|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
2-340 |
6.85e-141 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 418.78 E-value: 6.85e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 2 ALKEKGIAAEYLSSTQATHVKNKIHEDLDSGKpsVRLLYVTPELIATKGFMLKLRKLHsrglLNLIAIDEAHCISSWGHD 81
Cdd:COG0514 76 ALRAAGIRAAFLNSSLSAEERREVLRALRAGE--LKLLYVAPERLLNPRFLELLRRLK----ISLFAIDEAHCISQWGHD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 82 FRPSYRQLSTLRDSLADVPVLALTATAAPKVQKDVIDSLNLRNPLVLKSSFNRPNIFYEVRYKDLlDNAYTDLGNLLKSC 161
Cdd:COG0514 150 FRPDYRRLGELRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPP-DDKLAQLLDFLKEH 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 162 GNICAIIYCLERTTCDDLSVHLSSIGISSAAYHAGLNSKMRSTVLDDWLSSKKQIIVATVAFGMGIDKKDVRMVCHFNIP 241
Cdd:COG0514 229 PGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLP 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 242 KSMESFYQESGRAGRDQLPSRSVLYYGVDDRKKMEYLLRNSENKKSSSSKKpTSDFEQIVTYCEGSGCRRKKILESFGEE 321
Cdd:COG0514 309 KSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVE-RAKLDAMLAYAETTGCRRQFLLRYFGEE 387
|
330
....*....|....*....
gi 30690466 322 FPvQQCKKtCDACKHPNQV 340
Cdd:COG0514 388 LA-EPCGN-CDNCLGPPET 404
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
1-335 |
9.57e-108 |
|
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: 332.89 E-value: 9.57e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 1 MALKEKGIAAEYLSSTQATHVKNKIHEDLDSGKpsVRLLYVTPELIAT-KGFMlklRKLHSRGLLNLIAIDEAHCISSWG 79
Cdd:TIGR00614 69 LQLQALGIPATFLNSAQTKEQQLNVLTDLKDGK--IKLLYVTPEKISAsNRLL---QTLEERKGITLIAVDEAHCISQWG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 80 HDFRPSYRQLSTLRDSLADVPVLALTATAAPKVQKDVIDSLNLRNPLVLKSSFNRPNIFYEVRYKdlLDNAYTDLGNLL- 158
Cdd:TIGR00614 144 HDFRPDYKALGSLKQKFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRK--TPKILEDLLRFIr 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 159 KSCGNICAIIYCLERTTCDDLSVHLSSIGISSAAYHAGLNSKMRSTVLDDWLSSKKQIIVATVAFGMGIDKKDVRMVCHF 238
Cdd:TIGR00614 222 KEFEGKSGIIYCPSRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHY 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 239 NIPKSMESFYQESGRAGRDQLPSRSVLYYGVDDRKKMEYLLrnsenkksssSKKPTSDFEQI-------VTYC-EGSGCR 310
Cdd:TIGR00614 302 SLPKSMESYYQESGRAGRDGLPSECHLFYAPADMNRLRRLL----------MEEPDGNFRTYklklyemMEYClNSSTCR 371
|
330 340 350
....*....|....*....|....*....|
gi 30690466 311 RKKILESFGE-----EFPVQQCKKTCDACK 335
Cdd:TIGR00614 372 RLILLSYFGEkgfnkSFCIMGTEKCCDNCC 401
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
3-337 |
1.55e-87 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 284.30 E-value: 1.55e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 3 LKEKGIAAEYLSSTQATHVKNKIHEDLDSGKpsVRLLYVTPELIATKGFMLKLRKLHsrglLNLIAIDEAHCISSWGHDF 82
Cdd:PRK11057 85 LLANGVAAACLNSTQTREQQLEVMAGCRTGQ--IKLLYIAPERLMMDNFLEHLAHWN----PALLAVDEAHCISQWGHDF 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 83 RPSYRQLSTLRDSLADVPVLALTATAAPKVQKDVIDSLNLRNPLVLKSSFNRPNIFYEV--RYKDLldnayTDLGNLLKS 160
Cdd:PRK11057 159 RPEYAALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLveKFKPL-----DQLMRYVQE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 161 CGNICAIIYCLERTTCDDLSVHLSSIGISSAAYHAGLNSKMRSTVLDDWLSSKKQIIVATVAFGMGIDKKDVRMVCHFNI 240
Cdd:PRK11057 234 QRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDI 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 241 PKSMESFYQESGRAGRDQLPSRSVLYYgvdDRKKMEYLLRNSENkkssSSKKPTSDFEQ-----IVTYCEGSGCRRKKIL 315
Cdd:PRK11057 314 PRNIESYYQETGRAGRDGLPAEAMLFY---DPADMAWLRRCLEE----KPAGQQQDIERhklnaMGAFAEAQTCRRLVLL 386
|
330 340
....*....|....*....|..
