|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
255-609 |
2.44e-118 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 368.70 E-value: 2.44e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 255 ENLTKLLNLVYGYDSFRDGQLQAIKMILGGSSTMLVLPTGAGKSLCYQIPAMILPGITLVVSPLVSLMIDQLKHLPSI-I 333
Cdd:COG0514 3 DDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAgI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 334 KGGLLSSSQRPEEATETLRKLKEGIIKVLFVSPERLLNVEFLSMFRmSLSVSLVVVDEAHCVSEWSHNFRPSYMRLkaSM 413
Cdd:COG0514 83 RAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLR-RLKISLFAIDEAHCISQWGHDFRPDYRRL--GE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 414 LFSELKAECILAmtatattmtLQA---------VMSSLEIPSTNLIQKSQLRDNFELSV-SLSGANRMKDLL-ILMESPP 482
Cdd:COG0514 160 LRERLPNVPVLA---------LTAtatprvradIAEQLGLEDPRVFVGSFDRPNLRLEVvPKPPDDKLAQLLdFLKEHPG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 483 ykeiRSIIVYCKFQYETDMISKYLRDNNINAKGYHSGLPAKDRVRIQESFCSNKIRVVVATVAFGMGLDKGDVGAVIHFS 562
Cdd:COG0514 231 ----GSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYD 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1063686833 563 VPGSMEEYVQEIGRAGRDGRLSYCHLFYDNDTYLKLRSLAHSDGVDE 609
Cdd:COG0514 307 LPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDE 353
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
259-628 |
4.32e-93 |
|
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: 301.69 E-value: 4.32e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 259 KLLNLVYGYDSFRDGQLQAIKMILGGSSTMLVLPTGAGKSLCYQIPAMILPGITLVVSPLVSLMIDQLKHLPSI-IKGGL 337
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALgIPATF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 338 LSSSQRPEEATETLRKLKEGIIKVLFVSPERL-LNVEFLSMFRMSLSVSLVVVDEAHCVSEWSHNFRPSYMRLkaSMLFS 416
Cdd:TIGR00614 81 LNSAQTKEQQLNVLTDLKDGKIKLLYVTPEKIsASNRLLQTLEERKGITLIAVDEAHCISQWGHDFRPDYKAL--GSLKQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 417 ELKAECILAMTATATTMTLQAVMSSLEIPSTNLIQKSQLRDNFELSVSLSGANRMKDLL-ILMESPPYKeirSIIVYCKF 495
Cdd:TIGR00614 159 KFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTPKILEDLLrFIRKEFEGK---SGIIYCPS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 496 QYETDMISKYLRDNNINAKGYHSGLPAKDRVRIQESFCSNKIRVVVATVAFGMGLDKGDVGAVIHFSVPGSMEEYVQEIG 575
Cdd:TIGR00614 236 RKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESG 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1063686833 576 RAGRDGRLSYCHLFYDNDTYLKLRSLahsdgVDEYAVGKFLTHVFSTETKQHE 628
Cdd:TIGR00614 316 RAGRDGLPSECHLFYAPADMNRLRRL-----LMEEPDGNFRTYKLKLYEMMEY 363
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
258-455 |
1.71e-86 |
|
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: 274.13 E-value: 1.71e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 258 TKLLNLVYGYDSFRDGQLQAIKMILGGSSTMLVLPTGAGKSLCYQIPAMIL----PGITLVVSPLVSLMIDQLKHLPSII 333
Cdd:cd18018 1 LKLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLrrrgPGLTLVVSPLIALMKDQVDALPRAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 334 KGGLLSSSQRPEEATETLRKLKEGIIKVLFVSPERLLNVEFLSMFRMSLSVSLVVVDEAHCVSEWSHNFRPSYMRLkASM 413
Cdd:cd18018 81 KAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTPPISLLVVDEAHCISEWSHNFRPDYLRL-CRV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1063686833 414 LFSELKAECILAMTATATTMTLQAVMSSLEIPSTNLIQKSQL 455
Cdd:cd18018 160 LRELLGAPPVLALTATATKRVVEDIASHLGIPESGVVRGPLY 201
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
259-591 |
1.04e-74 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 256.56 E-value: 1.04e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 259 KLLNLVYGYDSFRDGQLQAIKMILGGSSTMLVLPTGAGKSLCYQIPAMILPGITLVVSPLVSLMIDQLKHLPSI-IKGGL 337
Cdd:PRK11057 15 QVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANgVAAAC 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 338 LSSSQRPEEATETLRKLKEGIIKVLFVSPERLLNVEFLSMFrMSLSVSLVVVDEAHCVSEWSHNFRPSYMRLkasmlfSE 417
Cdd:PRK11057 95 LNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHL-AHWNPALLAVDEAHCISQWGHDFRPEYAAL------GQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 418 LKAEC----ILAMTATATTMTLQAVMSSLEIPSTnLIQKSQL-RDNFELSVslsgANRMKDLLILMESPPYKEIRSIIVY 492
Cdd:PRK11057 168 LRQRFptlpFMALTATADDTTRQDIVRLLGLNDP-LIQISSFdRPNIRYTL----VEKFKPLDQLMRYVQEQRGKSGIIY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 493 CKFQYETDMISKYLRDNNINAKGYHSGLPAKDRVRIQESFCSNKIRVVVATVAFGMGLDKGDVGAVIHFSVPGSMEEYVQ 572
Cdd:PRK11057 243 CNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQ 322
|
330
....*....|....*....
