|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
1-408 |
4.10e-163 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 486.19 E-value: 4.10e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 1 MNGaEDVFVCMPTGAGKSLCYQLPALLASGITIVVSPLIALIQDQVDHLLALKVQVSSLNSKLSVQERKELLSDLERDkp 80
Cdd:COG0514 30 LAG-RDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIRAAFLNSSLSAEERREVLRALRAG-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 81 RTKLLYITPEMAASASFQptlnSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRLAHAPCVALTATATPQVQE 160
Cdd:COG0514 107 ELKLLYVAPERLLNPRFL----ELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGELRERLPNVPVLALTATATPRVRA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 161 DVFAALHLKQP---VASFktpcFRANLFYDVQFKElIPDVYGNLRDFcLKALGQkaengsssGCGIVYCRTREACEQLAI 237
Cdd:COG0514 183 DIAEQLGLEDPrvfVGSF----DRPNLRLEVVPKP-PDDKLAQLLDF-LKEHPG--------GSGIVYCLSRKKVEELAE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 238 ELSSRGVNAKAYHAGLKASDRTQVQNEWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPS 317
Cdd:COG0514 249 WLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 318 WCRLYYSRNDRDQVSFLIRKELAKLQEKRgnkpSDKATLlafDALVTFCEEVGCRHAAIAKYFGDAPPACAKGCDYCQNP 397
Cdd:COG0514 329 EALLLYGPEDVAIQRFFIEQSPPDEERKR----VERAKL---DAMLAYAETTGCRRQFLLRYFGEELAEPCGNCDNCLGP 401
|
410
....*....|.
gi 568971934 398 aaiTKKLDALE 408
Cdd:COG0514 402 ---PETFDGTE 409
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
1-394 |
6.86e-121 |
|
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: 376.03 E-value: 6.86e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 1 MNGaEDVFVCMPTGAGKSLCYQLPALLASGITIVVSPLIALIQDQVDHLLALKVQVSSLNSKLSVQERKELLSDLErdKP 80
Cdd:TIGR00614 24 LLG-RDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATFLNSAQTKEQQLNVLTDLK--DG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 81 RTKLLYITPE-MAASASFqptLNSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRLAHAPCVALTATATPQVQ 159
Cdd:TIGR00614 101 KIKLLYVTPEkISASNRL---LQTLEERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKFPNVPVMALTATASPSVR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 160 EDVFAALHLKQP---VASFKTPcfraNLFYDVQFKelipdvYGNLRDFCLKALgQKAENGSSsgcGIVYCRTREACEQLA 236
Cdd:TIGR00614 178 EDILRQLNLLNPqifCTSFDRP----NLYYEVRRK------TPKILEDLLRFI-RKEFEGKS---GIIYCPSRKKVEQVA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 237 IELSSRGVNAKAYHAGLKASDRTQVQNEWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKP 316
Cdd:TIGR00614 244 AELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGRDGLP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 317 SWCRLYYSRNDrdqvSFLIRKELakLQEKRGNKPSDKATLLafdALVTFCEEVG-CRHAAIAKYFGD---APPACAKGCD 392
Cdd:TIGR00614 324 SECHLFYAPAD----MNRLRRLL--MEEPDGNFRTYKLKLY---EMMEYCLNSStCRRLILLSYFGEkgfNKSFCIMGTE 394
|
..
gi 568971934 393 YC 394
Cdd:TIGR00614 395 KC 396
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
3-406 |
4.38e-120 |
|
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: 378.26 E-value: 4.38e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 3 GAEDVFVCMPTGAGKSLCYQLPALLASGITIVVSPLIALIQDQVDHLLALKVQVSSLNSKLSVQERKELLSDLerDKPRT 82
Cdd:TIGR01389 27 DGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAAAYLNSTLSAKEQQDIEKAL--VNGEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 83 KLLYITPEMAASASFQptlnSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRLAHAPCVALTATATPQVQEDV 162
Cdd:TIGR01389 105 KLLYVAPERLEQDYFL----NMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERFPQVPRIALTATADAETRQDI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 163 FAALHLKQPvASFKTPCFRANLFYDVQFKElipdvygNLRDFCLKALgqKAENGSSsgcGIVYCRTREACEQLAIELSSR 242
Cdd:TIGR01389 181 RELLRLADA-NEFITSFDRPNLRFSVVKKN-------NKQKFLLDYL--KKHRGQS---GIIYASSRKKVEELAERLESQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 243 GVNAKAYHAGLKASDRTQVQNEWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLY 322
Cdd:TIGR01389 248 GISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDGLPAEAILL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 323 YSRNDRDQVSFLIrkELAKLQEKRGNKPSDKatllaFDALVTFCEEVGCRHAAIAKYFGDAPPACAKGCDYC-QNPAAIT 401
Cdd:TIGR01389 328 YSPADIALLKRRI--EQSEADDDYKQIEREK-----LRAMIAYCETQTCRRAYILRYFGENEVEPCGNCDNClDPPKSYD 400
|
....*
gi 568971934 402 KKLDA 406
Cdd:TIGR01389 401 ATVEA 405
|
|
| RecQ5 |
pfam06959 |
RecQ helicase protein-like 5 (RecQ5); This family represents a conserved region approximately ... |
585-776 |
2.73e-111 |
|
RecQ helicase protein-like 5 (RecQ5); This family represents a conserved region approximately 200 residues long within eukaryotic RecQ helicase protein-like 5 (RecQ5). The RecQ helicases have been implicated in DNA repair and recombination, and RecQ5 may have an important role in DNA metabolism.
