|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
5-612 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 1277.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 5 LIAEQTPTPANDAQDILQDVFGYQSFRDGQQEVIDLAVEGKDSLVIMPTGGGKSLCYQIPALVRDGLTLVISPLISLMKD 84
Cdd:PRK11057 1 MAQAEVLNLESLAKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 85 QVDQLKANGVAAECINSSMPRDQLLSVFNRMNSGQLKMVYASPERVLMRDFIERLQGLPLSMIAVDEAHCISQWGHDFRP 164
Cdd:PRK11057 81 QVDQLLANGVAAACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 165 EYASLGQLKQYFPHVPYMALTATADDATRKDIISRLQLVDPHTHLGSFDRPNIRYNLVEKHKPVSQVVRYLETQKGNCGI 244
Cdd:PRK11057 161 EYAALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQLMRYVQEQRGKSGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 245 IYCGSRKKVEMVTEKLCNNGIRAAGYHAGMDTDERAYVQEAFQRDDIQIVVATVAFGMGINKPNVRFVVHFDIPRNIESY 324
Cdd:PRK11057 241 IYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 325 YQETGRAGRDGLPAEAMMLFDPADMGWLRRMLDEKEEGPQKQVEMHKLNAMSAFAEAQTCRRQVLLNYFGEYREKQCGNC 404
Cdd:PRK11057 321 YQETGRAGRDGLPAEAMLFYDPADMAWLRRCLEEKPAGQQQDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 405 DICLDPPKHFDATQEAQKALSCVYRVNQSFGMGYVVEVMRGMQNIRVRDNGHDKLSTYGIGRDHSHDYWISIFRQLIHKG 484
Cdd:PRK11057 401 DICLDPPKQYDGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 485 LLFQNITRNSTLQLTEEARPLLRGEMSLELAVPRLDTAvRNAKSDKLSSKNYDKKLFAKLRKLRKSIADEDGLPPYVVFS 564
Cdd:PRK11057 481 LVTQNIAQHSALQLTEAARPVLRGEVSLQLAVPRIVAL-KPRAMQKSFGGNYDRKLFAKLRKLRKSIADEENIPPYVVFN 559
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 501628854 565 DATLIDMAEILPTSYGEMLAVNGVGQRKLDKYADPFLDLIQEHITTHG 612
Cdd:PRK11057 560 DATLIEMAEQMPITASEMLSVNGVGQRKLERFGKPFMALIRAHVDGDD 607
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
17-607 |
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: 869.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 17 AQDILQDVFGYQSFRDGQQEVIDLAVEGKDSLVIMPTGGGKSLCYQIPALVRDGLTLVISPLISLMKDQVDQLKANGVAA 96
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 97 ECINSSMPRDQLLSVFNRMNSGQLKMVYASPERVLMRDFIERLQGLPLSMIAVDEAHCISQWGHDFRPEYASLGQLKQYF 176
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 177 PHVPYMALTATADDATRKDIISRLQLVDPHTHLGSFDRPNIRYNLVEKHKPVSQVVRYLETQKGNCGIIYCGSRKKVEMV 256
Cdd:TIGR01389 161 PQVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 257 TEKLCNNGIRAAGYHAGMDTDERAYVQEAFQRDDIQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGL 336
Cdd:TIGR01389 241 AERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 337 PAEAMMLFDPADMGWLRRMLDEKE-EGPQKQVEMHKLNAMSAFAEAQTCRRQVLLNYFGEYREKQCGNCDICLDPPKHFD 415
Cdd:TIGR01389 321 PAEAILLYSPADIALLKRRIEQSEaDDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENEVEPCGNCDNCLDPPKSYD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 416 ATQEAQKALSCVYRVNQSFGMGYVVEVMRGMQNIRVRDNGHDKLSTYGIGRDHSHDYWISIFRQLIHKGLLFQNITRNST 495
Cdd:TIGR01389 401 ATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEIYIG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 496 LQLTEEARPLLRGEMSLELAVPRLDtAVRNAKSDKLSSKNYDKKLFAKLRKLRKSIADEDGLPPYVVFSDATLIDMAEIL 575
Cdd:TIGR01389 481 LQLTEAARKVLKNEVEVLLRPFKVV-AKEKTRVQKNLSVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAEKR 559
|
570 580 590
....*....|....*....|....*....|..
gi 501628854 576 PTSYGEMLAVNGVGQRKLDKYADPFLDLIQEH 607
Cdd:TIGR01389 560 PATLNALLKIKGVGQNKLDRYGEAFLEVIREY 591
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
15-487 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 817.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 15 NDAQDILQDVFGYQSFRDGQQEVIDLAVEGKDSLVIMPTGGGKSLCYQIPALVRDGLTLVISPLISLMKDQVDQLKANGV 94
Cdd:COG0514 3 DDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 95 AAECINSSMPRDQLLSVFNRMNSGQLKMVYASPERVLMRDFIERLQGLPLSMIAVDEAHCISQWGHDFRPEYASLGQLKQ 174
Cdd:COG0514 83 RAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGELRE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 175 YFPHVPYMALTATADDATRKDIISRLQLVDPHTHLGSFDRPNIRYNLVEK--HKPVSQVVRYLETQKGNCGIIYCGSRKK 252
Cdd:COG0514 163 RLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKppDDKLAQLLDFLKEHPGGSGIVYCLSRKK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 253 VEMVTEKLCNNGIRAAGYHAGMDTDERAYVQEAFQRDDIQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAG 332
Cdd:COG0514 243 VEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 333 RDGLPAEAMMLFDPADMGWLRRMLDEKEEGP-QKQVEMHKLNAMSAFAEAQTCRRQVLLNYFGEYREKQCGNCDICLDPP 411
Cdd:COG0514 323 RDGLPAEALLLYGPEDVAIQRFFIEQSPPDEeRKRVERAKLDAMLAYAETTGCRRQFLLRYFGEELAEPCGNCDNCLGPP 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501628854 412 KHFDATQEAQKALSCVYRVNQSFGMGYVVEVMRGMQNIRVRDNGHDKLSTYGIGRDHSHDYWISIFRQLIHkgLLF 487
Cdd:COG0514 403 ETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLLA--QLF 476
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
19-467 |
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: 659.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 19 DILQDVFGYQSFRDGQQEVIDLAVEGKDSLVIMPTGGGKSLCYQIPALVRDGLTLVISPLISLMKDQVDQLKANGVAAEC 98
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 99 INSSMPRDQLLSVFNRMNSGQLKMVYASPERVLM-RDFIERLQG-LPLSMIAVDEAHCISQWGHDFRPEYASLGQLKQYF 176
Cdd:TIGR00614 81 LNSAQTKEQQLNVLTDLKDGKIKLLYVTPEKISAsNRLLQTLEErKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 177 PHVPYMALTATADDATRKDIISRLQLVDPHTHLGSFDRPNIRYNLVEK-HKPVSQVVRYL-ETQKGNCGIIYCGSRKKVE 254
Cdd:TIGR00614 161 PNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKtPKILEDLLRFIrKEFEGKSGIIYCPSRKKVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 255 MVTEKLCNNGIRAAGYHAGMDTDERAYVQEAFQRDDIQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRD 334
Cdd:TIGR00614 241 QVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGRD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 335 GLPAEAMMLFDPADMGWLRRMLDEKEEGPQKQVEMHKLNAMSAFAEAQTCRRQVLLNYFGE----------YREKQCGNC 404
