|
Name |
Accession |
Description |
Interval |
E-value |
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
665-1148 |
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: 805.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 665 KIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTIVISPLRSLIVDQVQKLTSFDIPATY 744
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 745 LTGDKTDSEAANIYLQLskKDPIIKLLYVTPEKVCASNRLISTLEnlyERKLLARFVIDEAHCVSQWGHDFRQDYKRMNM 824
Cdd:TIGR00614 81 LNSAQTKEQQLNVLTDL--KDGKIKLLYVTPEKISASNRLLQTLE---ERKGITLIAVDEAHCISQWGHDFRPDYKALGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 825 LRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFNRHNLKYYVLPKKPkKVAFDCLEWIRKHHPYDSGIIYCL 904
Cdd:TIGR00614 156 LKQKFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTP-KILEDLLRFIRKEFEGKSGIIYCP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 905 SRRECDTMADTLQREGLAALAYHAGLSDSARDEVQHKWInQDNCQVICATIAFGMGIDKPDVRFVIHASLPKSMEGYYQE 984
Cdd:TIGR00614 235 SRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQ-RDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 985 SGRAGRDGEISHCVLFYTYHDVTRLKRLIMMEKDGNyhtKETHVNNLYSMVHYCENITECRRIQLLAYFGEKGFNPDFCK 1064
Cdd:TIGR00614 314 SGRAGRDGLPSECHLFYAPADMNRLRRLLMEEPDGN---FRTYKLKLYEMMEYCLNSSTCRRLILLSYFGEKGFNKSFCI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 1065 KYPDVSCDNCCKTKDYKTKDVTDDVKNIIRFVQEHSSSPGTRNigpaGRFTLNMLVDIFLGSKSAKVKSGIFGKGTTYSR 1144
Cdd:TIGR00614 391 MGTEKCCDNCCKRLDYKTKDVTDKVYDFGPQAQKALSAVGRLN----QKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGR 466
|
....
gi 110225360 1145 HNAE 1148
Cdd:TIGR00614 467 GKDE 470
|
|
| BLM_N |
pfam16202 |
N-terminal region of Bloom syndrome protein; BLM_N is the very N-terminal region of chordate ... |
1-368 |
0e+00 |
|
N-terminal region of Bloom syndrome protein; BLM_N is the very N-terminal region of chordate Bloom syndrome proteins. The exact function is not known.
Pssm-ID: 465064 Cd Length: 370 Bit Score: 564.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 1 MAAVPLNNLQEQLQRHSARKLNNQPSLSKPKSLGFTFKKKTSEG-DVSVTSVSVVKTPALSDKDVNVSEAFSFTESPLHK 79
Cdd:pfam16202 1 MAAVPQNNLQEQLERHSARKLNNKLSLSKPKSSGFTFKKKTSSGnDVSVTSVSVAKTPVLSDKDVNVTEAFSFSEPLPHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 80 PKQQAKIEGFFKHFPGRQQSKGTCSEPSLPATVQTAQDTLCTTPKTPTAKKLPVAVFKKLEFSSSADS---LSDWADMDD 156
Cdd:pfam16202 81 TNQQTRINDFFKNAPAGQQTKRAGSKPLLPDSSQTPQEVSCTTQVTPAVKKPPDAVFKKLEFSSSFDSfisLNDWDDMDD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 157 FDMSA-SDAFASLAKNPATRVSTAQKMKKTKRNFFKPPPRKANAVKTDLTPPSPECLQVDLTKESEEEeeeeeeaegADC 235
Cdd:pfam16202 161 FDTSGnSKAFVTPPRNHFVRVSTAQKSKKSKRNFSKAQLSKANTVKADLTPSSGESKQVDLTKEQLDD---------SEW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 236 LSRDVICIDNDSASEELTEKDTQESQSLKAHLGAERGDSEKKSHEDEAVFHSVQNTEYFEHNDNDYDIDFVPPSPEE-II 314
Cdd:pfam16202 232 LSSDVICIDDDPISEELINEDTQESHSLKTHLGDERDNSEKKKHLEETELHSVEKSPCVELNEDDYDIDFVPPSPEEeVI 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 110225360 315 STASSSLKCSSMLKDLDDSDKEKGILSTSEELLSKPEEMTTHKSDAGTSKDCDA 368
Cdd:pfam16202 312 SSSSSSLKCFSMLKDLDTSDKEKDGLSTSEDLLSKPEKMTTQQPDQETSTDCDA 365
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
662-1142 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 555.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 662 EMMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTIVISPLRSLIVDQVQKLTSFDIP 741
Cdd:COG0514 4 DALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 742 ATYLTGDKTDSEAANIYLQLSKKDpiIKLLYVTPEkvcasnRLIS--TLENLYERKLlARFVIDEAHCVSQWGHDFRQDY 819
Cdd:COG0514 84 AAFLNSSLSAEERREVLRALRAGE--LKLLYVAPE------RLLNprFLELLRRLKI-SLFAIDEAHCISQWGHDFRPDY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 820 KRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFNRHNLKYYVLPKKPKKVAFDCLEWIRKHHPyDSG 899
Cdd:COG0514 155 RRLGELRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPPDDKLAQLLDFLKEHPG-GSG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 900 IIYCLSRRECDTMADTLQREGLAALAYHAGLSDSARDEVQHKWINqDNCQVICATIAFGMGIDKPDVRFVIHASLPKSME 979