Pssm-ID: 399738 Cd Length: 202 Bit Score: 340.69 E-value: 2.73e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 585 KSCGAAAEFSEPSDYDIPPTSHVYSLKPKRVGAGFSKGPCSFQTATELLGKSHSQKQAPEAMLEGGQEPPGWVCDLQDED 664
Cdd:pfam06959 1 KSCSAQAEPPEPTEYDIPPASHVYSLKPKRVGAGFPKGSCPFQTATELMEKTRAQEQAPQPVQGGEQEPPSQPCGLQDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 665 RSKPHPGYQEKALGSSVNCGDPSPEKKTKGSSQGS--AKARASKKQQLLATAARKDSQNITRFLCQRTESPPLPASVPRS 742
Cdd:pfam06959 81 RSEPLPGPRGEAPGSSAHCGGPSPEKKAKGSSGGSsvAKARASKKQQLLATAALKDSQNITRFFCQRAESPPPLASAPRA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568971934 743 EDASPSCGDV------PGKCT-QEVGAQGHLVAVFQT-EGPR 776
Cdd:pfam06959 161 EGASPSCEGVqgppmaPEKCTgEEDGAQGHLAAPPQTeECTR 202
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
3-180 |
9.36e-109 |
|
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: 334.44 E-value: 9.36e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 3 GAEDVFVCMPTGAGKSLCYQLPALLASGITIVVSPLIALIQDQVDHLLALKVQVSSLNSKLSVQERKELLSDLERDKPRT 82
Cdd:cd18014 28 GNKDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIRVDSLNSKLSAQERKRIIADLESEKPQT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 83 KLLYITPEMAASASFQPTLNSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRLAHAPCVALTATATPQVQEDV 162
Cdd:cd18014 108 KFLYITPEMAATSSFQPLLSSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRYGHVPWVALTATATPQVQEDI 187
|
170
....*....|....*...
gi 568971934 163 FAALHLKQPVASFKTPCF 180
Cdd:cd18014 188 FAQLRLKKPVAIFKTPCF 205
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
6-408 |
7.50e-97 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 317.43 E-value: 7.50e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 6 DVFVCMPTGAGKSLCYQLPALLASGITIVVSPLIALIQDQVDHLLALKVQVSSLNSKLSVQERKELLSDLERDkpRTKLL 85
Cdd:PRK11057 42 DCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAAACLNSTQTREQQLEVMAGCRTG--QIKLL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 86 YITPEMAASASFqptLNSLVSRNLlSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRLAHAPCVALTATATPQVQEDVFAA 165
Cdd:PRK11057 120 YIAPERLMMDNF---LEHLAHWNP-ALLAVDEAHCISQWGHDFRPEYAALGQLRQRFPTLPFMALTATADDTTRQDIVRL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 166 LHLKQP---VASFKTPCFRANLFYdvQFKELipdvygnlrDFCLKAL-GQKAEngsssgCGIVYCRTREACEQLAIELSS 241
Cdd:PRK11057 196 LGLNDPliqISSFDRPNIRYTLVE--KFKPL---------DQLMRYVqEQRGK------SGIIYCNSRAKVEDTAARLQS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 242 RGVNAKAYHAGLKASDRTQVQNEWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRL 321
Cdd:PRK11057 259 RGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAML 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 322 YYSRNDrdqVSFLIR----KELAKLQEKRGNKpsdkatllaFDALVTFCEEVGCRHAAIAKYFGDAPPACAKGCDYCQNP 397
Cdd:PRK11057 339 FYDPAD---MAWLRRcleeKPAGQQQDIERHK---------LNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNCDICLDP 406
|
410
....*....|.
