|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
94-518 |
1.03e-179 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 518.16 E-value: 1.03e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 94 SDEATKILKEQFHLEKFRPLQRAAINAVMSKEDAVVILSTGGGKSLCYQLPALLANGLALVVSPLISLVEDQILQLRSLG 173
Cdd:COG0514 2 RDDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 174 IDSSSLNANTSKEEAKRVEDAItnKDSKFRLLYVTPEKLAkSKKMMNKLeKSLSVGflkLIAIDEVHCCSQWGHDFRTDY 253
Cdd:COG0514 82 IRAAFLNSSLSAEERREVLRAL--RAGELKLLYVAPERLL-NPRFLELL-RRLKIS---LFAIDEAHCISQWGHDFRPDY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 254 SFLNVLKRQFKGVPILGLTATATSNVLDDVKDMLGIQAALTFRAGFNRSNLKYKVVQKPgsEDECTEEIAKTIKRdFAGQ 333
Cdd:COG0514 155 RRLGELRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKP--PDDKLAQLLDFLKE-HPGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 334 TGIIYCLSRNDCEKVAKALKSHGIKAKHYHAYMEPVDRSGAHQGWISGKIQVIVATVAFGMGIDKPNVRFVIHHSLPKSI 413
Cdd:COG0514 232 SGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 414 ENYYQESGRAGRDGQPATCILYYRLADIFKQSSMVQQE-------RTGIQNLYNMVRYaADSSTCRRVKLAEHFEEAwEP 486
Cdd:COG0514 312 EAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSppdeerkRVERAKLDAMLAY-AETTGCRRQFLLRYFGEE-LA 389
|
410 420 430
....*....|....*....|....*....|..
gi 71987993 487 SWCQKqCDTCENgngfvgtsSKESTDVSEAAK 518
Cdd:COG0514 390 EPCGN-CDNCLG--------PPETFDGTEAAQ 412
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
99-571 |
3.04e-176 |
|
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: 508.54 E-value: 3.04e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 99 KILKEQFHLEKFRPLQRAAINAVMSKEDAVVILSTGGGKSLCYQLPALLANGLALVVSPLISLVEDQILQLRSLGIDSSS 178
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 179 LNANTSKEEAKRVEDAItnKDSKFRLLYVTPEKLAKSKKMMNKLEKSLSVgflKLIAIDEVHCCSQWGHDFRTDYSFLNV 258
Cdd:TIGR00614 81 LNSAQTKEQQLNVLTDL--KDGKIKLLYVTPEKISASNRLLQTLEERKGI---TLIAVDEAHCISQWGHDFRPDYKALGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 259 LKRQFKGVPILGLTATATSNVLDDVKDMLGIQAALTFRAGFNRSNLKYKVVQKPGsedECTEEIAKTIKRDFAGQTGIIY 338
Cdd:TIGR00614 156 LKQKFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTP---KILEDLLRFIRKEFEGKSGIIY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 339 CLSRNDCEKVAKALKSHGIKAKHYHAYMEPVDRSGAHQGWISGKIQVIVATVAFGMGIDKPNVRFVIHHSLPKSIENYYQ 418
Cdd:TIGR00614 233 CPSRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 419 ESGRAGRDGQPATCILYYRLADIFKQSSMVQQERTGIQ-----NLYNMVRYAADSSTCRRVKLAEHFEEAW-EPSWC--- 489
Cdd:TIGR00614 313 ESGRAGRDGLPSECHLFYAPADMNRLRRLLMEEPDGNFrtyklKLYEMMEYCLNSSTCRRLILLSYFGEKGfNKSFCimg 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 490 -QKQCDTCENgngfvgTSSKESTDVSEAAKTTVRIIEEHLNSAKDGSGRITGNKLVELltkkLKGSRNREFCEKLIVNLL 568
Cdd:TIGR00614 393 tEKCCDNCCK------RLDYKTKDVTDKVYDFGPQAQKALSAVGRLNQKFGMGYPVDF----LRGSNSQKIRDGGFRKHS 462
|
...
gi 71987993 569 LEG 571
Cdd:TIGR00614 463 LYG 465
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
62-531 |
1.15e-139 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 436.63 E-value: 1.15e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 62 QKRQAIERKIELKTNEDSDvvTDRWDRDGFPWSDEATKILKEQFHLEKFRPLQRAAINAVMSKEDAVVILSTGGGKSLCY 141
Cdd:PLN03137 415 EREPYVPKFIDVTYTEGSN--DKKWSSRNFPWTKKLEVNNKKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTY 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 142 QLPALLANGLALVVSPLISLVEDQILQLRSLGIDSSSLNANTSKEEAKRVEDAITNKDSKFRLLYVTPEKLAKSKKMMNK 221
Cdd:PLN03137 493 QLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSAGMEWAEQLEILQELSSEYSKYKLLYVTPEKVAKSDSLLRH 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 222 LEKSLSVGFLKLIAIDEVHCCSQWGHDFRTDYSFLNVLKRQFKGVPILGLTATATSNVLDDVKDMLGIQAALTFRAGFNR 301
Cdd:PLN03137 573 LENLNSRGLLARFVIDEAHCVSQWGHDFRPDYQGLGILKQKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNR 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 302 SNLKYKVVQKpgsEDECTEEIAKTIKRDFAGQTGIIYCLSRNDCEKVAKALKSHGIKAKHYHAYMEPVDRSGAHQGWISG 381
Cdd:PLN03137 653 PNLWYSVVPK---TKKCLEDIDKFIKENHFDECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKD 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 382 KIQVIVATVAFGMGIDKPNVRFVIHHSLPKSIENYYQESGRAGRDGQPATCILYYRLADIFKQSSMVQQE---------- 451
Cdd:PLN03137 730 EINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMISQGgveqspmamg 809
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 452 -----------RTGIQNLYNMVRYAADSSTCRRVKLAEHFEEAWEPSWCQKQCDTCENGNGFVgtsskeSTDVSEAAKTT 520
Cdd:PLN03137 810 ynrmassgrilETNTENLLRMVSYCENEVDCRRFLQLVHFGEKFDSTNCKKTCDNCSSSKSLI------DKDVTEIARQL 883
|
490
....*....|....
