|
Name |
Accession |
Description |
Interval |
E-value |
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
34-496 |
0e+00 |
|
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are known are 3'-5' DNA-DNA helicases. These proteins are used for recombination, recombinational repair, and possibly maintenance of chromosome stability. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129701 [Multi-domain] Cd Length: 470 Bit Score: 767.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 34 DILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISATM 113
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 114 LNASSSKEHVKWVHAEMvnKNSELKLIYVTPEKIAKSKMFMSRLEkayEARRFTRIAVDEVHCCSQWGHDFRPDYKALGI 193
Cdd:TIGR00614 81 LNSAQTKEQQLNVLTDL--KDGKIKLLYVTPEKISASNRLLQTLE---ERKGITLIAVDEAHCISQWGHDFRPDYKALGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 194 LKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFNRPNLYYEVRQKPSNtedFIEDIVKLINGRYKGQSGIIY 273
Cdd:TIGR00614 156 LKQKFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTPK---ILEDLLRFIRKEFEGKSGIIY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 274 CFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQ 353
Cdd:TIGR00614 233 CPSRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 354 ESGRAGRDDMKADCILYYGFGDIFRISSMVVMENVGQQ-----KLYEMVSYCQNISKCRRVLMAQHFDEVWN-----SEA 423
Cdd:TIGR00614 313 ESGRAGRDGLPSECHLFYAPADMNRLRRLLMEEPDGNFrtyklKLYEMMEYCLNSSTCRRLILLSYFGEKGFnksfcIMG 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 282403582 424 CNKMCDNCCKDSAFERKNITEYCRDLIKILKQAEE----LNEKLTPLKLIDSWMGKGAAKLRVAGVVAPTL-PREDLE 496
Cdd:TIGR00614 393 TEKCCDNCCKRLDYKTKDVTDKVYDFGPQAQKALSavgrLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLyGRGKDE 470
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
31-481 |
2.05e-173 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 500.44 E-value: 2.05e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 31 KVKDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGIS 110
Cdd:COG0514 4 DALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 111 ATMLNASSSKEHVKWVHAEMvnKNSELKLIYVTPEKIAKSKmFMSRLEKAyearRFTRIAVDEVHCCSQWGHDFRPDYKA 190
Cdd:COG0514 84 AAFLNSSLSAEERREVLRAL--RAGELKLLYVAPERLLNPR-FLELLRRL----KISLFAIDEAHCISQWGHDFRPDYRR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 191 LGILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFNRPNLYYEVRQKPSntEDFIEDIVKLINGRyKGQSG 270
Cdd:COG0514 157 LGELRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPP--DDKLAQLLDFLKEH-PGGSG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 271 IIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMEN 350
Cdd:COG0514 234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 351 YYQESGRAGRDDMKADCILYYGFGDIFRISSMVVMEN-------VGQQKLYEMVSYCQnISKCRRVLMAQHFDEVwNSEA 423
Cdd:COG0514 314 YYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPpdeerkrVERAKLDAMLAYAE-TTGCRRQFLLRYFGEE-LAEP 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 282403582 424 CNKmCDNCCKDSafERKNITEYCRdliKILKQAEELNEKLTPLKLIDSWMGKGAAKLR 481
Cdd:COG0514 392 CGN-CDNCLGPP--ETFDGTEAAQ---KALSCVYRTGQRFGAGHVIDVLRGSKNEKIR 443
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
27-235 |
1.30e-155 |
|
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: 444.50 E-value: 1.30e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 27 PWSGKVKDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQ 106
Cdd:cd18015 1 PWSGKVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 107 LGISATMLNASSSKEHVKWVHAEMVNKNSELKLIYVTPEKIAKSKMFMSRLEKAYEARRFTRIAVDEVHCCSQWGHDFRP 186
Cdd:cd18015 81 LGISATMLNASSSKEHVKWVHAALTDKNSELKLLYVTPEKIAKSKRFMSKLEKAYNAGRLARIAIDEVHCCSQWGHDFRP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 282403582 187 DYKALGILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFN 235
Cdd:cd18015 161 DYKKLGILKRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
16-458 |