gi 568971934 398 AaitKKLDALE 408
Cdd:PRK11057 407 P---KQYDGLE 414
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
1-403 |
3.70e-94 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 323.00 E-value: 3.70e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 1 MNGAeDVFVCMPTGAGKSLCYQLPALLASGITIVVSPLIALIQDQVDHLLALKVQVSSLNSKLSVQERKELLSDLERDKP 80
Cdd:PLN03137 473 MSGY-DVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSAGMEWAEQLEILQELSSEYS 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 81 RTKLLYITPE-MAASASFQPTLNSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRLAHAPCVALTATATPQVQ 159
Cdd:PLN03137 552 KYKLLYVTPEkVAKSDSLLRHLENLNSRGLLARFVIDEAHCVSQWGHDFRPDYQGLGILKQKFPNIPVLALTATATASVK 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 160 EDVFAALHLKQPVAsFKTPCFRANLFYDVqfkelIPDVygnlrDFCLKALGQKAENGSSSGCGIVYCRTREACEQLAIEL 239
Cdd:PLN03137 632 EDVVQALGLVNCVV-FRQSFNRPNLWYSV-----VPKT-----KKCLEDIDKFIKENHFDECGIIYCLSRMDCEKVAERL 700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 240 SSRGVNAKAYHAGLKASDRTQVQNEWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWC 319
Cdd:PLN03137 701 QEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSSC 780
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 320 RLYYSRNDRDQVSFLIRK-ELAKLQEKRG-NKPSDKATLLAFDA-----LVTFCE-EVGCRHAAIAKYFGDAPPA--CAK 389
Cdd:PLN03137 781 VLYYSYSDYIRVKHMISQgGVEQSPMAMGyNRMASSGRILETNTenllrMVSYCEnEVDCRRFLQLVHFGEKFDStnCKK 860
|
410
....*....|....
gi 568971934 390 GCDYCQNPAAITKK 403
Cdd:PLN03137 861 TCDNCSSSKSLIDK 874
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
1-175 |
6.43e-86 |
|
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: 273.64 E-value: 6.43e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 1 MNGaEDVFVCMPTGAGKSLCYQLPALLASGITIVVSPLIALIQDQVDHLLALKVQVSSLNSKLSVQERKELLsdLERDKP 80
Cdd:cd17920 25 LAG-RDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAAALNSTLSPEEKREVL--LRIKNG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 81 RTKLLYITPEMAASASFQPTLNSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRLAHAPCVALTATATPQVQE 160
Cdd:cd17920 102 QYKLLYVTPERLLSPDFLELLQRLPERKRLALIVVDEAHCVSQWGHDFRPDYLRLGRLRRALPGVPILALTATATPEVRE 181
|
170
....*....|....*...
gi 568971934 161 DVFAALHLKQP---VASF 175
Cdd:cd17920 182 DILKRLGLRNPvifRASF 199
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
181-323 |
8.54e-64 |
|
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: 210.91 E-value: 8.54e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 181 RANLFYDVQFKELIPDVYGNLRDFCLKALGqkaengsssGCGIVYCRTREACEQLAIELSSRGVNAKAYHAGLKASDRTQ 260
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLKRIKVEHLG---------GSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRD 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568971934 261 VQNEWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYY 323
Cdd:cd18794 72 VQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
5-171 |
1.86e-62 |
|
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: 210.45 E-value: 1.86e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 5 EDVFVCMPTGAGKSLCYQLPALLASGITIVVSPLIALIQDQVDHLLALKVQVSSLNSKLSVQERKELLSDLERDKPRTKL 84
Cdd:cd18016 33 EDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATYLTGDKTDAEATKIYLQLSKKDPIIKL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 85 LYITPE-MAASASFQPTLNSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRLAHAPCVALTATATPQVQEDVF 163
Cdd:cd18016 113 LYVTPEkISASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRPDYKRLNMLRQKFPSVPMMALTATATPRVQKDIL 192
|
....*...
gi 568971934 164 AALHLKQP 171
Cdd:cd18016 193 NQLKMLRP 200
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
5-175 |
2.99e-59 |
|
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: 201.44 E-value: 2.99e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 5 EDVFVCMPTGAGKSLCYQLPALLASGITIVVSPLIALIQDQVDHLLALKVQVSSLNSKLSVQERKELLSDLERDKPRTKL 84
Cdd:cd18015 34 RDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISATMLNASSSKEHVKWVHAALTDKNSELKL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 85 LYITPE-MAASASFQPTLNSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRLAHAPCVALTATATPQVQEDVF 163
Cdd:cd18015 114 LYVTPEkIAKSKRFMSKLEKAYNAGRLARIAIDEVHCCSQWGHDFRPDYKKLGILKRQFPNVPILGLTATATSKVLKDVQ 193
|
170
....*....|....*
gi 568971934 164 AALHLKQPV---ASF 175
Cdd:cd18015 194 KILCIQKCLtftASF 208
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
1-166 |
1.62e-53 |
|
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: 185.15 E-value: 1.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 1 MNGaEDVFVCMPTGAGKSLCYQLPALL----ASGITIVVSPLIALIQDQVDHLLALkVQVSSLNSKLSVQERKELLSDLE 76
Cdd:cd18018 25 LSG-RSTLVVLPTGAGKSLCYQLPALLlrrrGPGLTLVVSPLIALMKDQVDALPRA-IKAAALNSSLTREERRRILEKLR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 77 RDKprTKLLYITPEMAASASFQPTLNSLVSrnlLSYLVVDEAHCVSQWGHDFRPDYLRLG-ALRSRLAHAPCVALTATAT 155
Cdd:cd18018 103 AGE--VKILYVSPERLVNESFRELLRQTPP---ISLLVVDEAHCISEWSHNFRPDYLRLCrVLRELLGAPPVLALTATAT 177
|
170
....*....|.