gi 71987993 521 VRIIE---EHLNSA 531
Cdd:PLN03137 884 VELVKltgERFSSA 897
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
92-300 |
4.44e-134 |
|
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: 390.96 E-value: 4.44e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 92 PWSDEATKILKEQFHLEKFRPLQRAAINAVMSKEDAVVILSTGGGKSLCYQLPALLANGLALVVSPLISLVEDQILQLRS 171
Cdd:cd18015 1 PWSGKVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 172 LGIDSSSLNANTSKEEAKRVEDAITNKDSKFRLLYVTPEKLAKSKKMMNKLEKSLSVGFLKLIAIDEVHCCSQWGHDFRT 251
Cdd:cd18015 81 LGISATMLNASSSKEHVKWVHAALTDKNSELKLLYVTPEKIAKSKRFMSKLEKAYNAGRLARIAIDEVHCCSQWGHDFRP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 71987993 252 DYSFLNVLKRQFKGVPILGLTATATSNVLDDVKDMLGIQAALTFRAGFN 300
Cdd:cd18015 161 DYKKLGILKRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
97-576 |
5.96e-134 |
|
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: 404.84 E-value: 5.96e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 97 ATKILKEQFHLEKFRPLQRAAINAVMSKEDAVVILSTGGGKSLCYQLPALLANGLALVVSPLISLVEDQILQLRSLGIDS 176
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 177 SSLNANTSKEEAKRVEDAITNKDskFRLLYVTPEKLaKSKKMMNKLEKSLsvgfLKLIAIDEVHCCSQWGHDFRTDYSFL 256
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGE--LKLLYVAPERL-EQDYFLNMLQRIP----IALVAVDEAHCVSQWGHDFRPEYQRL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 257 NVLKRQFKGVPILGLTATATSNVLDDVKDMLGIQAALTFRAGFNRSNLKYKVVQKPGSEDECTEEIAKTikrdfAGQTGI 336
Cdd:TIGR01389 154 GSLAERFPQVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKH-----RGQSGI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 337 IYCLSRNDCEKVAKALKSHGIKAKHYHAYMEPVDRSGAHQGWISGKIQVIVATVAFGMGIDKPNVRFVIHHSLPKSIENY 416
Cdd:TIGR01389 229 IYASSRKKVEELAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 417 YQESGRAGRDGQPATCILYYRLADI------FKQSSM-VQQERTGIQNLYNMVRYaADSSTCRRVKLAEHFEEAwEPSWC 489
Cdd:TIGR01389 309 YQEAGRAGRDGLPAEAILLYSPADIallkrrIEQSEAdDDYKQIEREKLRAMIAY-CETQTCRRAYILRYFGEN-EVEPC 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 490 QkQCDTCengngfvgTSSKESTDVSEAAKTTVRIIeehlnsakdgsGRITGNKLVELLTKKLKGSRN------------- 556
Cdd:TIGR01389 387 G-NCDNC--------LDPPKSYDATVEAQKALSCV-----------YRMGQRFGVGYIIEVLRGSKNdkilqkghdqlst 446
|
490 500
....*....|....*....|....*...
gi 71987993 557 ----REFCEK----LIVNLLLEGYLQED 576
Cdd:TIGR01389 447 ygigKDYTQKewrsLIDQLIAEGLLTEN 474
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
97-497 |
2.23e-114 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 354.79 E-value: 2.23e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 97 ATKILKEQFHLEKFRPLQRAAINAVMSKEDAVVILSTGGGKSLCYQLPALLANGLALVVSPLISLVEDQILQLRSLGIDS 176
Cdd:PRK11057 13 AKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 177 SSLNANTSKEEAKRVEDAItnKDSKFRLLYVTPEKLakskkMMNKLEKSLSVGFLKLIAIDEVHCCSQWGHDFRTDYSFL 256
Cdd:PRK11057 93 ACLNSTQTREQQLEVMAGC--RTGQIKLLYIAPERL-----MMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 257 NVLKRQFKGVPILGLTATATSNVLDDVKDMLGIQAALTFRAGFNRSNLKYKVVQKPGSEDECTEEIaktikRDFAGQTGI 336
Cdd:PRK11057 166 GQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQLMRYV-----QEQRGKSGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 337 IYCLSRNDCEKVAKALKSHGIKAKHYHAYMEPVDRSGAHQGWISGKIQVIVATVAFGMGIDKPNVRFVIHHSLPKSIENY 416
Cdd:PRK11057 241 IYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 417 YQESGRAGRDGQPATCILYYRLADIFKQSSMVQQERTGIQNL-----YNMVRYAADSSTCRRVKLAEHFEEAWepswcQK 491
Cdd:PRK11057 321 YQETGRAGRDGLPAEAMLFYDPADMAWLRRCLEEKPAGQQQDierhkLNAMGAFAEAQTCRRLVLLNYFGEGR-----QE 395
|
....*.
