|
Name |
Accession |
Description |
Interval |
E-value |
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
81-543 |
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: 767.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 81 DILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISATM 160
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 161 LNASSSKEHVKWVHAEMvnKNSELKLIYVTPEKIAKSKMFMSRLEkayEARRFTRIAVDEVHCCSQWGHDFRPDYKALGI 240
Cdd:TIGR00614 81 LNSAQTKEQQLNVLTDL--KDGKIKLLYVTPEKISASNRLLQTLE---ERKGITLIAVDEAHCISQWGHDFRPDYKALGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 241 LKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFNRPNLYYEVRQKPSNtedFIEDIVKLINGRYKGQSGIIY 320
Cdd:TIGR00614 156 LKQKFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTPK---ILEDLLRFIRKEFEGKSGIIY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 321 CFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQ 400
Cdd:TIGR00614 233 CPSRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 401 ESGRAGRDDMKADCILYYGFGDIFRISSMVVMENVGQQ-----KLYEMVSYCQNISKCRRVLMAQHFDEVWN-----SEA 470
Cdd:TIGR00614 313 ESGRAGRDGLPSECHLFYAPADMNRLRRLLMEEPDGNFrtyklKLYEMMEYCLNSSTCRRLILLSYFGEKGFnksfcIMG 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14591904 471 CNKMCDNCCKDSAFERKNITEYCRDLIKILKQAEE----LNEKLTPLKLIDSWMGKGAAKLRVAGVVAPTL-PREDLE 543
Cdd:TIGR00614 393 TEKCCDNCCKRLDYKTKDVTDKVYDFGPQAQKALSavgrLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLyGRGKDE 470
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
78-528 |
1.47e-172 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 500.44 E-value: 1.47e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 78 KVKDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGIS 157
Cdd:COG0514 4 DALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 158 ATMLNASSSKEHVKWVHAEMvnKNSELKLIYVTPEKIAKSKmFMSRLEKAyearRFTRIAVDEVHCCSQWGHDFRPDYKA 237
Cdd:COG0514 84 AAFLNSSLSAEERREVLRAL--RAGELKLLYVAPERLLNPR-FLELLRRL----KISLFAIDEAHCISQWGHDFRPDYRR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 238 LGILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFNRPNLYYEVRQKPSntEDFIEDIVKLINGRyKGQSG 317
Cdd:COG0514 157 LGELRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPP--DDKLAQLLDFLKEH-PGGSG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 318 IIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMEN 397
Cdd:COG0514 234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 398 YYQESGRAGRDDMKADCILYYGFGDIFRISSMVVMEN-------VGQQKLYEMVSYCQnISKCRRVLMAQHFDEVwNSEA 470
Cdd:COG0514 314 YYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPpdeerkrVERAKLDAMLAYAE-TTGCRRQFLLRYFGEE-LAEP 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 14591904 471 CNKmCDNCCKDSafERKNITEYCRdliKILKQAEELNEKLTPLKLIDSWMGKGAAKLR 528
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 ... |
74-282 |
8.66e-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: 8.66e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 74 PWSGKVKDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQ 153
Cdd:cd18015 1 PWSGKVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 154 LGISATMLNASSSKEHVKWVHAEMVNKNSELKLIYVTPEKIAKSKMFMSRLEKAYEARRFTRIAVDEVHCCSQWGHDFRP 233
Cdd:cd18015 81 LGISATMLNASSSKEHVKWVHAALTDKNSELKLLYVTPEKIAKSKRFMSKLEKAYNAGRLARIAIDEVHCCSQWGHDFRP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 14591904 234 DYKALGILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFN 282
Cdd:cd18015 161 DYKKLGILKRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
63-505 |
3.73e-151 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 467.84 E-value: 3.73e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 63 SSPAAWNKEDFPWSGKVKDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLIS 142