gi 30690466 316 ESFGEEFPvQQCkKTCDACKHP 337
Cdd:PRK11057 387 NYFGEGRQ-EPC-GNCDICLDP 406
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
134-267 |
3.84e-70 |
|
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: 222.85 E-value: 3.84e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 134 RPNIFYEVRYKDLLDNAYTDLGNLLKSCGNICAIIYCLERTTCDDLSVHLSSIGISSAAYHAGLNSKMRSTVLDDWLSSK 213
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 30690466 214 KQIIVATVAFGMGIDKKDVRMVCHFNIPKSMESFYQESGRAGRDQLPSRSVLYY 267
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DpdF |
NF041063 |
protein DpdF; |
17-278 |
1.30e-34 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 140.05 E-value: 1.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 17 QATHVKNKIHEDLDSGkpSVRLLYVTPElIATKGFMLKLRKLHSRGLLNLIAIDEAHCISSWGHDFRPSYRQLSTLRDSL 96
Cdd:NF041063 227 LSAEERAAIRQRIRDG--TQRILFTSPE-SLTGSLRPALFDAAEAGLLRYLVVDEAHLVDQWGDGFRPEFQLLAGLRRSL 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 97 ADVP-------VLALTATAAPKvQKDVIDSL--NLRNPLVLKSSFNRPNIFYEVRYKDLLDNaYTDLgnLLKScgnIC-- 165
Cdd:NF041063 304 LRLApsgrpfrTLLLSATLTES-TLDTLETLfgPPGPFIVVSAVQLRPEPAYWVAKCDSEEE-RRER--VLEA---LRhl 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 166 ---AIIYCLERTTCDDLSVHLSSIGISS-AAYHAGLNSKMRSTVLDDWlsSKKQ--IIVATVAFGMGIDKKDVRMVCHFN 239
Cdd:NF041063 377 prpLILYVTKVEDAEAWLQRLRAAGFRRvALFHGDTPDAERERLIEQW--RENEldIVVATSAFGLGMDKSDVRTVIHAC 454
|
250 260 270
....*....|....*....|....*....|....*....
gi 30690466 240 IPKSMESFYQESGRAGRDQLPSRSVLYYGVDDRKKMEYL 278
Cdd:NF041063 455 VPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDIAKSL 493
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
177-257 |
8.91e-21 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 86.88 E-value: 8.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 177 DDLSVHLSSIGISSAAYHAGLNSKMRSTVLDDWLSSKKQIIVATVAFGMGIDKKDVRMVCHFNIPKSMESFYQESGRAGR 256
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
.
gi 30690466 257 D 257
Cdd:smart00490 81 A 81
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
154-256 |
1.23e-18 |
|
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: 81.49 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 154 LGNLLKSCGNICAIIYCLERTTCDdLSVHLSSIGISSAAYHAGLNSKMRSTVLDDWLSSKKQIIVATVAFGMGIDKKDVR 233
Cdd:pfam00271 6 LLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVD 84
|
90 100
....*....|....*....|...
gi 30690466 234 MVCHFNIPKSMESFYQESGRAGR 256
Cdd:pfam00271 85 LVINYDLPWNPASYIQRIGRAGR 107
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
2-340 |
6.85e-141 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 418.78 E-value: 6.85e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 2 ALKEKGIAAEYLSSTQATHVKNKIHEDLDSGKpsVRLLYVTPELIATKGFMLKLRKLHsrglLNLIAIDEAHCISSWGHD 81
Cdd:COG0514 76 ALRAAGIRAAFLNSSLSAEERREVLRALRAGE--LKLLYVAPERLLNPRFLELLRRLK----ISLFAIDEAHCISQWGHD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 82 FRPSYRQLSTLRDSLADVPVLALTATAAPKVQKDVIDSLNLRNPLVLKSSFNRPNIFYEVRYKDLlDNAYTDLGNLLKSC 161
Cdd:COG0514 150 FRPDYRRLGELRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPP-DDKLAQLLDFLKEH 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 162 GNICAIIYCLERTTCDDLSVHLSSIGISSAAYHAGLNSKMRSTVLDDWLSSKKQIIVATVAFGMGIDKKDVRMVCHFNIP 241
Cdd:COG0514 229 PGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLP 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 242 KSMESFYQESGRAGRDQLPSRSVLYYGVDDRKKMEYLLRNSENKKSSSSKKpTSDFEQIVTYCEGSGCRRKKILESFGEE 321
Cdd:COG0514 309 KSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVE-RAKLDAMLAYAETTGCRRQFLLRYFGEE 387
|
330
....*....|....*....