Cdd:TIGR00614 321 GLPSECHLFYAPADMNRLRRLLMEEPDGNFRTYKLKLYEMMEYCLNSSTCRRLILLSYFGEkgfnksfcimGTEKCCDNC 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501628854 405 DICLD------PPKHFDATQEAQKALSCVYRVNQSFGMGYVVEVMRGMQNIRVRDNGHDKLSTYGIGRD 467
Cdd:TIGR00614 401 CKRLDyktkdvTDKVYDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGRGKD 469
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
24-611 |
1.23e-132 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 417.37 E-value: 1.23e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 24 VFGYQSFRDGQQEVIDLAVEGKDSLVIMPTGGGKSLCYQIPALVRDGLTLVISPLISLMKDQVDQLKANGVAAECINSSM 103
Cdd:PLN03137 455 VFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSAGM 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 104 PRDQLLSVFNRMNSG--QLKMVYASPERV-----LMRDfIERL--QGLpLSMIAVDEAHCISQWGHDFRPEYASLGQLKQ 174
Cdd:PLN03137 535 EWAEQLEILQELSSEysKYKLLYVTPEKVaksdsLLRH-LENLnsRGL-LARFVIDEAHCVSQWGHDFRPDYQGLGILKQ 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 175 YFPHVPYMALTATADDATRKDIISRLQLVDPHTHLGSFDRPNIRYNLVEKHKP----VSQVVRylETQKGNCGIIYCGSR 250
Cdd:PLN03137 613 KFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKKcledIDKFIK--ENHFDECGIIYCLSR 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 251 KKVEMVTEKLCNNGIRAAGYHAGMDTDERAYVQEAFQRDDIQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGR 330
Cdd:PLN03137 691 MDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGR 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 331 AGRDGLPAEAMMLFDPADMGWLRRMLDEK--EEGPQK-------------QVEMHKLNAMSAFAEAQT-CRRQVLLNYFG 394
Cdd:PLN03137 771 AGRDGQRSSCVLYYSYSDYIRVKHMISQGgvEQSPMAmgynrmassgrilETNTENLLRMVSYCENEVdCRRFLQLVHFG 850
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 395 E-YREKQCGN-CDICLDpPKHF---DATQEAQKALSCVYRVNQSFGMGYVVEVMRGMQNIRVRDNGHDKLSTYGIGRDHS 469
Cdd:PLN03137 851 EkFDSTNCKKtCDNCSS-SKSLidkDVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLSLHGAGKHLS 929
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 470 HDYWISIFRQLIHKGLLFQNITR-------NSTLQLTE-EARPLLRGEMSLELAVPRLDTAVRNAKSDKLSSK------- 534
Cdd:PLN03137 930 KGEASRILHYLVTEDILAEDVKKsdlygsvSSLLKVNEsKAYKLFSGGQTIIMRFPSSVKASKPSKFEATPAKgpltsgk 1009
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 535 ----------------NYDKKLFAKLRKLRKSIADE--DGLPPYVVFSDATLIDMAEILPTSYGEMLAVNGVGQRKLDKY 596
Cdd:PLN03137 1010 qstlpmatpaqppvdlNLSAILYTALRKLRTALVKEagDGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKAKVSKY 1089
|
650
....*....|....*
gi 501628854 597 ADPFLDLIQEHITTH 611
Cdd:PLN03137 1090 GDRLLETIESTINEY 1104
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
18-213 |
6.56e-107 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 320.25 E-value: 6.56e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 18 QDILQDVFGYQSFRDGQQEVIDLAVEGKDSLVIMPTGGGKSLCYQIPALVRDGLTLVISPLISLMKDQVDQLKANGVAAE 97
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 98 CINSSMPRDQLLSVFNRMNSGQLKMVYASPERVLMRDFIERLQGLP----LSMIAVDEAHCISQWGHDFRPEYASLGQLK 173
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLRLGRLR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 501628854 174 QYFPHVPYMALTATADDATRKDIISRLQLVDPHTHLGSFD 213
Cdd:cd17920 161 RALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
20-200 |
1.94e-72 |
|
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: 231.38 E-value: 1.94e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 20 ILQDVFGYQSFRDGQQEVIDLAVEGKDSLVIMPTGGGKSLCYQIPALV----RDGLTLVISPLISLMKDQVDQLKAnGVA 95
Cdd:cd18018 3 LLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLlrrrGPGLTLVVSPLIALMKDQVDALPR-AIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 96 AECINSSMPRDQLLSVFNRMNSGQLKMVYASPERVLMRDFIERLQGL-PLSMIAVDEAHCISQWGHDFRPEYASLGQLKQ 174
Cdd:cd18018 82 AAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTpPISLLVVDEAHCISEWSHNFRPDYLRLCRVLR 161
|
170 180
....*....|....*....|....*..
gi 501628854 175 YFPHV-PYMALTATADDATRKDIISRL 200
Cdd:cd18018 162 ELLGApPVLALTATATKRVVEDIASHL 188
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
17-213 |
1.35e-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: 1.35e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 17 AQDILQDVFGYQSFRDGQQEVIDLAVEGKDSLVIMPTGGGKSLCYQIPALVRDGLTLVISPLISLMKDQVDQLKANGVAA 96
Cdd:cd18015 6 VKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 97 ECINSSMPRDQLLSVFNRMNSG--QLKMVYASPERVLM-RDFIERLQ-----GLpLSMIAVDEAHCISQWGHDFRPEYAS 168
Cdd:cd18015 86 TMLNASSSKEHVKWVHAALTDKnsELKLLYVTPEKIAKsKRFMSKLEkaynaGR-LARIAIDEVHCCSQWGHDFRPDYKK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 501628854 169 LGQLKQYFPHVPYMALTATADDATRKDIISRLQLVDPHTHLGSFD 213
Cdd:cd18015 165 LGILKRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
214-344 |
8.66e-62 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 200.90 E-value: 8.66e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 214 RPNIRYNLVEKHKP---VSQVVRYLETQKGNCGIIYCGSRKKVEMVTEKLCNNGIRAAGYHAGMDTDERAYVQEAFQRDD 290
Cdd:cd18794 1 RPNLFYSVRPKDKKdekLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 501628854 291 IQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMMLF 344
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
19-213 |
9.67e-62 |
|
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: 203.08 E-value: 9.67e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 19 DILQDVFGYQSFRDGQQEVIDLAVE-GKDSLVIMPTGGGKSLCYQIPALVRDGLTLVISPLISLMKDQVDQLKANGVAAE 97
Cdd:cd18017 2 NALNEYFGHSSFRPVQWKVIRSVLEeRRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPAC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 98 CINSSMPRDqllsVFNRMNSGQLKMVYASPERVLMRDFIERLQGLPLSMIAVDEAHCISQWGHDFRPEYASLGQLKQYFP 177
Cdd:cd18017 82 FLGSAQSQN----VLDDIKMGKIRVIYVTPEFVSKGLELLQQLRNGITLIAIDEAHCVSQWGHDFRSSYRHLGSIRNRLP 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 501628854 178 HVPYMALTATADDATRKDIISRLQLVDPHTHLGSFD 213
Cdd:cd18017 158 NVPIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
19-213 |
1.48e-57 |
|