Cdd:PLN03137 432 SNDKKWSSRNFPWTKKLEVNNKKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVS 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 143 LMEDQLMVLKQLGISATMLNASSSKEHVKWVHAEMVNKNSELKLIYVTPEKIAKSKMFMSRLEKAYEARRFTRIAVDEVH 222
Cdd:PLN03137 512 LIQDQIMNLLQANIPAASLSAGMEWAEQLEILQELSSEYSKYKLLYVTPEKVAKSDSLLRHLENLNSRGLLARFVIDEAH 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 223 CCSQWGHDFRPDYKALGILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFNRPNLYYEVRQKpsnTEDFIE 302
Cdd:PLN03137 592 CVSQWGHDFRPDYQGLGILKQKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPK---TKKCLE 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 303 DIVKLINGRYKGQSGIIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPD 382
Cdd:PLN03137 669 DIDKFIKENHFDECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPD 748
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 383 VRFVIHHSMSKSMENYYQESGRAGRDDMKADCILYYGFGDIFRISSMVVMENVGQ---------------------QKLY 441
Cdd:PLN03137 749 VRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMISQGGVEQspmamgynrmassgriletntENLL 828
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14591904 442 EMVSYCQNISKCRRVLMAQHFDEVWNSEACNKMCDNCCKDSAFERKNITEYCRDLIKILKQAEE 505
Cdd:PLN03137 829 RMVSYCENEVDCRRFLQLVHFGEKFDSTNCKKTCDNCSSSKSLIDKDVTEIARQLVELVKLTGE 892
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
80-478 |
1.41e-129 |
|
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: 394.05 E-value: 1.41e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 80 KDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISAT 159
Cdd:TIGR01389 2 QQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 160 MLNASSSKEHVKwvHAEMVNKNSELKLIYVTPEkiakskmfmsRLEKAYEARRFTR-----IAVDEVHCCSQWGHDFRPD 234
Cdd:TIGR01389 82 YLNSTLSAKEQQ--DIEKALVNGELKLLYVAPE----------RLEQDYFLNMLQRipialVAVDEAHCVSQWGHDFRPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 235 YKALGILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFNRPNLYYEVRQKpSNTEDFIEDIVKlingRYKG 314
Cdd:TIGR01389 150 YQRLGSLAERFPQVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKK-NNKQKFLLDYLK----KHRG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 315 QSGIIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKS 394
Cdd:TIGR01389 225 QSGIIYASSRKKVEELAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 395 MENYYQESGRAGRDDMKADCILYYGFGDI----FRISSMVVMENVGQ---QKLYEMVSYCqNISKCRRVLMAQHFDEVwN 467
Cdd:TIGR01389 305 LESYYQEAGRAGRDGLPAEAILLYSPADIallkRRIEQSEADDDYKQierEKLRAMIAYC-ETQTCRRAYILRYFGEN-E 382
|
410
....*....|.
gi 14591904 468 SEACNKmCDNC 478
Cdd:TIGR01389 383 VEPCGN-CDNC 392
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
80-478 |
2.25e-116 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 360.57 E-value: 2.25e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 80 KDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISAT 159
Cdd:PRK11057 14 KQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 160 MLNASSSKEHVKWVHAEMvnKNSELKLIYVTPEKIAKSKmFMSRLEKAyearRFTRIAVDEVHCCSQWGHDFRPDYKALG 239
Cdd:PRK11057 94 CLNSTQTREQQLEVMAGC--RTGQIKLLYIAPERLMMDN-FLEHLAHW----NPALLAVDEAHCISQWGHDFRPEYAALG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 240 ILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFNRPNLYYEV--RQKPsntedfIEDIVKLINGRyKGQSG 317
Cdd:PRK11057 167 QLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLveKFKP------LDQLMRYVQEQ-RGKSG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 318 IIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMEN 397
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 398 YYQESGRAGRDDMKADCILYYGFGDIFRISSMVVMENVGQQ------KLYEMVSYCQnISKCRRVLMAQHFDEvWNSEAC 471
Cdd:PRK11057 320 YYQETGRAGRDGLPAEAMLFYDPADMAWLRRCLEEKPAGQQqdierhKLNAMGAFAE-AQTCRRLVLLNYFGE-GRQEPC 397
|
....*..