gi 30690466 322 FPvQQCKKtCDACKHPNQV 340
Cdd:COG0514 388 LA-EPCGN-CDNCLGPPET 404
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
1-335 |
9.57e-108 |
|
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: 332.89 E-value: 9.57e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 1 MALKEKGIAAEYLSSTQATHVKNKIHEDLDSGKpsVRLLYVTPELIAT-KGFMlklRKLHSRGLLNLIAIDEAHCISSWG 79
Cdd:TIGR00614 69 LQLQALGIPATFLNSAQTKEQQLNVLTDLKDGK--IKLLYVTPEKISAsNRLL---QTLEERKGITLIAVDEAHCISQWG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 80 HDFRPSYRQLSTLRDSLADVPVLALTATAAPKVQKDVIDSLNLRNPLVLKSSFNRPNIFYEVRYKdlLDNAYTDLGNLL- 158
Cdd:TIGR00614 144 HDFRPDYKALGSLKQKFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRK--TPKILEDLLRFIr 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 159 KSCGNICAIIYCLERTTCDDLSVHLSSIGISSAAYHAGLNSKMRSTVLDDWLSSKKQIIVATVAFGMGIDKKDVRMVCHF 238
Cdd:TIGR00614 222 KEFEGKSGIIYCPSRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHY 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 239 NIPKSMESFYQESGRAGRDQLPSRSVLYYGVDDRKKMEYLLrnsenkksssSKKPTSDFEQI-------VTYC-EGSGCR 310
Cdd:TIGR00614 302 SLPKSMESYYQESGRAGRDGLPSECHLFYAPADMNRLRRLL----------MEEPDGNFRTYklklyemMEYClNSSTCR 371
|
330 340 350
....*....|....*....|....*....|
gi 30690466 311 RKKILESFGE-----EFPVQQCKKTCDACK 335
Cdd:TIGR00614 372 RLILLSYFGEkgfnkSFCIMGTEKCCDNCC 401
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
2-337 |
2.83e-99 |
|
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: 314.70 E-value: 2.83e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 2 ALKEKGIAAEYLSSTQATHVKNKIHEDLDSGKpsVRLLYVTPELIATKGFMLKLrklhSRGLLNLIAIDEAHCISSWGHD 81
Cdd:TIGR01389 72 QLRAAGVAAAYLNSTLSAKEQQDIEKALVNGE--LKLLYVAPERLEQDYFLNML----QRIPIALVAVDEAHCVSQWGHD 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 82 FRPSYRQLSTLRDSLADVPVLALTATAAPKVQKDVIDSLNLRNPLVLKSSFNRPNIFYEVRYKDlldNAYTDLGNLLKSC 161
Cdd:TIGR01389 146 FRPEYQRLGSLAERFPQVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKN---NKQKFLLDYLKKH 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 162 GNICAIIYCLERTTCDDLSVHLSSIGISSAAYHAGLNSKMRSTVLDDWLSSKKQIIVATVAFGMGIDKKDVRMVCHFNIP 241
Cdd:TIGR01389 223 RGQSGIIYASSRKKVEELAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMP 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 242 KSMESFYQESGRAGRDQLPSRSVLYYGVDDRKKMEYLLRNSEnkksssskkPTSDFEQI--------VTYCEGSGCRRKK 313
Cdd:TIGR01389 303 GNLESYYQEAGRAGRDGLPAEAILLYSPADIALLKRRIEQSE---------ADDDYKQIereklramIAYCETQTCRRAY 373
|
330 340
....*....|....*....|....