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: 192.35 E-value: 1.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 19 DILQDVFGYQSFRDGQQEVIDLAVEGKDSLVIMPTGGGKSLCYQIPALVRDGLTLVISPLISLMKDQVDQLKANGVAAEC 98
Cdd:cd18016 7 KIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 99 INSSMPRDQLLSVFNRMNSGQ--LKMVYASPERVLMRD-FIERLQGLP----LSMIAVDEAHCISQWGHDFRPEYASLGQ 171
Cdd:cd18016 87 LTGDKTDAEATKIYLQLSKKDpiIKLLYVTPEKISASNrLISTLENLYerklLARFVIDEAHCVSQWGHDFRPDYKRLNM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 501628854 172 LKQYFPHVPYMALTATADDATRKDIISRLQLVDPHTHLGSFD 213
Cdd:cd18016 167 LRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
18-205 |
2.85e-57 |
|
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: 191.53 E-value: 2.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 18 QDILQDVFGYQSFR-DGQQEVIDLAVEGK-DSLVIMPTGGGKSLCYQIPALVRDGLTLVISPLISLMKDQVDQLKANGVA 95
Cdd:cd18014 1 RSTLKKVFGHSDFKsPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 96 AECINSSMPRDQLLSVFNRMNSG--QLKMVYASPERVLMRDFIERLQGL----PLSMIAVDEAHCISQWGHDFRPEYASL 169
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADLESEkpQTKFLYITPEMAATSSFQPLLSSLvsrnLLSYLVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 501628854 170 GQLKQYFPHVPYMALTATADDATRKDIISRLQLVDP 205
Cdd:cd18014 161 GALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKP 196
|
|
| DpdF |
NF041063 |
protein DpdF; |
20-355 |
5.65e-54 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 197.06 E-value: 5.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 20 ILQDVFGYQSFRD-GQQEVID---LAVEGKDSLVIMPTGGGKSLCYQIPALV---RDGLTLVISPLISLMKDQVDQLKAN 92
Cdd:NF041063 130 FLAEALGFTHYRSpGQREAVRaalLAPPGSTLIVNLPTGSGKSLVAQAPALLasrQGGLTLVVVPTVALAIDQERRAREL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 93 GVAAECIN-------SSMPRDQLLSVFNRMNSGQLKMVYASPERVLM--RDFIERL--QGLpLSMIAVDEAHCISQWGHD 161
Cdd:NF041063 210 LRRAGPDLggplawhGGLSAEERAAIRQRIRDGTQRILFTSPESLTGslRPALFDAaeAGL-LRYLVVDEAHLVDQWGDG 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 162 FRPEYASLGQL------KQYFPHVP-YMALTATADDATRKDI------ISRLQLVDphthlGSFDRPNIRY------NLV 222
Cdd:NF041063 289 FRPEFQLLAGLrrsllrLAPSGRPFrTLLLSATLTESTLDTLetlfgpPGPFIVVS-----AVQLRPEPAYwvakcdSEE 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 223 EKHKPVSQVVRYLetqkgncgIIYCGSRKKVEMVTEKLCNNGI-RAAGYHAGMDTDERAYVQEAFQRDDIQIVVATVAFG 301
Cdd:NF041063 364 ERRERVLEALRHLpr----plILYVTKVEDAEAWLQRLRAAGFrRVALFHGDTPDAERERLIEQWRENELDIVVATSAFG 439
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 501628854 302 MGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMMLFDPADMGWLRRM 355
Cdd:NF041063 440 LGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDIAKSL 493
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
410-517 |
1.86e-43 |
|
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: 150.77 E-value: 1.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 410 PPKHFDATQEAQKALSCVYRVNQSFGMGYVVEVMRGMQNIRVRDNGHDKLSTYGIGRDHSHDYWISIFRQLIHKGLLFQN 489
Cdd:pfam09382 1 PPETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVD 80
|
90 100
....*....|....*....|....*...
gi 501628854 490 ITRNSTLQLTEEARPLLRGEMSLELAVP 517
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 ... |
415-506 |
1.76e-40 |
|
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: 142.23 E-value: 1.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 415 DATQEAQKALSCVYRVNQSFGMGYVVEVMRGMQNIRVRDNGHDKLSTYGIGRDHSHDYWISIFRQLIHKGLLFQNITRNS 494
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYP 80
|
90
....*....|..
gi 501628854 495 TLQLTEEARPLL 506
Cdd:smart00956 81 YLKLTEKARPVL 92
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
31-190 |
1.88e-28 |
|
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: 111.57 E-value: 1.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 31 RDGQQEVIDLAVEGKDSLVIMPTGGGKSLCYQIPALVR------DGLTLVISPLISLMKDQVDQLKA----NGVAAECIN 100
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAldkldnGPQALVLAPTRELAEQIYEELKKlgkgLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 101 SSMPRDQLLSVFNRmnsgqLKMVYASPERVLmrDFIERLQGLP-LSMIAVDEAHCISQWGhdFRPEYASLgqLKQYFPHV 179
Cdd:pfam00270 81 GGDSRKEQLEKLKG-----PDILVGTPGRLL--DLLQERKLLKnLKLLVLDEAHRLLDMG--FGPDLEEI--LRRLPKKR 149
|
170
....*....|.
gi 501628854 180 PYMALTATADD 190
Cdd:pfam00270 150 QILLLSATLPR 160
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
254-335 |
2.84e-25 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 99.59 E-value: 2.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 254 EMVTEKLCNNGIRAAGYHAGMDTDERAYVQEAFQRDDIQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGR 333
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 501628854 334 DG 335
Cdd:smart00490 81 AG 82
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
25-215 |
3.61e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 100.26 E-value: 3.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 25 FGYQSFRDGQQEVIDLAVEG-KDSLVIMPTGGGKSLCYQIPAL-----VRDGLTLVISPLISLMKDQVDQLKA-----NG 93
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALealkrGKGGRVLVLVPTRELAEQWAEELKKlgpslGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 94 VAAECINSSMPRDQLlsvfNRMNSGQLKMVYASPERvLMRDFIERLQGLP-LSMIAVDEAHCISQWGhdFRPEYASLgqL 172
Cdd:smart00487 84 KVVGLYGGDSKREQL----RKLESGKTDILVTTPGR-LLDLLENDKLSLSnVDLVILDEAHRLLDGG--FGDQLEKL--L 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 501628854 173 KQYFPHVPYMALTATADDATRKdiISRLQLVDPHTHLGSFDRP 215
Cdd:smart00487 155 KLLPKNVQLLLLSATPPEEIEN--LLELFLNDPVFIDVGFTPL 195
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
228-335 |
5.30e-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: 96.90 E-value: 5.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 228 VSQVVRYLETQKGNCGIIYCGSRKKVEMvtEKLCN-NGIRAAGYHAGMDTDERAYVQEAFQRDDIQIVVATVAFGMGINK 306
Cdd:pfam00271 3 LEALLELLKKERGGKVLIFSQTKKTLEA--ELLLEkEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*....