2.94e-153 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 470.92 E-value: 2.94e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 16 SSPAAWNKEDFPWSGKVKDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLIS 95
Cdd:PLN03137 432 SNDKKWSSRNFPWTKKLEVNNKKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVS 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 96 LMEDQLMVLKQLGISATMLNASSSKEHVKWVHAEMVNKNSELKLIYVTPEKIAKSKMFMSRLEKAYEARRFTRIAVDEVH 175
Cdd:PLN03137 512 LIQDQIMNLLQANIPAASLSAGMEWAEQLEILQELSSEYSKYKLLYVTPEKVAKSDSLLRHLENLNSRGLLARFVIDEAH 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 176 CCSQWGHDFRPDYKALGILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFNRPNLYYEVRQKpsnTEDFIE 255
Cdd:PLN03137 592 CVSQWGHDFRPDYQGLGILKQKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPK---TKKCLE 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 256 DIVKLINGRYKGQSGIIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPD 335
Cdd:PLN03137 669 DIDKFIKENHFDECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPD 748
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 336 VRFVIHHSMSKSMENYYQESGRAGRDDMKADCILYYGFGDIFRISSMVVMENVGQ---------------------QKLY 394
Cdd:PLN03137 749 VRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMISQGGVEQspmamgynrmassgriletntENLL 828
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 282403582 395 EMVSYCQNISKCRRVLMAQHFDEVWNSEACNKMCDNCCKDSAFERKNITEYCRDLIKILKQAEE 458
Cdd:PLN03137 829 RMVSYCENEVDCRRFLQLVHFGEKFDSTNCKKTCDNCSSSKSLIDKDVTEIARQLVELVKLTGE 892
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
33-431 |
3.02e-131 |
|
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: 396.37 E-value: 3.02e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 33 KDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISAT 112
Cdd:TIGR01389 2 QQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 113 MLNASSSKEHVKwvHAEMVNKNSELKLIYVTPEkiakskmfmsRLEKAYEARRFTR-----IAVDEVHCCSQWGHDFRPD 187
Cdd:TIGR01389 82 YLNSTLSAKEQQ--DIEKALVNGELKLLYVAPE----------RLEQDYFLNMLQRipialVAVDEAHCVSQWGHDFRPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 188 YKALGILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFNRPNLYYEVRQKpSNTEDFIEDIVKlingRYKG 267
Cdd:TIGR01389 150 YQRLGSLAERFPQVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKK-NNKQKFLLDYLK----KHRG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 268 QSGIIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKS 347
Cdd:TIGR01389 225 QSGIIYASSRKKVEELAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 348 MENYYQESGRAGRDDMKADCILYYGFGDI----FRISSMVVMENVGQ---QKLYEMVSYCqNISKCRRVLMAQHFDEVwN 420
Cdd:TIGR01389 305 LESYYQEAGRAGRDGLPAEAILLYSPADIallkRRIEQSEADDDYKQierEKLRAMIAYC-ETQTCRRAYILRYFGEN-E 382
|
410
....*....|.
gi 282403582 421 SEACNKmCDNC 431
Cdd:TIGR01389 383 VEPCGN-CDNC 392
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
33-431 |
4.00e-117 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 360.57 E-value: 4.00e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 33 KDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISAT 112
Cdd:PRK11057 14 KQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 113 MLNASSSKEHVKWVHAEMvnKNSELKLIYVTPEKIAKSKmFMSRLEKAyearRFTRIAVDEVHCCSQWGHDFRPDYKALG 192
Cdd:PRK11057 94 CLNSTQTREQQLEVMAGC--RTGQIKLLYIAPERLMMDN-FLEHLAHW----NPALLAVDEAHCISQWGHDFRPEYAALG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 193 ILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFNRPNLYYEV--RQKPsntedfIEDIVKLINGRyKGQSG 270
Cdd:PRK11057 167 QLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLveKFKP------LDQLMRYVQEQ-RGKSG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 271 IIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMEN 350
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 351 YYQESGRAGRDDMKADCILYYGFGDIFRISSMVVMENVGQQ------KLYEMVSYCQnISKCRRVLMAQHFDEvWNSEAC 424
Cdd:PRK11057 320 YYQETGRAGRDGLPAEAMLFYDPADMAWLRRCLEEKPAGQQqdierhKLNAMGAFAE-AQTCRRLVLLNYFGE-GRQEPC 397
|
....*..