gi 30690466 314 ILESFGEEFpVQQCKKtCDACKHP 337
Cdd:TIGR01389 374 ILRYFGENE-VEPCGN-CDNCLDP 395
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
3-337 |
1.55e-87 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 284.30 E-value: 1.55e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 3 LKEKGIAAEYLSSTQATHVKNKIHEDLDSGKpsVRLLYVTPELIATKGFMLKLRKLHsrglLNLIAIDEAHCISSWGHDF 82
Cdd:PRK11057 85 LLANGVAAACLNSTQTREQQLEVMAGCRTGQ--IKLLYIAPERLMMDNFLEHLAHWN----PALLAVDEAHCISQWGHDF 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 83 RPSYRQLSTLRDSLADVPVLALTATAAPKVQKDVIDSLNLRNPLVLKSSFNRPNIFYEV--RYKDLldnayTDLGNLLKS 160
Cdd:PRK11057 159 RPEYAALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLveKFKPL-----DQLMRYVQE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 161 CGNICAIIYCLERTTCDDLSVHLSSIGISSAAYHAGLNSKMRSTVLDDWLSSKKQIIVATVAFGMGIDKKDVRMVCHFNI 240
Cdd:PRK11057 234 QRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDI 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 241 PKSMESFYQESGRAGRDQLPSRSVLYYgvdDRKKMEYLLRNSENkkssSSKKPTSDFEQ-----IVTYCEGSGCRRKKIL 315
Cdd:PRK11057 314 PRNIESYYQETGRAGRDGLPAEAMLFY---DPADMAWLRRCLEE----KPAGQQQDIERhklnaMGAFAEAQTCRRLVLL 386
|
330 340
....*....|....*....|..
gi 30690466 316 ESFGEEFPvQQCkKTCDACKHP 337
Cdd:PRK11057 387 NYFGEGRQ-EPC-GNCDICLDP 406
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
1-360 |
3.24e-78 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 269.84 E-value: 3.24e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 1 MALKEKGIAAEYLSSTQATHVKNKIHEDLDSGKPSVRLLYVTPELIATKGFMLK-LRKLHSRGLLNLIAIDEAHCISSWG 79
Cdd:PLN03137 518 MNLLQANIPAASLSAGMEWAEQLEILQELSSEYSKYKLLYVTPEKVAKSDSLLRhLENLNSRGLLARFVIDEAHCVSQWG 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 80 HDFRPSYRQLSTLRDSLADVPVLALTATAAPKVQKDVIDSLNLRNPLVLKSSFNRPNIFYEV--RYKDLLDnaytDLGNL 157
Cdd:PLN03137 598 HDFRPDYQGLGILKQKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVvpKTKKCLE----DIDKF 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 158 LKSCG-NICAIIYCLERTTCDDLSVHLSSIGISSAAYHAGLNSKMRSTVLDDWLSSKKQIIVATVAFGMGIDKKDVRMVC 236
Cdd:PLN03137 674 IKENHfDECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVI 753
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 237 HFNIPKSMESFYQESGRAGRDQLPSRSVLYYGVDDRKKMEYLL-------------RNSENKKSSSSKKPTSDFEQIVTY 303
Cdd:PLN03137 754 HHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMIsqggveqspmamgYNRMASSGRILETNTENLLRMVSY 833
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30690466 304 CEGS-GCRRKKILESFGEEFPVQQCKKTCDAC--------KHPNQVAHCLEELMTTASRRHNSSRI 360
Cdd:PLN03137 834 CENEvDCRRFLQLVHFGEKFDSTNCKKTCDNCssskslidKDVTEIARQLVELVKLTGERFSSAHI 899
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
134-267 |
3.84e-70 |
|
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: 222.85 E-value: 3.84e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 134 RPNIFYEVRYKDLLDNAYTDLGNLLKSCGNICAIIYCLERTTCDDLSVHLSSIGISSAAYHAGLNSKMRSTVLDDWLSSK 213
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 30690466 214 KQIIVATVAFGMGIDKKDVRMVCHFNIPKSMESFYQESGRAGRDQLPSRSVLYY 267
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
1-133 |
2.48e-55 |
|
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: 186.20 E-value: 2.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 1 MALKEKGIAAEYLSSTQATHVKNKIHEDLDSGKpsVRLLYVTPELIATKGFMLKLRKLHSRGLLNLIAIDEAHCISSWGH 80