gi 501628854 307 PNVRFVVHFDIPRNIESYYQETGRAGRDG 335
Cdd:pfam00271 81 PDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
34-355 |
5.42e-24 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 104.84 E-value: 5.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 34 QQEVIDLAVEGKDSLVIMPTGGGKSLCYQIPAL-------VRDGLTLVISP-----------LISL-------------- 81
Cdd:COG0513 29 QAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLqrldpsrPRAPQALILAPtrelalqvaeeLRKLakylglrvatvygg 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 82 --MKDQVDQLKaNGVAaecinssmprdqllsvfnrmnsgqlkMVYASPERVLmrDFIER----LQGLplSMIAVDEAhci 155
Cdd:COG0513 109 vsIGRQIRALK-RGVD--------------------------IVVATPGRLL--DLIERgaldLSGV--ETLVLDEA--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 156 sqwghD------FRPEyaslgqLKQYFPHVP----YMALTATADDATRKdIISRLqLVDPHTHlgSFDRPNI-------R 218
Cdd:COG0513 155 -----DrmldmgFIED------IERILKLLPkerqTLLFSATMPPEIRK-LAKRY-LKNPVRI--EVAPENAtaetieqR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 219 YNLVEKHKPVSQVVRYLETQKGNCGIIYCGSRKKVEMVTEKLCNNGIRAAGYHAGMDTDERAYVQEAFQRDDIQIVVAT- 297
Cdd:COG0513 220 YYLVDKRDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATd 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501628854 298 VAfGMGINKPNVRFVVHFDIPRNIESYyq---eTGRAGRDGlpaEAMMLFDPADMGWLRRM 355
Cdd:COG0513 300 VA-ARGIDIDDVSHVINYDLPEDPEDYvhrigrTGRAGAEG---TAISLVTPDERRLLRAI 356
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
537-604 |
3.31e-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: 90.29 E-value: 3.31e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501628854 537 DKKLFAKLRKLRKSIADEDGLPPYVVFSDATLIDMAEILPTSYGEMLAVNGVGQRKLDKYADPFLDLI 604
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
535-609 |
6.85e-22 |
|
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: 90.05 E-value: 6.85e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501628854 535 NYDKKLFAKLRKLRKSIADEDGLPPYVVFSDATLIDMAEILPTSYGEMLAVNGVGQRKLDKYADPFLDLIQEHIT 609
Cdd:smart00341 2 ERQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEASD 76
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
346-408 |
4.16e-21 |
|
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: 86.96 E-value: 4.16e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501628854 346 PADMGWLRRMLDEKEEGP-QKQVEMHKLNAMSAFAEAQT-CRRQVLLNYFGE-YREKQCGNCDICL 408
Cdd:pfam16124 1 YQDVVRLRFLIEQSEADEeRKEVELQKLQAMVAYCENTTdCRRKQLLRYFGEeFDSEPCGNCDNCL 66
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
223-336 |
5.09e-20 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 86.41 E-value: 5.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 223 EKHKPVSQVVRYLETQKGNCGIIYCGSRKKVEMVTEKLCNNGIRAAGYHAGMDTDERAYVQEAFQRDDIQIVVAT-VAfG 301
Cdd:cd18787 10 EEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATdVA-A 88
|
90 100 110
....*....|....*....|....*....|....*...
gi 501628854 302 MGINKPNVRFVVHFDIPRNIESYYQ---ETGRAGRDGL 336
Cdd:cd18787 89 RGLDIPGVDHVINYDLPRDAEDYVHrigRTGRAGRKGT 126
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
31-333 |
2.79e-18 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 88.54 E-value: 2.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 31 RDGQQEVID-----LAVEGKDSLVIMPTGGGKSL----CYQipALVRDGLTLVISPLISLmkdqVDQLkangvaaecins 101
Cdd:COG1061 82 RPYQQEALEallaaLERGGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRREL----LEQW------------ 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 102 smpRDQLLSVFNRMNSGQLK------MVYASPERVLMRDFIERLQGLPlSMIAVDEAHcisqwgHDFRPEYAslgQLKQY 175
Cdd:COG1061 144 ---AEELRRFLGDPLAGGGKkdsdapITVATYQSLARRAHLDELGDRF-GLVIIDEAH------HAGAPSYR---RILEA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 176 FPHVPYMALTAT----------------------ADDATRKDIISRLQLVDPHTHLGS----FDRPN--IRYNLVEKHKP 227
Cdd:COG1061 211 FPAAYRLGLTATpfrsdgreillflfdgivyeysLKEAIEDGYLAPPEYYGIRVDLTDeraeYDALSerLREALAADAER 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 228 VSQVVRYLETQKGNC--GIIYCGSRKKVEMVTEKLCNNGIRAAGYHAGMDTDERAYVQEAFQRDDIQIVVATVAFGMGIN 305
Cdd:COG1061 291 KDKILRELLREHPDDrkTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVD 370
|
330 340 350
....*....|....*....|....*....|.
gi 501628854 306 KPNVRFVVHFdipRNIES---YYQetgRAGR 333
Cdd:COG1061 371 VPRLDVAILL---RPTGSpreFIQ---RLGR 395
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
34-348 |
5.60e-16 |
|
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: 81.42 E-value: 5.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 34 QQEVIDLAVEGKDSLVIMPTGGGKSLCYQIPAL-----VRDGLTLVISPLISLMKDQVDQLKA------NGVAAECINSS 102
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLealleDPGATALYLYPTKALARDQLRRLRElaealgLGVRVATYDGD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 103 MPRDQllsvfnRmnsgqlKMVYASPeRVLM-----------------RDFIERLqglplSMIAVDEAHcisqwghdfrpE 165
Cdd:COG1205 141 TPPEE------R------RWIREHP-DIVLtnpdmlhygllphhtrwARFFRNL-----RYVVIDEAH-----------T 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 166 Y-----ASLGQL--------KQYFPHVPYMALTATADDAtrKDIISRL-----QLVD----PH---THLgsFDRPNIRYN 220
Cdd:COG1205 192 YrgvfgSHVANVlrrlrricRHYGSDPQFILASATIGNP--AEHAERLtgrpvTVVDedgsPRgerTFV--LWNPPLVDD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 221 LVEK--HKPVSQVVRYLeTQKGNCGIIYCGSRKKVEMVTEKLCNN------GIRAAGYHAGMDTDERAYVQEAFQRDDIQ 292
Cdd:COG1205 268 GIRRsaLAEAARLLADL-VREGLRTLVFTRSRRGAELLARYARRAlrepdlADRVAAYRAGYLPEERREIERGLRSGELL 346
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 501628854 293 IVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMMLF--DPAD 348
Cdd:COG1205 347 GVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLVAgdDPLD 404
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
26-341 |
6.66e-14 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 74.44 E-value: 6.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 26 GYQSFRDGQQEVIDLAVEGKDSLVIMPTGGGKSLCYQIP-----ALVRDG--------LTLVISPLISLMKDQVDQLKAN 92
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPiisrcCTIRSGhpseqrnpLAMVLTPTRELCVQVEDQAKVL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 93 G------VAAECINSSMPRdQLlsvfNRMNSGqLKMVYASPER---VLMRDFIErLQGLplSMIAVDEAHCISQWGhdFR 163
Cdd:PLN00206 220 GkglpfkTALVVGGDAMPQ-QL----YRIQQG-VELIVGTPGRlidLLSKHDIE-LDNV--SVLVLDEVDCMLERG--FR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 164 PEyasLGQLKQYFPHVPYMALTATADDATRK---DIISRLQLVDphthLGSFDRPNirynlvekhKPVSQVVRYLETQKG 240
Cdd:PLN00206 289 DQ---VMQIFQALSQPQVLLFSATVSPEVEKfasSLAKDIILIS----IGNPNRPN---------KAVKQLAIWVETKQK 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 241 N---------------CGIIYCGSRKKVEMVTEKLC-NNGIRAAGYHAGMDTDERAYVQEAFQRDDIQIVVATVAFGMGI 304
Cdd:PLN00206 353 KqklfdilkskqhfkpPAVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGV 432
|
330 340 350
....*....|....*....|....*....|....*..
