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Conserved domains on  [gi|530399341|ref|XP_005253518|]
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ATP-dependent DNA helicase Q1 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

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 530399341   81 DILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISATM 160
Cdd:TIGR00614   1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  161 LNASSSKEHVKWVHAEMvnKNSELKLIYVTPEKIAKSKMFMSRLEkayEARRFTRIAVDEVHCCSQWGHDFRPDYKALGI 240
Cdd:TIGR00614  81 LNSAQTKEQQLNVLTDL--KDGKIKLLYVTPEKISASNRLLQTLE---ERKGITLIAVDEAHCISQWGHDFRPDYKALGS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  241 LKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFNRPNLYYEVRQKPSNtedFIEDIVKLINGRYKGQSGIIY 320
Cdd:TIGR00614 156 LKQKFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTPK---ILEDLLRFIRKEFEGKSGIIY 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  321 CFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQ 400
Cdd:TIGR00614 233 CPSRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQ 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  401 ESGRAGRDDMKADCILYYGFGDIFRISSMVVMENVGQQ-----KLYEMVSYCQNISKCRRVLMAQHFDEVWN-----SEA 470
Cdd:TIGR00614 313 ESGRAGRDGLPSECHLFYAPADMNRLRRLLMEEPDGNFrtyklKLYEMMEYCLNSSTCRRLILLSYFGEKGFnksfcIMG 392
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530399341  471 CNKMCDNCCKDSAFERKNITEYCRDLIKILKQAEE----LNEKLTPLKLIDSWMGKGAAKLRVAGVVAPTL-PREDLE 543
Cdd:TIGR00614 393 TEKCCDNCCKRLDYKTKDVTDKVYDFGPQAQKALSavgrLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLyGRGKDE 470
 
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 530399341   81 DILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISATM 160
Cdd:TIGR00614   1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  161 LNASSSKEHVKWVHAEMvnKNSELKLIYVTPEKIAKSKMFMSRLEkayEARRFTRIAVDEVHCCSQWGHDFRPDYKALGI 240
Cdd:TIGR00614  81 LNSAQTKEQQLNVLTDL--KDGKIKLLYVTPEKISASNRLLQTLE---ERKGITLIAVDEAHCISQWGHDFRPDYKALGS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  241 LKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFNRPNLYYEVRQKPSNtedFIEDIVKLINGRYKGQSGIIY 320
Cdd:TIGR00614 156 LKQKFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTPK---ILEDLLRFIRKEFEGKSGIIY 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  321 CFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQ 400
Cdd:TIGR00614 233 CPSRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQ 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  401 ESGRAGRDDMKADCILYYGFGDIFRISSMVVMENVGQQ-----KLYEMVSYCQNISKCRRVLMAQHFDEVWN-----SEA 470
Cdd:TIGR00614 313 ESGRAGRDGLPSECHLFYAPADMNRLRRLLMEEPDGNFrtyklKLYEMMEYCLNSSTCRRLILLSYFGEKGFnksfcIMG 392
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530399341  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 530399341  78 KVKDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGIS 157
Cdd:COG0514    4 DALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 158 ATMLNASSSKEHVKWVHAEMvnKNSELKLIYVTPEKIAKSKmFMSRLEKAyearRFTRIAVDEVHCCSQWGHDFRPDYKA 237
Cdd:COG0514   84 AAFLNSSLSAEERREVLRAL--RAGELKLLYVAPERLLNPR-FLELLRRL----KISLFAIDEAHCISQWGHDFRPDYRR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 238 LGILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFNRPNLYYEVRQKPSntEDFIEDIVKLINGRyKGQSG 317
Cdd:COG0514  157 LGELRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPP--DDKLAQLLDFLKEH-PGGSG 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 318 IIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMEN 397
Cdd:COG0514  234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEA 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 398 YYQESGRAGRDDMKADCILYYGFGDIFRISSMVVMEN-------VGQQKLYEMVSYCQnISKCRRVLMAQHFDEVwNSEA 470