Cdd:cd17920 70 DRLQQLGIRAAALNSTLSPEEKREVLLRIKNGQ--YKLLYVTPERLLSPDFLELLQRLPERKRLALIVVDEAHCVSQWGH 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 30690466 81 DFRPSYRQLSTLRDSLADVPVLALTATAAPKVQKDVIDSLNLRNPLVLKSSFN 133
Cdd:cd17920 148 DFRPDYLRLGRLRRALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
1-133 |
8.46e-45 |
|
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: 158.30 E-value: 8.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 1 MALKEKGIAAEYLSSTQATHVKNKIHEDLDSGKPSVRLLYVTPELIA-TKGFMLKLRKLHSRGLLNLIAIDEAHCISSWG 79
Cdd:cd18015 76 MALKKLGISATMLNASSSKEHVKWVHAALTDKNSELKLLYVTPEKIAkSKRFMSKLEKAYNAGRLARIAIDEVHCCSQWG 155
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 30690466 80 HDFRPSYRQLSTLRDSLADVPVLALTATAAPKVQKDVIDSLNLRNPLVLKSSFN 133
Cdd:cd18015 156 HDFRPDYKKLGILKRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
1-133 |
3.91e-43 |
|
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: 153.83 E-value: 3.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 1 MALKEKGIAAEYLSSTQATHVKNKIHEDLDSGKPSVRLLYVTPELIATKG-FMLKLRKLHSRGLLNLIAIDEAHCISSWG 79
Cdd:cd18016 75 QKLTSLDIPATYLTGDKTDAEATKIYLQLSKKDPIIKLLYVTPEKISASNrLISTLENLYERKLLARFVIDEAHCVSQWG 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 30690466 80 HDFRPSYRQLSTLRDSLADVPVLALTATAAPKVQKDVIDSLNLRNPLVLKSSFN 133
Cdd:cd18016 155 HDFRPDYKRLNMLRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
2-127 |
2.53e-37 |
|
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: 137.60 E-value: 2.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 2 ALKEKGIAAEYLSSTQATHVKNKIHEDLDSGKPSVRLLYVTPELIATKGFMLKLRKLHSRGLLNLIAIDEAHCISSWGHD 81
Cdd:cd18014 73 HLKTLKIRVDSLNSKLSAQERKRIIADLESEKPQTKFLYITPEMAATSSFQPLLSSLVSRNLLSYLVVDEAHCVSQWGHD 152
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 30690466 82 FRPSYRQLSTLRDSLADVPVLALTATAAPKVQKDVIDSLNLRNPLV 127
Cdd:cd18014 153 FRPDYLRLGALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKPVA 198
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
3-133 |
5.31e-37 |
|
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: 136.44 E-value: 5.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 3 LKEKGIAAEYLSSTQATHVKNkiheDLDSGKpsVRLLYVTPELIaTKGFMLkLRKLHSRglLNLIAIDEAHCISSWGHDF 82
Cdd:cd18017 73 LVMSNIPACFLGSAQSQNVLD----DIKMGK--IRVIYVTPEFV-SKGLEL-LQQLRNG--ITLIAIDEAHCVSQWGHDF 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 30690466 83 RPSYRQLSTLRDSLADVPVLALTATAAPKVQKDVIDSLNLRNPLVLKSSFN 133
Cdd:cd18017 143 RSSYRHLGSIRNRLPNVPIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| DpdF |
NF041063 |
protein DpdF; |
17-278 |
1.30e-34 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 140.05 E-value: 1.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 17 QATHVKNKIHEDLDSGkpSVRLLYVTPElIATKGFMLKLRKLHSRGLLNLIAIDEAHCISSWGHDFRPSYRQLSTLRDSL 96
Cdd:NF041063 227 LSAEERAAIRQRIRDG--TQRILFTSPE-SLTGSLRPALFDAAEAGLLRYLVVDEAHLVDQWGDGFRPEFQLLAGLRRSL 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 97 ADVP-------VLALTATAAPKvQKDVIDSL--NLRNPLVLKSSFNRPNIFYEVRYKDLLDNaYTDLgnLLKScgnIC-- 165
Cdd:NF041063 304 LRLApsgrpfrTLLLSATLTES-TLDTLETLfgPPGPFIVVSAVQLRPEPAYWVAKCDSEEE-RRER--VLEA---LRhl 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 166 ---AIIYCLERTTCDDLSVHLSSIGISS-AAYHAGLNSKMRSTVLDDWlsSKKQ--IIVATVAFGMGIDKKDVRMVCHFN 239
Cdd:NF041063 377 prpLILYVTKVEDAEAWLQRLRAAGFRRvALFHGDTPDAERERLIEQW--RENEldIVVATSAFGLGMDKSDVRTVIHAC 454
|
250 260 270
....*....|....*....|....*....|....*....