gi 1063686833 573 EIGRAGRDGRLSYCHLFYD 591
Cdd:PRK11057 323 ETGRAGRDGLPAEAMLFYD 341
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
264-424 |
8.31e-63 |
|
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: 210.47 E-value: 8.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 264 VYGYDSFRDGQLQAIKMILGGSSTMLVLPTGAGKSLCYQIPAMILPGITLVVSPLVSLMIDQLKHLPSI-IKGGLLSSSQ 342
Cdd:cd17920 7 VFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLgIRAAALNSTL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 343 RPEEATETLRKLKEGIIKVLFVSPERLLNVEFLSMFR---MSLSVSLVVVDEAHCVSEWSHNFRPSYMRLkaSMLFSELK 419
Cdd:cd17920 87 SPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQrlpERKRLALIVVDEAHCVSQWGHDFRPDYLRL--GRLRRALP 164
|
....*
gi 1063686833 420 AECIL 424
Cdd:cd17920 165 GVPIL 169
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
456-590 |
2.66e-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: 206.29 E-value: 2.66e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 456 RDNFELSVSLSGANRMKDLLiLMESPPYKEIRSIIVYCKFQYETDMISKYLRDNNINAKGYHSGLPAKDRVRIQESFCSN 535
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDL-LKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRD 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1063686833 536 KIRVVVATVAFGMGLDKGDVGAVIHFSVPGSMEEYVQEIGRAGRDGRLSYCHLFY 590
Cdd:cd18794 80 KIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
263-609 |
1.13e-53 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 203.20 E-value: 1.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 263 LVYGYDSFRDGQLQAIKMILGGSSTMLVLPTGAGKSLCYQIPAMILPGITLVVSPLVSLMIDQLKHL-PSIIKGGLLSSS 341
Cdd:PLN03137 454 KVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLlQANIPAASLSAG 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 342 QRPEEATETLRKLKEGIIK--VLFVSPERLLNVEFLSMFRMSLS----VSLVVVDEAHCVSEWSHNFRPSYMRLkaSMLF 415
Cdd:PLN03137 534 MEWAEQLEILQELSSEYSKykLLYVTPEKVAKSDSLLRHLENLNsrglLARFVIDEAHCVSQWGHDFRPDYQGL--GILK 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 416 SELKAECILAMTATATTMTLQAVMSSLEIPSTNLIQKSQLRDNFELSVSLSGANRMKDLLILMESPPYKEIRsiIVYCKF 495
Cdd:PLN03137 612 QKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKKCLEDIDKFIKENHFDECG--IIYCLS 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 496 QYETDMISKYLRDNNINAKGYHSGLPAKDRVRIQESFCSNKIRVVVATVAFGMGLDKGDVGAVIHFSVPGSMEEYVQEIG 575
Cdd:PLN03137 690 RMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECG 769
|
330 340 350
....*....|....*....|....*....|....
gi 1063686833 576 RAGRDGRLSYCHLFYDNDTYLKLRSLAHSDGVDE 609
Cdd:PLN03137 770 RAGRDGQRSSCVLYYSYSDYIRVKHMISQGGVEQ 803
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
254-409 |
1.67e-39 |
|
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: 145.59 E-value: 1.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 254 DENLTKLLNLVYGYDSFRDGQLQAIKMILGGSSTMLVLPTGAGKSLCYQIPAMILPGITLVVSPLVSLMIDQLKHLPSI- 332
Cdd:cd18015 3 SGKVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 333 IKGGLLSSSQRPEEATETLRKLKEGI--IKVLFVSPERLLNVE-FLSMFRMSLSV---SLVVVDEAHCVSEWSHNFRPSY 406
Cdd:cd18015 83 ISATMLNASSSKEHVKWVHAALTDKNseLKLLYVTPEKIAKSKrFMSKLEKAYNAgrlARIAIDEVHCCSQWGHDFRPDY 162
|
...
gi 1063686833 407 MRL 409
Cdd:cd18015 163 KKL 165
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
255-409 |
2.49e-39 |
|
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: 144.97 E-value: 2.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 255 ENLTKLLNLVYGYDSFRDGQLQAIKMILGGSSTMLVLPTGAGKSLCYQIPAMILPGITLVVSPLVSLMIDQLKHLPSI-I 333
Cdd:cd18016 3 KEMMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLdI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 334 KGGLLSSSQRPEEATETLRKL--KEGIIKVLFVSPERL-----LNVEFLSMFRMSLsVSLVVVDEAHCVSEWSHNFRPSY 406
Cdd:cd18016 83 PATYLTGDKTDAEATKIYLQLskKDPIIKLLYVTPEKIsasnrLISTLENLYERKL-LARFVIDEAHCVSQWGHDFRPDY 161
|
...
gi 1063686833 407 MRL 409
Cdd:cd18016 162 KRL 164
|
|
| DpdF |
NF041063 |
protein DpdF; |
260-602 |
3.34e-39 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 156.61 E-value: 3.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 260 LLNLVYGYDSFRD-GQLQAIKMIL---GGSSTMLVLPTGAGKSLCYQIPAMILP---GITLVVSPLVSLMIDQ------- 325
Cdd:NF041063 130 FLAEALGFTHYRSpGQREAVRAALlapPGSTLIVNLPTGSGKSLVAQAPALLASrqgGLTLVVVPTVALAIDQerrarel 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 326 LKHLPSIIKGGL-LSSSQRPEEATETLRKLKEGIIKVLFVSPERLLnveflsmfrMSLSVSL-----------VVVDEAH 393
Cdd:NF041063 210 LRRAGPDLGGPLaWHGGLSAEERAAIRQRIRDGTQRILFTSPESLT---------GSLRPALfdaaeagllryLVVDEAH 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 394 CVSEWSHNFRPSYMRLKAsmLFSELKAEC--------ILamtatattmtlqavMS------SLE--------IPSTNLIQ 451
Cdd:NF041063 281 LVDQWGDGFRPEFQLLAG--LRRSLLRLApsgrpfrtLL--------------LSatltesTLDtletlfgpPGPFIVVS 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 452 KSQLRD----NFELSVSLsgANRMKDLL-ILMESPpykeiRSIIVYCKFQYETDMISKYLRdnninAKGY------HSGL 520
Cdd:NF041063 345 AVQLRPepayWVAKCDSE--EERRERVLeALRHLP-----RPLILYVTKVEDAEAWLQRLR-----AAGFrrvalfHGDT 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 521 PAKDRVRIQESFCSNKIRVVVATVAFGMGLDKGDVGAVIHFSVPGSMEEYVQEIGRAGRDGRLSYCHLFYDNDTYLKLRS 600
Cdd:NF041063 413 PDAERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDIAKS 492
|
..