gi 282403582 425 NKmCDNC 431
Cdd:PRK11057 398 GN-CDIC 403
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
33-235 |
2.04e-96 |
|
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: 292.90 E-value: 2.04e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 33 KDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISAT 112
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 113 MLNASSSKEHVKWVHAEMvnKNSELKLIYVTPEKIAkSKMFMSRLEKAYEARRFTRIAVDEVHCCSQWGHDFRPDYKALG 192
Cdd:cd17920 81 ALNSTLSPEEKREVLLRI--KNGQYKLLYVTPERLL-SPDFLELLQRLPERKRLALIVVDEAHCVSQWGHDFRPDYLRLG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 282403582 193 ILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFN 235
Cdd:cd17920 158 RLRRALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
236-371 |
5.77e-74 |
|
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: 232.10 E-value: 5.77e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 236 RPNLYYEVRQKPSNTEDFieDIVKLINGRYKGQSGIIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSA 315
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKL--DLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 282403582 316 NEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGRDDMKADCILYY 371
Cdd:cd18794 79 DKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
29-235 |
1.24e-72 |
|
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: 231.64 E-value: 1.24e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 29 SGKVKDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLG 108
Cdd:cd18016 2 SKEMMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 109 ISATMLNASSSKEHVKWVHAEMVNKNSELKLIYVTPEKIAKSKMFMSRLEKAYEARRFTRIAVDEVHCCSQWGHDFRPDY 188
Cdd:cd18016 82 IPATYLTGDKTDAEATKIYLQLSKKDPIIKLLYVTPEKISASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRPDY 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 282403582 189 KALGILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFN 235
Cdd:cd18016 162 KRLNMLRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
35-235 |
1.50e-52 |
|
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: 178.60 E-value: 1.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 35 ILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALC----SDGFTLVICPLISLMEDQLMVLKQLgIS 110
Cdd:cd18018 3 LLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLlrrrGPGLTLVVSPLIALMKDQVDALPRA-IK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 111 ATMLNaSSSKEHVKWVHAEMVNKNsELKLIYVTPEKIAkSKMFMSRLEkayEARRFTRIAVDEVHCCSQWGHDFRPDYKA 190
Cdd:cd18018 82 AAALN-SSLTREERRRILEKLRAG-EVKILYVSPERLV-NESFRELLR---QTPPISLLVVDEAHCISEWSHNFRPDYLR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 282403582 191 LGILKRQFPNA-SLIGLTATATNHVLTDAQKILCIEKCFTFTASFN 235
Cdd:cd18018 156 LCRVLRELLGApPVLALTATATKRVVEDIASHLGIPESGVVRGPLY 201
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
34-235 |
1.07e-51 |
|
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: 175.73 E-value: 1.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 34 DILQNVFKLEKFRPLQLETI-NVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISAT 112
Cdd:cd18017 2 NALNEYFGHSSFRPVQWKVIrSVLEERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPAC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 113 MLNASSSKEHVKwvhaemVNKNSELKLIYVTPEKIAKSKMFMSRLEKayearRFTRIAVDEVHCCSQWGHDFRPDYKALG 192
Cdd:cd18017 82 FLGSAQSQNVLD------DIKMGKIRVIYVTPEFVSKGLELLQQLRN-----GITLIAIDEAHCVSQWGHDFRSSYRHLG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 282403582 193 ILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFN 235
Cdd:cd18017 151 SIRNRLPNVPIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
33-233 |
1.16e-48 |
|
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: 168.03 E-value: 1.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 33 KDILQNVFKLEKFR-PLQLETINVTMAGK-EVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGIS 110
Cdd:cd18014 1 RSTLKKVFGHSDFKsPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 111 ATMLNASSSKEHVKWVHAEMVNKNSELKLIYVTPEKiAKSKMFMSRLEKAYEARRFTRIAVDEVHCCSQWGHDFRPDYKA 190
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADLESEKPQTKFLYITPEM-AATSSFQPLLSSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 282403582 191 LGILKRQFPNASLIGLTATATNHVLTDAQKILCIEK-CFTFTAS 233
Cdd:cd18014 160 LGALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKpVAIFKTP 203
|
|
| DpdF |
NF041063 |
protein DpdF; |
58-376 |
1.65e-39 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 154.68 E-value: 1.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 58 AGKEVFLVMPTGGGKSLCYQLPALCS---DGFTLVICPLISL---MEDQLM-VLKQLGISATMLNA---SSSKEhvkwVH 127
Cdd:NF041063 157 PGSTLIVNLPTGSGKSLVAQAPALLAsrqGGLTLVVVPTVALaidQERRAReLLRRAGPDLGGPLAwhgGLSAE----ER 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 128 AEMVN--KNSELKLIYVTPEKIAKSkmFMSRLEKAYEARRFTRIAVDEVHCCSQWGHDFRPDYKALGILKRQFPNASLIG 205
Cdd:NF041063 233 AAIRQriRDGTQRILFTSPESLTGS--LRPALFDAAEAGLLRYLVVDEAHLVDQWGDGFRPEFQLLAGLRRSLLRLAPSG 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 206 -------LTATATNHVLTDAQKILCIEKCFT-FTASFNRPNLYYEVRQKPSnTEDFIEDIVKLIngRYKGQSGIIYCFSQ 277