gi 30690466 240 IPKSMESFYQESGRAGRDQLPSRSVLYYGVDDRKKMEYL 278
Cdd:NF041063 455 VPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDIAKSL 493
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
8-133 |
6.69e-31 |
|
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: 119.67 E-value: 6.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 8 IAAEYLSSTQATHVKNKIHEDLDSGKpsVRLLYVTPELIATKGFmlkLRKLHSRGLLNLIAIDEAHCISSWGHDFRPSYR 87
Cdd:cd18018 80 IKAAALNSSLTREERRRILEKLRAGE--VKILYVSPERLVNESF---RELLRQTPPISLLVVDEAHCISEWSHNFRPDYL 154
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 30690466 88 QL-STLRDSLADVPVLALTATAAPKVQKDVIDSLNLRNPLVLKSSFN 133
Cdd:cd18018 155 RLcRVLRELLGAPPVLALTATATKRVVEDIASHLGIPESGVVRGPLY 201
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
177-257 |
8.91e-21 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 86.88 E-value: 8.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 177 DDLSVHLSSIGISSAAYHAGLNSKMRSTVLDDWLSSKKQIIVATVAFGMGIDKKDVRMVCHFNIPKSMESFYQESGRAGR 256
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
.
gi 30690466 257 D 257
Cdd:smart00490 81 A 81
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
154-256 |
1.23e-18 |
|
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: 81.49 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 154 LGNLLKSCGNICAIIYCLERTTCDdLSVHLSSIGISSAAYHAGLNSKMRSTVLDDWLSSKKQIIVATVAFGMGIDKKDVR 233
Cdd:pfam00271 6 LLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVD 84
|
90 100
....*....|....*....|...
gi 30690466 234 MVCHFNIPKSMESFYQESGRAGR 256
Cdd:pfam00271 85 LVINYDLPWNPASYIQRIGRAGR 107
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
45-256 |
2.60e-11 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 65.94 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 45 LIATKGfmlKLRKLHSRGLLNL-----IAIDEAhcisswghD------FRPSYRQLstlrdsLADVP----VLALTATAA 109
Cdd:COG0513 125 VVATPG---RLLDLIERGALDLsgvetLVLDEA--------DrmldmgFIEDIERI------LKLLPkerqTLLFSATMP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 110 PKVQKdVIDSLnLRNPL---VLKSSFNRPNI---FYEVRYKDLLDnaytDLGNLLKSCGNICAIIYCLERTTCDDLSVHL 183
Cdd:COG0513 188 PEIRK-LAKRY-LKNPVrieVAPENATAETIeqrYYLVDKRDKLE----LLRRLLRDEDPERAIVFCNTKRGADRLAEKL 261
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30690466 184 SSIGISSAAYHAGLNSKMRSTVLDDWLSSKKQIIVAT-VAfGMGIDKKDVRMVCHFNIPKSMESFYQESGRAGR 256
Cdd:COG0513 262 QKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATdVA-ARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGR 334
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
271-335 |
4.77e-10 |
|
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: 55.76 E-value: 4.77e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30690466 271 DRKKMEYLLRNSENKKSSSSKKpTSDFEQIVTYCEG-SGCRRKKILESFGEEFPVQQCkKTCDACK 335
Cdd:pfam16124 3 DVVRLRFLIEQSEADEERKEVE-LQKLQAMVAYCENtTDCRRKQLLRYFGEEFDSEPC-GNCDNCL 66
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
210-267 |
1.16e-09 |
|
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: 55.02 E-value: 1.16e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 30690466 210 LSSKKQIIVATVAFGMGIDKKDVRMVCHFNIPKSMESFYQESGRAGRD-QLPSRSVLYY 267
Cdd:cd18785 19 IASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGgKDEGEVILFV 77
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
167-265 |
1.57e-08 |
|
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: 53.80 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 167 IIYCLERTTCDDLSVHLSSIGISS-------AAYHAGLNSKMRSTVLDDWLSSKKQIIVATVAFGMGIDKKDVRMVCHFN 239
Cdd:cd18797 39 IVFCRSRKLAELLLRYLKARLVEEgplaskvASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|....*.