gi 501628854 305 NKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAM 341
Cdd:PLN00206 433 DLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAI 469
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
44-187 |
9.61e-14 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 68.97 E-value: 9.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 44 GKDSLVIMPTGGGKSLCYQIPALVRD----GLTLVISPLISLMKDQVDQLKA---NGVAAECINSSMPRDQLLSVFNRmn 116
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLlkkgKKVLVLVPTKALALQTAERLRElfgPGIRVAVLVGGSSAEEREKNKLG-- 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501628854 117 sgQLKMVYASPERVLM-RDFIERLQGLPLSMIAVDEAHCISQWGHDFRPEYASLGQLKqyFPHVPYMALTAT 187
Cdd:cd00046 79 --DADIIIATPDMLLNlLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAG--LKNAQVILLSAT 146
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
18-355 |
1.80e-13 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 72.55 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 18 QDILQDVFGYQSFRDG--QQEVIDLAVEGKDSLVIMPTGGGKSLCYQIPAL------VRDGLTLVISPLISLMKDQVDQL 89
Cdd:PTZ00424 37 EDLLRGIYSYGFEKPSaiQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALqlidydLNACQALILAPTRELAQQIQKVV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 90 KANGVAAE-----CINSSMPRDQLlsvfNRMNSGQlKMVYASPERVLmrDFIER--LQGLPLSMIAVDEAHCISQWGhdF 162
Cdd:PTZ00424 117 LALGDYLKvrchaCVGGTVVRDDI----NKLKAGV-HMVVGTPGRVY--DMIDKrhLRVDDLKLFILDEADEMLSRG--F 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 163 RpeyaslGQLKQYFPHVPYMALTATADdATRKDIISRLQ---LVDPHTHLGSFDR---PNIR--YNLVEKHK-PVSQVVR 233
Cdd:PTZ00424 188 K------GQIYDVFKKLPPDVQVALFS-ATMPNEILELTtkfMRDPKRILVKKDEltlEGIRqfYVAVEKEEwKFDTLCD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 234 YLETQKGNCGIIYCGSRKKVEMVTEKLCNNGIRAAGYHAGMDTDERAYVQEAFQRDDIQIVVATVAFGMGINKPNVRFVV 313
Cdd:PTZ00424 261 LYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVI 340
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 501628854 314 HFDIPRNIESYYQETGRAGRDGLPAEAMMLFDPADMGWLRRM 355
Cdd:PTZ00424 341 NYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEI 382
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
40-346 |
2.60e-12 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 69.42 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 40 LAVEGKDSLVIMPTGGGKSLCYQIPALVR----------DG-LTLVISP---LISLMKDQVDQLKANG-VAAECINSSMP 104
Cdd:PTZ00110 163 IALSGRDMIGIAETGSGKTLAFLLPAIVHinaqpllrygDGpIVLVLAPtreLAEQIREQCNKFGASSkIRNTVAYGGVP 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 105 -RDQLLSVFNrmnsgQLKMVYASPERVLmrDFIE-RLQGLP-LSMIAVDEAHCISQWGhdFRPEYASLgqLKQYFPHVPY 181
Cdd:PTZ00110 243 kRGQIYALRR-----GVEILIACPGRLI--DFLEsNVTNLRrVTYLVLDEADRMLDMG--FEPQIRKI--VSQIRPDRQT 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 182 MALTAT--------ADDATRKDIIsrlqlvdpHTHLGSFDRP---NIRYN--LVEKHKPVSQVVRYLET--QKGNCGIIY 246
Cdd:PTZ00110 312 LMWSATwpkevqslARDLCKEEPV--------HVNVGSLDLTachNIKQEvfVVEEHEKRGKLKMLLQRimRDGDKILIF 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 247 CGSRKKVEMVTEKLCNNGIRAAGYHAGMDTDERAYVQEAFQRDDIQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQ 326
Cdd:PTZ00110 384 VETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVH 463
|
330 340
....*....|....*....|
gi 501628854 327 ETGRAGRDGLPAEAMMLFDP 346
Cdd:PTZ00110 464 RIGRTGRAGAKGASYTFLTP 483
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
291-345 |
3.73e-12 |
|
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: 61.95 E-value: 3.73e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 501628854 291 IQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMMLFD 345
Cdd:cd18785 23 LEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
25-336 |
5.87e-12 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 68.38 E-value: 5.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 25 FGYQSFRDGQQEVIDLAVEGKDSLVI-MPTGGGKSLCYQIP---ALVRDGLTLVISPLISLMKDQVDQLKAN----GV-A 95
Cdd:COG1204 18 RGIEELYPPQAEALEAGLLEGKNLVVsAPTASGKTLIAELAilkALLNGGKALYIVPLRALASEKYREFKRDfeelGIkV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 96 AECINSSMPRDQLLsvfnrmnsGQLKMVYASPERV--LMR---DFIERLqglplSMIAVDEAHCIsqwGHDFR-PEY-AS 168
Cdd:COG1204 98 GVSTGDYDSDDEWL--------GRYDILVATPEKLdsLLRngpSWLRDV-----DLVVVDEAHLI---DDESRgPTLeVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 169 LGQLKQYFPHVPYMALTATADDAtrkDIISRL---QLVDpHT------HLGSFDRPNIRY---NLVEKHKPVSQVVRYLE 236
Cdd:COG1204 162 LARLRRLNPEAQIVALSATIGNA---EEIAEWldaELVK-SDwrpvplNEGVLYDGVLRFddgSRRSKDPTLALALDLLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 237 tQKGNCgIIYCGSRKKVEMVTEKL---CNNGI----------------------------------RAAGYHAGMDTDER 279
Cdd:COG1204 238 -EGGQV-LVFVSSRRDAESLAKKLadeLKRRLtpeereeleelaeellevseethtnekladclekGVAFHHAGLPSELR 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501628854 280 AYVQEAFQRDDIQIVVATVAFGMGINKPnVRFVVHFDIPRNIES------YYQETGRAGRDGL 336
Cdd:COG1204 316 RLVEDAFREGLIKVLVATPTLAAGVNLP-ARRVIIRDTKRGGMVpipvleFKQMAGRAGRPGY 377
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
244-343 |
1.39e-11 |
|
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: 62.66 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 244 IIYCGSRKKVEMVT-------EKLCNNGIRAAGYHAGMDTDERAYVQEAFQRDDIQIVVATVAFGMGINKPNVRFVVHFD 316
Cdd:cd18797 39 IVFCRSRKLAELLLrylkarlVEEGPLASKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|....*..