gi 14591904 472 NKmCDNC 478
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 ... |
80-282 |
9.36e-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: 9.36e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 80 KDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISAT 159
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 160 MLNASSSKEHVKWVHAEMvnKNSELKLIYVTPEKIAkSKMFMSRLEKAYEARRFTRIAVDEVHCCSQWGHDFRPDYKALG 239
Cdd:cd17920 81 ALNSTLSPEEKREVLLRI--KNGQYKLLYVTPERLL-SPDFLELLQRLPERKRLALIVVDEAHCVSQWGHDFRPDYLRLG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14591904 240 ILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFN 282
Cdd:cd17920 158 RLRRALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
283-418 |
1.19e-73 |
|
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: 232.87 E-value: 1.19e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 283 RPNLYYEVRQKPSNTEDFieDIVKLINGRYKGQSGIIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSA 362
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKL--DLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 14591904 363 NEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGRDDMKADCILYY 418
Cdd:cd18794 79 DKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
76-282 |
4.93e-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: 231.25 E-value: 4.93e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 76 SGKVKDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLG 155
Cdd:cd18016 2 SKEMMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 156 ISATMLNASSSKEHVKWVHAEMVNKNSELKLIYVTPEKIAKSKMFMSRLEKAYEARRFTRIAVDEVHCCSQWGHDFRPDY 235
Cdd:cd18016 82 IPATYLTGDKTDAEATKIYLQLSKKDPIIKLLYVTPEKISASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRPDY 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 14591904 236 KALGILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFN 282
Cdd:cd18016 162 KRLNMLRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
82-282 |
3.59e-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: 3.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 82 ILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALC----SDGFTLVICPLISLMEDQLMVLKQLgIS 157
Cdd:cd18018 3 LLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLlrrrGPGLTLVVSPLIALMKDQVDALPRA-IK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 158 ATMLNaSSSKEHVKWVHAEMVNKNsELKLIYVTPEKIAkSKMFMSRLEkayEARRFTRIAVDEVHCCSQWGHDFRPDYKA 237
Cdd:cd18018 82 AAALN-SSLTREERRRILEKLRAG-EVKILYVSPERLV-NESFRELLR---QTPPISLLVVDEAHCISEWSHNFRPDYLR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 14591904 238 LGILKRQFPNA-SLIGLTATATNHVLTDAQKILCIEKCFTFTASFN 282
Cdd:cd18018 156 LCRVLRELLGApPVLALTATATKRVVEDIASHLGIPESGVVRGPLY 201
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
81-282 |
2.28e-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: 176.12 E-value: 2.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 81 DILQNVFKLEKFRPLQLETI-NVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISAT 159
Cdd:cd18017 2 NALNEYFGHSSFRPVQWKVIrSVLEERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPAC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 160 MLNASSSKEHVKwvhaemVNKNSELKLIYVTPEKIAKSKMFMSRLEKayearRFTRIAVDEVHCCSQWGHDFRPDYKALG 239
Cdd:cd18017 82 FLGSAQSQNVLD------DIKMGKIRVIYVTPEFVSKGLELLQQLRN-----GITLIAIDEAHCVSQWGHDFRSSYRHLG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14591904 240 ILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFN 282
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 ... |
80-280 |
3.82e-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: 167.65 E-value: 3.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 80 KDILQNVFKLEKFR-PLQLETINVTMAGK-EVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGIS 157
Cdd:cd18014 1 RSTLKKVFGHSDFKsPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 158 ATMLNASSSKEHVKWVHAEMVNKNSELKLIYVTPEKiAKSKMFMSRLEKAYEARRFTRIAVDEVHCCSQWGHDFRPDYKA 237
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADLESEKPQTKFLYITPEM-AATSSFQPLLSSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 14591904 238 LGILKRQFPNASLIGLTATATNHVLTDAQKILCIEK-CFTFTAS 280
Cdd:cd18014 160 LGALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKpVAIFKTP 203
|
|
| DpdF |
NF041063 |
protein DpdF; |
105-423 |
3.30e-39 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 154.68 E-value: 3.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 105 AGKEVFLVMPTGGGKSLCYQLPALCS---DGFTLVICPLISL---MEDQLM-VLKQLGISATMLNA---SSSKEhvkwVH 174
Cdd:NF041063 157 PGSTLIVNLPTGSGKSLVAQAPALLAsrqGGLTLVVVPTVALaidQERRAReLLRRAGPDLGGPLAwhgGLSAE----ER 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 175 AEMVN--KNSELKLIYVTPEKIAKSkmFMSRLEKAYEARRFTRIAVDEVHCCSQWGHDFRPDYKALGILKRQFPNASLIG 252
Cdd:NF041063 233 AAIRQriRDGTQRILFTSPESLTGS--LRPALFDAAEAGLLRYLVVDEAHLVDQWGDGFRPEFQLLAGLRRSLLRLAPSG 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 253 -------LTATATNHVLTDAQKILCIEKCFT-FTASFNRPNLYYEVRQKPSnTEDFIEDIVKLIngRYKGQSGIIYCFSQ 324