gi 1063686833 601 LA 602
Cdd:NF041063 493 LN 494
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
261-409 |
9.98e-32 |
|
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: 122.58 E-value: 9.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 261 LNLVYGYDSFRDGQLQAIKMILG-GSSTMLVLPTGAGKSLCYQIPAMILPGITLVVSPLVSLMIDQLKHLP-SIIKGGLL 338
Cdd:cd18017 4 LNEYFGHSSFRPVQWKVIRSVLEeRRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVmSNIPACFL 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063686833 339 SSSQRPEEATEtlrkLKEGIIKVLFVSPERLL-NVEFLSmfRMSLSVSLVVVDEAHCVSEWSHNFRPSYMRL 409
Cdd:cd18017 84 GSAQSQNVLDD----IKMGKIRVIYVTPEFVSkGLELLQ--QLRNGITLIAIDEAHCVSQWGHDFRSSYRHL 149
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
259-409 |
4.37e-31 |
|
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: 121.04 E-value: 4.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 259 KLLNLVYGYDSFR-DGQLQAIKMILGGSSTMLV-LPTGAGKSLCYQIPAMILPGITLVVSPLVSLMIDQLKHLPSI-IKG 335
Cdd:cd18014 2 STLKKVFGHSDFKsPLQEKATMAVVKGNKDVFVcMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLkIRV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063686833 336 GLLSSSQRPEEATETLRKLKEGI--IKVLFVSPERLLNVEFLSMFRMSLSVSL---VVVDEAHCVSEWSHNFRPSYMRL 409
Cdd:cd18014 82 DSLNSKLSAQERKRIIADLESEKpqTKFLYITPEMAATSSFQPLLSSLVSRNLlsyLVVDEAHCVSQWGHDFRPDYLRL 160
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
500-581 |
1.14e-24 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 98.44 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 500 DMISKYLRDNNINAKGYHSGLPAKDRVRIQESFCSNKIRVVVATVAFGMGLDKGDVGAVIHFSVPGSMEEYVQEIGRAGR 579
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1063686833 580 DG 581
Cdd:smart00490 81 AG 82
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
271-416 |
6.45e-22 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 93.46 E-value: 6.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 271 RDGQLQAIKMILGGSSTMLVLPTGAGKSLCYQIPAM-----ILPGI-TLVVSPLVSLMIDQLKHLPSIIK--GGLLSSSQ 342
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdkLDNGPqALVLAPTRELAEQIYEELKKLGKglGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 343 RPEEATETLRKLKEgiIKVLFVSPERLLNVeFLSMFRMSlSVSLVVVDEAHCVSEWShnFRPSYMRLKAS-------MLF 415
Cdd:pfam00270 81 GGDSRKEQLEKLKG--PDILVGTPGRLLDL-LQERKLLK-NLKLLVLDEAHRLLDMG--FGPDLEEILRRlpkkrqiLLL 154
|
.
gi 1063686833 416 S 416
Cdd:pfam00270 155 S 155
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
265-413 |
8.85e-22 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 94.10 E-value: 8.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 265 YGYDSFRDGQLQAIKMIL-GGSSTMLVLPTGAGKSLCYQIPAMIL-----PGITLVVSPLVSLMIDQLKHL------PSI 332
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLsGLRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELkklgpsLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 333 IKGGLLSSSQRPEEatetLRKLKEGIIKVLFVSPERLLNveFLSMFRMSLS-VSLVVVDEAHCVSEWshNFRPSYMRLKA 411
Cdd:smart00487 84 KVVGLYGGDSKREQ----LRKLESGKTDILVTTPGRLLD--LLENDKLSLSnVDLVILDEAHRLLDG--GFGDQLEKLLK 155
|
..
gi 1063686833 412 SM 413
Cdd:smart00487 156 LL 157
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
484-581 |
3.21e-21 |
|
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: 89.58 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 484 KEIRSIIVYCKFQYETDmISKYLRDNNINAKGYHSGLPAKDRVRIQESFCSNKIRVVVATVAFGMGLDKGDVGAVIHFSV 563
Cdd:pfam00271 13 ERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYDL 91
|
90
....*....|....*...
gi 1063686833 564 PGSMEEYVQEIGRAGRDG 581
Cdd:pfam00271 92 PWNPASYIQRIGRAGRAG 109
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
469-590 |
2.14e-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: 84.87 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 469 NRMKDLLILMESPPYKEIRSIIVYCKFQYETDMISKYLRDNNINAKGYHSGLPAKDRVRIQESFCSNKIRVVVAT-VAfG 547
Cdd:cd18787 10 EEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATdVA-A 88
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1063686833 548 MGLDKGDVGAVIHFSVPGSMEEYVQEIGRAGRDGRLSYCHLFY 590
Cdd:cd18787 89 RGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
274-585 |
3.78e-18 |
|
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: 89.51 E-value: 3.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 274 QLQAIKMILGGSSTMLVLPTGAGKSLCYQIPAM--IL--PGIT-LVVSPLVSLMIDQLKHLPSIIKGGLLsssqRPEEAT 348
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLeaLLedPGATaLYLYPTKALARDQLRRLRELAEALGL----GVRVAT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 349 ---ETLRKLKEGIIK---VLFVSPErLLNVEFL-------SMFRmslSVSLVVVDEAHC---V--SEWSHNFRpsymRLK 410
Cdd:COG1205 137 ydgDTPPEERRWIREhpdIVLTNPD-MLHYGLLphhtrwaRFFR---NLRYVVIDEAHTyrgVfgSHVANVLR----RLR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 411 -------ASMLFselkaecilamtatattmtlqaVMSSLEI--P---STNLIQKSqlrdnFELsVSLSGANRMKDLLILM 478
Cdd:COG1205 209 ricrhygSDPQF----------------------ILASATIgnPaehAERLTGRP-----VTV-VDEDGSPRGERTFVLW 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 479 ESPPYKEI--RSI------------------IVYCKFQYETDMISKYLRDNNINA------KGYHSGLPAKDRVRIQESF 532
Cdd:COG1205 261 NPPLVDDGirRSAlaeaarlladlvreglrtLVFTRSRRGAELLARYARRALREPdladrvAAYRAGYLPEERREIERGL 340
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1063686833 533 CSNKIRVVVATVAFGMGLDKGDVGAVIHFSVPGSMEEYVQEIGRAGRDGRLSY 585
Cdd:COG1205 341 RSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSL 393
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
490-585 |
1.70e-16 |
|
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: 77.30 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 490 IVYCKFQYETDMISKYLRDN----NINAK---GYHSGLPAKDRVRIQESFCSNKIRVVVATVAFGMGLDKGDVGAVIHFS 562
Cdd:cd18797 39 IVFCRSRKLAELLLRYLKARlveeGPLASkvaSYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|...