gi 501628854 317 IPRNIESYYQETGRAGRDGLPAEAMML 343
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDSLVILV 145
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
212-336 |
2.63e-11 |
|
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: 61.80 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 212 FDRPNIRYNLVEKHKPVSQVvryletqkgncgIIYCGSRKKVEMVTEKLcnNGIraAGYHAGMDTDERAYVQEAFQRDDI 291
Cdd:cd18795 27 FDSDIIVLLKIETVSEGKPV------------LVFCSSRKECEKTAKDL--AGI--AFHHAGLTREDRELVEELFREGLI 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 501628854 292 QIVVATVAFGMGINKPNVRFVV----HFDIPRNIE----SYYQETGRAGRDGL 336
Cdd:cd18795 91 KVLVATSTLAAGVNLPARTVIIkgtqRYDGKGYRElsplEYLQMIGRAGRPGF 143
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
26-356 |
4.91e-10 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 62.56 E-value: 4.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 26 GYQSFRDGQQEVIDLAVEGKDSLVIMPTGGGKSLCYQIPAL------VRDGLTLVISPLISL-------MKDQVDQLKAN 92
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLhnldpeLKAPQILVLAPTRELavqvaeaMTDFSKHMRGV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 93 GVAAecinssMPRDQLLSVFNRMNSGQLKMVYASPERVLmrDFIER--LQGLPLSMIAVDEAHCISQWGhdFRPEYASLg 170
Cdd:PRK11634 105 NVVA------LYGGQRYDVQLRALRQGPQIVVGTPGRLL--DHLKRgtLDLSKLSGLVLDEADEMLRMG--FIEDVETI- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 171 qLKQyFPHVPYMAL-TATADDATRKdiISRLQLVDPH---THLGSFDRPNIR--YNLVEKHKPVSQVVRYLETQKGNCGI 244
Cdd:PRK11634 174 -MAQ-IPEGHQTALfSATMPEAIRR--ITRRFMKEPQevrIQSSVTTRPDISqsYWTVWGMRKNEALVRFLEAEDFDAAI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 245 IYCGSRKKVEMVTEKLCNNGIRAAGYHAGMDTDERAYVQEAFQRDDIQIVVATVAFGMGINKPNVRFVVHFDIPRNIESY 324
Cdd:PRK11634 250 IFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESY 329
|
330 340 350
....*....|....*....|....*....|..
gi 501628854 325 YQETGRAGRDGLPAEAMMLFDPADmgwlRRML 356
Cdd:PRK11634 330 VHRIGRTGRAGRAGRALLFVENRE----RRLL 357
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
34-335 |
9.65e-10 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 61.08 E-value: 9.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 34 QQEVIDLAVEGKDSLVIMPTGGGKSLCYQIpALVRDGL--------------TLVISP----LISLMKDQVDQLKANGVA 95
Cdd:PRK01297 114 QAQVLGYTLAGHDAIGRAQTGTGKTAAFLI-SIINQLLqtpppkerymgeprALIIAPtrelVVQIAKDAAALTKYTGLN 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 96 AECINSSMPRDQLLsvfNRMNSGQLKMVYASPERVLmrDFIERLQgLPLSMIAV---DEAHCISQWGhdFRPeyaslgQL 172
Cdd:PRK01297 193 VMTFVGGMDFDKQL---KQLEARFCDILVATPGRLL--DFNQRGE-VHLDMVEVmvlDEADRMLDMG--FIP------QV 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 173 KQYFPHVPY------MALTAT-ADDATRkdiISRLQLVDPHThlGSFDRPNIRYNLVEKH-KPVSQVVRY-----LETQK 239
Cdd:PRK01297 259 RQIIRQTPRkeerqtLLFSATfTDDVMN---LAKQWTTDPAI--VEIEPENVASDTVEQHvYAVAGSDKYkllynLVTQN 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 240 GNCGIIYCGSRK-KVEMVTEKLCNNGIRAAGYHAGMDTDERAYVQEAFQRDDIQIVVATVAFGMGINKPNVRFVVHFDIP 318
Cdd:PRK01297 334 PWERVMVFANRKdEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLP 413
|
330
....*....|....*..
gi 501628854 319 RNIESYYQETGRAGRDG 335
Cdd:PRK01297 414 EDPDDYVHRIGRTGRAG 430
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
244-333 |
1.81e-09 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 60.68 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 244 IIYCGSRKKVEMVTEKLcnnGIRAAGYHAGMDTDERAYVQEAFQRDDIQIVVATVAFGMGINKPNVRfvVHFDIPR---- 319
Cdd:COG1202 431 IIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQ--VIFDSLAmgie 505
|
90
....*....|....*.
gi 501628854 320 --NIESYYQETGRAGR 333
Cdd:COG1202 506 wlSVQEFHQMLGRAGR 521
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
244-333 |
3.17e-07 |
|
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: 49.96 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 244 IIYCGSRKKVEMVTEKL------CNNGIRAAGYHAGMDTDERAYVQEAFQRDDIQIVVATVAFGMGINKPNVRFVVHFDI 317
Cdd:cd18796 42 LVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGS 121
|
90
....*....|....*.
gi 501628854 318 PRNIESYYQETGRAGR 333
Cdd:cd18796 122 PKSVARLLQRLGRSGH 137
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
244-335 |
9.91e-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: 48.24 E-value: 9.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 244 IIYCGSRKKVEMVTEKLCNNGIRAAGYHAGMDTDERAYVQEAFQRDD--IQIVVATVAFGMGINKPNVRFVVHFDIPRN- 320
Cdd:cd18793 31 LIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGVGLNLTAANRVILYDPWWNp 110
|
90
....*....|....*.
gi 501628854 321 -IESyyQETGRAGRDG 335
Cdd:cd18793 111 aVEE--QAIDRAHRIG 124
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
34-191 |
1.82e-06 |
|
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: 48.41 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 34 QQEVIDLAVEGKDSLVI-MPTGGGKSLCYQIpALVR-----DGLTLVISPLISLMKDQVDQLKangvaaECINSSMPRDQ 107
Cdd:cd17921 6 QREALRALYLSGDSVLVsAPTSSGKTLIAEL-AILRalatsGGKAVYIAPTRALVNQKEADLR------ERFGPLGKNVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 108 LL---SVFNRMNSGQLKMVYASPER--VLMRDFIERLqGLPLSMIAVDEAHCISQwghdfrPEYA-----SLGQLKQYFP 177
Cdd:cd17921 79 LLtgdPSVNKLLLAEADILVATPEKldLLLRNGGERL-IQDVRLVVVDEAHLIGD------GERGvvlelLLSRLLRINK 151
|
170
....*....|....