Cdd:NF041063 311 rpfrtllLSATLTESTLDTLETLFGPPGPFIvVSAVQLRPEPAYWVAKCDS-EEERRERVLEAL--RHLPRPLILYVTKV 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 325 KDSEQVTVSLQNLGIH-AGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESG 403
Cdd:NF041063 388 EDAEAWLQRLRAAGFRrVALFHGDTPDAERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVG 467
|
330 340
....*....|....*....|
gi 14591904 404 RAGRDDMKADCILYYGFGDI 423
Cdd:NF041063 468 RGGRDGKASLSLLIYTPDDL 487
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
106-256 |
1.01e-31 |
|
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: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 106 GKEVFLVMPTGGGKSLCYQLPALCSD----GFTLVICPLISLMEDQLMVLKQL---GISATMLNASSSKEHVKwvhaemV 178
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLlkkgKKVLVLVPTKALALQTAERLRELfgpGIRVAVLVGGSSAEERE------K 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14591904 179 NKNSELKLIYVTPEKIAKSKMFMSRLEKayeaRRFTRIAVDEVHCCSQWGHDFRPDYkaLGILKRQFPNASLIGLTAT 256
Cdd:cd00046 75 NKLGDADIIIATPDMLLNLLLREDRLFL----KDLKLIIVDEAHALLIDSRGALILD--LAVRKAGLKNAQVILLSAT 146
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
93-258 |
2.72e-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: 2.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 93 RPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPAL------CSDGFTLVICPLISLMEDQLMVLKQLGISATMLNASSS 166
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 167 KEHVKWvhaEMVNKNSELKLIYVTPEKIAKskmfMSRLEKAYEARRFtrIAVDEVHCCSQWGhdFRPDYKAlgILKRQFP 246
Cdd:pfam00270 81 GGDSRK---EQLEKLKGPDILVGTPGRLLD----LLQERKLLKNLKL--LVLDEAHRLLDMG--FGPDLEE--ILRRLPK 147
|
170
....*....|..
gi 14591904 247 NASLIGLTATAT 258
Cdd:pfam00270 148 KRQILLLSATLP 159
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
87-291 |
2.77e-23 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 97.95 E-value: 2.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 87 FKLEKFRPLQLETINVTMAG-KEVFLVMPTGGGKSLCYQLPALC-----SDGFTLVICPLISLMEDQLMVLKQLGISATM 160
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEalkrgKGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 161 LNASSSKEHVKWVHAEMVNKNsELKLIYVTPEkiakskMFMSRLEKAY-EARRFTRIAVDEVHCCSQWGhdFRPDYKalG 239
Cdd:smart00487 84 KVVGLYGGDSKREQLRKLESG-KTDILVTTPG------RLLDLLENDKlSLSNVDLVILDEAHRLLDGG--FGDQLE--K 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 14591904 240 ILKRQFPNASLIGLTATATNHVLTDAQKILciEKCFTFTASFnRPNLYYEVR 291
Cdd:smart00487 153 LLKLLPKNVQLLLLSATPPEEIENLLELFL--NDPVFIDVGF-TPLEPIEQF 201
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
328-408 |
6.50e-22 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 89.96 E-value: 6.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 328 EQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGR 407
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
.
gi 14591904 408 D 408
Cdd:smart00490 81 A 81
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
301-407 |
7.20e-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: 7.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 301 IEDIVKLINGRYKGQSgIIYCFSQKDSEqVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDK 380
Cdd:pfam00271 3 LEALLELLKKERGGKV-LIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*..
gi 14591904 381 PDVRFVIHHSMSKSMENYYQESGRAGR 407
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. |
420-479 |
5.20e-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: 72.71 E-value: 5.20e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14591904 420 FGDIFRISSMVVMEN-------VGQQKLYEMVSYCQNISKCRRVLMAQHFDEVWNSEACnKMCDNCC 479
Cdd:pfam16124 1 YQDVVRLRFLIEQSEadeerkeVELQKLQAMVAYCENTTDCRRKQLLRYFGEEFDSEPC-GNCDNCL 66
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
111-417 |
6.16e-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: 6.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 111 LVMPTGGGKSL----CYQlpALCSDGFTLVICPLISLMEdQLM--VLKQLGISATMLNASSSKEHVkwvhaemvnknsel 184
Cdd:COG1061 105 VVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLE-QWAeeLRRFLGDPLAGGGKKDSDAPI-------------- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 185 klIYVTPEKIAKSKMFmSRLEkayeaRRFTRIAVDEVHccsqwgHDFRPDYKAlgILKRqFPNASLIGLTAT----ATNH 260
Cdd:COG1061 168 --TVATYQSLARRAHL-DELG-----DRFGLVIIDEAH------HAGAPSYRR--ILEA-FPAAYRLGLTATpfrsDGRE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 261 VLTD---------------AQKILCIEKCFTFTASFNRPNLYYEVRQKP------SNTEDFIEDIVKLINGRYKGQSGII 319
Cdd:COG1061 231 ILLFlfdgivyeyslkeaiEDGYLAPPEYYGIRVDLTDERAEYDALSERlrealaADAERKDKILRELLREHPDDRKTLV 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 320 YCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYY 399
Cdd:COG1061 311 FCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFI 390
|
330 340
....*....|....*....|..