Cdd:COG0514  314 YYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPpdeerkrVERAKLDAMLAYAE-TTGCRRQFLLRYFGEE-LAEP 391
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530399341 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 530399341  74 PWSGKVKDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQ 153
Cdd:cd18015    1 PWSGKVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 154 LGISATMLNASSSKEHVKWVHAEMVNKNSELKLIYVTPEKIAKSKMFMSRLEKAYEARRFTRIAVDEVHCCSQWGHDFRP 233
Cdd:cd18015   81 LGISATMLNASSSKEHVKWVHAALTDKNSELKLLYVTPEKIAKSKRFMSKLEKAYNAGRLARIAIDEVHCCSQWGHDFRP 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 530399341 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 530399341   63 SSPAAWNKEDFPWSGKVKDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLIS 142
Cdd:PLN03137  432 SNDKKWSSRNFPWTKKLEVNNKKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVS 511
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  143 LMEDQLMVLKQLGISATMLNASSSKEHVKWVHAEMVNKNSELKLIYVTPEKIAKSKMFMSRLEKAYEARRFTRIAVDEVH 222
Cdd:PLN03137  512 LIQDQIMNLLQANIPAASLSAGMEWAEQLEILQELSSEYSKYKLLYVTPEKVAKSDSLLRHLENLNSRGLLARFVIDEAH 591
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  223 CCSQWGHDFRPDYKALGILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFNRPNLYYEVRQKpsnTEDFIE 302
Cdd:PLN03137  592 CVSQWGHDFRPDYQGLGILKQKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPK---TKKCLE 668
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  303 DIVKLINGRYKGQSGIIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPD 382
Cdd:PLN03137  669 DIDKFIKENHFDECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPD 748
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  383 VRFVIHHSMSKSMENYYQESGRAGRDDMKADCILYYGFGDIFRISSMVVMENVGQ---------------------QKLY 441
Cdd:PLN03137  749 VRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMISQGGVEQspmamgynrmassgriletntENLL 828
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530399341  442 EMVSYCQNISKCRRVLMAQHFDEVWNSEACNKMCDNCCKDSAFERKNITEYCRDLIKILKQAEE 505
Cdd:PLN03137  829 RMVSYCENEVDCRRFLQLVHFGEKFDSTNCKKTCDNCSSSKSLIDKDVTEIARQLVELVKLTGE 892
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 530399341 105 AGKEVFLVMPTGGGKSLCYQLPALCS---DGFTLVICPLISL---MEDQLM-VLKQLGISATMLNA---SSSKEhvkwVH 174
Cdd:NF041063 157 PGSTLIVNLPTGSGKSLVAQAPALLAsrqGGLTLVVVPTVALaidQERRAReLLRRAGPDLGGPLAwhgGLSAE----ER 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 175 AEMVN--KNSELKLIYVTPEKIAKSkmFMSRLEKAYEARRFTRIAVDEVHCCSQWGHDFRPDYKALGILKRQFPNASLIG 252
Cdd:NF041063 233 AAIRQriRDGTQRILFTSPESLTGS--LRPALFDAAEAGLLRYLVVDEAHLVDQWGDGFRPEFQLLAGLRRSLLRLAPSG 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 253 -------LTATATNHVLTDAQKILCIEKCFT-FTASFNRPNLYYEVRQKPSnTEDFIEDIVKLIngRYKGQSGIIYCFSQ 324
Cdd:NF041063 311 rpfrtllLSATLTESTLDTLETLFGPPGPFIvVSAVQLRPEPAYWVAKCDS-EEERRERVLEAL--RHLPRPLILYVTKV 387
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 325 KDSEQVTVSLQNLGIH-AGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESG 403
Cdd:NF041063 388 EDAEAWLQRLRAAGFRrVALFHGDTPDAERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVG 467
                        330       340
                 ....*....|....*....|
gi 530399341 404 RAGRDDMKADCILYYGFGDI 423
Cdd:NF041063 468 RGGRDGKASLSLLIYTPDDL 487
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 530399341   93 RPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPAL------CSDGFTLVICPLISLMEDQLMVLKQLGISATMLNASSS 166
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  167 KEHVKWvhaEMVNKNSELKLIYVTPEKIAKskmfMSRLEKAYEARRFtrIAVDEVHCCSQWGhdFRPDYKAlgILKRQFP 246
Cdd:pfam00270  81 GGDSRK---EQLEKLKGPDILVGTPGRLLD----LLQERKLLKNLKL--LVLDEAHRLLDMG--FGPDLEE--ILRRLPK 147
                         170
                  ....*....|..