Cdd:NF041063 311 rpfrtllLSATLTESTLDTLETLFGPPGPFIvVSAVQLRPEPAYWVAKCDS-EEERRERVLEAL--RHLPRPLILYVTKV 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 278 KDSEQVTVSLQNLGIH-AGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESG 356
Cdd:NF041063 388 EDAEAWLQRLRAAGFRrVALFHGDTPDAERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVG 467
|
330 340
....*....|....*....|
gi 282403582 357 RAGRDDMKADCILYYGFGDI 376
Cdd:NF041063 468 RGGRDGKASLSLLIYTPDDL 487
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
59-209 |
7.61e-32 |
|
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: 120.20 E-value: 7.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 59 GKEVFLVMPTGGGKSLCYQLPALCSD----GFTLVICPLISLMEDQLMVLKQL---GISATMLNASSSKEHVKwvhaemV 131
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLlkkgKKVLVLVPTKALALQTAERLRELfgpGIRVAVLVGGSSAEERE------K 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 282403582 132 NKNSELKLIYVTPEKIAKSKMFMSRLEKayeaRRFTRIAVDEVHCCSQWGHDFRPDYkaLGILKRQFPNASLIGLTAT 209
Cdd:cd00046 75 NKLGDADIIIATPDMLLNLLLREDRLFL----KDLKLIIVDEAHALLIDSRGALILD--LAVRKAGLKNAQVILLSAT 146
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
46-211 |
2.25e-27 |
|
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: 108.10 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 46 RPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPAL------CSDGFTLVICPLISLMEDQLMVLKQLGISATMLNASSS 119
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 120 KEHVKWvhaEMVNKNSELKLIYVTPEKIAKskmfMSRLEKAYEARRFtrIAVDEVHCCSQWGhdFRPDYKAlgILKRQFP 199
Cdd:pfam00270 81 GGDSRK---EQLEKLKGPDILVGTPGRLLD----LLQERKLLKNLKL--LVLDEAHRLLDMG--FGPDLEE--ILRRLPK 147
|
170
....*....|..
gi 282403582 200 NASLIGLTATAT 211
Cdd:pfam00270 148 KRQILLLSATLP 159
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
40-244 |
1.72e-23 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 98.33 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 40 FKLEKFRPLQLETINVTMAG-KEVFLVMPTGGGKSLCYQLPALC-----SDGFTLVICPLISLMEDQLMVLKQLGISATM 113
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEalkrgKGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 114 LNASSSKEHVKWVHAEMVNKNsELKLIYVTPEkiakskMFMSRLEKAY-EARRFTRIAVDEVHCCSQWGhdFRPDYKalG 192
Cdd:smart00487 84 KVVGLYGGDSKREQLRKLESG-KTDILVTTPG------RLLDLLENDKlSLSNVDLVILDEAHRLLDGG--FGDQLE--K 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 282403582 193 ILKRQFPNASLIGLTATATNHVLTDAQKILciEKCFTFTASFnRPNLYYEVR 244
Cdd:smart00487 153 LLKLLPKNVQLLLLSATPPEEIENLLELFL--NDPVFIDVGF-TPLEPIEQF 201
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
281-361 |
5.84e-22 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 89.96 E-value: 5.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 281 EQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGR 360
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
.
gi 282403582 361 D 361
Cdd:smart00490 81 A 81
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
254-360 |
4.93e-20 |
|
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: 85.34 E-value: 4.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 254 IEDIVKLINGRYKGQSgIIYCFSQKDSEqVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDK 333
Cdd:pfam00271 3 LEALLELLKKERGGKV-LIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*..
gi 282403582 334 PDVRFVIHHSMSKSMENYYQESGRAGR 360
Cdd:pfam00271 81 PDVDLVINYDLPWNPASYIQRIGRAGR 107
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
373-432 |
5.79e-16 |
|
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: 72.32 E-value: 5.79e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 282403582 373 FGDIFRISSMVVMEN-------VGQQKLYEMVSYCQNISKCRRVLMAQHFDEVWNSEACnKMCDNCC 432
Cdd:pfam16124 1 YQDVVRLRFLIEQSEadeerkeVELQKLQAMVAYCENTTDCRRKQLLRYFGEEFDSEPC-GNCDNCL 66
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
64-370 |
5.12e-15 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 78.14 E-value: 5.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 64 LVMPTGGGKSL----CYQlpALCSDGFTLVICPLISLMEdQLM--VLKQLGISATMLNASSSKEHVkwvhaemvnknsel 137
Cdd:COG1061 105 VVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLE-QWAeeLRRFLGDPLAGGGKKDSDAPI-------------- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 138 klIYVTPEKIAKSKMFmSRLEkayeaRRFTRIAVDEVHccsqwgHDFRPDYKAlgILKRqFPNASLIGLTAT----ATNH 213
Cdd:COG1061 168 --TVATYQSLARRAHL-DELG-----DRFGLVIIDEAH------HAGAPSYRR--ILEA-FPAAYRLGLTATpfrsDGRE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 214 VLTD---------------AQKILCIEKCFTFTASFNRPNLYYEVRQKP------SNTEDFIEDIVKLINGRYKGQSGII 272
Cdd:COG1061 231 ILLFlfdgivyeyslkeaiEDGYLAPPEYYGIRVDLTDERAEYDALSERlrealaADAERKDKILRELLREHPDDRKTLV 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 273 YCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYY 352
Cdd:COG1061 311 FCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFI 390
|
330 340
....*....|....*....|..