gi 1063686833 563 VPGSMEEYVQEIGRAGRDGRLSY 585
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDSL 141
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
473-582 |
1.48e-15 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 79.81 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 473 DLLI-LMESppyKEIRSIIVYCKFQYETDMISKYLRDNNINAKGYHSGLPAKDRVRIQESFCSNKIRVVVAT-VAfGMGL 550
Cdd:COG0513 230 ELLRrLLRD---EDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATdVA-ARGI 305
|
90 100 110
....*....|....*....|....*....|..
gi 1063686833 551 DKGDVGAVIHFSVPGSMEEYVQEIGRAGRDGR 582
Cdd:COG0513 306 DIDDVSHVINYDLPEDPEDYVHRIGRTGRAGA 337
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
284-415 |
2.83e-13 |
|
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: 67.81 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 284 GSSTMLVLPTGAGKSLCYQIPA---MILPGI-TLVVSPLVSLMIDQLKHLPSIIKGGL----LSSSQRPEEatetLRKLK 355
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAAlllLLKKGKkVLVLVPTKALALQTAERLRELFGPGIrvavLVGGSSAEE----REKNK 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063686833 356 EGIIKVLFVSPERLLN-VEFLSMFRmSLSVSLVVVDEAHCVSEWSHNFRPSYMRLKASMLF 415
Cdd:cd00046 77 LGDADIIIATPDMLLNlLLREDRLF-LKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLK 136
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
190-612 |
3.82e-13 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 73.14 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 190 YKGVSKSRSSYSFRGKRYKKKEADGDGESLLEEESDLQKQIEDEANGFISSVEDAILAVKTEASDENLTkllnlvygyds 269
Cdd:COG1061 12 DKLRSSLLLLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFE----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 270 FRDGQLQAIKMIL-----GGSSTMLVLPTGAGKSL----CYQipAMILPGITLVVSPLVSLMIDQLKHLPSIIKGGLLSS 340
Cdd:COG1061 81 LRPYQQEALEALLaalerGGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEELRRFLGDPLAGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 341 SQRPEEAtetlrklkegiiKVLFVSPERLLNVEFLSMFRmsLSVSLVVVDEAHcvsewsHNFRPSYMRlkasmLFSELKA 420
Cdd:COG1061 159 GKKDSDA------------PITVATYQSLARRAHLDELG--DRFGLVIIDEAH------HAGAPSYRR-----ILEAFPA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 421 ECILamtatattmTLQAV---MSSLEIPSTNLIQ-------KSQLRDN-------FELSVSLSG--------ANRMKDLL 475
Cdd:COG1061 214 AYRL---------GLTATpfrSDGREILLFLFDGivyeyslKEAIEDGylappeyYGIRVDLTDeraeydalSERLREAL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 476 ILMES----------PPYKEIRSIIVYCKFQYETDMISKYLRDNNINAKGYHSGLPAKDRVRIQESFCSNKIRVVVATVA 545
Cdd:COG1061 285 AADAErkdkilrellREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDV 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 546 FGMGLDKGDVGAVIHFSVPGSMEEYVQEIGRA---GRDGRLSYCHLFYDNDTYLKLRSLAHSDGVDEYAV 612
Cdd:COG1061 365 LNEGVDVPRLDVAILLRPTGSPREFIQRLGRGlrpAPGKEDALVYDFVGNDVPVLEELAKDLRDLAGYRV 434
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
274-393 |
5.16e-12 |
|
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: 65.30 E-value: 5.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 274 QLQAIKMILGGSSTMLVLPTGAGKSLCYQIPAM--IL--PGIT-LVVSPLVSLMIDQLKHLPSIIKGGLLSSS------Q 342
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILeaLLrdPGSRaLYLYPTKALAQDQLRSLRELLEQLGLGIRvatydgD 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 343 RPEEATETLRKLKEGIIkvlFVSPERL---------LNVEFLSMFRmslsvsLVVVDEAH 393
Cdd:cd17923 85 TPREERRAIIRNPPRIL---LTNPDMLhyallphhdRWARFLRNLR------YVVLDEAH 135
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
260-593 |
4.28e-11 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 66.35 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 260 LLNL-VYGYDSFRDGQLQAIKMILGGSSTMLVLPTGAGKSLCYQIP-----AMILPG--------ITLVVSPLVSLMI-- 323
Cdd:PLN00206 133 LLNLeTAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPiisrcCTIRSGhpseqrnpLAMVLTPTRELCVqv 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 324 -DQLK----HLP---SIIKGGLLSSSQrpeeatetLRKLKEGIiKVLFVSPERLLNVefLSMFRMSLS-VSLVVVDEAHC 394
Cdd:PLN00206 213 eDQAKvlgkGLPfktALVVGGDAMPQQ--------LYRIQQGV-ELIVGTPGRLIDL--LSKHDIELDnVSVLVLDEVDC 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 395 VSEwsHNFRPSYMRLkasmlFSELKAEcilamtatattmtlQAVMSSLEIPSTnlIQK--SQLRDNFeLSVSLSGANR-- 470
Cdd:PLN00206 282 MLE--RGFRDQVMQI-----FQALSQP--------------QVLLFSATVSPE--VEKfaSSLAKDI-ILISIGNPNRpn 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 471 --MKDLLILMESPPYKE-----IRS-------IIVYCKFQYETDMISKYLR-DNNINAKGYHSGLPAKDRVRIQESFCSN 535
Cdd:PLN00206 338 kaVKQLAIWVETKQKKQklfdiLKSkqhfkppAVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVG 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063686833 536 KIRVVVATVAFGMGLDKGDVGAVIHFSVPGSMEEYVQEIGRAGRDGRLSYCHLFYDND 593
Cdd:PLN00206 418 EVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEE 475
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
486-601 |
7.90e-11 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 64.85 E-value: 7.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 486 IRSIIVYCKFQYETDMISKYLRDNNINAKGYHSGLPAKDRVRIQESFCSNKIRVVVATVAFGMGLDKGDVGAVIHFSVPG 565
Cdd:PTZ00424 267 ITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPA 346
|
90 100 110
....*....|....*....|....*....|....*.