Cdd:COG0514 234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLR-DEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 980 GYYQESGRAGRDGEISHCVLFYTYHDVTRLKRLImMEKDGNYHTKETHVNNLYSMVHYCEnITECRRIQLLAYFGEKGFN 1059
Cdd:COG0514 313 AYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFI-EQSPPDEERKRVERAKLDAMLAYAE-TTGCRRQFLLRYFGEELAE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 1060 PdfCKKypdvsCDNCCKTKdyKTKDVTDDVKNIIRFVqehssspgtRNIGPagRFTLNMLVDIFLGSKSAKVKSGIFGKG 1139
Cdd:COG0514 391 P--CGN-----CDNCLGPP--ETFDGTEAAQKALSCV---------YRTGQ--RFGAGHVIDVLRGSKNEKIRQFGHDKL 450
|
...
gi 110225360 1140 TTY 1142
Cdd:COG0514 451 STY 453
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
643-1284 |
5.88e-160 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 514.06 E-value: 5.88e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 643 SSKNPKhehFQSLNFPHTKEMMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTIVIS 722
Cdd:PLN03137 431 GSNDKK---WSSRNFPWTKKLEVNNKKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVIS 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 723 PLRSLIVDQVQKLTSFDIPATYLTGDKTDSEAANIYLQLSKKDPIIKLLYVTPEKVCASNRLISTLENLYERKLLARFVI 802
Cdd:PLN03137 508 PLVSLIQDQIMNLLQANIPAASLSAGMEWAEQLEILQELSSEYSKYKLLYVTPEKVAKSDSLLRHLENLNSRGLLARFVI 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 803 DEAHCVSQWGHDFRQDYKRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFNRHNLKYYVLPKKPKkv 882
Cdd:PLN03137 588 DEAHCVSQWGHDFRPDYQGLGILKQKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKK-- 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 883 afdCLE----WIRKHHPYDSGIIYCLSRRECDTMADTLQREGLAALAYHAGLSDSARDEVQHKWiNQDNCQVICATIAFG 958
Cdd:PLN03137 666 ---CLEdidkFIKENHFDECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQW-SKDEINIICATVAFG 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 959 MGIDKPDVRFVIHASLPKSMEGYYQESGRAGRDGEISHCVLFYTYHDVTRLKRLIMMEKDGNYHTK-------------E 1025
Cdd:PLN03137 742 MGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMISQGGVEQSPMAmgynrmassgrilE 821
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 1026 THVNNLYSMVHYCENITECRRIQLLAYFGEKgFNPDFCKKypdvSCDNCCKTKDYKTKDVTDDVKNIIRFVQEhssspgT 1105
Cdd:PLN03137 822 TNTENLLRMVSYCENEVDCRRFLQLVHFGEK-FDSTNCKK----TCDNCSSSKSLIDKDVTEIARQLVELVKL------T 890
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 1106 RNigpagRFTLNMLVDIFLGSKSAKVKS------GIFGKGTTYSRHNAERLFKKLILDKILDEDLYINANDQPIAYVML- 1178
Cdd:PLN03137 891 GE-----RFSSAHILEVYRGSLNQYVKKhrhetlSLHGAGKHLSKGEASRILHYLVTEDILAEDVKKSDLYGSVSSLLKv 965
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 1179 -GTKAHSVLSGHLKV--DFMETENSSSIKKQKALVAKVS--------------QREEVVKKCLGELTEVCKLLGKVF--- 1238
Cdd:PLN03137 966 nESKAYKLFSGGQTIimRFPSSVKASKPSKFEATPAKGPltsgkqstlpmatpAQPPVDLNLSAILYTALRKLRTALvke 1045
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 110225360 1239 ---GVHYFNIFNTATLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVI 1284
Cdd:PLN03137 1046 agdGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKAKVSKYGDRLL 1094
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
659-866 |
2.11e-147 |
|
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: 446.20 E-value: 2.11e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 659 HTKEMMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTIVISPLRSLIVDQVQKLTSF 738
Cdd:cd18016 1 HSKEMMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 739 DIPATYLTGDKTDSEAANIYLQLSKKDPIIKLLYVTPEKVCASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRQD 818
Cdd:cd18016 81 DIPATYLTGDKTDAEATKIYLQLSKKDPIIKLLYVTPEKISASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 110225360 819 YKRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFN 866
Cdd:cd18016 161 YKRLNMLRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| BDHCT_assoc |
pfam16204 |
BDHCT-box associated domain on Bloom syndrome protein; This family is found on Bloom ... |
430-655 |
1.41e-109 |
|
BDHCT-box associated domain on Bloom syndrome protein; This family is found on Bloom syndrome-associated DEAD-box helicases in higher eukaryotes. It lies between the BDHCT, and DEAD-box families, pfam08072 and pfam00270.