gi 71987993 492 QCDTCE 497
Cdd:PRK11057 396 PCGNCD 401
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
99-300 |
4.24e-90 |
|
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: 277.49 E-value: 4.24e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 99 KILKEQFHLEKFRPLQRAAINAVMSKEDAVVILSTGGGKSLCYQLPALLANGLALVVSPLISLVEDQILQLRSLGIDSSS 178
Cdd:cd17920 2 QILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 179 LNANTSKEEAKRVEDAItnKDSKFRLLYVTPEKLAkSKKMMNKLEKSLSVGFLKLIAIDEVHCCSQWGHDFRTDYSFLNV 258
Cdd:cd17920 82 LNSTLSPEEKREVLLRI--KNGQYKLLYVTPERLL-SPDFLELLQRLPERKRLALIVVDEAHCVSQWGHDFRPDYLRLGR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 71987993 259 LKRQFKGVPILGLTATATSNVLDDVKDMLGIQAALTFRAGFN 300
Cdd:cd17920 159 LRRALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
301-436 |
6.17e-75 |
|
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: 235.57 E-value: 6.17e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 301 RSNLKYKVVQKPGSEDECTEEiaKTIKRDFAGQTGIIYCLSRNDCEKVAKALKSHGIKAKHYHAYMEPVDRSGAHQGWIS 380
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLL--KRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 71987993 381 GKIQVIVATVAFGMGIDKPNVRFVIHHSLPKSIENYYQESGRAGRDGQPATCILYY 436
Cdd:cd18794 79 DKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
94-300 |
3.37e-65 |
|
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: 213.15 E-value: 3.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 94 SDEATKILKEQFHLEKFRPLQRAAINAVMSKEDAVVILSTGGGKSLCYQLPALLANGLALVVSPLISLVEDQILQLRSLG 173
Cdd:cd18016 2 SKEMMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 174 IDSSSLNANTSKEEAKRVEDAITNKDSKFRLLYVTPEKLAKSKKMMNKLEKSLSVGFLKLIAIDEVHCCSQWGHDFRTDY 253
Cdd:cd18016 82 IPATYLTGDKTDAEATKIYLQLSKKDPIIKLLYVTPEKISASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRPDY 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 71987993 254 SFLNVLKRQFKGVPILGLTATATSNVLDDVKDMLGIQAALTFRAGFN 300
Cdd:cd18016 162 KRLNMLRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
101-300 |
4.21e-58 |
|
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: 193.84 E-value: 4.21e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 101 LKEQFHLEKFRPLQRAAI-NAVMSKEDAVVILSTGGGKSLCYQLPALLANGLALVVSPLISLVEDQILQLRSLGIDSSSL 179
Cdd:cd18017 4 LNEYFGHSSFRPVQWKVIrSVLEERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 180 NANTSKEEakrVEDaitNKDSKFRLLYVTPEKLAKSKKMMNKLEKSLSvgflkLIAIDEVHCCSQWGHDFRTDYSFLNVL 259
Cdd:cd18017 84 GSAQSQNV---LDD---IKMGKIRVIYVTPEFVSKGLELLQQLRNGIT-----LIAIDEAHCVSQWGHDFRSSYRHLGSI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 71987993 260 KRQFKGVPILGLTATATSNVLDDVKDMLGIQAALTFRAGFN 300
Cdd:cd18017 153 RNRLPNVPIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
98-300 |
3.34e-55 |
|
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: 186.31 E-value: 3.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 98 TKILKEQFHLEKFRPLQRAAINAVMSKEDAVVILSTGGGKSLCYQLPALL----ANGLALVVSPLISLVEDQILQLRSLg 173
Cdd:cd18018 1 LKLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLlrrrGPGLTLVVSPLIALMKDQVDALPRA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 174 IDSSSLNANTSKEEAKRVEDAITNKDSKfrLLYVTPEKLAkSKKMMNKLEKSLSVGFLkliAIDEVHCCSQWGHDFRTDY 253
Cdd:cd18018 80 IKAAALNSSLTREERRRILEKLRAGEVK--ILYVSPERLV-NESFRELLRQTPPISLL---VVDEAHCISEWSHNFRPDY 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 71987993 254 SFLNVLKRQFKGV-PILGLTATATSNVLDDVKDMLGIQAALTFRAGFN 300
Cdd:cd18018 154 LRLCRVLRELLGApPVLALTATATKRVVEDIASHLGIPESGVVRGPLY 201
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
99-290 |
7.55e-52 |
|
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: 177.28 E-value: 7.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 99 KILKEQFHLEKFR-PLQRAAINAVMSKE-DAVVILSTGGGKSLCYQLPALLANGLALVVSPLISLVEDQILQLRSLGIDS 176
Cdd:cd18014 2 STLKKVFGHSDFKsPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 177 SSLNANTSKEEAKRVEDAITNKDSKFRLLYVTPEKLAKS--KKMMNKLeksLSVGFLKLIAIDEVHCCSQWGHDFRTDYS 254
Cdd:cd18014 82 DSLNSKLSAQERKRIIADLESEKPQTKFLYITPEMAATSsfQPLLSSL---VSRNLLSYLVVDEAHCVSQWGHDFRPDYL 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 71987993 255 FLNVLKRQFKGVPILGLTATATSNVLDDVKDMLGIQ 290