gi 530399341  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 530399341    87 FKLEKFRPLQLETINVTMAG-KEVFLVMPTGGGKSLCYQLPALC-----SDGFTLVICPLISLMEDQLMVLKQLGISATM 160
Cdd:smart00487   4 FGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEalkrgKGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341   161 LNASSSKEHVKWVHAEMVNKNsELKLIYVTPEkiakskMFMSRLEKAY-EARRFTRIAVDEVHCCSQWGhdFRPDYKalG 239
Cdd:smart00487  84 KVVGLYGGDSKREQLRKLESG-KTDILVTTPG------RLLDLLENDKlSLSNVDLVILDEAHRLLDGG--FGDQLE--K 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 530399341   240 ILKRQFPNASLIGLTATATNHVLTDAQKILciEKCFTFTASFnRPNLYYEVR 291
Cdd:smart00487 153 LLKLLPKNVQLLLLSATPPEEIENLLELFL--NDPVFIDVGF-TPLEPIEQF 201
 
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 530399341   81 DILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISATM 160
Cdd:TIGR00614   1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  161 LNASSSKEHVKWVHAEMvnKNSELKLIYVTPEKIAKSKMFMSRLEkayEARRFTRIAVDEVHCCSQWGHDFRPDYKALGI 240
Cdd:TIGR00614  81 LNSAQTKEQQLNVLTDL--KDGKIKLLYVTPEKISASNRLLQTLE---ERKGITLIAVDEAHCISQWGHDFRPDYKALGS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  241 LKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFNRPNLYYEVRQKPSNtedFIEDIVKLINGRYKGQSGIIY 320
Cdd:TIGR00614 156 LKQKFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTPK---ILEDLLRFIRKEFEGKSGIIY 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  321 CFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQ 400
Cdd:TIGR00614 233 CPSRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQ 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  401 ESGRAGRDDMKADCILYYGFGDIFRISSMVVMENVGQQ-----KLYEMVSYCQNISKCRRVLMAQHFDEVWN-----SEA 470
Cdd:TIGR00614 313 ESGRAGRDGLPSECHLFYAPADMNRLRRLLMEEPDGNFrtyklKLYEMMEYCLNSSTCRRLILLSYFGEKGFnksfcIMG 392
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530399341  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 530399341  78 KVKDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGIS 157
Cdd:COG0514    4 DALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 158 ATMLNASSSKEHVKWVHAEMvnKNSELKLIYVTPEKIAKSKmFMSRLEKAyearRFTRIAVDEVHCCSQWGHDFRPDYKA 237
Cdd:COG0514   84 AAFLNSSLSAEERREVLRAL--RAGELKLLYVAPERLLNPR-FLELLRRL----KISLFAIDEAHCISQWGHDFRPDYRR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 238 LGILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFNRPNLYYEVRQKPSntEDFIEDIVKLINGRyKGQSG 317
Cdd:COG0514  157 LGELRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPP--DDKLAQLLDFLKEH-PGGSG 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 318 IIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMEN 397
Cdd:COG0514  234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEA 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 398 YYQESGRAGRDDMKADCILYYGFGDIFRISSMVVMEN-------VGQQKLYEMVSYCQnISKCRRVLMAQHFDEVwNSEA 470
Cdd:COG0514  314 YYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPpdeerkrVERAKLDAMLAYAE-TTGCRRQFLLRYFGEE-LAEP 391
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530399341 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 530399341  74 PWSGKVKDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQ 153
Cdd:cd18015    1 PWSGKVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 154 LGISATMLNASSSKEHVKWVHAEMVNKNSELKLIYVTPEKIAKSKMFMSRLEKAYEARRFTRIAVDEVHCCSQWGHDFRP 233
Cdd:cd18015   81 LGISATMLNASSSKEHVKWVHAALTDKNSELKLLYVTPEKIAKSKRFMSKLEKAYNAGRLARIAIDEVHCCSQWGHDFRP 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 530399341 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 530399341   63 SSPAAWNKEDFPWSGKVKDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLIS 142
Cdd:PLN03137  432 SNDKKWSSRNFPWTKKLEVNNKKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVS 511
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  143 LMEDQLMVLKQLGISATMLNASSSKEHVKWVHAEMVNKNSELKLIYVTPEKIAKSKMFMSRLEKAYEARRFTRIAVDEVH 222
Cdd:PLN03137  512 LIQDQIMNLLQANIPAASLSAGMEWAEQLEILQELSSEYSKYKLLYVTPEKVAKSDSLLRHLENLNSRGLLARFVIDEAH 591
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  223 CCSQWGHDFRPDYKALGILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFNRPNLYYEVRQKpsnTEDFIE 302
Cdd:PLN03137  592 CVSQWGHDFRPDYQGLGILKQKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPK---TKKCLE 668
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  303 DIVKLINGRYKGQSGIIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPD 382
Cdd:PLN03137  669 DIDKFIKENHFDECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPD 748
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  383 VRFVIHHSMSKSMENYYQESGRAGRDDMKADCILYYGFGDIFRISSMVVMENVGQ---------------------QKLY 441
Cdd:PLN03137  749 VRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMISQGGVEQspmamgynrmassgriletntENLL 828
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530399341  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 530399341   80 KDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISAT 159
Cdd:TIGR01389   2 QQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAAA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  160 MLNASSSKEHVKwvHAEMVNKNSELKLIYVTPEkiakskmfmsRLEKAYEARRFTR-----IAVDEVHCCSQWGHDFRPD 234
Cdd:TIGR01389  82 YLNSTLSAKEQQ--DIEKALVNGELKLLYVAPE----------RLEQDYFLNMLQRipialVAVDEAHCVSQWGHDFRPE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  235 YKALGILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFNRPNLYYEVRQKpSNTEDFIEDIVKlingRYKG 314
Cdd:TIGR01389 150 YQRLGSLAERFPQVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKK-NNKQKFLLDYLK----KHRG 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  315 QSGIIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKS 394
Cdd:TIGR01389 225 QSGIIYASSRKKVEELAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGN 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  395 MENYYQESGRAGRDDMKADCILYYGFGDI----FRISSMVVMENVGQ---QKLYEMVSYCqNISKCRRVLMAQHFDEVwN 467
Cdd:TIGR01389 305 LESYYQEAGRAGRDGLPAEAILLYSPADIallkRRIEQSEADDDYKQierEKLRAMIAYC-ETQTCRRAYILRYFGEN-E 382
                         410
                  ....*....|.