Pssm-ID: 465065 Cd Length: 223 Bit Score: 345.25 E-value: 1.41e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 430 GSLWRHRPDSLDNTVQGDSCPVGHPNKELNSPYLLSHSPSTEECLPTTTPGKTGFSATPKNLFERPLLNSHLQKSFVSSN 509
Cdd:pfam16204 1 GSVWRCRPDSLGSPVKGDSCPTGNSVKELNFPHLPSNSLSTGECLLTTTPGKTGFSATTKNLSERPLFSSHLQKSFVSSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 510 WAETPRMENRNESTDFPGSVLTSTTVKAQSKQAASGWNVERHGQASYDIDNFNIDDFdddDDDDDWENIMHNFPASKSST 589
Cdd:pfam16204 81 WAETPRTEKRNESSYFPGNVLTSTAVKDQNKHTASVNDLEREIQASCDIDNFDIDDF---DDDDDWENIMHNLAASKSST 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110225360 590 ATYPPIKEGGPVKSLSERISSAKAKFLPVVSTAQNTNLSESIQNCSDKLAQNLSSKNPKHEHFQSL 655
Cdd:pfam16204 158 AAYQPIKEGGPVKSVSERISSAKTNCLPVASTAQNKNFSESIQNYTDKSAQNLASRNLKHEHFQSL 223
|
|
| DpdF |
NF041063 |
protein DpdF; |
680-1017 |
1.96e-49 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 190.12 E-value: 1.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 680 QLEAINAALL---GEDCFILMPTGGGKSLCYQLPACVSP---GVTIVISPLRSLIVDQVQKLTSF-------DIPATYLT 746
Cdd:NF041063 145 QREAVRAALLappGSTLIVNLPTGSGKSLVAQAPALLASrqgGLTLVVVPTVALAIDQERRARELlrragpdLGGPLAWH 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 747 GDKTDSEAANIYLQLskKDPIIKLLYVTPEKVCASnrLISTLENLYERKLLARFVIDEAHCVSQWGHDFRQDYKRMNMLR 826
Cdd:NF041063 225 GGLSAEERAAIRQRI--RDGTQRILFTSPESLTGS--LRPALFDAAEAGLLRYLVVDEAHLVDQWGDGFRPEFQLLAGLR 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 827 QKFPSVP-------VMALTATanprvqkdiLTQ-----LKIL-----RPQVFSMSFNRHNLKYYVLPKKPKKVAFDC-LE 888
Cdd:NF041063 301 RSLLRLApsgrpfrTLLLSAT---------LTEstldtLETLfgppgPFIVVSAVQLRPEPAYWVAKCDSEEERRERvLE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 889 WIRkhH---PYdsgIIYCLSRRECDTMADTLQREGLAALA-YHAGLSDSARDEVQHKWiNQDNCQVICATIAFGMGIDKP 964
Cdd:NF041063 372 ALR--HlprPL---ILYVTKVEDAEAWLQRLRAAGFRRVAlFHGDTPDAERERLIEQW-RENELDIVVATSAFGLGMDKS 445
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 110225360 965 DVRFVIHASLPKSMEGYYQESGRAGRDGEISHCVLFYTYHDVT---RL--KRLIMMEK 1017
Cdd:NF041063 446 DVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDiakSLnrPKLISVEK 503
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
677-849 |
3.86e-30 |
|
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: 117.73 E-value: 3.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 677 RTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPAC------VSPGVTIVISPLRSLIVDQVQKLTSFDIPATY-----L 745
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGLkvaslL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 746 TGDKTDSEAANIylqlsKKdpiIKLLYVTPEKVCASNRLISTLENLyerKLLarfVIDEAHCVSQWGhdFRQDYKRmnML 825
Cdd:pfam00270 81 GGDSRKEQLEKL-----KG---PDILVGTPGRLLDLLQERKLLKNL---KLL---VLDEAHRLLDMG--FGPDLEE--IL 142
|
170 180
....*....|....*....|....