Cdd:cd18014 159 RLGALRSRYGHVPWVALTATATPQVQEDIFAQLRLK 194
|
|
| DpdF |
NF041063 |
protein DpdF; |
114-441 |
1.00e-50 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 188.20 E-value: 1.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 114 QRAAINAVM-SKEDA--VVILSTGGGKSLCYQLPALLA---NGLALVVSPLISLVEDQILQLRSL----GIDSSSLNA-- 181
Cdd:NF041063 145 QREAVRAALlAPPGStlIVNLPTGSGKSLVAQAPALLAsrqGGLTLVVVPTVALAIDQERRARELlrraGPDLGGPLAwh 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 182 -NTSKEEAKRVEDAItnKDSKFRLLYVTPEKLAKSkkmmnkLEKSL----SVGFLKLIAIDEVHCCSQWGHDFRTDYSFL 256
Cdd:NF041063 225 gGLSAEERAAIRQRI--RDGTQRILFTSPESLTGS------LRPALfdaaEAGLLRYLVVDEAHLVDQWGDGFRPEFQLL 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 257 -----NVLKRQFKGVPI--LGLTATATSNVLDDVKDMLGIQAALT-FRAGFNRSNLKYKVVQKPgSEDECTEEIAKTIK- 327
Cdd:NF041063 297 aglrrSLLRLAPSGRPFrtLLLSATLTESTLDTLETLFGPPGPFIvVSAVQLRPEPAYWVAKCD-SEEERRERVLEALRh 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 328 --RDFagqtgIIYCLSRNDCEKVAKALKSHGIK-AKHYHAYMEPVDRSGAHQGWISGKIQVIVATVAFGMGIDKPNVRFV 404
Cdd:NF041063 376 lpRPL-----ILYVTKVEDAEAWLQRLRAAGFRrVALFHGDTPDAERERLIEQWRENELDIVVATSAFGLGMDKSDVRTV 450
|
330 340 350
....*....|....*....|....*....|....*..
gi 71987993 405 IHHSLPKSIENYYQESGRAGRDGQPATCILYYRLADI 441
Cdd:NF041063 451 IHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDL 487
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
111-281 |
1.31e-28 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 111.95 E-value: 1.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 111 RPLQRAAINAVMSKEDAVVILSTGGGKSLCYQLPAL------LANGLALVVSPLISLVEDQILQLRSLGID-----SSSL 179
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGlglkvASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 180 NANTSKEEAKRVEDAitnkdskfRLLYVTPEKLAKSKKMMNKLEKslsvgfLKLIAIDEVHCCSQWGhdFRTDYSflNVL 259
Cdd:pfam00270 81 GGDSRKEQLEKLKGP--------DILVGTPGRLLDLLQERKLLKN------LKLLVLDEAHRLLDMG--FGPDLE--EIL 142
|
170 180
....*....|....*....|..
gi 71987993 260 KRQFKGVPILGLTATATSNVLD 281
Cdd:pfam00270 143 RRLPKKRQILLLSATLPRNLED 164
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
346-427 |
9.62e-23 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 92.27 E-value: 9.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 346 EKVAKALKSHGIKAKHYHAYMEPVDRSGAHQGWISGKIQVIVATVAFGMGIDKPNVRFVIHHSLPKSIENYYQESGRAGR 425
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 71987993 426 DG 427
Cdd:smart00490 81 AG 82
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
103-287 |
9.75e-23 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 96.41 E-value: 9.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 103 EQFHLEKFRPLQRAAINAVMSKE-DAVVILSTGGGKSLCYQLPALLA-----NGLALVVSPLISLVEDQILQLRSLGIDS 176
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 177 SSLNAN-TSKEEAKRVEDAITNKdsKFRLLYVTPEKLAKskkmmNKLEKSLSVGFLKLIAIDEVHCCSQWGhdFRTDYsf 255
Cdd:smart00487 82 GLKVVGlYGGDSKREQLRKLESG--KTDILVTTPGRLLD-----LLENDKLSLSNVDLVILDEAHRLLDGG--FGDQL-- 150
|
170 180 190
....*....|....*....|....*....|..
gi 71987993 256 LNVLKRQFKGVPILGLTATATSNVLDDVKDML 287
Cdd:smart00487 151 EKLLKLLPKNVQLLLLSATPPEEIENLLELFL 182
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
125-274 |
2.64e-19 |
|
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: 84.76 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 125 EDAVVILSTGGGKSLCYQLPALLAN----GLALVVSPLISLVEDQILQLRSLGIDSSSLNANTSKEEAKRVEDAITNKDs 200
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLLlkkgKKVLVLVPTKALALQTAERLRELFGPGIRVAVLVGGSSAEEREKNKLGDA- 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71987993 201 kfRLLYVTPEKLAKSKKMMNKLEKSLsvgfLKLIAIDEVHCCSQWGHDFRTDYsfLNVLKRQFKGVPILGLTAT 274
Cdd:cd00046 81 --DIIIATPDMLLNLLLREDRLFLKD----LKLIIVDEAHALLIDSRGALILD--LAVRKAGLKNAQVILLSAT 146
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
320-427 |
6.15e-19 |
|
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: 82.64 E-value: 6.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 320 EEIAKTIKRDFAGQTgIIYCLSRNDCEkVAKALKSHGIKAKHYHAYMEPVDRSGAHQGWISGKIQVIVATVAFGMGIDKP 399
Cdd:pfam00271 4 EALLELLKKERGGKV-LIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLP 81
|
90 100
....*....|....*....|....*...