gi 530399341  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 530399341  80 KDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISAT 159
Cdd:PRK11057  14 KQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAAA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 160 MLNASSSKEHVKWVHAEMvnKNSELKLIYVTPEKIAKSKmFMSRLEKAyearRFTRIAVDEVHCCSQWGHDFRPDYKALG 239
Cdd:PRK11057  94 CLNSTQTREQQLEVMAGC--RTGQIKLLYIAPERLMMDN-FLEHLAHW----NPALLAVDEAHCISQWGHDFRPEYAALG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 240 ILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFNRPNLYYEV--RQKPsntedfIEDIVKLINGRyKGQSG 317
Cdd:PRK11057 167 QLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLveKFKP------LDQLMRYVQEQ-RGKSG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 318 IIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMEN 397
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 398 YYQESGRAGRDDMKADCILYYGFGDIFRISSMVVMENVGQQ------KLYEMVSYCQnISKCRRVLMAQHFDEvWNSEAC 471
Cdd:PRK11057 320 YYQETGRAGRDGLPAEAMLFYDPADMAWLRRCLEEKPAGQQqdierhKLNAMGAFAE-AQTCRRLVLLNYFGE-GRQEPC 397

                 ....*..
gi 530399341 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 530399341  80 KDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISAT 159
Cdd:cd17920    1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 160 MLNASSSKEHVKWVHAEMvnKNSELKLIYVTPEKIAkSKMFMSRLEKAYEARRFTRIAVDEVHCCSQWGHDFRPDYKALG 239
Cdd:cd17920   81 ALNSTLSPEEKREVLLRI--KNGQYKLLYVTPERLL-SPDFLELLQRLPERKRLALIVVDEAHCVSQWGHDFRPDYLRLG 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 530399341 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 530399341 283 RPNLYYEVRQKPSNTEDFieDIVKLINGRYKGQSGIIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSA 362
Cdd:cd18794    1 RPNLFYSVRPKDKKDEKL--DLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLR 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530399341 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 530399341  76 SGKVKDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLG 155
Cdd:cd18016    2 SKEMMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 156 ISATMLNASSSKEHVKWVHAEMVNKNSELKLIYVTPEKIAKSKMFMSRLEKAYEARRFTRIAVDEVHCCSQWGHDFRPDY 235
Cdd:cd18016   82 IPATYLTGDKTDAEATKIYLQLSKKDPIIKLLYVTPEKISASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRPDY 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 530399341 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 530399341  82 ILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALC----SDGFTLVICPLISLMEDQLMVLKQLgIS 157
Cdd:cd18018    3 LLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLlrrrGPGLTLVVSPLIALMKDQVDALPRA-IK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 158 ATMLNaSSSKEHVKWVHAEMVNKNsELKLIYVTPEKIAkSKMFMSRLEkayEARRFTRIAVDEVHCCSQWGHDFRPDYKA 237
Cdd:cd18018   82 AAALN-SSLTREERRRILEKLRAG-EVKILYVSPERLV-NESFRELLR---QTPPISLLVVDEAHCISEWSHNFRPDYLR 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 530399341 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 530399341  81 DILQNVFKLEKFRPLQLETI-NVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISAT 159
Cdd:cd18017    2 NALNEYFGHSSFRPVQWKVIrSVLEERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPAC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 160 MLNASSSKEHVKwvhaemVNKNSELKLIYVTPEKIAKSKMFMSRLEKayearRFTRIAVDEVHCCSQWGHDFRPDYKALG 239
Cdd:cd18017   82 FLGSAQSQNVLD------DIKMGKIRVIYVTPEFVSKGLELLQQLRN-----GITLIAIDEAHCVSQWGHDFRSSYRHLG 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 530399341 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 530399341  80 KDILQNVFKLEKFR-PLQLETINVTMAGK-EVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGIS 157
Cdd:cd18014    1 RSTLKKVFGHSDFKsPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 158 ATMLNASSSKEHVKWVHAEMVNKNSELKLIYVTPEKiAKSKMFMSRLEKAYEARRFTRIAVDEVHCCSQWGHDFRPDYKA 237
Cdd:cd18014   81 VDSLNSKLSAQERKRIIADLESEKPQTKFLYITPEM-AATSSFQPLLSSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLR 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 530399341 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 530399341 105 AGKEVFLVMPTGGGKSLCYQLPALCS---DGFTLVICPLISL---MEDQLM-VLKQLGISATMLNA---SSSKEhvkwVH 174