gi 30690466 240 IPKSMESFYQESGRAGRDQLPSRSVL 265
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDSLVIL 144
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
36-114 |
2.84e-08 |
|
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: 53.40 E-value: 2.84e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30690466 36 VRLLYVTPELIATkgfMLKLRKLHSRglLNLIAIDEAHCISSWGhdFRPSYRQLstLRDSLADVPVLALTATAAPKVQK 114
Cdd:pfam00270 95 PDILVGTPGRLLD---LLQERKLLKN--LKLLVLDEAHRLLDMG--FGPDLEEI--LRRLPKKRQILLLSATLPRNLED 164
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
20-142 |
3.69e-08 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 54.04 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 20 HVKNKIHEDLDSGKPSVrllyvtpeLIATKGFMLKLRKLHSRGL--LNLIAIDEAHCISSWGhdFRPSYRQLstLRDSLA 97
Cdd:smart00487 92 DSKREQLRKLESGKTDI--------LVTTPGRLLDLLENDKLSLsnVDLVILDEAHRLLDGG--FGDQLEKL--LKLLPK 159
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 30690466 98 DVPVLALTATAAPKVQKDVidSLNLRNPLVLKSSFnRPNIFYEVR 142
Cdd:smart00487 160 NVQLLLLSATPPEEIENLL--ELFLNDPVFIDVGF-TPLEPIEQF 201
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
163-265 |
7.31e-08 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains 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: 350189 [Multi-domain] Cd Length: 142 Bit Score: 51.82 E-value: 7.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 163 NICAIIYCLERTTCDDLS-------VHLSSI--------GISSAAYHAGLNSKMRSTVLDDWLSSKKQIIVATVAFGMGI 227
Cdd:cd18802 25 DFRGIIFVERRATAVVLSrllkehpSTLAFIrcgfligrGNSSQRKRSLMTQRKQKETLDKFRDGELNLLIATSVLEEGI 104
|
90 100 110
....*....|....*....|....*....|....*...
gi 30690466 228 DKKDVRMVCHFNIPKSMESFYQESGRAGRDQlpSRSVL 265
Cdd:cd18802 105 DVPACNLVIRFDLPKTLRSYIQSRGRARAPN--SKYIL 140
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
44-272 |
1.41e-07 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 54.41 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 44 ELI-ATKGFMLKLRKLHSRGLLNLI--AIDEAHCISSWGhdFRpsyRQLSTLRDSLADVPVLALTATAAPKVQKdVIDSL 120
Cdd:PLN00206 248 ELIvGTPGRLIDLLSKHDIELDNVSvlVLDEVDCMLERG--FR---DQVMQIFQALSQPQVLLFSATVSPEVEK-FASSL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 121 nLRNPLVLK-SSFNRPN-------IFYEVRYKDlldnayTDLGNLLKSCGNIC--AIIYCLERTTCDDLSVHLSSI-GIS 189
Cdd:PLN00206 322 -AKDIILISiGNPNRPNkavkqlaIWVETKQKK------QKLFDILKSKQHFKppAVVFVSSRLGADLLANAITVVtGLK 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 190 SAAYHAGLNSKMRSTVLDDWLSSKKQIIVATVAFGMGIDKKDVRMVCHFNIPKSMESFYQESGRAGRDQLPSRSVLYYGV 269
Cdd:PLN00206 395 ALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNE 474
|
...
gi 30690466 270 DDR 272
Cdd:PLN00206 475 EDR 477
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
66-256 |
1.85e-07 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 54.26 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 66 LIAIDEAHcisswgHDFRPSYRQLstlRDSLADVPVLALTATaaPkvqkdviDSLNLRNPLVlkssFNRPNIFYEVRYKD 145
Cdd:COG1061 190 LVIIDEAH------HAGAPSYRRI---LEAFPAAYRLGLTAT--P-------FRSDGREILL----FLFDGIVYEYSLKE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 146 LLD--------------------NAYTDLGNLL--------------------KSCGNICAIIYCLERTTCDDLSVHLSS 185
Cdd:COG1061 248 AIEdgylappeyygirvdltderAEYDALSERLrealaadaerkdkilrellrEHPDDRKTLVFCSSVDHAEALAELLNE 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30690466 186 IGISSAAYHAGLNSKMRSTVLDDWLSSKKQIIVATVAFGMGIDKKDVRMVCHFNIPKSMESFYQesgRAGR 256
Cdd:COG1061 328 AGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQ---RLGR 395
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
166-283 |
4.32e-07 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 52.93 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 166 AIIYCLERTTCDDLSVHLSSIGISSAAYHAGLNSKMRSTVLDDWLSSKKQIIVATVAFGMGIDKKDVRMVCHFNIPKSME 245
Cdd:PRK11634 248 AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSE 327
|
90 100 110
....*....|....*....|....*....|....*...