gi 14591904 400 QesgRAGR----DDMKADCILY 417
Cdd:COG1061 391 Q---RLGRglrpAPGKEDALVY 409
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
362-418 |
7.62e-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: 7.62e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 14591904 362 ANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGRD-DMKADCILYY 418
Cdd:cd18785 20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGgKDEGEVILFV 77
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
96-407 |
1.68e-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: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 96 QLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCS-----DGFTLVICPLISLMEDQLMVLKQL------GISATMLNAS 164
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAlledpGATALYLYPTKALARDQLRRLRELaealglGVRVATYDGD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 165 SSKEHVKWV--HAEmvnknselkLIYVTPEKI--------AKSKMFMSRLekayearRFtrIAVDEVHCcsqwghdfrpd 234
Cdd:COG1205 141 TPPEERRWIreHPD---------IVLTNPDMLhygllphhTRWARFFRNL-------RY--VVIDEAHT----------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 235 YK-ALG-----ILKR------------QFpnaslIGLTATATN---HV--LTDaQKILCIEKCF------TFtaSFNRPN 285
Cdd:COG1205 192 YRgVFGshvanVLRRlrricrhygsdpQF-----ILASATIGNpaeHAerLTG-RPVTVVDEDGsprgerTF--VLWNPP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 286 LYYEVRQKPSNTE--DFIEDIVKlingryKGQSGIIYCFSQKDSEQVTVSLQN------LGIHAGAYHANLEPEDKTTVH 357
Cdd:COG1205 264 LVDDGIRRSALAEaaRLLADLVR------EGLRTLVFTRSRRGAELLARYARRalrepdLADRVAAYRAGYLPEERREIE 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 14591904 358 RKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGR 407
Cdd:COG1205 338 RGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGR 387
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
286-407 |
1.92e-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: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 286 LYYEVrqkpsNTEDFIEDIVKLINGRYKGQSGIIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEI 365
Cdd:cd18787 4 LYVVV-----EEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKV 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 14591904 366 QVVVAT-VAfGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGR 407
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 ... |
287-417 |
4.12e-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: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 287 YYEVRQKPSNTEDFIEDIVKLINGRYKGQSgIIYCFSQKDSEQVTVSLQNLGIHagayHANLEPEDKTTVHRKWSANEIQ 366
Cdd:cd18795 17 IKLRVDVMNKFDSDIIVLLKIETVSEGKPV-LVFCSSRKECEKTAKDLAGIAFH----HAGLTREDRELVEELFREGLIK 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14591904 367 VVVATVAFGMGIDKPdVRFVIHHSMSK---------SMENYYQESGRAGR---DDmKADCILY 417
Cdd:cd18795 92 VLVATSTLAAGVNLP-ARTVIIKGTQRydgkgyrelSPLEYLQMIGRAGRpgfDT-RGEAIIM 152
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
287-407 |
5.66e-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: 5.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 287 YYEVRQKpsnteDFIEDIVKLINgRYKGQSGIIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQ 366
Cdd:COG0513 220 YYLVDKR-----DKLELLRRLLR-DEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIR 293
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 14591904 367 VVVAT-VAfGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGR 407
Cdd:COG0513 294 VLVATdVA-ARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGR 334
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
241-410 |
1.83e-09 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 61.06 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 241 LKRQFPNASLIGLTATATN-HVLtdAQKILC-----------IEKCFTFTASFNRPNLYYE-VRQKPSNTEDFiedivkl 307
Cdd:COG1202 354 LKYYCPGAQWIYLSATVGNpEEL--AKKLGAklveyeerpvpLERHLTFADGREKIRIINKlVKREFDTKSSK------- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 308 inGrYKGQSgIIYCFSQKDSEQVTvslQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRfVI 387
Cdd:COG1202 425 --G-YRGQT-IIFTNSRRRCHEIA---RALGYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQ-VI 496
|
170 180
....*....|....*....|....*...
gi 14591904 388 HHS--MSK---SMENYYQESGRAGRDDM 410
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 ... |
318-412 |
1.99e-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: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 318 IIYCFSQKDSEQVTVSLQNLGIHAG-------AYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHS 390
Cdd:cd18797 39 IVFCRSRKLAELLLRYLKARLVEEGplaskvaSYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|..