gi 501628854 178 HVPYMALTATADDA 191
Cdd:cd17921 152 NARFVGLSATLPNA 165
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
34-359 |
2.70e-06 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 49.94 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 34 QQEVIDLAVEGKDSLVIMPTGGGKSLCYQIPALV--------RDGLT--LVISP---LISLMKDQVDQLKAN-------- 92
Cdd:PRK11192 28 QAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQhlldfprrKSGPPriLILTPtreLAMQVADQARELAKHthldiati 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 93 --GVAaecinsSMPRDQLLsvfnrmnSGQLKMVYASPERVLmrDFI--ERLQGLPLSMIAVDEAHCISQWGhdFRPEYAS 168
Cdd:PRK11192 108 tgGVA------YMNHAEVF-------SENQDIVVATPGRLL--QYIkeENFDCRAVETLILDEADRMLDMG--FAQDIET 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 169 LG----QLKQyfphvpYMALTATADDATRKDIISRLqLVDPhTHLGSfdRPNIR--------YNLVE--KHKpVSQVVRY 234
Cdd:PRK11192 171 IAaetrWRKQ------TLLFSATLEGDAVQDFAERL-LNDP-VEVEA--EPSRRerkkihqwYYRADdlEHK-TALLCHL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 235 LETQKGNCGIIYCGSRKKVEMVTEKLCNNGIRAAGYHAGMDTDERAYVQEAFQRDDIQIVVAT-VAfGMGINKPNVRFVV 313
Cdd:PRK11192 240 LKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATdVA-ARGIDIDDVSHVI 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 501628854 314 HFDIPRNIESYYQETGRAGRDGLPAEAMMLFDPADMGWL---RRMLDEK 359
Cdd:PRK11192 319 NFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLgkiERYIEEP 367
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
32-335 |
2.84e-06 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 50.27 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 32 DGQQEVIDLAVEGKDSLVIMPTGGGKSLC--YQIPALVRDGL-TLVISPLISLMKDQVDQLkangvaaecinsSMPRDQL 108
Cdd:PRK01172 25 DHQRMAIEQLRKGENVIVSVPTAAGKTLIaySAIYETFLAGLkSIYIVPLRSLAMEKYEEL------------SRLRSLG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 109 LSVfnRMNSGQlkmvYASPErvlmrDFIERLQGLPLS-------------------MIAVDEAHCIsqwGHDFR-PEYAS 168
Cdd:PRK01172 93 MRV--KISIGD----YDDPP-----DFIKRYDVVILTsekadslihhdpyiindvgLIVADEIHII---GDEDRgPTLET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 169 LGQLKQYF-PHVPYMALTATADDAT--------------------RKDIISRLQLVdphthLGSFDRPNIRYNLVEKHKp 227
Cdd:PRK01172 159 VLSSARYVnPDARILALSATVSNANelaqwlnasliksnfrpvplKLGILYRKRLI-----LDGYERSQVDINSLIKET- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 228 vsqvvryleTQKGNCGIIYCGSRKKVEMVTEKLC---------------NNGIR----------AAGYHAGMDTDERAYV 282
Cdd:PRK01172 233 ---------VNDGGQVLVFVSSRKNAEDYAEMLIqhfpefndfkvssenNNVYDdslnemlphgVAFHHAGLSNEQRRFI 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501628854 283 QEAFQRDDIQIVVATVAFGMGINKPnVRFVVHFDIPR----------NIEsYYQETGRAGRDG 335
Cdd:PRK01172 304 EEMFRNRYIKVIVATPTLAAGVNLP-ARLVIVRDITRygnggirylsNME-IKQMIGRAGRPG 364
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
268-333 |
3.07e-06 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 50.20 E-value: 3.07e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501628854 268 AGYHAGMDTDERAYVQEAFQRDDIQIVVATVAFGMGINKPNVRFVVH----------FDIPrnIESYYQETGRAGR 333
Cdd:PRK00254 299 AFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRdtkrysnfgwEDIP--VLEIQQMMGRAGR 372
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
34-91 |
5.58e-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: 5.58e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501628854 34 QQEVIDLAVEGKDSLVIMPTGGGKSLCYQIP---ALVRDGLT--LVISPLISLMKDQVDQLKA 91
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPileALLRDPGSraLYLYPTKALAQDQLRSLRE 67
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
267-349 |
2.28e-05 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 47.64 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 267 AAGYHAGMDTDERAYVQEAFQRDDIQIVVATVAFGMGINKPNVRFVV----HFD-----IPRNIESYYQETGRAGRDGL- 336
Cdd:PRK02362 306 AAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIrdyrRYDggagmQPIPVLEYHQMAGRAGRPGLd 385
|
90
....*....|....
gi 501628854 337 P-AEAMMLFDPADM 349
Cdd:PRK02362 386 PyGEAVLLAKSYDE 399
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
271-336 |
4.50e-05 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 46.47 E-value: 4.50e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501628854 271 HAGMDTDERAYVQEAFQRDDIQIVVATVAFGMGINKPnVRFVV-----------HFDI-PRnieSYYQETGRAGRDGL 336
Cdd:COG4581 306 HAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMP-ARTVVftklskfdgerHRPLtAR---EFHQIAGRAGRRGI 379
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
235-341 |
7.20e-05 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 45.71 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 235 LETQKGNCGIIYCGSRKKVEMVTEKLCNNGIRAAGYHAGMDTDERAYVQEAFQRDDIQIVVATVAFGMGINKPNVRFVVH 314
Cdd:PRK04537 252 LSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYN 331
|
90 100
....*....|....*....|....*..
gi 501628854 315 FDIPRNIESYYQETGRAGRDGLPAEAM 341
Cdd:PRK04537 332 YDLPFDAEDYVHRIGRTARLGEEGDAI 358
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
244-333 |
8.03e-05 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 45.60 E-value: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 244 IIYCGSRKKVEMVTEKLCNNGIRAAGYHAGMDTDERAYVQEAFQRDD--IQIVVATVAFGMGINKPNVRFVVHFDIPRNI 321
Cdd:COG0553 553 LVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEGLNLTAADHVIHYDLWWNP 632
|
90
....*....|..
gi 501628854 322 ESYYQETGRAGR 333
Cdd:COG0553 633 AVEEQAIDRAHR 644
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
542-606 |
9.24e-05 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 44.86 E-value: 9.24e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501628854 542 AKLRKL---RKSIADEDGLPPYVVFSDATLIDMAEILPTSYGEMLAVNGVGQRKLDKYADPFLDLIQE 606
Cdd:COG0349 211 AVLRELaawREREARKRDVPRNRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAVAE 278
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
13-137 |
9.67e-05 |
|
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 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: 350807 [Multi-domain] Cd Length: 234 Bit Score: 44.23 E-value: 9.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 13 PANdaqdiLQDVFGYQSFRDG---QQEVIDLAVEGKDSLVIMPTGGGKSLCYQIPALVR----------DG-LTLVISPL 78
Cdd:cd18049 32 PAN-----VMDVIARQNFTEPtaiQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHinhqpflergDGpICLVLAPT 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501628854 79 ISLMKdQVDQL-----KANGVAAECINSSMPRDQLLSVFNRmnsgQLKMVYASPERVLmrDFIE 137
Cdd:cd18049 107 RELAQ-QVQQVaaeygRACRLKSTCIYGGAPKGPQIRDLER----GVEICIATPGRLI--DFLE 163
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
26-77 |
9.85e-05 |
|
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 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: 350699 [Multi-domain] Cd Length: 198 Bit Score: 43.82 E-value: 9.85e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501628854 26 GYQSFRDGQQEVIDLAVEGKDSLVIMPTGGGKSLCYQIPALVR---------DGL-TLVISP 77
Cdd:cd17941 9 GFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKlyrerwtpeDGLgALIISP 70
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
30-187 |
1.79e-04 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 41.91 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 30 FRDGQQEVID--LAVEGKD-SLVIMPTGGGKSLC-YQIPALVRDGLTLVISPLISLMKDQVDQL-KANGVAAECINSSMP 104
Cdd:cd17926 1 LRPYQEEALEawLAHKNNRrGILVLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFeDFLGDSSIGLIGGGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 105 RDQLLS---VFNRMNSGqlkMVYASPERVLMRDFierlqglplSMIAVDEAHCIS--QWGHdfrpeyaslgqLKQYFPHV 179
Cdd:cd17926 81 KKDFDDanvVVATYQSL---SNLAEEEKDLFDQF---------GLLIVDEAHHLPakTFSE-----------ILKELNAK 137
|
....*...
gi 501628854 180 PYMALTAT 187
Cdd:cd17926 138 YRLGLTAT 145
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
258-343 |
1.83e-04 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 44.41 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 258 EKLCNNGIRAAGYHAGMDTDERAYVQEAFQRDDIQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLP 337
Cdd:PRK10590 263 EQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAAT 342
|
....*.
