 185
Cdd:cd18028 143 LRRLNPNTQIIGLSAT 158
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
242-333 |
2.89e-04 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 43.42 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 242 IIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 321
Cdd:PRK04837 259 IIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCED 338
|
90
....*....|..
gi 7428315 322 YYQETGRAGRDG 333
Cdd:PRK04837 339 YVHRIGRTGRAG 350
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
32-185 |
5.27e-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: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 32 QEEIIDTVLSGRDCLVVMPTGGGKSLC--YQIPALLL---NGLTVVVSPLISLmkdqVDQLQANGVA---------AACL 97
Cdd:cd18025 6 QRELLDIVDRRESALIVAPTSSGKTFIsyYCMEKVLResdDGVVVYVAPTKAL----VNQVVAEVYArfskkyppsGKSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 98 NSTQTREQQLEVMTGCrtgQIrlLYIAPERLMLDNFLEHLAHWNPVLLAV--DEAHCISQWGHdfrpeyaalGQLRQRFP 175
Cdd:cd18025 82 WGVFTRDYRHNNPMNC---QV--LITVPECLEILLLSPHNASWVPRIKYVifDEIHSIGQSED---------GAVWEQLL 147
|
170
....*....|...
gi 7428315 176 TL---PFMALTAT 185
Cdd:cd18025 148 LLipcPFLALSAT 160
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
226-342 |
6.10e-04 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 42.99 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 226 LDQLMRYvqeqrgKSGIIYCNSRAKVEDTAARL---------QSKGISAAA------------------------YHAGL 272
Cdd:PRK09751 238 LDEVLRH------RSTIVFTNSRGLAEKLTARLnelyaarlqRSPSIAVDAahfestsgatsnrvqssdvfiarsHHGSV 311
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 273 ENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFY 342
Cdd:PRK09751 312 SKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGHQVGGVSKGLFF 381
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
28-202 |
6.96e-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: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 28 FRPGQEEIIDTV-LSGRDCLVVMPTGGGKSLC--YQIPALLL--NGLTVVVSPLISLMKDQVDQLQ-----ANGVAAAC- 96
Cdd:cd17921 2 LNPIQREALRALyLSGDSVLVSAPTSSGKTLIaeLAILRALAtsGGKAVYIAPTRALVNQKEADLRerfgpLGKNVGLLt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 97 ----LNSTQTREQQLEVMTgcrtgqirllyiaPERL--MLDNfLEHLAHWNPVLLAVDEAHCISQwghdfrPEYAALGQ- 169
Cdd:cd17921 82 gdpsVNKLLLAEADILVAT-------------PEKLdlLLRN-GGERLIQDVRLVVVDEAHLIGD------GERGVVLEl 141
|
170 180 190
....*....|....*....|....*....|....*..
gi 7428315 170 ----LRQRFPTLPFMALTATADDTtrQDIVRLLGLND 202
Cdd:cd17921 142 llsrLLRINKNARFVGLSATLPNA--EDLAEWLGVED 176
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
227-330 |
7.01e-04 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 42.57 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 227 DQLMRYVQEQRgkSGIIYCNSRAKVEDTAARLQSK-----GISA-AAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGM 300
Cdd:PRK13767 275 ETLHELIKEHR--TTLIFTNTRSGAERVLYNLRKRfpeeyDEDNiGAHHSSLSREVRLEVEEKLKRGELKVVVSSTSLEL 352
|
90 100 110
....*....|....*....|....*....|
gi 7428315 301 GINKPNVRFVVHFDIPRNIESYYQETGRAG 330
Cdd:PRK13767 353 GIDIGYIDLVVLLGSPKSVSRLLQRIGRAG 382
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
21-65 |
7.99e-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: 7.99e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 7428315 21 ETFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALL 65
Cdd:cd17957 6 EESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQ 50
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
24-112 |
9.65e-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: 9.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 24 GYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALL-----------LNGLTV-VVSP---LISLMKDQVDQLQ 88
Cdd:cd17958 9 GFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIhldlqpipreqRNGPGVlVLTPtreLALQIEAECSKYS 88
|
90 100
....*....|....*....|....
gi 7428315 89 ANGVAAACLNSTQTREQQLEVMTG 112
Cdd:cd17958 89 YKGLKSVCVYGGGNRNEQIEDLSK 112
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
16-150 |
9.73e-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: 9.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 16 KQVLQEtFGYQQFRPGQEEIIDTVLSG---------RDCLVVMPTGGGKSLCYQIP---ALL------LNGLTVV-VSPL 76
Cdd:cd17956 2 LKNLQN-NGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPivqALSkrvvprLRALIVVpTKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 77 ISLMKDQVDQLQANGV--AAACLNSTQTREQQLEVMTGCRTGQ---IRLLYIAPERLM--LDN---F-LEHLAhwnpvLL 145
Cdd:cd17956 81 VQQVYKVFESLCKGTGlkVVSLSGQKSFKKEQKLLLVDTSGRYlsrVDILVATPGRLVdhLNStpgFtLKHLR-----FL 155
|
....*
gi 7428315 146 AVDEA 150
Cdd:cd17956 156 VIDEA 160
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
16-75 |
1.63e-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: 1.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7428315 16 KQVLQEtFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPAL--LLNGLT---------VVVSP 75
Cdd:cd17960 2 LDVVAE-LGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLeiLLKRKAnlkkgqvgaLIISP 71
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
265-340 |
1.74e-03 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 41.48 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 265 AAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVV----HFD-----IPRNIESYYQETGRAGRDGL- 334
Cdd:PRK02362 306 AAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIrdyrRYDggagmQPIPVLEYHQMAGRAGRPGLd 385
|
....*..
gi 7428315 335 P-AEAML 340
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 ... |
24-64 |
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 7428315 24 GYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPAL 64
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) ... |
17-64 |
5.88e-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: 5.88e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 7428315 17 QVLQEtFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPAL 64
Cdd:cd17953 25 DLIKK-LGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMF 71
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
27-151 |
7.01e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 37.65 E-value: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7428315 27 QFRPGQEEIIDTVLSGRDC-----LVVMPTGGGKSLCY-QIPALLLNGL----TVVVSPLISLMKDQVDQLQANGVAAAC 96
Cdd:pfam04851 3 ELRPYQIEAIENLLESIKNgqkrgLIVMATGSGKTLTAaKLIARLFKKGpikkVLFLVPRKDLLEQALEEFKKFLPNYVE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7428315 97 LNstqtreqqlEVMTGCR----TGQIRLLYIAPERLM--LDNFLEHLAHWNPVLLAVDEAH 151
Cdd:pfam04851 83 IG---------EIISGDKkdesVDDNKIVVTTIQSLYkaLELASLELLPDFFDVIIIDEAH 134
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
24-64 |
9.53e-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: 9.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 7428315 24 GYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPAL 64
Cdd:cd17952 9 EYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPML 49
|
|
| |