Cdd:NF041063 157 PGSTLIVNLPTGSGKSLVAQAPALLAsrqGGLTLVVVPTVALaidQERRAReLLRRAGPDLGGPLAwhgGLSAE----ER 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 175 AEMVN--KNSELKLIYVTPEKIAKSkmFMSRLEKAYEARRFTRIAVDEVHCCSQWGHDFRPDYKALGILKRQFPNASLIG 252
Cdd:NF041063 233 AAIRQriRDGTQRILFTSPESLTGS--LRPALFDAAEAGLLRYLVVDEAHLVDQWGDGFRPEFQLLAGLRRSLLRLAPSG 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 253 -------LTATATNHVLTDAQKILCIEKCFT-FTASFNRPNLYYEVRQKPSnTEDFIEDIVKLIngRYKGQSGIIYCFSQ 324
Cdd:NF041063 311 rpfrtllLSATLTESTLDTLETLFGPPGPFIvVSAVQLRPEPAYWVAKCDS-EEERRERVLEAL--RHLPRPLILYVTKV 387
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 325 KDSEQVTVSLQNLGIH-AGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESG 403
Cdd:NF041063 388 EDAEAWLQRLRAAGFRrVALFHGDTPDAERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVG 467
                        330       340
                 ....*....|....*....|
gi 530399341 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 530399341 106 GKEVFLVMPTGGGKSLCYQLPALCSD----GFTLVICPLISLMEDQLMVLKQL---GISATMLNASSSKEHVKwvhaemV 178
Cdd:cd00046    1 GENVLITAPTGSGKTLAALLAALLLLlkkgKKVLVLVPTKALALQTAERLRELfgpGIRVAVLVGGSSAEERE------K 74
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530399341 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 530399341   93 RPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPAL------CSDGFTLVICPLISLMEDQLMVLKQLGISATMLNASSS 166
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  167 KEHVKWvhaEMVNKNSELKLIYVTPEKIAKskmfMSRLEKAYEARRFtrIAVDEVHCCSQWGhdFRPDYKAlgILKRQFP 246
Cdd:pfam00270  81 GGDSRK---EQLEKLKGPDILVGTPGRLLD----LLQERKLLKNLKL--LVLDEAHRLLDMG--FGPDLEE--ILRRLPK 147
                         170
                  ....*....|..
gi 530399341  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 530399341    87 FKLEKFRPLQLETINVTMAG-KEVFLVMPTGGGKSLCYQLPALC-----SDGFTLVICPLISLMEDQLMVLKQLGISATM 160
Cdd:smart00487   4 FGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEalkrgKGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341   161 LNASSSKEHVKWVHAEMVNKNsELKLIYVTPEkiakskMFMSRLEKAY-EARRFTRIAVDEVHCCSQWGhdFRPDYKalG 239
Cdd:smart00487  84 KVVGLYGGDSKREQLRKLESG-KTDILVTTPG------RLLDLLENDKlSLSNVDLVILDEAHRLLDGG--FGDQLE--K 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 530399341   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 530399341   328 EQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGR 407
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   .
gi 530399341   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 530399341  301 IEDIVKLINGRYKGQSgIIYCFSQKDSEqVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDK 380
Cdd:pfam00271   3 LEALLELLKKERGGKV-LIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
                          90       100
                  ....*....|....*....|....*..
gi 530399341  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 530399341  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 530399341 111 LVMPTGGGKSL----CYQlpALCSDGFTLVICPLISLMEdQLM--VLKQLGISATMLNASSSKEHVkwvhaemvnknsel 184
Cdd:COG1061  105 VVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLE-QWAeeLRRFLGDPLAGGGKKDSDAPI-------------- 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 185 klIYVTPEKIAKSKMFmSRLEkayeaRRFTRIAVDEVHccsqwgHDFRPDYKAlgILKRqFPNASLIGLTAT----ATNH 260
Cdd:COG1061  168 --TVATYQSLARRAHL-DELG-----DRFGLVIIDEAH------HAGAPSYRR--ILEA-FPAAYRLGLTATpfrsDGRE 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 261 VLTD---------------AQKILCIEKCFTFTASFNRPNLYYEVRQKP------SNTEDFIEDIVKLINGRYKGQSGII 319
Cdd:COG1061  231 ILLFlfdgivyeyslkeaiEDGYLAPPEYYGIRVDLTDERAEYDALSERlrealaADAERKDKILRELLREHPDDRKTLV 310
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 320 YCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYY 399
Cdd:COG1061  311 FCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFI 390
                        330       340
                 ....*....|....*....|..