gi 282403582 353 QesgRAGR----DDMKADCILY 370
Cdd:COG1061 391 Q---RLGRglrpAPGKEDALVY 409
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
315-371 |
6.91e-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: 6.91e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 282403582 315 ANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGRD-DMKADCILYY 371
Cdd:cd18785 20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGgKDEGEVILFV 77
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
49-360 |
1.42e-11 |
|
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: 67.55 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 49 QLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCS-----DGFTLVICPLISLMEDQLMVLKQL------GISATMLNAS 117
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAlledpGATALYLYPTKALARDQLRRLRELaealglGVRVATYDGD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 118 SSKEHVKWV--HAEmvnknselkLIYVTPEKI--------AKSKMFMSRLekayearRFtrIAVDEVHCcsqwghdfrpd 187
Cdd:COG1205 141 TPPEERRWIreHPD---------IVLTNPDMLhygllphhTRWARFFRNL-------RY--VVIDEAHT----------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 188 YK-ALG-----ILKR------------QFpnaslIGLTATATN---HV--LTDaQKILCIEKCF------TFtaSFNRPN 238
Cdd:COG1205 192 YRgVFGshvanVLRRlrricrhygsdpQF-----ILASATIGNpaeHAerLTG-RPVTVVDEDGsprgerTF--VLWNPP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 239 LYYEVRQKPSNTE--DFIEDIVKlingryKGQSGIIYCFSQKDSEQVTVSLQN------LGIHAGAYHANLEPEDKTTVH 310
Cdd:COG1205 264 LVDDGIRRSALAEaaRLLADLVR------EGLRTLVFTRSRRGAELLARYARRalrepdLADRVAAYRAGYLPEERREIE 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 282403582 311 RKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGR 360
Cdd:COG1205 338 RGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGR 387
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
239-360 |
1.72e-11 |
|
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: 61.75 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 239 LYYEVrqkpsNTEDFIEDIVKLINGRYKGQSGIIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEI 318
Cdd:cd18787 4 LYVVV-----EEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKV 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 282403582 319 QVVVAT-VAfGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGR 360
Cdd:cd18787 79 RVLVATdVA-ARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGR 120
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
240-370 |
3.69e-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: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 240 YYEVRQKPSNTEDFIEDIVKLINGRYKGQSgIIYCFSQKDSEQVTVSLQNLGIHagayHANLEPEDKTTVHRKWSANEIQ 319
Cdd:cd18795 17 IKLRVDVMNKFDSDIIVLLKIETVSEGKPV-LVFCSSRKECEKTAKDLAGIAFH----HAGLTREDRELVEELFREGLIK 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 282403582 320 VVVATVAFGMGIDKPdVRFVIHHSMSK---------SMENYYQESGRAGR---DDmKADCILY 370
Cdd:cd18795 92 VLVATSTLAAGVNLP-ARTVIIKGTQRydgkgyrelSPLEYLQMIGRAGRpgfDT-RGEAIIM 152
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
240-360 |
4.88e-10 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 61.70 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 240 YYEVRQKpsnteDFIEDIVKLINgRYKGQSGIIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQ 319
Cdd:COG0513 220 YYLVDKR-----DKLELLRRLLR-DEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIR 293
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 282403582 320 VVVAT-VAfGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGR 360
Cdd:COG0513 294 VLVATdVA-ARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGR 334
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
194-363 |
1.19e-09 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 61.45 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 194 LKRQFPNASLIGLTATATN-HVLtdAQKILC-----------IEKCFTFTASFNRPNLYYE-VRQKPSNTEDFiedivkl 260
Cdd:COG1202 354 LKYYCPGAQWIYLSATVGNpEEL--AKKLGAklveyeerpvpLERHLTFADGREKIRIINKlVKREFDTKSSK------- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 261 inGrYKGQSgIIYCFSQKDSEQVTvslQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRfVI 340
Cdd:COG1202 425 --G-YRGQT-IIFTNSRRRCHEIA---RALGYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQ-VI 496
|
170 180
....*....|....*....|....*...