gi 568971934 156 PQVQEDVFAAL 166
Cdd:cd18018 178 KRVVEDIASHL 188
|
|
| DpdF |
NF041063 |
protein DpdF; |
7-330 |
4.61e-50 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 190.51 E-value: 4.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 7 VFVCMPTGAGKSLCYQLPALLAS---GITIVVSPLIALIQDQ-------VDHLLALKVQVSSLNSKLSVQERKELLSDLE 76
Cdd:NF041063 161 LIVNLPTGSGKSLVAQAPALLASrqgGLTLVVVPTVALAIDQerrarelLRRAGPDLGGPLAWHGGLSAEERAAIRQRIR 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 77 RDKPRtkLLYITPEmAASASFQPTLNSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRL-AHAP------CVA 149
Cdd:NF041063 241 DGTQR--ILFTSPE-SLTGSLRPALFDAAEAGLLRYLVVDEAHLVDQWGDGFRPEFQLLAGLRRSLlRLAPsgrpfrTLL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 150 LTATATPQVQE------------DVFAALHLKQPVASFKTPCFRANlfydvqfkelipdvygNLRDFCLKALgqkaengs 217
Cdd:NF041063 318 LSATLTESTLDtletlfgppgpfIVVSAVQLRPEPAYWVAKCDSEE----------------ERRERVLEAL-------- 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 218 ssgCG-----IVYCRTREACEQLAIELSSRGVN-AKAYHAGLKASDRTQVQNEWMEEKVPVIVATISFGMGVDKANVRFV 291
Cdd:NF041063 374 ---RHlprplILYVTKVEDAEAWLQRLRAAGFRrVALFHGDTPDAERERLIEQWRENELDIVVATSAFGLGMDKSDVRTV 450
|
330 340 350
....*....|....*....|....*....|....*....
gi 568971934 292 AHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQ 330
Cdd:NF041063 451 IHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDI 489
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
6-172 |
3.00e-47 |
|
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: 166.87 E-value: 3.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 6 DVFVCMPTGAGKSLCYQLPALLASGITIVVSPLIALIQDQVDHLLALKVQVSSLNSklsvQERKELLSDLERDKPRtkLL 85
Cdd:cd18017 30 DNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFLGS----AQSQNVLDDIKMGKIR--VI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 86 YITPEMAASASFqpTLNSLvsRNLLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRLAHAPCVALTATATPQVQEDVFAA 165
Cdd:cd18017 104 YVTPEFVSKGLE--LLQQL--RNGITLIAIDEAHCVSQWGHDFRSSYRHLGSIRNRLPNVPIVALTATATPSVRDDIIKN 179
|
....*..
gi 568971934 166 LHLKQPV 172
Cdd:cd18017 180 LNLRNPQ 186
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
5-160 |
2.14e-26 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 106.17 E-value: 2.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 5 EDVFVCMPTGAGKSLCYQLPAL------LASGITIVVSPLIALIQDQVDHLLAL-KVQVSSLNSKLSVQERKELLSDLEr 77
Cdd:pfam00270 15 RDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLgKGLGLKVASLLGGDSRKEQLEKLK- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 78 dkpRTKLLYITPEMAASasfqpTLNSLVSRNLLSYLVVDEAHCVSQWGhdFRPDYLRLgaLRSRLAHAPCVALTATATPQ 157
Cdd:pfam00270 94 ---GPDILVGTPGRLLD-----LLQERKLLKNLKLLVLDEAHRLLDMG--FGPDLEEI--LRRLPKKRQILLLSATLPRN 161
|
...
gi 568971934 158 VQE 160
Cdd:pfam00270 162 LED 164
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1-188 |
6.61e-23 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 97.56 E-value: 6.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 1 MNGAEDVFVCMPTGAGKSLCYQLPALLA-----SGITIVVSPLIALIQDQVDHLLAL----KVQVSSLNSKLSVQERKEL 71
Cdd:smart00487 21 LSGLRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLgpslGLKVVGLYGGDSKREQLRK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 72 LSdlerdKPRTKLLYITPEMAasasFQPTLNSLVSRNLLSYLVVDEAHCVSQWGhdFRPDYLRLGALRSRlaHAPCVALT 151
Cdd:smart00487 101 LE-----SGKTDILVTTPGRL----LDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKLLKLLPK--NVQLLLLS 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 568971934 152 ATATPQVQEdvFAALHLKQPVasFKTPCFRANLFYDV 188
Cdd:smart00487 168 ATPPEEIEN--LLELFLNDPV--FIDVGFTPLEPIEQ 200
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
233-314 |
7.54e-19 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 81.87 E-value: 7.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 233 EQLAIELSSRGVNAKAYHAGLKASDRTQVQNEWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGR 312
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 568971934 313 DG 314
Cdd:smart00490 81 AG 82
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
217-314 |
1.93e-15 |
|
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: 73.01 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 217 SSSGCGIVYCRTREACEqLAIELSSRGVNAKAYHAGLKASDRTQVQNEWMEEKVPVIVATISFGMGVDKANVRFVAHWNI 296
Cdd:pfam00271 13 ERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYDL 91
|
90
....*....|....*...