gi 71987993 400 NVRFVIHHSLPKSIENYYQESGRAGRDG 427
Cdd:pfam00271 82 DVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
114-434 |
4.95e-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: 88.35 E-value: 4.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 114 QRAAINAVMSKEDAVVILSTGGGKSLCYQLPALLA-----NGLALVVSPLISLVEDQILQLRSL------GIDSSSLNAN 182
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAlledpGATALYLYPTKALARDQLRRLRELaealglGVRVATYDGD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 183 TSKEEAKRVEDA----ITNKD----------SKFRLLyvtpeklakskkmmnkLEKslsvgfLKLIAIDEVHCcsqwghd 248
Cdd:COG1205 141 TPPEERRWIREHpdivLTNPDmlhygllphhTRWARF----------------FRN------LRYVVIDEAHT------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 249 frtdYS------FLNVLKR------------QFkgvpILgltATATsnvLDDVKDMLgiqAALTfragfnrsNLKYKVVQ 310
Cdd:COG1205 192 ----YRgvfgshVANVLRRlrricrhygsdpQF----IL---ASAT---IGNPAEHA---ERLT--------GRPVTVVD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 311 KPGS-----------------------EDECTEEIAKTIKRDFagQTgIIYCLSRNDCEKVAKALKSHGIKAKH------ 361
Cdd:COG1205 247 EDGSprgertfvlwnpplvddgirrsaLAEAARLLADLVREGL--RT-LVFTRSRRGAELLARYARRALREPDLadrvaa 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71987993 362 YHAYMEPVDRSGAHQGWISGKIQVIVATVAFGMGIDKPNVRFVIHHSLPKSIENYYQESGRAGRDGQPATCIL 434
Cdd:COG1205 324 YRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVL 396
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
64-425 |
8.73e-18 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 87.00 E-value: 8.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 64 RQAIERKIELKTNEDSDVVTDRWDRDGFPWSDEATKILKEQFHLE-KFRPLQRAAINAVMS-----KEDAVVILSTGGGK 137
Cdd:COG1061 34 LVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSfELRPYQQEALEALLAalergGGRGLVVAPTGTGK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 138 SL----CYQlpALLANGLALVVSPLISLVEdqilQLRslgidssslnantskEEAKRVEDAITN----KDSKFRLLYVTP 209
Cdd:COG1061 114 TVlalaLAA--ELLRGKRVLVLVPRRELLE----QWA---------------EELRRFLGDPLAgggkKDSDAPITVATY 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 210 EKLAKsKKMMNKLEKSLSvgflkLIAIDEVHccsqwgHdFRTDySFLNVLKRqFKGVPILGLTAT--------ATSNVLD 281
Cdd:COG1061 173 QSLAR-RAHLDELGDRFG-----LVIIDEAH------H-AGAP-SYRRILEA-FPAAYRLGLTATpfrsdgreILLFLFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 282 DVKDMLGIQAAL-----------TFRAGFNRSNLKYKVVQKP-----GSEDECTEEIAKTIKRDFAGQT-GIIYCLSRND 344
Cdd:COG1061 238 GIVYEYSLKEAIedgylappeyyGIRVDLTDERAEYDALSERlrealAADAERKDKILRELLREHPDDRkTLVFCSSVDH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 345 CEKVAKALKSHGIKAKHYHAYMEPVDRSGAHQGWISGKIQVIVATVAFGMGIDKPNVRFVIHHSLPKSIENYYQesgRAG 424
Cdd:COG1061 318 AEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQ---RLG 394
|
.
gi 71987993 425 R 425
Cdd:COG1061 395 R 395
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
326-434 |
6.27e-16 |
|
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: 74.47 E-value: 6.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 326 IKRDFAGQTgIIYCLSRNDCEKVAKALKSHGIKAKHYHAYMEPVDRSGAHQGWISGKIQVIVAT-VAfGMGIDKPNVRFV 404
Cdd:cd18787 22 LEKLKPGKA-IIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATdVA-ARGLDIPGVDHV 99
|
90 100 110
....*....|....*....|....*....|
gi 71987993 405 IHHSLPKSIENYYQESGRAGRDGQPATCIL 434
Cdd:cd18787 100 INYDLPRDAEDYVHRIGRTGRAGRKGTAIT 129
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
336-434 |
7.94e-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: 69.21 E-value: 7.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 336 IIYCLSRNDCEKVAKALKSHGIKAKH-------YHAYMEPVDRSGAHQGWISGKIQVIVATVAFGMGIDKPNVRFVIHHS 408
Cdd:cd18797 39 IVFCRSRKLAELLLRYLKARLVEEGPlaskvasYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|....*.