gi 1063686833 566 SMEEYVQEIGRAGRDGRLSYCHLFYDNDTYLKLRSL 601
Cdd:PTZ00424 347 SPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEI 382
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
533-590 |
1.45e-10 |
|
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: 58.10 E-value: 1.45e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063686833 533 CSNKIRVVVATVAFGMGLDKGDVGAVIHFSVPGSMEEYVQEIGRAGRDGRLSY-CHLFY 590
Cdd:cd18785 19 IASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGeVILFV 77
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
274-601 |
1.20e-09 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 61.71 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 274 QLQAIKMILGGSSTMLVLPTGAGKSLCYQIPAMI--------LPG---ITLVVSPLVSLM------------IDQLKHlp 330
Cdd:PTZ00110 157 QVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVhinaqpllRYGdgpIVLVLAPTRELAeqireqcnkfgaSSKIRN-- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 331 SIIKGGLLSSSQRPEeatetlrkLKEGIiKVLFVSPERLlnVEFLSMFRMSLS-VSLVVVDEAHCVSEWShnFRPSYMRL 409
Cdd:PTZ00110 235 TVAYGGVPKRGQIYA--------LRRGV-EILIACPGRL--IDFLESNVTNLRrVTYLVLDEADRMLDMG--FEPQIRKI 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 410 -------KASMLFSEL-KAECILAMTATATTMTLQAVMSSLEI-PSTNLIQKSQLRDNFELSVSLsganrMKDLLILMES 480
Cdd:PTZ00110 302 vsqirpdRQTLMWSATwPKEVQSLARDLCKEEPVHVNVGSLDLtACHNIKQEVFVVEEHEKRGKL-----KMLLQRIMRD 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 481 PPykeirSIIVYCKFQYETDMISKYLRDNNINAKGYHSGLPAKDRVRIQESFCSNKIRVVVATVAFGMGLDKGDVGAVIH 560
Cdd:PTZ00110 377 GD-----KILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVIN 451
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1063686833 561 FSVPGSMEEYVQEIGRAGRDGRLSYCHLFYDNDTYLKLRSL 601
Cdd:PTZ00110 452 FDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDL 492
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
266-579 |
2.00e-09 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 60.98 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 266 GYDSFRDGQLQAIKMILGGSSTMLVLPTGAGKSLCYQIPAMIL------------PGITLVVSPLVSL-------MIDQL 326
Cdd:PRK10590 20 GYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHlitrqphakgrrPVRALILTPTRELaaqigenVRDYS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 327 KHLPS---IIKGGLlssSQRPEeatetLRKLKEGIiKVLFVSPERLLNVEFLSMFRMSlSVSLVVVDEAHCVSE--WSHN 401
Cdd:PRK10590 100 KYLNIrslVVFGGV---SINPQ-----MMKLRGGV-DVLVATPGRLLDLEHQNAVKLD-QVEILVLDEADRMLDmgFIHD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 402 FRPSYMRLKA---SMLFSELKAECILAMTATATTMTLQAVMSSLEIPSTNLIQksqlrdnfelSVSLSGANRMKDLLILM 478
Cdd:PRK10590 170 IRRVLAKLPAkrqNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQ----------HVHFVDKKRKRELLSQM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 479 ESPpyKEIRSIIVYCKFQYETDMISKYLRDNNINAKGYHSGLPAKDRVRIQESFCSNKIRVVVATVAFGMGLDKGDVGAV 558
Cdd:PRK10590 240 IGK--GNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHV 317
|
330 340
....*....|....*....|.
gi 1063686833 559 IHFSVPGSMEEYVQEIGRAGR 579
Cdd:PRK10590 318 VNYELPNVPEDYVHRIGRTGR 338
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
351-581 |
3.20e-09 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 60.31 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 351 LRKLKEGIIKVLFVSPERLLnvEFLSMFRMSLS-VSLVVVDEAHCVSEWShnFRPSYMRL---------KASMLFSELKA 420
Cdd:PRK01297 206 LKQLEARFCDILVATPGRLL--DFNQRGEVHLDmVEVMVLDEADRMLDMG--FIPQVRQIirqtprkeeRQTLLFSATFT 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 421 ECILAMTATATTMTlqavmSSLEIPSTNLIQksqlrDNFELSV-SLSGANRMKDLLILMESPPYKEIrsiIVYCKFQYET 499
Cdd:PRK01297 282 DDVMNLAKQWTTDP-----AIVEIEPENVAS-----DTVEQHVyAVAGSDKYKLLYNLVTQNPWERV---MVFANRKDEV 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 500 DMISKYLRDNNINAKGYHSGLPAKDRVRIQESFCSNKIRVVVATVAFGMGLDKGDVGAVIHFSVPGSMEEYVQEIGRAGR 579
Cdd:PRK01297 349 RRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGR 428
|
..
gi 1063686833 580 DG 581
Cdd:PRK01297 429 AG 430
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
488-581 |
8.15e-07 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 52.50 E-value: 8.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 488 SIIVYCKFQYETDMISKYLRDNNINAKGYHSGLPAKDRVRIQESFcSNK-IRVVVAT-VAfGMGLDKGDVGAVIHFSVPG 565
Cdd:PRK11776 244 SCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRF-ANRsCSVLVATdVA-ARGLDIKALEAVINYELAR 321
|
90
....*....|....*.