gi 568971934 297 AKSMAGYYQESGRAGRDG 314
Cdd:pfam00271 92 PWNPASYIQRIGRAGRAG 109
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
5-317 |
7.22e-15 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 79.11 E-value: 7.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 5 EDVFVCMPTGAGKSLCYQLPALLA----SGIT-IVVSPLIALIQDQVDHLLALkvqVSSLNSKLSV---------QERKE 70
Cdd:COG1205 72 KNVVIATPTASGKSLAYLLPVLEAlledPGATaLYLYPTKALARDQLRRLREL---AEALGLGVRVatydgdtppEERRW 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 71 LlsdleRDKPRtkLLYITPEM------AASASFQPTLnslvsRNlLSYLVVDEAHC---V--SQWGHDFRpdylRLgalr 139
Cdd:COG1205 149 I-----REHPD--IVLTNPDMlhygllPHHTRWARFF-----RN-LRYVVIDEAHTyrgVfgSHVANVLR----RL---- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 140 SRLAH----AP-CVALTATatpqvqedvfaalhLKQPVASFktpcfrANLFyDVQFkELI-----------------PDV 197
Cdd:COG1205 208 RRICRhygsDPqFILASAT--------------IGNPAEHA------ERLT-GRPV-TVVdedgsprgertfvlwnpPLV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 198 YGNLRDFCLKA----LGQKAENGSSSgcgIVYCRTREACEQLAIELSSR------GVNAKAYHAGLKASDRTQVQNEWME 267
Cdd:COG1205 266 DDGIRRSALAEaarlLADLVREGLRT---LVFTRSRRGAELLARYARRAlrepdlADRVAAYRAGYLPEERREIERGLRS 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 568971934 268 EKVPVIVATISFGMGVDKANVRFV--AHWniAKSMAGYYQESGRAGRDGKPS 317
Cdd:COG1205 343 GELLGVVSTNALELGIDIGGLDAVvlAGY--PGTRASFWQQAGRAGRRGQDS 392
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
4-153 |
2.57e-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: 70.90 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 4 AEDVFVCMPTGAGKSLCYQLPALLAS----GITIVVSPLIALIQDQ---VDHLLALKVQVSSLNSKLSVQERKellsdlE 76
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLlkkgKKVLVLVPTKALALQTaerLRELFGPGIRVAVLVGGSSAEERE------K 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568971934 77 RDKPRTKLLYITPEMAASASFQptlNSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRLgaLRSRLAHAPCVALTAT 153
Cdd:cd00046 75 NKLGDADIIIATPDMLLNLLLR---EDRLFLKDLKLIIVDEAHALLIDSRGALILDLAV--RKAGLKNAQVILLSAT 146
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
223-317 |
3.58e-14 |
|
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: 70.75 E-value: 3.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 223 IVYCRTREACEQLAIELSSRGVNAK-------AYHAGLKASDRTQVQNEWMEEKVPVIVATISFGMGVDKANVRFVAHWN 295
Cdd:cd18797 39 IVFCRSRKLAELLLRYLKARLVEEGplaskvaSYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|..
gi 568971934 296 IAKSMAGYYQESGRAGRDGKPS 317
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDS 140
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
5-119 |
6.15e-11 |
|
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: 62.22 E-value: 6.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 5 EDVFVCMPTGAGKSLCYQLPALLA----SGIT-IVVSPLIALIQDQVDHLLAL------KVQVSSLNSKLSVQERKELLs 73
Cdd:cd17923 16 RSVVVTTGTASGKSLCYQLPILEAllrdPGSRaLYLYPTKALAQDQLRSLRELleqlglGIRVATYDGDTPREERRAII- 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 568971934 74 dleRDKPRtkLLYITPEM---------AASASFQptlnslvsRNlLSYLVVDEAH 119
Cdd:cd17923 95 ---RNPPR--ILLTNPDMlhyallphhDRWARFL--------RN-LRYVVLDEAH 135
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
223-315 |
1.66e-10 |
|
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: 59.44 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 223 IVYCRTREACEQLAIELSSRGVNAKAYHAGLKASDRTQVQNEWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAG 302
Cdd:cd18787 31 IIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAARGLDIPGVDHVINYDLPRDAED 110
|
90
....*....|...