gi 282403582 341 HHS--MSK---SMENYYQESGRAGRDDM 363
Cdd:COG1202 497 FDSlaMGIewlSVQEFHQMLGRAGRPDY 524
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
271-365 |
1.79e-09 |
|
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: 56.50 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 271 IIYCFSQKDSEQVTVSLQNLGIHAG-------AYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHS 343
Cdd:cd18797 39 IVFCRSRKLAELLLRYLKARLVEEGplaskvaSYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|..
gi 282403582 344 MSKSMENYYQESGRAGRDDMKA 365
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDS 140
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
28-360 |
1.78e-07 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 54.13 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 28 WSGKVKDILQNvFKLEKFRPLQLETI-NVTMAGKEVFLVMPTGGGKSLCYQLP---ALCSDGFTLVICPLISL---MEDQ 100
Cdd:COG1204 7 PLEKVIEFLKE-RGIEELYPPQAEALeAGLLEGKNLVVSAPTASGKTLIAELAilkALLNGGKALYIVPLRALaseKYRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 101 LM-VLKQLGISATMlnasSSKEHVkwVHAEMVNKNSelklIYV-TPEKiakskmFMSRLEKAYE-ARRFTRIAVDEVHcc 177
Cdd:COG1204 86 FKrDFEELGIKVGV----STGDYD--SDDEWLGRYD----ILVaTPEK------LDSLLRNGPSwLRDVDLVVVDEAH-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 178 sQWGHDFR-PDYK-ALGILKRQFPNASLIGLTATATNhvltdAQKILCIEKCFTFTASFnRPN-----LYY----EVRQK 246
Cdd:COG1204 148 -LIDDESRgPTLEvLLARLRRLNPEAQIVALSATIGN-----AEEIAEWLDAELVKSDW-RPVplnegVLYdgvlRFDDG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 247 PSNTEDFIEDIV-KLINGRykGQSgIIYCFSQKDSEQ-----------------------VTVSLQNLGIHAG------- 295
Cdd:COG1204 221 SRRSKDPTLALAlDLLEEG--GQV-LVFVSSRRDAESlakkladelkrrltpeereeleeLAEELLEVSEETHtneklad 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 282403582 296 ------AYH-ANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMEN-----YYQESGRAGR 360
Cdd:COG1204 298 clekgvAFHhAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDTKRGGMVPipvleFKQMAGRAGR 374
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
271-360 |
6.22e-07 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 52.14 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 271 IIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMEN 350
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90
....*....|
gi 282403582 351 YYQESGRAGR 360
Cdd:PTZ00424 351 YIHRIGRSGR 360
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
49-175 |
1.95e-06 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 48.35 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 49 QLETINVTMAGKEVFLVMPTGGGKSLCYQLP---ALCSDGFT--LVICPLISLMEDQLMVLKQL------GISATMLNAS 117
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPileALLRDPGSraLYLYPTKALAQDQLRSLRELleqlglGIRVATYDGD 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 282403582 118 SSKEHVKWVHAEMVNknselkLIYVTPEKI--------AKSKMFMSRLekayearRFtrIAVDEVH 175
Cdd:cd17923 85 TPREERRAIIRNPPR------ILLTNPDMLhyallphhDRWARFLRNL-------RY--VVLDEAH 135
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
44-209 |
3.96e-06 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 47.28 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 44 KFRPLQLETINVTMAG-----KEVFLVMPTGGGKSLCY-QLPALCSDGF----TLVICPLISLMEDQLMVLKQLGISATM 113
Cdd:pfam04851 3 ELRPYQIEAIENLLESikngqKRGLIVMATGSGKTLTAaKLIARLFKKGpikkVLFLVPRKDLLEQALEEFKKFLPNYVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 114 LNASSSKEhvkwvhaEMVNKNSELKLIYVTPEKIAKSKMfMSRLEKAYEARRFtrIAVDEVHccsqwgHDFRPDYKAlgi 193
Cdd:pfam04851 83 IGEIISGD-------KKDESVDDNKIVVTTIQSLYKALE-LASLELLPDFFDV--IIIDEAH------RSGASSYRN--- 143
|
170
....*....|....*.