gi 530399341 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 530399341 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 530399341  96 QLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCS-----DGFTLVICPLISLMEDQLMVLKQL------GISATMLNAS 164
Cdd:COG1205   61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAlledpGATALYLYPTKALARDQLRRLRELaealglGVRVATYDGD 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 165 SSKEHVKWV--HAEmvnknselkLIYVTPEKI--------AKSKMFMSRLekayearRFtrIAVDEVHCcsqwghdfrpd 234
Cdd:COG1205  141 TPPEERRWIreHPD---------IVLTNPDMLhygllphhTRWARFFRNL-------RY--VVIDEAHT----------- 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 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 530399341 286 LYYEVRQKPSNTE--DFIEDIVKlingryKGQSGIIYCFSQKDSEQVTVSLQN------LGIHAGAYHANLEPEDKTTVH 357
Cdd:COG1205  264 LVDDGIRRSALAEaaRLLADLVR------EGLRTLVFTRSRRGAELLARYARRalrepdLADRVAAYRAGYLPEERREIE 337
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 530399341 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 530399341 286 LYYEVrqkpsNTEDFIEDIVKLINGRYKGQSGIIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEI 365
Cdd:cd18787    4 LYVVV-----EEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKV 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 530399341 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 530399341 287 YYEVRQKPSNTEDFIEDIVKLINGRYKGQSgIIYCFSQKDSEQVTVSLQNLGIHagayHANLEPEDKTTVHRKWSANEIQ 366
Cdd:cd18795   17 IKLRVDVMNKFDSDIIVLLKIETVSEGKPV-LVFCSSRKECEKTAKDLAGIAFH----HAGLTREDRELVEELFREGLIK 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530399341 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 530399341 287 YYEVRQKpsnteDFIEDIVKLINgRYKGQSGIIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQ 366
Cdd:COG0513  220 YYLVDKR-----DKLELLRRLLR-DEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIR 293
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 530399341 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 530399341 241 LKRQFPNASLIGLTATATN-HVLtdAQKILC-----------IEKCFTFTASFNRPNLYYE-VRQKPSNTEDFiedivkl 307
Cdd:COG1202  354 LKYYCPGAQWIYLSATVGNpEEL--AKKLGAklveyeerpvpLERHLTFADGREKIRIINKlVKREFDTKSSK------- 424
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 308 inGrYKGQSgIIYCFSQKDSEQVTvslQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRfVI 387
Cdd:COG1202  425 --G-YRGQT-IIFTNSRRRCHEIA---RALGYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQ-VI 496
                        170       180
                 ....*....|....*....|....*...
gi 530399341 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 530399341 318 IIYCFSQKDSEQVTVSLQNLGIHAG-------AYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHS 390
Cdd:cd18797   39 IVFCRSRKLAELLLRYLKARLVEEGplaskvaSYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
                         90       100
                 ....*....|....*....|..