gi 71987993 409 LPKSIENYYQESGRAGRDGQPATCIL 434
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDSLVIL 144
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
438-496 |
2.10e-12 |
|
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: 62.31 E-value: 2.10e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71987993 438 LADIFKQSSMVQQE-------RTGIQNLYNMVRYAADSSTCRRVKLAEHFEEAWEPSWCqKQCDTC 496
Cdd:pfam16124 1 YQDVVRLRFLIEQSeadeerkEVELQKLQAMVAYCENTTDCRRKQLLRYFGEEFDSEPC-GNCDNC 65
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
93-428 |
3.83e-12 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 69.15 E-value: 3.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 93 WSDEATKILKEQFhLEKFRPLQRAAINA-VMSKEDAVVILSTGGGKSLCYQLP---ALLANGLALVVSPLISLVeDQILQ 168
Cdd:COG1204 7 PLEKVIEFLKERG-IEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAELAilkALLNGGKALYIVPLRALA-SEKYR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 169 -----LRSLGIDSS-SLNANTSKEEAkrvedaITNKDskfrLLYVTPEKLA----KSKKMMNKLekslsvgflKLIAIDE 238
Cdd:COG1204 85 efkrdFEELGIKVGvSTGDYDSDDEW------LGRYD----ILVATPEKLDsllrNGPSWLRDV---------DLVVVDE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 239 VHccsQWGHDFR--TDYSFLNVLKRQFKGVPILGLTATAtSNVlDDVKDMLGiqAAL---TFRA-----GFnrsnLKYKV 308
Cdd:COG1204 146 AH---LIDDESRgpTLEVLLARLRRLNPEAQIVALSATI-GNA-EEIAEWLD--AELvksDWRPvplneGV----LYDGV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 309 VQKPGSEDECTEEIAKTIKRDFA--GQTgIIYCLSRNDCEKVAKALK--------------------------------- 353
Cdd:COG1204 215 LRFDDGSRRSKDPTLALALDLLEegGQV-LVFVSSRRDAESLAKKLAdelkrrltpeereeleelaeellevseethtne 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 354 ------SHGIkAKHyHAYMEPVDRSGAHQGWISGKIQVIVATVAFGMGIDKPnVRFVIHHSL------PKSIENYYQESG 421
Cdd:COG1204 294 kladclEKGV-AFH-HAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLP-ARRVIIRDTkrggmvPIPVLEFKQMAG 370
|
....*..
gi 71987993 422 RAGRDGQ 428
Cdd:COG1204 371 RAGRPGY 377
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
379-436 |
7.26e-12 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 61.18 E-value: 7.26e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 71987993 379 ISGKIQVIVATVAFGMGIDKPNVRFVIHHSLPKSIENYYQESGRAGRDGQ-PATCILYY 436
Cdd:cd18785 19 IASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKdEGEVILFV 77
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
328-441 |
2.07e-11 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 66.32 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 328 RDFAGQTGIIYCLSRNDCEKVAKALKSHGIKAKHYHAYMEPVDRSGAHQGWISGKIQVIVAT-VAfGMGIDKPNVRFVIH 406
Cdd:COG0513 237 RDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATdVA-ARGIDIDDVSHVIN 315
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 71987993 407 HSLPKSIENYYQESGRAGRDGQPATCIL------YYRLADI 441
Cdd:COG0513 316 YDLPEDPEDYVHRIGRTGRAGAEGTAISlvtpdeRRLLRAI 356
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
114-240 |
2.89e-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: 62.60 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 114 QRAAINAVMSKEDAVVILSTGGGKSLCYQLPALLA-----NGLALVVSPLISLVEDQILQLRSL------GIDSSSLNAN 182
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEAllrdpGSRALYLYPTKALAQDQLRSLRELleqlglGIRVATYDGD 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71987993 183 TSKEEAKRVEDA-----ITNKDSkfrLLY-VTPEKLAKSKKMMNklekslsvgfLKLIAIDEVH 240
Cdd:cd17923 85 TPREERRAIIRNpprilLTNPDM---LHYaLLPHHDRWARFLRN----------LRYVVLDEAH 135
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
314-427 |
3.65e-10 |
|
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: 58.72 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 314 SEDECTEEIAKTIKRDfaGQTgIIYCLSRNDCEKVAKALKshGIKAkhYHAYMEPVDRSGAHQGWISGKIQVIVATVAFG 393
Cdd:cd18795 28 DSDIIVLLKIETVSEG--KPV-LVFCSSRKECEKTAKDLA--GIAF--HHAGLTREDRELVEELFREGLIKVLVATSTLA 100
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 71987993 394 MGIDKPnVRFVIHHSLPK---------SIENYYQESGRAGRDG 427
Cdd:cd18795 101 AGVNLP-ARTVIIKGTQRydgkgyrelSPLEYLQMIGRAGRPG 142
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
336-458 |
4.47e-08 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 55.60 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 336 IIYCLSRNDCEKVAKALKSHGIKAKHYHAYMEPVDRSGAHQGWISGKIQVIVATVAFGMGIDKPNVRFVIHHSLPKSIEN 415
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 71987993 416 YYQESGRAGRDGQPATCILYYRLADIFKQSSMVQQERTGIQNL 458
Cdd:PTZ00424 351 YIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEM 393
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
335-435 |
8.80e-08 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 55.18 E-value: 8.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 335 GIIYCLSRNDCEKVAKAL-KSHGIKAKHYHAYMEPVDRSGAHQGWISGKIQVIVATVAFGMGIDKPNVRFVIHHSLPKSI 413
Cdd:PLN00206 370 AVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTI 449
|
90 100
....*....|....*....|..
gi 71987993 414 ENYYQESGRAGRDGQPATCILY 435
Cdd:PLN00206 450 KEYIHQIGRASRMGEKGTAIVF 471
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
109-274 |
6.88e-07 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 49.59 E-value: 6.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 109 KFRPLQRAAINAVMS-----KEDAVVILSTGGGKSLCY-QLPALLANGL----ALVVSPLISLVEDQILQLRSLGIDSSS 178
Cdd:pfam04851 3 ELRPYQIEAIENLLEsikngQKRGLIVMATGSGKTLTAaKLIARLFKKGpikkVLFLVPRKDLLEQALEEFKKFLPNYVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 179 LNANTSKEEAKRVEDAItnkdskfRLLYVTPEKLAKSkkmMNKLEKSLSVGFLKLIAIDEVHccsqwghdfRTDYSFLNV 258
Cdd:pfam04851 83 IGEIISGDKKDESVDDN-------KIVVTTIQSLYKA---LELASLELLPDFFDVIIIDEAH---------RSGASSYRN 143
|
170
....*....|....*.