gi 568971934 303 YYQESGRAGRDGK 315
Cdd:cd18787 111 YVHRIGRTGRAGR 123
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
5-359 |
2.29e-10 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 64.15 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 5 EDVFVCMPTGAGKSLCYQLPAL--LASGITIV-VSPLIALIQDQVDHL------LALKVQVSSlnsklsvqerkellSDL 75
Cdd:COG1204 39 KNLVVSAPTASGKTLIAELAILkaLLNGGKALyIVPLRALASEKYREFkrdfeeLGIKVGVST--------------GDY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 76 ERDKPRTK---LLYITPEMAASA-SFQPtlnSLVSRnlLSYLVVDEAHCVsqwGHDFR-PDY-LRLGALRSRLAHAPCVA 149
Cdd:COG1204 105 DSDDEWLGrydILVATPEKLDSLlRNGP---SWLRD--VDLVVVDEAHLI---DDESRgPTLeVLLARLRRLNPEAQIVA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 150 LTATAT-PQVQEDVFAALHLK---QPVASfktpcfRANLFYD--VQFKELIPDVYGNLRDFCLKALGqkaENGSSsgcgI 223
Cdd:COG1204 177 LSATIGnAEEIAEWLDAELVKsdwRPVPL------NEGVLYDgvLRFDDGSRRSKDPTLALALDLLE---EGGQV----L 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 224 VYCRTREACEQLAIELS---------------------------------------SRGVnakAYH-AGLKASDRTQVQn 263
Cdd:COG1204 244 VFVSSRRDAESLAKKLAdelkrrltpeereeleelaeellevseethtnekladclEKGV---AFHhAGLPSELRRLVE- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 264 EWMEE-KVPVIVATISFGMGVdkaN--VRFV----AHWNIAKSMAG--YYQESGRAGRDGK-P---SWCRLYYSRNDRDQ 330
Cdd:COG1204 320 DAFREgLIKVLVATPTLAAGV---NlpARRViirdTKRGGMVPIPVleFKQMAGRAGRPGYdPygeAILVAKSSDEADEL 396
|
410 420
....*....|....*....|....*....
gi 568971934 331 VSFLIRKELAKLQEKRGNKPSDKATLLAF 359
Cdd:COG1204 397 FERYILGEPEPIRSKLANESALRTHLLAL 425
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
5-119 |
2.60e-10 |
|
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: 59.90 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 5 EDVFVCMPTGAGKSLCYQLPALL------ASGITIV-VSPLIALIQDQVDHL------LALKVQVSSLNSKLSVQERKEL 71
Cdd:cd17922 2 RNVLIAAPTGSGKTEAAFLPALSsladepEKGVQVLyISPLKALINDQERRLeepldeIDLEIPVAVRHGDTSQSEKAKQ 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 568971934 72 LsdlerDKPRTKLLyITPEmaasaSFQPTLNSLVSRNLLS---YLVVDEAH 119
Cdd:cd17922 82 L-----KNPPGILI-TTPE-----SLELLLVNKKLRELFAglrYVVVDEIH 121
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
9-312 |
6.73e-09 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 59.65 E-value: 6.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 9 VCMPTGAGKSL----CYQlpALLASGITIVVSPLIALIQDQVDHLLALkvqvssLNSKLSVQERKELLSDlerdkprtkl 84
Cdd:COG1061 105 VVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEELRRF------LGDPLAGGGKKDSDAP---------- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 85 LYITpeMAASASFQPTLNSLVSRnlLSYLVVDEAHcvsqwghdfrpdylRLGA-----LRSRLAHAPCVALtaTATP--- 156
Cdd:COG1061 167 ITVA--TYQSLARRAHLDELGDR--FGLVIIDEAH--------------HAGApsyrrILEAFPAAYRLGL--TATPfrs 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 157 ---------------------QVQEDVFAALHLKQPVASFKTPCFRANLFYDVQFKELIPDVYGNLRDfcLKALGQKAEN 215
Cdd:COG1061 227 dgreillflfdgivyeyslkeAIEDGYLAPPEYYGIRVDLTDERAEYDALSERLREALAADAERKDKI--LRELLREHPD 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 216 GSSsgcGIVYCRTREACEQLAIELSSRGVNAKAYHAGLKASDRTQVQNEWMEEKVPVIVATISFGMGVDKANVRFVAHWN 295
Cdd:COG1061 305 DRK---TLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLR 381
|
330
....*....|....*..