gi 282403582 194 LKRQFPNASLIGLTAT 209
Cdd:pfam04851 144 ILEYFKPAFLLGLTAT 159
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
47-364 |
5.04e-06 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 49.39 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 47 PLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALC----------SDG-FTLVICPLISLMEDqlmvlkqlgISATMLN 115
Cdd:PTZ00110 155 PIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVhinaqpllryGDGpIVLVLAPTRELAEQ---------IREQCNK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 116 -ASSSKEHVKWVHAEMVNKNSELKLIYVTPEKIAKSKMFMSRLEKAY-EARRFTRIAVDEVHCCSQWGhdFRPDYKAlgI 193
Cdd:PTZ00110 226 fGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVtNLRRVTYLVLDEADRMLDMG--FEPQIRK--I 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 194 LKRQFPNASLIGLTATATNHVLTDAQKiLCIEK-------CFTFTASFN-RPNLY-YEVRQKPSNTEDFIEDIVKlingr 264
Cdd:PTZ00110 302 VSQIRPDRQTLMWSATWPKEVQSLARD-LCKEEpvhvnvgSLDLTACHNiKQEVFvVEEHEKRGKLKMLLQRIMR----- 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 265 yKGQSGIIYCFSQKDSEQVTVSLQNLGIHAGAYHAnlepeDKTTVHRKWSANEIQ-----VVVATVAFGMGIDKPDVRFV 339
Cdd:PTZ00110 376 -DGDKILIFVETKKGADFLTKELRLDGWPALCIHG-----DKKQEERTWVLNEFKtgkspIMIATDVASRGLDVKDVKYV 449
|
330 340
....*....|....*....|....*
gi 282403582 340 IHHSMSKSMENYYQESGRAGRDDMK 364
Cdd:PTZ00110 450 INFDFPNQIEDYVHRIGRTGRAGAK 474
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
437-543 |
2.91e-05 |
|
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix structure. The RQC domain, found only in RecQ family enzymes, is a high affinity G4 DNA binding domain.
Pssm-ID: 462780 [Multi-domain] Cd Length: 108 Bit Score: 43.30 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 437 FERKNITEYCRDLIKILKqaeELNEKLTPLKLIDSWMGKGAAKLR--------VAGVVAPtLPREDLEKIIAHFLIQQYL 508
Cdd:pfam09382 2 PETVDVTEEAQKILSCVY---RTGQRFGAGHLIDVLRGSKNKKIRqlghdklsTFGIGKD-LSKKEWRRIIRQLIAEGYL 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 282403582 509 KEDYSFTayatiSYLKIGPKA-NLLNNEAHaITMQV 543
Cdd:pfam09382 78 EVDIEFY-----SVLKLTPKArEVLKGEEK-VMLRV 107
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
45-212 |
4.52e-05 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 44.56 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 45 FRPLQLETINVTM-AGKEVFLVMPTGGGKSLCYQLPAL----CSDGFTLVICPLISLMEDQLM----VLKQLGISATMLN 115
Cdd:cd17921 2 LNPIQREALRALYlSGDSVLVSAPTSSGKTLIAELAILralaTSGGKAVYIAPTRALVNQKEAdlreRFGPLGKNVGLLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 116 ASSSkehvkwvhaemVNKNSELKL-IYV-TPEKIAkskmFMSRLEKAYEARRFTRIAVDEVHCCSQwghdfrPDYKA--- 190
Cdd:cd17921 82 GDPS-----------VNKLLLAEAdILVaTPEKLD----LLLRNGGERLIQDVRLVVVDEAHLIGD------GERGVvle 140
|
170 180
....*....|....*....|....
gi 282403582 191 --LGILKRQFPNASLIGLTATATN 212
Cdd:cd17921 141 llLSRLLRINKNARFVGLSATLPN 164
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
45-209 |
7.07e-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: 43.06 E-value: 7.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 45 FRPLQLETINVtMAGKEVF----LVMPTGGGKSLC-YQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISATMLNASSS 119
Cdd:cd17926 1 LRPYQEEALEA-WLAHKNNrrgiLVLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFEDFLGDSSIGLIGGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 120 KehvkwvhaemvNKNSELKLIYV-TPEKIakskmfmSRLEKAYEA--RRFTRIAVDEVH--CCSQWGHdfrpdykalgIL 194
Cdd:cd17926 80 K-----------KKDFDDANVVVaTYQSL-------SNLAEEEKDlfDQFGLLIVDEAHhlPAKTFSE----------IL 131
|
170
....*....|....*
gi 282403582 195 KRqFPNASLIGLTAT 209
Cdd:cd17926 132 KE-LNAKYRLGLTAT 145
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
298-398 |
8.18e-05 |
|
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: 43.10 E-value: 8.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 298 HANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVR-FVIHHSMSKSMENYYQESGRAGRDDMKADCILYYGfgdi 376
Cdd:cd18811 68 HGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATvMVIEDAERFGLSQLHQLRGRVGRGDHQSYCLLVYK---- 143
|
90 100
....*....|....*....|..