gi 30690466 246 SFYQESGRAGRDQLPSRSVLYygVDDRKKMeyLLRNSE 283
Cdd:PRK11634 328 SYVHRIGRTGRAGRAGRALLF--VENRERR--LLRNIE 361
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
166-256 |
9.06e-07 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 51.37 E-value: 9.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 166 AIIYCLERTTCDDLSVHLSSIGISSAAYHAGLNSKMRSTVLDDWLSSKKQIIVATVAFGMGIDKKDVRMVCHFNIPKSME 245
Cdd:PTZ00424 270 AIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPE 349
|
90
....*....|.
gi 30690466 246 SFYQESGRAGR 256
Cdd:PTZ00424 350 NYIHRIGRSGR 360
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
154-256 |
2.00e-06 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 50.93 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 154 LGNLLKSCGNIcaIIYCLERTTCDDLSVHLSSIGISSAAYHAGLNSKMRSTVLDDWLSSKKQIIVATVAFGMGIDKKDVR 233
Cdd:PTZ00110 370 LQRIMRDGDKI--LIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVK 447
|
90 100
....*....|....*....|...
gi 30690466 234 MVCHFNIPKSMESFYQESGRAGR 256
Cdd:PTZ00110 448 YVINFDFPNQIEDYVHRIGRTGR 470
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
167-256 |
1.11e-05 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 48.73 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 167 IIYCLERTTCDDLSvhlSSIGISSAAYHAGLNSKMRSTVLDDWLSSKKQIIVATVAFGMGIDkkdvrmvchFniPKS--- 243
Cdd:COG1202 431 IIFTNSRRRCHEIA---RALGYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVD---------F--PASqvi 496
|
90 100
....*....|....*....|....*
gi 30690466 244 ------------MESFYQESGRAGR 256
Cdd:COG1202 497 fdslamgiewlsVQEFHQMLGRAGR 521
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
166-259 |
1.84e-05 |
|
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: 45.24 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 166 AIIYCLERTTCDDLSVHLSSIGIssaaYHAGLNSKMRSTVLDDWLSSKKQIIVATVAFGMGidkkdVRMVCH-------- 237
Cdd:cd18795 46 VLVFCSSRKECEKTAKDLAGIAF----HHAGLTREDRELVEELFREGLIKVLVATSTLAAG-----VNLPARtviikgtq 116
|
90 100
....*....|....*....|....*...
gi 30690466 238 -FNiPKSME-----SFYQESGRAGRDQL 259
Cdd:cd18795 117 rYD-GKGYRelsplEYLQMIGRAGRPGF 143
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
37-107 |
1.56e-04 |
|
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: 42.39 E-value: 1.56e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30690466 37 RLLYVTPELIatkgFMLKLRKLHSRGL-LNLIAIDEAHCISSWGHDFRPSYrqLSTLRDSLADVPVLALTAT 107
Cdd:cd00046 81 DIIIATPDML----LNLLLREDRLFLKdLKLIIVDEAHALLIDSRGALILD--LAVRKAGLKNAQVILLSAT 146
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
179-283 |
1.58e-03 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 41.33 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690466 179 LSVHLSSIGISSAAYHAGLNSKMRSTVLDDWLSSKKQIIVATVAFGMGIDKKDVRMVCHFNIPKSMESFYQESGRAGRDQ 258
Cdd:PRK10590 261 LAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAA 340
|
90 100
....*....|....*....|....*
gi 30690466 259 LPSRSVLYYGVDDRKkmeyLLRNSE 283
Cdd:PRK10590 341 ATGEALSLVCVDEHK----LLRDIE 361
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
191-265 |
5.09e-03 |
|
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: 39.82 E-value: 5.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30690466 191 AAYHAGLNSKMRSTVLDDwLSSKK-QIIVATVAFGMGID--KKDVRMVCHFniPKSMESFYQESGRAGRDQLPSRSVL 265
Cdd:COG1205 322 AAYRAGYLPEERREIERG-LRSGElLGVVSTNALELGIDigGLDAVVLAGY--PGTRASFWQQAGRAGRRGQDSLVVL 396
|
|
| |