gi 568971934 296 IAKSMAGYYQesgRAGR 312
Cdd:COG1061 382 PTGSPREFIQ---RLGR 395
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
203-314 |
6.98e-09 |
|
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: 55.64 E-value: 6.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 203 DFCLKALGQKAENGSSsgcgIVYCRTREACEQLAIELSsrGVnaKAYHAGLKASDRTQVQNEWMEEKVPVIVATISFGMG 282
Cdd:cd18795 31 IIVLLKIETVSEGKPV----LVFCSSRKECEKTAKDLA--GI--AFHHAGLTREDRELVEELFREGLIKVLVATSTLAAG 102
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 568971934 283 VD--------KANVRFVAHWNIAKSMAGYYQESGRAGRDG 314
Cdd:cd18795 103 VNlpartviiKGTQRYDGKGYRELSPLEYLQMIGRAGRPG 142
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
325-394 |
8.10e-08 |
|
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: 49.98 E-value: 8.10e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568971934 325 RNDRDQVSFLIRKELAKLQEKRGNkpsdkatLLAFDALVTFCE-EVGCRHAAIAKYFGDA--PPACaKGCDYC 394
Cdd:pfam16124 1 YQDVVRLRFLIEQSEADEERKEVE-------LQKLQAMVAYCEnTTDCRRKQLLRYFGEEfdSEPC-GNCDNC 65
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
7-123 |
5.08e-07 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 50.72 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 7 VFVCMPTGAGKSLCYQL---PALLASGITIV-VSPLIALIqDQVdhllalkvqVSSLNSKLSVQERK--ELLSDLERDK- 79
Cdd:cd17921 20 VLVSAPTSSGKTLIAELailRALATSGGKAVyIAPTRALV-NQK---------EADLRERFGPLGKNvgLLTGDPSVNKl 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 568971934 80 --PRTKLLYITPEMAASAsfqptLNSLVSRNL--LSYLVVDEAHCVSQ 123
Cdd:cd17921 90 llAEADILVATPEKLDLL-----LRNGGERLIqdVRLVVVDEAHLIGD 132
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
222-276 |
7.72e-07 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 52.46 E-value: 7.72e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 568971934 222 GIVYCRTREACEQLAIELSSRGVNAKAYHAGLKASDRTQVQNEWMEEKVPVIVAT 276
Cdd:COG0513 244 AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVAT 298
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
223-351 |
1.26e-06 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 52.08 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 223 IVYCRTREACEQLAIELSSRGVNAKAYHAGLKASDRTQVQNEWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAG 302
Cdd:PTZ00110 381 LIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIED 460
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568971934 303 YYQESGRAGRDG---------KPSWCRLyysrnDRDQVSFL------IRKELAKLQEKRGNKPS 351
Cdd:PTZ00110 461 YVHRIGRTGRAGakgasytflTPDKYRL-----ARDLVKVLreakqpVPPELEKLSNERSNGTE 519
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
221-315 |
1.43e-06 |
|
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: 46.93 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 221 CGIVYCRTREACEQLAIELSsrgvnakayhaglkasdrtqvqnewmeekvpVIVATISFGMGVDKANVRFVAHWNIAKSM 300
Cdd:cd18785 5 KIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSA 53
|
90
....*....|....*
gi 568971934 301 AGYYQESGRAGRDGK 315
Cdd:cd18785 54 ASYIQRVGRAGRGGK 68
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
223-312 |
1.44e-06 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 52.20 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 223 IVYCRTREACEQLAIELssrGVNAKAYHAGLKASDRTQVQNEWMEEKVPVIVATISFGMGVDkanvrFVAHWNIAKSMA- 301
Cdd:COG1202 431 IIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVD-----FPASQVIFDSLAm 502
|
90
....*....|....*....
gi 568971934 302 G--------YYQESGRAGR 312
Cdd:COG1202 503 GiewlsvqeFHQMLGRAGR 521
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
223-315 |
1.40e-05 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 48.67 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 223 IVYCRTREACEQLAIELSSRGVNAKAYHAGLKASDRTQVQNEWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAG 302
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90
....*....|...
gi 568971934 303 YYQESGRAGRDGK 315
Cdd:PTZ00424 351 YIHRIGRSGRFGR 363
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
9-153 |
2.11e-05 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 45.37 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 9 VCMPTGAGKSLC-YQLPALLASGITIVVSPLIALIQDQVDHLLALkvqvsslnskLSVQERKELLSDLERDKPRTKLLYI 87
Cdd:cd17926 23 LVLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFEDF----------LGDSSIGLIGGGKKKDFDDANVVVA 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568971934 88 TPEmaaSASFQPTLNSLVSrNLLSYLVVDEAH--CVSQWGHdfrpdylrlgaLRSRLAHAPCVALTAT 153
Cdd:cd17926 93 TYQ---SLSNLAEEEKDLF-DQFGLLIVDEAHhlPAKTFSE-----------ILKELNAKYRLGLTAT 145
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
6-118 |
2.77e-04 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 43.39 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 6 DVFVCMPTGAGKSLCYQLP---ALLASGIT----IVVSPLIALIQdQVDHLL-----ALKVQVSSLNSKLSVQERKELLS 73