gi 282403582 377 frissmVVMENVGQQKLYEMVS 398
Cdd:cd18811 144 ------DPLTETAKQRLRVMTE 159
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
291-360 |
1.59e-04 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 44.54 E-value: 1.59e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 282403582 291 GIhaGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPdVRFVIHHSMSK----SMEN-----YYQESGRAGR 360
Cdd:COG4581 301 GI--AVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMP-ARTVVFTKLSKfdgeRHRPltareFHQIAGRAGR 376
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
62-324 |
2.85e-04 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 43.92 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 62 VFLVMPTGGGK---SLCY---QLPALCSDGFTLVIcPLISLMEDQLMVLKQLG---I----SATMLNASSSKEHVKWVHA 128
Cdd:COG1203 150 FILTAPTGGGKteaALLFalrLAAKHGGRRIIYAL-PFTSIINQTYDRLRDLFgedVllhhSLADLDLLEEEEEYESEAR 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 129 EMVNkNSEL---KLIYVTPEKIAKSkMFMSRleKAYEaRRFTRIA-----VDEVHCCSQwgHDFRPDYKALGILKRQfpN 200
Cdd:COG1203 229 WLKL-LKELwdaPVVVTTIDQLFES-LFSNR--KGQE-RRLHNLAnsviiLDEVQAYPP--YMLALLLRLLEWLKNL--G 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 201 ASLIGLTAT---ATNHVLTDAQKILCIEKC--FTFTASFNRPNlyYEVRQKPSNTEDFIEDIVKLINgryKGQSGIIYCF 275
Cdd:COG1203 300 GSVILMTATlppLLREELLEAYELIPDEPEelPEYFRAFVRKR--VELKEGPLSDEELAELILEALH---KGKSVLVIVN 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 282403582 276 SQKDSEQVTVSLQNLGIHAGAY--HANLEPEDKTTVHRKW----SANEIQVVVAT 324
Cdd:COG1203 375 TVKDAQELYEALKEKLPDEEVYllHSRFCPADRSEIEKEIkerlERGKPCILVST 429
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
32-92 |
1.00e-03 |
|
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 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: 350707 [Multi-domain] Cd Length: 214 Bit Score: 40.65 E-value: 1.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 282403582 32 VKDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALC-----------SDG-FTLVICP 92
Cdd:cd17949 1 LVSHLKSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQrllsleprvdrSDGtLALVLVP 73
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
280-370 |
2.01e-03 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 40.93 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 280 SEQVTVSLqnlGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAG 359
Cdd:PLN00206 384 ANAITVVT---GLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRAS 460
|
90
....*....|.
gi 282403582 360 RDDMKADCILY 370
Cdd:PLN00206 461 RMGEKGTAIVF 471
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
59-212 |
3.14e-03 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 38.85 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 59 GKEVFLVMPTGGGKSLCYQL---PALCSDGFTLVICPLISLMEDQLMVLKQL-------GISATMLNassskEHVKWVHa 128
Cdd:cd18028 17 GENLLISIPTASGKTLIAEMamvNTLLEGGKALYLVPLRALASEKYEEFKKLeeiglkvGISTGDYD-----EDDEWLG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 129 emvnknsELKLIYVTPEKIAkskmFMSRLEKAYeARRFTRIAVDEVHCCSqwghdfrpDYK-------ALGILKRQFPNA 201
Cdd:cd18028 91 -------DYDIIVATYEKFD----SLLRHSPSW-LRDVGVVVVDEIHLIS--------DEErgptlesIVARLRRLNPNT 150
|
170
....*....|.
gi 282403582 202 SLIGLTATATN 212
Cdd:cd18028 151 QIIGLSATIGN 161
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
298-372 |
3.76e-03 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. 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: 350179 [Multi-domain] Cd Length: 160 Bit Score: 38.40 E-value: 3.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 282403582 298 HANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVR-FVIHHSMSKSMENYYQESGRAGRDDMKADCILYYG 372
Cdd:cd18792 67 HGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANtMIIEDADRFGLSQLHQLRGRVGRGKHQSYCYLLYP 142
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
29-81 |
3.87e-03 |
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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: 39.28 E-value: 3.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 282403582 29 SGKVKDILQNvFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPAL 81
Cdd:cd17953 20 SEKVLDLIKK-LGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMF 71
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| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
246-360 |
4.05e-03 |
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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: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403582 246 KPSNTEDFIEDIVKLINgryKGQSGIIYCFSQKDSEQVTVSLQNL------GIHAGAYHANLEPEDKTTVHRKWSANEIQ 319
Cdd:cd18796 20 AGESGADAYAEVIFLLE---RHKSTLVFTNTRSQAERLAQRLRELcpdrvpPDFIALHHGSLSRELREEVEAALKRGDLK 96
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90 100 110 120
....*....|....*....|....*....|....*....|.
gi 282403582 320 VVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGR 360
Cdd:cd18796 97 VVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
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