gi 501628854 338 AEAMML 343
Cdd:PRK10590 343 GEALSL 348
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
31-198 |
2.47e-04 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members 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: 350790 [Multi-domain] Cd Length: 163 Bit Score: 41.78 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 31 RDGQQE----VIDLAVEGKD-SLVIMPTGGGK-----SLCYQIPALVRDGLTLVISPLISLMKDQVDQLKANGVAAECIN 100
Cdd:cd18032 2 RYYQQEaieaLEEAREKGQRrALLVMATGTGKtytaaFLIKRLLEANRKKRILFLAHREELLEQAERSFKEVLPDGSFGN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 101 SSMprdqllsvfNRMNSGQLKMVYASPERVLMRdfiERLQGLPLS---MIAVDEAHcisqwghdfRPEYASLGQLKQYFP 177
Cdd:cd18032 82 LKG---------GKKKPDDARVVFATVQTLNKR---KRLEKFPPDyfdLIIIDEAH---------HAIASSYRKILEYFE 140
|
170 180
....*....|....*....|.
gi 501628854 178 HVPYMALTATADDATRKDIIS 198
Cdd:cd18032 141 PAFLLGLTATPERTDGLDTYE 161
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
34-152 |
2.52e-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: 42.43 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 34 QQEVIDLAVEGKDSLVIMPTGGGKSLCYQIPALVR---------DGL-TLVISP---L---ISlmkDQVDQL-KANGVAA 96
Cdd:cd00268 17 QAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKllpepkkkgRGPqALVLAPtreLamqIA---EVARKLgKGTGLKV 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 97 ECINSSMPRDQLLsvfnRMNSGQLKMVYASPERVLmrDFIER----LQGlpLSMIAVDEA 152
Cdd:cd00268 94 AAIYGGAPIKKQI----EALKKGPDIVVGTPGRLL--DLIERgkldLSN--VKYLVLDEA 145
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
14-137 |
2.83e-04 |
|
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 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: 350808 [Multi-domain] Cd Length: 271 Bit Score: 43.08 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 14 ANDAQDILqDVFGYQSFRDG---QQEVIDLAVEGKDSLVIMPTGGGKSLCYQIPALVR----------DG-LTLVISPLI 79
Cdd:cd18050 67 ANFPQYVM-DVLLDQNFKEPtpiQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHinhqpylergDGpICLVLAPTR 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501628854 80 SLMKdQVDQL-----KANGVAAECINSSMPRDQLLSVFNRmnsgQLKMVYASPERVLmrDFIE 137
Cdd:cd18050 146 ELAQ-QVQQVaddygKSSRLKSTCIYGGAPKGPQIRDLER----GVEICIATPGRLI--DFLE 201
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
44-104 |
3.50e-04 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 41.41 E-value: 3.50e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501628854 44 GKDSLVIMPTGGGKSLCYQIPALVR------DGL-TLVISPLISLMKDQVDQLKAngvAAECINSSMP 104
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSladepeKGVqVLYISPLKALINDQERRLEE---PLDEIDLEIP 65
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
16-76 |
7.69e-04 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 42.60 E-value: 7.69e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501628854 16 DAQDILQDVFGYQSFRDGQQEVIDL---AVEGKDSLVI-MPTGGGKSLCYQIPAL---VRDGLTLVIS 76
Cdd:COG1199 1 ADDGLLALAFPGFEPRPGQREMAEAvarALAEGRHLLIeAGTGTGKTLAYLVPALlaaRETGKKVVIS 68
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
267-332 |
9.15e-04 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 42.60 E-value: 9.15e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501628854 267 AAGYHAGMDTDERAYVQEAFQRDDIQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAG 332
Cdd:PRK09751 304 ARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
243-333 |
1.21e-03 |
|
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: 39.08 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 243 GIIYCGSRKKVEMVTEKLCNNGIRAAGYHAGMDTDERAY-VQEAFQRDDIQIVVA-TVA-FGMGINKPNVRFVVhFDipR 319
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDeALILLFFGELKPPILvTVDlLTTGVDIPEVDNVV-FL--R 85
|
90
....*....|....*..
gi 501628854 320 NIES---YYQETGRAGR 333
Cdd:cd18799 86 PTESrtlFLQMLGRGLR 102
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
34-66 |
1.48e-03 |
|
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 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: 350719 [Multi-domain] Cd Length: 206 Bit Score: 40.26 E-value: 1.48e-03
10 20 30
....*....|....*....|....*....|...
gi 501628854 34 QQEVIDLAVEGKDSLVIMPTGGGKSLCYQIPAL 66
Cdd:cd17961 21 QSKAIPLALEGKDILARARTGSGKTAAYALPII 53
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
284-335 |
3.08e-03 |
|
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: 38.34 E-value: 3.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 501628854 284 EAFQRDDIQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDG 335
Cdd:cd18802 84 DKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN 135
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
251-300 |
5.25e-03 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350682 [Multi-domain] Cd Length: 189 Bit Score: 38.46 E-value: 5.25e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 501628854 251 KKVEMVTEKLCNNgIRAAGYHAGMDTDERAYVQEAFQRDDIQIVVATVAF 300
Cdd:cd17924 78 ERLSKYAEKAGVE-VKILVYHSRLKKKEKEELLEKIEKGDFDILVTTNQF 126
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
240-333 |
5.50e-03 |
|
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: 38.05 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 240 GNCGIIYCGSRK---KVEMVTEKLCNNGIRAAGYHAGmdtDERAYvqEAFQRDDIQIVVATVAF-GM---GINKPN-VRF 311
Cdd:cd18798 24 GDGGLIFVSIDYgkeYAEELKEFLERHGIKAELALSS---TEKNL--EKFEEGEIDVLIGVASYyGVlvrGIDLPErIKY 98
|
90 100
....*....|....*....|..
gi 501628854 312 VVHFDIPrnIESYYQETGRAGR 333
Cdd:cd18798 99 AIFYGVP--VTTYIQASGRTSR 118
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
29-187 |
5.72e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 38.04 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 29 SFRDGQQEVID-----LAVEGKDSLVIMPTGGGKSLCY-QIPALVRDGL----TLVISPLISLMKDQVDQLKANGVAAEC 98
Cdd:pfam04851 3 ELRPYQIEAIEnllesIKNGQKRGLIVMATGSGKTLTAaKLIARLFKKGpikkVLFLVPRKDLLEQALEEFKKFLPNYVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501628854 99 IN-SSMPRDQLLSVFNRmnsgqlKMVYASPERvLMRDFIERLQGLPLS---MIAVDEAHcisqwghdfRPEYASLGQLKQ 174
Cdd:pfam04851 83 IGeIISGDKKDESVDDN------KIVVTTIQS-LYKALELASLELLPDffdVIIIDEAH---------RSGASSYRNILE 146
|
170
....*....|...
gi 501628854 175 YFPHVPYMALTAT 187
Cdd:pfam04851 147 YFKPAFLLGLTAT 159
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
18-66 |
6.47e-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: 38.33 E-value: 6.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 501628854 18 QDILQDvFGYQSFRDGQQEVIDLAVEGKDSLVIMPTGGGKSLCYQIPAL 66
Cdd:cd17960 2 LDVVAE-LGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVL 49
|
|
| |