gi 14591904 391 MSKSMENYYQESGRAGRDDMKA 412
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDS 140
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
75-407 |
2.05e-07 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 54.13 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 75 WSGKVKDILQNvFKLEKFRPLQLETI-NVTMAGKEVFLVMPTGGGKSLCYQLP---ALCSDGFTLVICPLISL---MEDQ 147
Cdd:COG1204 7 PLEKVIEFLKE-RGIEELYPPQAEALeAGLLEGKNLVVSAPTASGKTLIAELAilkALLNGGKALYIVPLRALaseKYRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 148 LM-VLKQLGISATMlnasSSKEHVkwVHAEMVNKNSelklIYV-TPEKiakskmFMSRLEKAYE-ARRFTRIAVDEVHcc 224
Cdd:COG1204 86 FKrDFEELGIKVGV----STGDYD--SDDEWLGRYD----ILVaTPEK------LDSLLRNGPSwLRDVDLVVVDEAH-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 225 sQWGHDFR-PDYK-ALGILKRQFPNASLIGLTATATNhvltdAQKILCIEKCFTFTASFnRPN-----LYY----EVRQK 293
Cdd:COG1204 148 -LIDDESRgPTLEvLLARLRRLNPEAQIVALSATIGN-----AEEIAEWLDAELVKSDW-RPVplnegVLYdgvlRFDDG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 294 PSNTEDFIEDIV-KLINGRykGQSgIIYCFSQKDSEQ-----------------------VTVSLQNLGIHAG------- 342
Cdd:COG1204 221 SRRSKDPTLALAlDLLEEG--GQV-LVFVSSRRDAESlakkladelkrrltpeereeleeLAEELLEVSEETHtneklad 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14591904 343 ------AYH-ANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMEN-----YYQESGRAGR 407
Cdd:COG1204 298 clekgvAFHhAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDTKRGGMVPipvleFKQMAGRAGR 374
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
318-407 |
8.78e-07 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 51.75 E-value: 8.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 318 IIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMEN 397
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90
....*....|
gi 14591904 398 YYQESGRAGR 407
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 ... |
96-222 |
2.19e-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: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 96 QLETINVTMAGKEVFLVMPTGGGKSLCYQLP---ALCSDGFT--LVICPLISLMEDQLMVLKQL------GISATMLNAS 164
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPileALLRDPGSraLYLYPTKALAQDQLRSLRELleqlglGIRVATYDGD 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14591904 165 SSKEHVKWVHAEMVNknselkLIYVTPEKI--------AKSKMFMSRLekayearRFtrIAVDEVH 222
Cdd:cd17923 85 TPREERRAIIRNPPR------ILLTNPDMLhyallphhDRWARFLRNL-------RY--VVLDEAH 135
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
94-411 |
5.76e-06 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 49.39 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 94 PLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALC----------SDG-FTLVICPLISLMEDqlmvlkqlgISATMLN 162
Cdd:PTZ00110 155 PIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVhinaqpllryGDGpIVLVLAPTRELAEQ---------IREQCNK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 163 -ASSSKEHVKWVHAEMVNKNSELKLIYVTPEKIAKSKMFMSRLEKAY-EARRFTRIAVDEVHCCSQWGhdFRPDYKAlgI 240
Cdd:PTZ00110 226 fGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVtNLRRVTYLVLDEADRMLDMG--FEPQIRK--I 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 241 LKRQFPNASLIGLTATATNHVLTDAQKiLCIEK-------CFTFTASFN-RPNLY-YEVRQKPSNTEDFIEDIVKlingr 311
Cdd:PTZ00110 302 VSQIRPDRQTLMWSATWPKEVQSLARD-LCKEEpvhvnvgSLDLTACHNiKQEVFvVEEHEKRGKLKMLLQRIMR----- 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 312 yKGQSGIIYCFSQKDSEQVTVSLQNLGIHAGAYHAnlepeDKTTVHRKWSANEIQ-----VVVATVAFGMGIDKPDVRFV 386
Cdd:PTZ00110 376 -DGDKILIFVETKKGADFLTKELRLDGWPALCIHG-----DKKQEERTWVLNEFKtgkspIMIATDVASRGLDVKDVKYV 449
|
330 340
....*....|....*....|....*
gi 14591904 387 IHHSMSKSMENYYQESGRAGRDDMK 411
Cdd:PTZ00110 450 INFDFPNQIEDYVHRIGRTGRAGAK 474
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
91-256 |
5.99e-06 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 46.90 E-value: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 91 KFRPLQLETINVTMAG-----KEVFLVMPTGGGKSLCY-QLPALCSDGF----TLVICPLISLMEDQLMVLKQLGISATM 160
Cdd:pfam04851 3 ELRPYQIEAIENLLESikngqKRGLIVMATGSGKTLTAaKLIARLFKKGpikkVLFLVPRKDLLEQALEEFKKFLPNYVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 161 LNASSSKEhvkwvhaEMVNKNSELKLIYVTPEKIAKSKMfMSRLEKAYEARRFtrIAVDEVHccsqwgHDFRPDYKAlgi 240
Cdd:pfam04851 83 IGEIISGD-------KKDESVDDNKIVVTTIQSLYKALE-LASLELLPDFFDV--IIIDEAH------RSGASSYRN--- 143
|
170
....*....|....*.