gi 71987993 259 LKRQFKGVPILGLTAT 274
Cdd:pfam04851 144 ILEYFKPAFLLGLTAT 159
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
111-274 |
1.46e-06 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350790 [Multi-domain] Cd Length: 163 Bit Score: 48.71 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 111 RPLQRAAINAVM-----SKEDAVVILSTGGGK-----SLCYQLPALLANGLALVVSPLISLVEDQILQLRSLGIDSSSLN 180
Cdd:cd18032 2 RYYQQEAIEALEearekGQRRALLVMATGTGKtytaaFLIKRLLEANRKKRILFLAHREELLEQAERSFKEVLPDGSFGN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 181 ANTSKEeakrvedaitnKDSKFRLLYVTPEKLakskkMMNKLEKSLSVGFLKLIAIDEVHccsqwghdfRTDY-SFLNVL 259
Cdd:cd18032 82 LKGGKK-----------KPDDARVVFATVQTL-----NKRKRLEKFPPDYFDLIIIDEAH---------HAIAsSYRKIL 136
|
170
....*....|....*
gi 71987993 260 KrQFKGVPILGLTAT 274
Cdd:cd18032 137 E-YFEPAFLLGLTAT 150
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
110-296 |
4.05e-06 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 47.64 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 110 FRPLQRAAINAVMSKEDAVVILS-TGGGKSLCYQLPALLA----NGLALVVSPLISLVeDQILQ-----LRSLGIDSSSL 179
Cdd:cd17921 2 LNPIQREALRALYLSGDSVLVSApTSSGKTLIAELAILRAlatsGGKAVYIAPTRALV-NQKEAdlrerFGPLGKNVGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 180 NANTSkeeakrvEDAitNKDSKFRLLYVTPEKLAkskKMMNKLEkSLSVGFLKLIAIDEVHCCSQwGHDFRTDYSFLNVL 259
Cdd:cd17921 81 TGDPS-------VNK--LLLAEADILVATPEKLD---LLLRNGG-ERLIQDVRLVVVDEAHLIGD-GERGVVLELLLSRL 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 71987993 260 KRQFKGVPILGLTATATSnvLDDVKDMLGIQAALTFR 296
Cdd:cd17921 147 LRINKNARFVGLSATLPN--AEDLAEWLGVEDLIRFD 181
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
110-274 |
5.99e-06 |
|
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: 46.53 E-value: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 110 FRPLQRAAINAV---MSKEDAVVILSTGGGKSLC-YQLPALLANGLALVVSPLISLVE---DQILQLRSlgidSSSLNAN 182
Cdd:cd17926 1 LRPYQEEALEAWlahKNNRRGILVLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDqwkERFEDFLG----DSSIGLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 183 TSKEeakrvedaitNKDSKFRLLYV-TPEKLAKSkkmmNKLEKSLSVGFLKLIAiDEVHccsqwghdfRTDYSFLNVLKR 261
Cdd:cd17926 77 GGGK----------KKDFDDANVVVaTYQSLSNL----AEEEKDLFDQFGLLIV-DEAH---------HLPAKTFSEILK 132
|
170
....*....|...
gi 71987993 262 QFKGVPILGLTAT 274
Cdd:cd17926 133 ELNAKYRLGLTAT 145
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
331-430 |
1.55e-05 |
|
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: 45.33 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 331 AGQTGIIYCLSRNDCEKVAKALKShgikakhYHAYMEPVDRSGAHQGWIS-------------GKIQVIVATVAFGMGID 397
Cdd:cd18796 37 RHKSTLVFTNTRSQAERLAQRLRE-------LCPDRVPPDFIALHHGSLSrelreeveaalkrGDLKVVVATSSLELGID 109
|
90 100 110
....*....|....*....|....*....|...
gi 71987993 398 KPNVRFVIHHSLPKSIENYYQESGRAGRDGQPA 430
Cdd:cd18796 110 IGDVDLVIQIGSPKSVARLLQRLGRSGHRPGAA 142
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
125-240 |
3.30e-05 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 44.50 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 125 EDAVVILSTGGGKSLCYQLPALL------ANGLALV-VSPLISLVEDQ------ILQLRSLGIDSSSLNANTSKEEAKRv 191
Cdd:cd17922 2 RNVLIAAPTGSGKTEAAFLPALSsladepEKGVQVLyISPLKALINDQerrleePLDEIDLEIPVAVRHGDTSQSEKAK- 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 71987993 192 edAITNKDSkfrLLYVTPEKLAkskKMMN--KLEKSLSVgfLKLIAIDEVH 240
Cdd:cd17922 81 --QLKNPPG---ILITTPESLE---LLLVnkKLRELFAG--LRYVVVDEIH 121
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
336-427 |
3.93e-05 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 46.69 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 336 IIYCLSRNDCEKVAKALKSHGIKAKHYHAymepvDRSGAHQGWI-----SGKIQVIVATVAFGMGIDKPNVRFVIHHSLP 410
Cdd:PTZ00110 381 LIFVETKKGADFLTKELRLDGWPALCIHG-----DKKQEERTWVlnefkTGKSPIMIATDVASRGLDVKDVKYVINFDFP 455
|
90
....*....|....*..
gi 71987993 411 KSIENYYQESGRAGRDG 427
Cdd:PTZ00110 456 NQIEDYVHRIGRTGRAG 472
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
336-433 |
4.98e-05 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 46.06 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 336 IIYCLSRNDCEKVAKALKSHGIKAKHYHAYMEPVDRSGAHQGWISGKIQVIVATVAFGMGIDKPNVRFVIHHSLPKSIEN 415
Cdd:PRK01297 339 MVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDD 418
|
90
....*....|....*...
gi 71987993 416 YYQESGRAGRDGQPATCI 433
Cdd:PRK01297 419 YVHRIGRTGRAGASGVSI 436
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
104-299 |
1.27e-04 |
|
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.