gi 530399341 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 530399341  75 WSGKVKDILQNvFKLEKFRPLQLETI-NVTMAGKEVFLVMPTGGGKSLCYQLP---ALCSDGFTLVICPLISL---MEDQ 147
Cdd:COG1204    7 PLEKVIEFLKE-RGIEELYPPQAEALeAGLLEGKNLVVSAPTASGKTLIAELAilkALLNGGKALYIVPLRALaseKYRE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 148 LM-VLKQLGISATMlnasSSKEHVkwVHAEMVNKNSelklIYV-TPEKiakskmFMSRLEKAYE-ARRFTRIAVDEVHcc 224
Cdd:COG1204   86 FKrDFEELGIKVGV----STGDYD--SDDEWLGRYD----ILVaTPEK------LDSLLRNGPSwLRDVDLVVVDEAH-- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 225 sQWGHDFR-PDYK-ALGILKRQFPNASLIGLTATATNhvltdAQKILCIEKCFTFTASFnRPN-----LYY----EVRQK 293
Cdd:COG1204  148 -LIDDESRgPTLEvLLARLRRLNPEAQIVALSATIGN-----AEEIAEWLDAELVKSDW-RPVplnegVLYdgvlRFDDG 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 294 PSNTEDFIEDIV-KLINGRykGQSgIIYCFSQKDSEQ-----------------------VTVSLQNLGIHAG------- 342
Cdd:COG1204  221 SRRSKDPTLALAlDLLEEG--GQV-LVFVSSRRDAESlakkladelkrrltpeereeleeLAEELLEVSEETHtneklad 297
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530399341 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 530399341 318 IIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMEN 397
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
                         90
                 ....*....|
gi 530399341 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 530399341  96 QLETINVTMAGKEVFLVMPTGGGKSLCYQLP---ALCSDGFT--LVICPLISLMEDQLMVLKQL------GISATMLNAS 164
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPileALLRDPGSraLYLYPTKALAQDQLRSLRELleqlglGIRVATYDGD 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530399341 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 530399341  94 PLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALC----------SDG-FTLVICPLISLMEDqlmvlkqlgISATMLN 162
Cdd:PTZ00110 155 PIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVhinaqpllryGDGpIVLVLAPTRELAEQ---------IREQCNK 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 163 -ASSSKEHVKWVHAEMVNKNSELKLIYVTPEKIAKSKMFMSRLEKAY-EARRFTRIAVDEVHCCSQWGhdFRPDYKAlgI 240
Cdd:PTZ00110 226 fGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVtNLRRVTYLVLDEADRMLDMG--FEPQIRK--I 301
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 241 LKRQFPNASLIGLTATATNHVLTDAQKiLCIEK-------CFTFTASFN-RPNLY-YEVRQKPSNTEDFIEDIVKlingr 311
Cdd:PTZ00110 302 VSQIRPDRQTLMWSATWPKEVQSLARD-LCKEEpvhvnvgSLDLTACHNiKQEVFvVEEHEKRGKLKMLLQRIMR----- 375
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 312 yKGQSGIIYCFSQKDSEQVTVSLQNLGIHAGAYHAnlepeDKTTVHRKWSANEIQ-----VVVATVAFGMGIDKPDVRFV 386
Cdd:PTZ00110 376 -DGDKILIFVETKKGADFLTKELRLDGWPALCIHG-----DKKQEERTWVLNEFKtgkspIMIATDVASRGLDVKDVKYV 449
                        330       340
                 ....*....|....*....|....*
gi 530399341 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 530399341   91 KFRPLQLETINVTMAG-----KEVFLVMPTGGGKSLCY-QLPALCSDGF----TLVICPLISLMEDQLMVLKQLGISATM 160
Cdd:pfam04851   3 ELRPYQIEAIENLLESikngqKRGLIVMATGSGKTLTAaKLIARLFKKGpikkVLFLVPRKDLLEQALEEFKKFLPNYVE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  161 LNASSSKEhvkwvhaEMVNKNSELKLIYVTPEKIAKSKMfMSRLEKAYEARRFtrIAVDEVHccsqwgHDFRPDYKAlgi 240
Cdd:pfam04851  83 IGEIISGD-------KKDESVDDNKIVVTTIQSLYKALE-LASLELLPDFFDV--IIIDEAH------RSGASSYRN--- 143
                         170
                  ....*....|....*.
gi 530399341  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 530399341  484 FERKNITEYCRDLIKILKqaeELNEKLTPLKLID--------SWMGKGAAKLRVAGVVAPtLPREDLEKIIAHFLIQQYL 555
Cdd:pfam09382   2 PETVDVTEEAQKILSCVY---RTGQRFGAGHLIDvlrgsknkKIRQLGHDKLSTFGIGKD-LSKKEWRRIIRQLIAEGYL 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 530399341  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 530399341  92 FRPLQLETINVTM-AGKEVFLVMPTGGGKSLCYQLPAL----CSDGFTLVICPLISLMEDQLM----VLKQLGISATMLN 162
Cdd:cd17921    2 LNPIQREALRALYlSGDSVLVSAPTSSGKTLIAELAILralaTSGGKAVYIAPTRALVNQKEAdlreRFGPLGKNVGLLT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 163 ASSSkehvkwvhaemVNKNSELKL-IYV-TPEKIAkskmFMSRLEKAYEARRFTRIAVDEVHCCSQwghdfrPDYKA--- 237
Cdd:cd17921   82 GDPS-----------VNKLLLAEAdILVaTPEKLD----LLLRNGGERLIQDVRLVVVDEAHLIGD------GERGVvle 140
                        170       180
                 ....*....|....*....|....