gi 14591904 241 LKRQFPNASLIGLTAT 256
Cdd:pfam04851 144 ILEYFKPAFLLGLTAT 159
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
484-590 |
4.85e-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: 42.91 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 484 FERKNITEYCRDLIKILKqaeELNEKLTPLKLID--------SWMGKGAAKLRVAGVVAPtLPREDLEKIIAHFLIQQYL 555
Cdd:pfam09382 2 PETVDVTEEAQKILSCVY---RTGQRFGAGHLIDvlrgsknkKIRQLGHDKLSTFGIGKD-LSKKEWRRIIRQLIAEGYL 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 14591904 556 KEDYSFTayatiSYLKIGPKA-NLLNNEAHaITMQV 590
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 ... |
92-259 |
5.06e-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: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 92 FRPLQLETINVTM-AGKEVFLVMPTGGGKSLCYQLPAL----CSDGFTLVICPLISLMEDQLM----VLKQLGISATMLN 162
Cdd:cd17921 2 LNPIQREALRALYlSGDSVLVSAPTSSGKTLIAELAILralaTSGGKAVYIAPTRALVNQKEAdlreRFGPLGKNVGLLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 163 ASSSkehvkwvhaemVNKNSELKL-IYV-TPEKIAkskmFMSRLEKAYEARRFTRIAVDEVHCCSQwghdfrPDYKA--- 237
Cdd:cd17921 82 GDPS-----------VNKLLLAEAdILVaTPEKLD----LLLRNGGERLIQDVRLVVVDEAHLIGD------GERGVvle 140
|
170 180
....*....|....*....|....
gi 14591904 238 --LGILKRQFPNASLIGLTATATN 259
Cdd:cd17921 141 llLSRLLRINKNARFVGLSATLPN 164
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
92-256 |
7.87e-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: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 92 FRPLQLETINVtMAGKEVF----LVMPTGGGKSLC-YQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISATMLNASSS 166
Cdd:cd17926 1 LRPYQEEALEA-WLAHKNNrrgiLVLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFEDFLGDSSIGLIGGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 167 KehvkwvhaemvNKNSELKLIYV-TPEKIakskmfmSRLEKAYEA--RRFTRIAVDEVH--CCSQWGHdfrpdykalgIL 241
Cdd:cd17926 80 K-----------KKDFDDANVVVaTYQSL-------SNLAEEEKDlfDQFGLLIVDEAHhlPAKTFSE----------IL 131
|
170
....*....|....*
gi 14591904 242 KRqFPNASLIGLTAT 256
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 ... |
345-445 |
9.47e-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: 9.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 345 HANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVR-FVIHHSMSKSMENYYQESGRAGRDDMKADCILYYGfgdi 423
Cdd:cd18811 68 HGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATvMVIEDAERFGLSQLHQLRGRVGRGDHQSYCLLVYK---- 143
|
90 100
....*....|....*....|..