Pssm-ID: 350784 [Multi-domain] Cd Length: 202 Bit Score: 43.36 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 104 QFHLEKFRPLQRAAINA--VMSKEDAVVILSTGGGKSLCYQ---LPALLANG-LALVVSPLISLVEDQILQLRSLGIDSS 177
Cdd:cd18026 11 KKGIKKLYDWQKECLSLpgLLEGRNLVYSLPTSGGKTLVAEilmLKRLLERRkKALFVLPYVSIVQEKVDALSPLFEELG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 178 slnantskeeaKRVED------AITNKDSKFRLLYV-TPEKlAKSkkMMNKLEKSLSVGFLKLIAIDEVHCCSQwGHDFR 250
Cdd:cd18026 91 -----------FRVEGyagnkgRSPPKRRKSLSVAVcTIEK-ANS--LVNSLIEEGRLDELGLVVVDELHMLGD-GHRGA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 71987993 251 TDYSFLN--VLKRQfKGVPILGLTATAtSNvLDDVKDMLgiQAALtFRAGF 299
Cdd:cd18026 156 LLELLLTklLYAAQ-KNIQIVGMSATL-PN-LEELASWL--RAEL-YTTNF 200
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
86-146 |
2.90e-04 |
|
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350711 [Multi-domain] Cd Length: 222 Bit Score: 42.75 E-value: 2.90e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71987993 86 WDRDGFPwsdEATKILKEQFHLEKFRPLQRAAINAVMSKEDAVVILSTGGGKSLCYQLPAL 146
Cdd:cd17953 14 WSQCGLS---EKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMF 71
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
336-435 |
4.51e-04 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 43.30 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 336 IIYCLSRNDCEKVAKALKSHGIKAKHYHAYMEPVDRSGAHQGWISGKIQVIVATVAFGMGIDKPNVRFVIHHSLPKSIEN 415
Cdd:PRK11634 249 IIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSES 328
|
90 100
....*....|....*....|
gi 71987993 416 YYQESGRAGRDGQPATCILY 435
Cdd:PRK11634 329 YVHRIGRTGRAGRAGRALLF 348
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
25-110 |
7.46e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.93 E-value: 7.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 25 SDVLLSKLSTELADLDGEIGQIDQQISQLRRKKSELTQKRQAIERKIELKTNEDSDVVTD-------RWDRDGFPWSDEA 97
Cdd:smart00787 195 EDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEiaeaekkLEQCRGFTFKEIE 274
|
90
....*....|....
gi 71987993 98 TkiLKEQFH-LEKF 110
Cdd:smart00787 275 K--LKEQLKlLQSL 286
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
359-437 |
8.46e-04 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 42.60 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 359 AKHYHAYMEPVDRSGAHQGWISGKIQVIVATVAFGMGIDKPNVRFVIHHSLPKSIENYYQESGRAGRD-GQPATCILYYR 437
Cdd:PRK09751 304 ARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGHQvGGVSKGLFFPR 383
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|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
363-436 |
2.18e-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: 39.25 E-value: 2.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71987993 363 HAYMEPVDRSGAHQGWISGKIQVIVATVAFGMGIDKPNVR-FVIHHSLPKSIENYYQESGRAGRDGQPATCILYY 436
Cdd:cd18811 68 HGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATvMVIEDAERFGLSQLHQLRGRVGRGDHQSYCLLVY 142
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|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
348-425 |
2.24e-03 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 40.95 E-value: 2.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71987993 348 VAKALKSHGIKAKHYHAYMEPVDRSGAHQGWISGKIQVIVATVAFGMGIDKPNVRFVIHHSLPKSIENYYQESGRAGR 425
Cdd:PRK10590 261 LAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGR 338
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
320-425 |
3.08e-03 |
|
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350185 [Multi-domain] Cd Length: 174 Bit Score: 38.82 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987993 320 EEIAKTIKRDFAGqtGIIYC---LSRNDCEKVAKALKSHGIKAKHYHAymepvDRSGAHQGWISGKIQVIVATVAF-GM- 394
Cdd:cd18798 14 EKLLELVKKLGDG--GLIFVsidYGKEYAEELKEFLERHGIKAELALS-----STEKNLEKFEEGEIDVLIGVASYyGVl 86
|
90 100 110
....*....|....*....|....*....|....
gi 71987993 395 --GIDKPN-VRFVIHHSLPksIENYYQESGRAGR 425
Cdd:cd18798 87 vrGIDLPErIKYAIFYGVP--VTTYIQASGRTSR 118
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
112-157 |
6.81e-03 |
|
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: 38.19 E-value: 6.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 71987993 112 PLQRAAINAVMSKEDAVVILSTGGGKSLCYQLPAL---LANGL-------ALVVSP 157
Cdd:cd00268 15 PIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILeklLPEPKkkgrgpqALVLAP 70
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
100-147 |
6.82e-03 |
|
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350716 [Multi-domain] Cd Length: 197 Bit Score: 38.21 E-value: 6.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 71987993 100 ILKEQFhlEKFRPLQRAAINAVMSKEDAVVILSTGGGKSLCYQLPALL 147
Cdd:cd17958 5 IKKQGF--EKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFI 50
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