gi 530399341 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 530399341  92 FRPLQLETINVtMAGKEVF----LVMPTGGGKSLC-YQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISATMLNASSS 166
Cdd:cd17926    1 LRPYQEEALEA-WLAHKNNrrgiLVLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFEDFLGDSSIGLIGGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 167 KehvkwvhaemvNKNSELKLIYV-TPEKIakskmfmSRLEKAYEA--RRFTRIAVDEVH--CCSQWGHdfrpdykalgIL 241
Cdd:cd17926   80 K-----------KKDFDDANVVVaTYQSL-------SNLAEEEKDlfDQFGLLIVDEAHhlPAKTFSE----------IL 131
                        170
                 ....*....|....*
gi 530399341 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 530399341 345 HANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVR-FVIHHSMSKSMENYYQESGRAGRDDMKADCILYYGfgdi 423
Cdd:cd18811   68 HGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATvMVIEDAERFGLSQLHQLRGRVGRGDHQSYCLLVYK---- 143
                         90       100
                 ....*....|....*....|..
gi 530399341 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 530399341 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 530399341   9 EELDSITSELHAVEIQIQELTERQQELIQKKKVLTKKIKQCLEDSDAGASNEYDSSPAAWnkeDFPWSGKVKDILQNVFK 88
Cdd:COG1203   47 LLLAALELALLLLLLLLLLLLLLLLLLDLLLDDLAFLFLLLLIDADWLDSANFDMARQAL---DHLLAERLERLLPKKSK 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341  89 LEKFR-PLQLE----TINVTMAGKEVFLVM-PTGGGK---SLCY---QLPALCSDGFTLVIcPLISLMEDQLMVLKQLG- 155
Cdd:COG1203  124 PRTPInPLQNEalelALEAAEEEPGLFILTaPTGGGKteaALLFalrLAAKHGGRRIIYAL-PFTSIINQTYDRLRDLFg 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 156 --I----SATMLNASSSKEHVKWVHAEMVNkNSEL---KLIYVTPEKIAKSkMFMSRleKAYEaRRFTRIA-----VDEV 221
Cdd:COG1203  203 edVllhhSLADLDLLEEEEEYESEARWLKL-LKELwdaPVVVTTIDQLFES-LFSNR--KGQE-RRLHNLAnsviiLDEV 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 222 HCCSQwgHDFRPDYKALGILKRQfpNASLIGLTAT---ATNHVLTDAQKILCIEKC--FTFTASFNRPNlyYEVRQKPSN 296
Cdd:COG1203  278 QAYPP--YMLALLLRLLEWLKNL--GGSVILMTATlppLLREELLEAYELIPDEPEelPEYFRAFVRKR--VELKEGPLS 351
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 297 TEDFIEDIVKLINgryKGQSGIIYCFSQKDSEQVTVSLQNLGIHAGAY--HANLEPEDKTTVHRKW----SANEIQVVVA 370
Cdd:COG1203  352 DEELAELILEALH---KGKSVLVIVNTVKDAQELYEALKEKLPDEEVYllHSRFCPADRSEIEKEIkerlERGKPCILVS 428

                 .
gi 530399341 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 530399341  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 530399341 327 SEQVTVSLqnlGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAG 406
Cdd:PLN00206 384 ANAITVVT---GLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRAS 460
                         90
                 ....*....|.
gi 530399341 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 530399341 106 GKEVFLVMPTGGGKSLCYQL---PALCSDGFTLVICPLISLMEDQLMVLKQL-------GISATMLNassskEHVKWVHa 175
Cdd:cd18028   17 GENLLISIPTASGKTLIAEMamvNTLLEGGKALYLVPLRALASEKYEEFKKLeeiglkvGISTGDYD-----EDDEWLG- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 176 emvnknsELKLIYVTPEKIAkskmFMSRLEKAYeARRFTRIAVDEVHCCSqwghdfrpDYK-------ALGILKRQFPNA 248
Cdd:cd18028   91 -------DYDIIVATYEKFD----SLLRHSPSW-LRDVGVVVVDEIHLIS--------DEErgptlesIVARLRRLNPNT 150
                        170
                 ....*....|.
gi 530399341 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 530399341  76 SGKVKDILQNvFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPAL 128
Cdd:cd17953   20 SEKVLDLIKK-LGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMF 71
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
293-407 4.51e-03

C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 38.01  E-value: 4.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399341 293 KPSNTEDFIEDIVKLINgryKGQSGIIYCFSQKDSEQVTVSLQNL------GIHAGAYHANLEPEDKTTVHRKWSANEIQ 366
Cdd:cd18796   20 AGESGADAYAEVIFLLE---RHKSTLVFTNTRSQAERLAQRLRELcpdrvpPDFIALHHGSLSRELREEVEAALKRGDLK 96
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 530399341 367 VVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGR 407
Cdd:cd18796   97 VVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
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

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 530399341 345 HANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVR-FVIHHSMSKSMENYYQESGRAGRDDMKADCILYYG 419
Cdd:cd18792   67 HGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANtMIIEDADRFGLSQLHQLRGRVGRGKHQSYCYLLYP 142
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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