Cdd:cd17956 38 DLCVSAPTGSGKTLAYVLPivqALSKRVVPrlraLIVVPTKELVQ-QVYKVFeslckGTGLKVVSLSGQKSFKKEQKLLL 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568971934 74 DLERDK--PRTKLLYITPemaasASFQPTLNSLVSRNL--LSYLVVDEA 118
Cdd:cd17956 117 VDTSGRylSRVDILVATP-----GRLVDHLNSTPGFTLkhLRFLVIDEA 160
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
12-156 |
9.41e-04 |
|
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' superfamily 2 DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA 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: 350687 [Multi-domain] Cd Length: 178 Bit Score: 41.04 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 12 PTGAGKSLCY--QLPALLASGIT-IVVSPLIALIQDQVDHLLA-LKVQVSSLNSKLSVQERKELLSDLERDKPRTKLlyi 87
Cdd:cd17929 23 VTGSGKTEVYieLIEKVLAKGKQvLVLVPEISLTPQLIKRFKKrFGDKVAVLHSKLSDKERADEWRKIKRGEAKVVI--- 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568971934 88 tpeMAASASFQPTLNslvsrnlLSYLVVDEAHcVSQWGHDFRPDY-LRLGAL-RSRLAHAPCValTATATP 156
Cdd:cd17929 100 ---GARSALFAPFKN-------LGLIIVDEEH-DSSYKQDSGPRYhARDVAIyRAKLENAPVV--LGSATP 157
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
5-153 |
1.02e-03 |
|
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an IFN-inducible cytoplasmic helicase that plays a role in RIG-I-mediated type I interferon (IFN) nuclease-mediated viral RNA degradation. DDX60 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350783 [Multi-domain] Cd Length: 192 Bit Score: 41.20 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 5 EDVFVCMPTGAGKSLC--YQLPALLAS---GITIVVSPLIALIQDQVDHLLAL--KVQVSSLNSKLSVQERkellsDLER 77
Cdd:cd18025 17 ESALIVAPTSSGKTFIsyYCMEKVLREsddGVVVYVAPTKALVNQVVAEVYARfsKKYPPSGKSLWGVFTR-----DYRH 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568971934 78 DKPRTKLLYIT-PEMAASASFQPTLNSLVSRnlLSYLVVDEAHCVSQWGHDFRPDYLRLgalrsrLAHAPCVALTAT 153
Cdd:cd18025 92 NNPMNCQVLITvPECLEILLLSPHNASWVPR--IKYVIFDEIHSIGQSEDGAVWEQLLL------LIPCPFLALSAT 160
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
222-316 |
1.73e-03 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 42.08 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 222 GIVYCRTREACEQLAIELS-SRGVNAKAYHAGLKASDRTQVQNEWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSM 300
Cdd:PLN00206 370 AVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTI 449
|
90
....*....|....*.
gi 568971934 301 AGYYQESGRAGRDGKP 316
Cdd:PLN00206 450 KEYIHQIGRASRMGEK 465
|
|
| Cas3_I-D |
cd09710 |
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; ... |
2-119 |
3.28e-03 |
|
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Diverged DNA helicase Cas3'; signature gene for Type I and subtype I-D
Pssm-ID: 187841 [Multi-domain] Cd Length: 353 Bit Score: 41.01 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 2 NGAEDVFV-CMPTGAGKSLCYQLPALLASGITIVVSPLIALIQDQ---------------VDHLLALKvQVSSLNSKLSV 65
Cdd:cd09710 11 SKDADIIFnTAPTGAGKTLAWLTPLLHGENKAIALYPTNALIEDQteaikefvddanprhQVKSLSAS-DITLWPNDKNV 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568971934 66 QERK-ELLSDLERDKPRTK---LLYITPEMAASASFQ----PTLNSLVSRNLLSYLVVDEAH 119
Cdd:cd09710 90 GSSKgEKLYNLLRNDIGTStpiILLTNPDIFVYLTRFayidRGDIAAGFYTKFSTVIFDEFH 151
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
13-127 |
7.40e-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: 38.72 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 13 TGAGKSLCYQLPA----LLASGITIVVSPLIALI-------QDQV-DHLLAL------KVQVSSLNSKLSVQERKELLSD 74
Cdd:cd17961 40 TGSGKTAAYALPIiqkiLKAKAESGEEQGTRALIlvptrelAQQVsKVLEQLtaycrkDVRVVNLSASSSDSVQRALLAE 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 568971934 75 lerdKPrtKLLYITPEMAASASFQptlNSLVSRNLLSYLVVDEAHCVSQWGHD 127
Cdd:cd17961 120 ----KP--DIVVSTPARLLSHLES---GSLLLLSTLKYLVIDEADLVLSYGYE 163
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
217-316 |
8.16e-03 |
|
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: 38.01 E-value: 8.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971934 217 SSSGCGIVYCRTREACEQLAIELssrgvNAKAYHAGLKASDRTQVQNEWMEEKVPVIVATISFGMGVDKANVRFVAHWNI 296
Cdd:cd18796 47 TRSQAERLAQRLRELCPDRVPPD-----FIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGS 121
|
90 100
....*....|....*....|
gi 568971934 297 AKSMAGYYQESGRAGRDGKP 316
Cdd:cd18796 122 PKSVARLLQRLGRSGHRPGA 141
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
250-323 |
8.67e-03 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It 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: 350198 [Multi-domain] Cd Length: 159 Bit Score: 38.09 E-value: 8.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568971934 250 HAGLKASDRTQVQNEWMEEKVPVIVAT--ISFGMGVDKANVRFVAHwniAK--SMAGYYQESGRAGRDGKPSWCRLYY 323
Cdd:cd18811 68 HGRLKSDEKDAVMAEFREGEVDILVSTtvIEVGVDVPNATVMVIED---AErfGLSQLHQLRGRVGRGDHQSYCLLVY 142
|
|
| |