gi 14591904 424 frissmVVMENVGQQKLYEMVS 445
Cdd:cd18811 144 ------DPLTETAKQRLRVMTE 159
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
338-407 |
1.81e-04 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 44.54 E-value: 1.81e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14591904 338 GIhaGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPdVRFVIHHSMSK----SMEN-----YYQESGRAGR 407
Cdd:COG4581 301 GI--AVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMP-ARTVVFTKLSKfdgeRHRPltareFHQIAGRAGR 376
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
9-371 |
2.37e-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: 44.30 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 9 EELDSITSELHAVEIQIQELTERQQELIQKKKVLTKKIKQCLEDSDAGASNEYDSSPAAWnkeDFPWSGKVKDILQNVFK 88
Cdd:COG1203 47 LLLAALELALLLLLLLLLLLLLLLLLLDLLLDDLAFLFLLLLIDADWLDSANFDMARQAL---DHLLAERLERLLPKKSK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 89 LEKFR-PLQLE----TINVTMAGKEVFLVM-PTGGGK---SLCY---QLPALCSDGFTLVIcPLISLMEDQLMVLKQLG- 155
Cdd:COG1203 124 PRTPInPLQNEalelALEAAEEEPGLFILTaPTGGGKteaALLFalrLAAKHGGRRIIYAL-PFTSIINQTYDRLRDLFg 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 156 --I----SATMLNASSSKEHVKWVHAEMVNkNSEL---KLIYVTPEKIAKSkMFMSRleKAYEaRRFTRIA-----VDEV 221
Cdd:COG1203 203 edVllhhSLADLDLLEEEEEYESEARWLKL-LKELwdaPVVVTTIDQLFES-LFSNR--KGQE-RRLHNLAnsviiLDEV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 222 HCCSQwgHDFRPDYKALGILKRQfpNASLIGLTAT---ATNHVLTDAQKILCIEKC--FTFTASFNRPNlyYEVRQKPSN 296
Cdd:COG1203 278 QAYPP--YMLALLLRLLEWLKNL--GGSVILMTATlppLLREELLEAYELIPDEPEelPEYFRAFVRKR--VELKEGPLS 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 297 TEDFIEDIVKLINgryKGQSGIIYCFSQKDSEQVTVSLQNLGIHAGAY--HANLEPEDKTTVHRKW----SANEIQVVVA 370
Cdd:COG1203 352 DEELAELILEALH---KGKSVLVIVNTVKDAQELYEALKEKLPDEEVYllHSRFCPADRSEIEKEIkerlERGKPCILVS 428
|
.
gi 14591904 371 T 371
Cdd:COG1203 429 T 429
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
79-139 |
1.40e-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: 1.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14591904 79 VKDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALC-----------SDG-FTLVICP 139
Cdd:cd17949 1 LVSHLKSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQrllsleprvdrSDGtLALVLVP 73
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
327-417 |
2.43e-03 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 40.93 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 327 SEQVTVSLqnlGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAG 406
Cdd:PLN00206 384 ANAITVVT---GLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRAS 460
|
90
....*....|.
gi 14591904 407 RDDMKADCILY 417
Cdd:PLN00206 461 RMGEKGTAIVF 471
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
106-259 |
3.51e-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: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 106 GKEVFLVMPTGGGKSLCYQL---PALCSDGFTLVICPLISLMEDQLMVLKQL-------GISATMLNassskEHVKWVHa 175
Cdd:cd18028 17 GENLLISIPTASGKTLIAEMamvNTLLEGGKALYLVPLRALASEKYEEFKKLeeiglkvGISTGDYD-----EDDEWLG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 176 emvnknsELKLIYVTPEKIAkskmFMSRLEKAYeARRFTRIAVDEVHCCSqwghdfrpDYK-------ALGILKRQFPNA 248
Cdd:cd18028 91 -------DYDIIVATYEKFD----SLLRHSPSW-LRDVGVVVVDEIHLIS--------DEErgptlesIVARLRRLNPNT 150
|
170
....*....|.
gi 14591904 249 SLIGLTATATN 259
Cdd:cd18028 151 QIIGLSATIGN 161
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
76-128 |
4.33e-03 |
|
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: 4.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 14591904 76 SGKVKDILQNvFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPAL 128
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 ... |
293-407 |
4.51e-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: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14591904 293 KPSNTEDFIEDIVKLINgryKGQSGIIYCFSQKDSEQVTVSLQNL------GIHAGAYHANLEPEDKTTVHRKWSANEIQ 366
Cdd:cd18796 20 AGESGADAYAEVIFLLE---RHKSTLVFTNTRSQAERLAQRLRELcpdrvpPDFIALHHGSLSRELREEVEAALKRGDLK 96
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90 100 110 120
....*....|....*....|....*....|....*....|.
gi 14591904 367 VVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGR 407
Cdd:cd18796 97 VVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
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| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
345-419 |
4.83e-03 |
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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: 4.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14591904 345 HANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVR-FVIHHSMSKSMENYYQESGRAGRDDMKADCILYYG 419
Cdd:cd18792 67 HGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANtMIIEDADRFGLSQLHQLRGRVGRGKHQSYCYLLYP 142
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