gi 110225360 826 RQKFPSVPVMALTATAnPRVQKDI 849
Cdd:pfam00270 143 RRLPKKRQILLLSATL-PRNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
669-849 |
1.23e-23 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 100.26 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 669 KKFGLHNFRTNQLEAINAALLGE-DCFILMPTGGGKSLCYQLPA-----CVSPGVTIVISPLRSLIVDQVQKLTSF---- 738
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPAlealkRGKGGRVLVLVPTRELAEQWAEELKKLgpsl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 739 -DIPATYLTGDKTDSEAANIylqlskKDPIIKLLYVTPEKVcasnrLISTLENLYERKLLARFVIDEAHCVSQWGhdFRQ 817
Cdd:smart00487 82 gLKVVGLYGGDSKREQLRKL------ESGKTDILVTTPGRL-----LDLLENDKLSLSNVDLVILDEAHRLLDGG--FGD 148
|
170 180 190
....*....|....*....|....*....|..
gi 110225360 818 DYKRmnMLRQKFPSVPVMALTATANPRVQKDI 849
Cdd:smart00487 149 QLEK--LLKLLPKNVQLLLLSATPPEEIENLL 178
|
|
| BDHCT |
pfam08072 |
BDHCT (NUC031) domain; This is a C-terminal domain in Bloom's syndrome DEAD helicase subfamily. |
379-417 |
8.60e-20 |
|
BDHCT (NUC031) domain; This is a C-terminal domain in Bloom's syndrome DEAD helicase subfamily.
Pssm-ID: 462356 Cd Length: 41 Bit Score: 83.48 E-value: 8.60e-20
10 20 30
....*....|....*....|....*....|....*....
gi 110225360 379 HVMEHICKLVDTVPTDELEALNCGTELLQQRNIRRKLLA 417
Cdd:pfam08072 3 SVMEEICKLVDTIPIHELKALSCGNELLQQRDIRRKLLA 41
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
1218-1294 |
6.18e-18 |
|
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the HRDC domain cause human disease.
Pssm-ID: 128635 [Multi-domain] Cd Length: 81 Bit Score: 79.65 E-value: 6.18e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110225360 1218 EVVKKCLGELTEVCKLLGKVFGVHYFNIFNTATLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVIPVLQKYSEWT 1294
Cdd:smart00341 2 ERQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEASDSP 78
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
1221-1287 |
8.23e-12 |
|
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic acid binding. Mutations in the HRDC domain cause human disease. It is interesting to note that the RecQ helicase in Deinococcus radiodurans has three tandem HRDC domains.
Pssm-ID: 425755 [Multi-domain] Cd Length: 68 Bit Score: 61.78 E-value: 8.23e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110225360 1221 KKCLGELTEVCKLLGKVFGVHYFNIFNTATLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVIPVL 1287
Cdd:pfam00570 2 LALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
665-1148 |
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: 805.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 665 KIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTIVISPLRSLIVDQVQKLTSFDIPATY 744
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 745 LTGDKTDSEAANIYLQLskKDPIIKLLYVTPEKVCASNRLISTLEnlyERKLLARFVIDEAHCVSQWGHDFRQDYKRMNM 824
Cdd:TIGR00614 81 LNSAQTKEQQLNVLTDL--KDGKIKLLYVTPEKISASNRLLQTLE---ERKGITLIAVDEAHCISQWGHDFRPDYKALGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 825 LRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFNRHNLKYYVLPKKPkKVAFDCLEWIRKHHPYDSGIIYCL 904
Cdd:TIGR00614 156 LKQKFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTP-KILEDLLRFIRKEFEGKSGIIYCP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 905 SRRECDTMADTLQREGLAALAYHAGLSDSARDEVQHKWInQDNCQVICATIAFGMGIDKPDVRFVIHASLPKSMEGYYQE 984
Cdd:TIGR00614 235 SRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQ-RDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 985 SGRAGRDGEISHCVLFYTYHDVTRLKRLIMMEKDGNyhtKETHVNNLYSMVHYCENITECRRIQLLAYFGEKGFNPDFCK 1064
Cdd:TIGR00614 314 SGRAGRDGLPSECHLFYAPADMNRLRRLLMEEPDGN---FRTYKLKLYEMMEYCLNSSTCRRLILLSYFGEKGFNKSFCI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 1065 KYPDVSCDNCCKTKDYKTKDVTDDVKNIIRFVQEHSSSPGTRNigpaGRFTLNMLVDIFLGSKSAKVKSGIFGKGTTYSR 1144
Cdd:TIGR00614 391 MGTEKCCDNCCKRLDYKTKDVTDKVYDFGPQAQKALSAVGRLN----QKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGR 466
|
....