gi 1063686833 566 SMEEYVQEIGRAGRDG 581
Cdd:PRK11776 322 DPEVHVHRIGRTGRAG 337
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
466-581 |
2.19e-06 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 51.13 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 466 SGANRMKDLLILMESP-PYKeirsIIVYCKFQYETDMISKYLrdnniNAKGYHSGL-----PAKDRVRIQESFCSNKIRV 539
Cdd:PRK04837 238 SNEEKMRLLQTLIEEEwPDR----AIIFANTKHRCEEIWGHL-----AADGHRVGLltgdvAQKKRLRILEEFTRGDLDI 308
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1063686833 540 VVATVAFGMGLDKGDVGAVIHFSVPGSMEEYVQEIGRAGRDG 581
Cdd:PRK04837 309 LVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAG 350
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
516-581 |
2.84e-06 |
|
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: 47.93 E-value: 2.84e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063686833 516 YHSGLPAKDRVRIQESFCSNKIRVVVATVAFGMGLD--------KGDVgaviHFSVPGSME----EYVQEIGRAGRDG 581
Cdd:cd18795 69 HHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpartviiKGTQ----RYDGKGYRElsplEYLQMIGRAGRPG 142
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
513-578 |
3.00e-06 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 51.46 E-value: 3.00e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063686833 513 AKGYHSGLPAKDRVRIQESFCSNKIRVVVATVAFGMGLDKGDVGAVIHFSVPGSMEEYVQEIGRAG 578
Cdd:PRK09751 304 ARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
499-579 |
5.43e-06 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 50.27 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 499 TDMISKYLRdnnINAKGYHSGLPAKDRVRIQESFCSNKIRVVVATVAFGMGLDkgdvgavihFsvPGS------------ 566
Cdd:COG1202 440 CHEIARALG---YKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVD---------F--PASqvifdslamgie 505
|
90
....*....|....*.
gi 1063686833 567 ---MEEYVQEIGRAGR 579
Cdd:COG1202 506 wlsVQEFHQMLGRAGR 521
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
490-582 |
1.06e-05 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 48.79 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 490 IVYCKFQYETDMISKYLRDNNINAkGYHSG-LPAKDRVRIQESFCSNKIRVVVAT-VAfGMGLDKGDVGAVIHFSVPGSM 567
Cdd:PRK11192 249 IVFVRTRERVHELAGWLRKAGINC-CYLEGeMVQAKRNEAIKRLTDGRVNVLVATdVA-ARGIDIDDVSHVINFDMPRSA 326
|
90
....*....|....*
gi 1063686833 568 EEYVQEIGRAGRDGR 582
Cdd:PRK11192 327 DTYLHRIGRTGRAGR 341
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
469-581 |
2.94e-05 |
|
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: 44.39 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 469 NRMKDLLILMESPPYKeirsIIVYCKFQYETDMISKYLRDNNINAKGYHSGLPAKDRVRIQESF--CSNKIRVVVATVAF 546
Cdd:cd18793 14 EALLELLEELREPGEK----VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFneDPDIRVFLLSTKAG 89
|
90 100 110
....*....|....*....|....*....|....*....
gi 1063686833 547 GMGLDKgdVGA--VIHFSVPG--SMEEyvQEIGRAGRDG 581
Cdd:cd18793 90 GVGLNL--TAAnrVILYDPWWnpAVEE--QAIDRAHRIG 124
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
274-396 |
3.64e-05 |
|
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: 45.33 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 274 QLQAIKMILG-GSSTMLVLPTGAGKSLCYQIpAMIL-----PGITLVVSPLVSL---MIDQLKHL--PSIIKGGLLSSSq 342
Cdd:cd17921 6 QREALRALYLsGDSVLVSAPTSSGKTLIAEL-AILRalatsGGKAVYIAPTRALvnqKEADLRERfgPLGKNVGLLTGD- 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1063686833 343 rpeeatETLRKLKEGIIKVLFVSPERLLNVEFLSMFRMSLSVSLVVVDEAHCVS 396
Cdd:cd17921 84 ------PSVNKLLLAEADILVATPEKLDLLLRNGGERLIQDVRLVVVDEAHLIG 131
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
266-601 |
7.25e-05 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 46.38 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 266 GYDSFRDGQLQAIKMILGGSSTMLVLPTGAGKSLCYQIPAM--ILPGI----TLVVSPLVSL-------MIDQLKHLPSI 332
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLhnLDPELkapqILVLAPTRELavqvaeaMTDFSKHMRGV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 333 ----IKGGllsssQRPEEateTLRKLKEGIiKVLFVSPERLLnvEFLSMFRMSLS-VSLVVVDEAHcvsewshnfrpSYM 407
Cdd:PRK11634 105 nvvaLYGG-----QRYDV---QLRALRQGP-QIVVGTPGRLL--DHLKRGTLDLSkLSGLVLDEAD-----------EML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 408 RlkasMLFSElKAECILAMTATATTMTL-QAVMSS---------LEIPSTNLIQKS-QLRDNFELSV-SLSGANRMKDLL 475
Cdd:PRK11634 163 R----MGFIE-DVETIMAQIPEGHQTALfSATMPEairritrrfMKEPQEVRIQSSvTTRPDISQSYwTVWGMRKNEALV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 476 ILMESppyKEIRSIIVYCKFQYETDMISKYLRDNNINAKGYHSGLPAKDRVRIQESFCSNKIRVVVATVAFGMGLDKGDV 555
Cdd:PRK11634 238 RFLEA---EDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERI 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1063686833 556 GAVIHFSVPGSMEEYVQEIGRAGRDGRLSYCHLFYDNDTYLKLRSL 601
Cdd:PRK11634 315 SLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNI 360
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
284-393 |
7.33e-05 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 44.11 E-value: 7.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 284 GSSTMLVLPTGAGKSLCYQIPAMI------LPGI-TLVVSPLVSLMIDQLKHLPSIIKGGLL-----------SSSQRpe 345
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSsladepEKGVqVLYISPLKALINDQERRLEEPLDEIDLeipvavrhgdtSQSEK-- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1063686833 346 eaTETLRKLKEgiikVLFVSPERL----LNVEFLSMFRmslSVSLVVVDEAH 393
Cdd:cd17922 79 --AKQLKNPPG----ILITTPESLelllVNKKLRELFA---GLRYVVVDEIH 121
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
517-579 |
2.94e-04 |
|
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: 41.87 E-value: 2.94e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063686833 517 HSGLPAKDRVRIQESFCSNKIRVVVATVAFGMGLDKGDVGAVIHFSVPGSMEEYVQEIGRAGR 579
Cdd:cd18796 75 HGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
270-407 |
3.02e-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: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 270 FRDGQLQAIKMILGGSST---MLVLPTGAGKSLC-YQIPAMILPGITLVVSPLVSLMiDQlkhlpsiIKGGLLSSSQrpe 345
Cdd:cd17926 1 LRPYQEEALEAWLAHKNNrrgILVLPTGSGKTLTaLALIAYLKELRTLIVVPTDALL-DQ-------WKERFEDFLG--- 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063686833 346 eaTETLRKLKEGIIK------VLFVSPERLLNVEFLSMFrMSLSVSLVVVDEAH--CVSEWSH---NFRPSYM 407
Cdd:cd17926 70 --DSSIGLIGGGKKKdfddanVVVATYQSLSNLAEEEKD-LFDQFGLLIVDEAHhlPAKTFSEilkELNAKYR 139
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
274-392 |
3.97e-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: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 274 QLQAIKMILGGSSTMLVLPTGAGKSLCYQIPAM--ILPG--------ITLVVSP---L---VSLMIDQLKHLPSI----I 333
Cdd:cd00268 17 QAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILekLLPEpkkkgrgpQALVLAPtreLamqIAEVARKLGKGTGLkvaaI 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 334 KGGllsSSQRPEEatetlRKLKEGiIKVLFVSPERLLnvEFLSMFRMSLS-VSLVVVDEA 392
Cdd:cd00268 97 YGG---APIKKQI-----EALKKG-PDIVVGTPGRLL--DLIERGKLDLSnVKYLVLDEA 145
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
266-579 |
4.98e-04 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 43.73 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 266 GYDSFRDGQLQAI-KMILGGSSTMLVLPTGAGKSLCYQIpAMI----LPGITLVVSPLVSL-------MIDQLKHLP--- 330
Cdd:COG1204 19 GIEELYPPQAEALeAGLLEGKNLVVSAPTASGKTLIAEL-AILkallNGGKALYIVPLRALasekyreFKRDFEELGikv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 331 SIIKGGLLSSSQRPEEATetlrklkegiikVLFVSPERllnveFLSMFRMSLS----VSLVVVDEAH------------- 393
Cdd:COG1204 98 GVSTGDYDSDDEWLGRYD------------ILVATPEK-----LDSLLRNGPSwlrdVDLVVVDEAHliddesrgptlev 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 394 --------C-----------------VSEW------SHNFRPSYMRL----KASMLFSElkaecilaMTATATTMTLQAV 438
Cdd:COG1204 161 llarlrrlNpeaqivalsatignaeeIAEWldaelvKSDWRPVPLNEgvlyDGVLRFDD--------GSRRSKDPTLALA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 439 MSSLEIPSTNLIQKSQLRDNFELSVSLsgANRMKDLLILMESPPYKEIRSIIVYCKfqyETDMISKYLRDnnINAKGY-- 516
Cdd:COG1204 233 LDLLEEGGQVLVFVSSRRDAESLAKKL--ADELKRRLTPEEREELEELAEELLEVS---EETHTNEKLAD--CLEKGVaf 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063686833 517 -HSGLPAKDRVRIQESFCSNKIRVVVAT--VAFGMGL--------DKGDVGavihfSVPGSMEEYVQEIGRAGR 579
Cdd:COG1204 306 hHAGLPSELRRLVEDAFREGLIKVLVATptLAAGVNLparrviirDTKRGG-----MVPIPVLEFKQMAGRAGR 374
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
266-392 |
7.17e-04 |
|
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: 41.79 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 266 GYDSFRDGQLQAIKMILGGSSTMLVLPTGAGKSLCYQIPAM-IL---------PGIT-LVVSP-------LVSLMIDQLK 327
Cdd:cd17960 9 GFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLeILlkrkanlkkGQVGaLIISPtrelatqIYEVLQSFLE 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063686833 328 HLPSIIKGGLLSSSQRPEEATETLRKLKEGIikvLFVSPERLLnvEFLSMFRMSLSVS---LVVVDEA 392
Cdd:cd17960 89 HHLPKLKCQLLIGGTNVEEDVKKFKRNGPNI---LVGTPGRLE--ELLSRKADKVKVKsleVLVLDEA 151
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
287-582 |
9.49e-04 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 42.44 E-value: 9.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 287 TMLVLPTGAGKS------LCYQIPAMILPGITLVVSPLVSL--MIDQLKHLPSIIKGGLLSSSQRP-------EEATETL 351
Cdd:TIGR01587 2 LVIEAPTGYGKTeaallwALHSIKSQKADRVIIALPTRATInaMYRRAKELFGSELVGLHHSSSFSrikemgdSEEFEHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 352 RKLKEGIIKVLFVSP-----------ERLLNVEFLSMFRMSLSVSLVVVDEAHcvsewshnFRPSYMR---LKASMLFSE 417
Cdd:TIGR01587 82 FPLYIHSNDKLFLDPitvctidqvlkSVFGEFGHYEFTLASIANSLLIFDEVH--------FYDEYTLaliLAVLEVLKD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 418 LKAECILAMTA-----TATTMTLQAVMSSLEIPSTNLIQKSQLRDNFELSVSLSGANRMKDLLILmesppYKEIRSIIVY 492
Cdd:TIGR01587 154 NDVPILLMSATlpkflKEYAEKIGYVEFNEPLDLKEERRFENHRFILIESDKVGEISSLERLLEF-----IKKGGSIAII 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 493 CKFQYETDMISKYLRDNNINAKG--YHSGLPAKDRVR-----IQESFCSNKIRVVVATVAFGMGLDKgDVGAVIhfSVPG 565
Cdd:TIGR01587 229 VNTVDRAQEFYQQLKEKAPEEEIilYHSRFTEKDRAKkeaelLREMKKSNEKFVIVATQVIEASLDI-SADVMI--TELA 305
|
330
....*....|....*..
gi 1063686833 566 SMEEYVQEIGRAGRDGR 582
Cdd:TIGR01587 306 PIDSLIQRLGRLHRYGR 322
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
274-392 |
9.86e-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: 41.42 E-value: 9.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 274 QLQAIKMILGGSSTMLVLPTGAGKSLCYQIPaMIL--------PGI-TLVVSP---LVSLMIDQLKHLpsiIKGGLLSSS 341
Cdd:cd17957 17 QMQAIPILLHGRDLLACAPTGSGKTLAFLIP-ILQklgkprkkKGLrALILAPtreLASQIYRELLKL---SKGTGLRIV 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1063686833 342 QRPEEATETLRKLKEGIIK--VLFVSPERLLNveFLSMFRMSLS-VSLVVVDEA 392
Cdd:cd17957 93 LLSKSLEAKAKDGPKSITKydILVSTPLRLVF--LLKQGPIDLSsVEYLVLDEA 144
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
489-590 |
1.87e-03 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB 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: 350176 [Multi-domain] Cd Length: 153 Bit Score: 39.93 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 489 IIVYCKFQYETDMISKYLRDNNINAKgyhsgLPAKDRVRIQESFCSNKIRVVVA-TVA-FGMGLDKGDVGAVIHfSVPGS 566
Cdd:cd18789 52 IIVFTDNVEALYRYAKRLLKPFITGE-----TPQSEREEILQNFREGEYNTLVVsKVGdEGIDLPEANVAIQIS-GHGGS 125
|
90 100
....*....|....*....|....*..
gi 1063686833 567 MEEYVQEIG---RAGRDGRLSYchLFY 590
Cdd:cd18789 126 RRQEAQRLGrilRPKKGGGKNA--FFY 150
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
482-579 |
2.50e-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: 38.69 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 482 PYKEIR-SIIVYCKFQYETDMISKYLRDNNINAKGYHSGLPAKDRVR--IQESFCSNKIRVVVATVA-FGMGLDKGDVGA 557
Cdd:cd18799 1 PYKYVEiKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDeaLILLFFGELKPPILVTVDlLTTGVDIPEVDN 80
|
90 100
....*....|....*....|..
gi 1063686833 558 VIHFSVPGSMEEYVQEIGRAGR 579
Cdd:cd18799 81 VVFLRPTESRTLFLQMLGRGLR 102
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
266-395 |
3.32e-03 |
|
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 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: 350720 [Multi-domain] Cd Length: 193 Bit Score: 39.84 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 266 GYDSFRDGQLQAIKMILGGSSTMLVLPTGAGKSLCYQIPAMIL------PGITLVVSPLVSLMI---DQLKHLPS----- 331
Cdd:cd17962 9 GYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRcltehrNPSALILTPTRELAVqieDQAKELMKglppm 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063686833 332 ---IIKGGLLSSSQrpeeatetLRKLKEGiIKVLFVSPERLLnvEFLSMFRMSL-SVSLVVVDEAHCV 395
Cdd:cd17962 89 ktaLLVGGLPLPPQ--------LYRLQQG-VKVIIATPGRLL--DILKQSSVELdNIKIVVVDEADTM 145
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
272-392 |
5.88e-03 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 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: 350696 [Multi-domain] Cd Length: 204 Bit Score: 39.23 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 272 DGQLQAIKMILGGSSTMLVLPTGAGKSLCYQIPaMILPGITLVVSP---LVSLMIDQLKHLPSIIKG-----GLLSSSqr 343
Cdd:cd17938 24 DIQAEAIPLILGGGDVLMAAETGSGKTGAFCLP-VLQIVVALILEPsreLAEQTYNCIENFKKYLDNpklrvALLIGG-- 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1063686833 344 pEEATETLRKLKEGiIKVLFVSPERLLnvEFLSMFRMSLS-VSLVVVDEA 392
Cdd:cd17938 101 -VKAREQLKRLESG-VDIVVGTPGRLE--DLIKTGKLDLSsVRFFVLDEA 146
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
269-393 |
7.62e-03 |
|
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member 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: 350791 [Multi-domain] Cd Length: 182 Bit Score: 38.46 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 269 SFRDGQLQAIKMILGgSSTMLVLPTGAGKSLcyqIPAMIL-------PGITLV----VSPLVSLMIDQLKH---LPSIIK 334
Cdd:cd18033 2 PLRDYQFTIVQKALF-QNTLVALPTGLGKTF---IAAVVMlnyyrwfPKGKIVfmapTKPLVSQQIEACYKitgIPSSQT 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063686833 335 GGLLSSSQRPEEATETLRKlkegiiKVLFVSPERLLNvEFLSMFRMSLSVSLVVVDEAH 393
Cdd:cd18033 78 AELTGSVPPTKRAELWASK------RVFFLTPQTLEN-DLKEGDCDPKSIVCLVIDEAH 129
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
284-412 |
8.74e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 37.74 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063686833 284 GSSTMLVLPTGAGKS-----LCYQIPAMILPGITLVVSPLVSLMIDQLKHLPSIIKGGLLSSSQRPEEATETLRKLKegi 358
Cdd:smart00382 2 GEVILIVGPPGSGKTtlaraLARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLK--- 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063686833 359 IKVLFV-SPERLLNVEFLSMFRMSLSVSLVVVDEAH------CVSEWSHNFRPSYMRLKAS 412
Cdd:smart00382 79 PDVLILdEITSLLDAEQEALLLLLEELRLLLLLKSEknltviLTTNDEKDLGPALLRRRFD 139
|
|
| |