gi 110225360 1145 HNAE 1148
Cdd:TIGR00614 467 GKDE 470
|
|
| BLM_N |
pfam16202 |
N-terminal region of Bloom syndrome protein; BLM_N is the very N-terminal region of chordate ... |
1-368 |
0e+00 |
|
N-terminal region of Bloom syndrome protein; BLM_N is the very N-terminal region of chordate Bloom syndrome proteins. The exact function is not known.
Pssm-ID: 465064 Cd Length: 370 Bit Score: 564.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 1 MAAVPLNNLQEQLQRHSARKLNNQPSLSKPKSLGFTFKKKTSEG-DVSVTSVSVVKTPALSDKDVNVSEAFSFTESPLHK 79
Cdd:pfam16202 1 MAAVPQNNLQEQLERHSARKLNNKLSLSKPKSSGFTFKKKTSSGnDVSVTSVSVAKTPVLSDKDVNVTEAFSFSEPLPHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 80 PKQQAKIEGFFKHFPGRQQSKGTCSEPSLPATVQTAQDTLCTTPKTPTAKKLPVAVFKKLEFSSSADS---LSDWADMDD 156
Cdd:pfam16202 81 TNQQTRINDFFKNAPAGQQTKRAGSKPLLPDSSQTPQEVSCTTQVTPAVKKPPDAVFKKLEFSSSFDSfisLNDWDDMDD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 157 FDMSA-SDAFASLAKNPATRVSTAQKMKKTKRNFFKPPPRKANAVKTDLTPPSPECLQVDLTKESEEEeeeeeeaegADC 235
Cdd:pfam16202 161 FDTSGnSKAFVTPPRNHFVRVSTAQKSKKSKRNFSKAQLSKANTVKADLTPSSGESKQVDLTKEQLDD---------SEW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 236 LSRDVICIDNDSASEELTEKDTQESQSLKAHLGAERGDSEKKSHEDEAVFHSVQNTEYFEHNDNDYDIDFVPPSPEE-II 314
Cdd:pfam16202 232 LSSDVICIDDDPISEELINEDTQESHSLKTHLGDERDNSEKKKHLEETELHSVEKSPCVELNEDDYDIDFVPPSPEEeVI 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 110225360 315 STASSSLKCSSMLKDLDDSDKEKGILSTSEELLSKPEEMTTHKSDAGTSKDCDA 368
Cdd:pfam16202 312 SSSSSSLKCFSMLKDLDTSDKEKDGLSTSEDLLSKPEKMTTQQPDQETSTDCDA 365
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
662-1142 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 555.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 662 EMMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTIVISPLRSLIVDQVQKLTSFDIP 741
Cdd:COG0514 4 DALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 742 ATYLTGDKTDSEAANIYLQLSKKDpiIKLLYVTPEkvcasnRLIS--TLENLYERKLlARFVIDEAHCVSQWGHDFRQDY 819
Cdd:COG0514 84 AAFLNSSLSAEERREVLRALRAGE--LKLLYVAPE------RLLNprFLELLRRLKI-SLFAIDEAHCISQWGHDFRPDY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 820 KRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFNRHNLKYYVLPKKPKKVAFDCLEWIRKHHPyDSG 899
Cdd:COG0514 155 RRLGELRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPPDDKLAQLLDFLKEHPG-GSG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 900 IIYCLSRRECDTMADTLQREGLAALAYHAGLSDSARDEVQHKWINqDNCQVICATIAFGMGIDKPDVRFVIHASLPKSME 979
Cdd:COG0514 234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLR-DEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 980 GYYQESGRAGRDGEISHCVLFYTYHDVTRLKRLImMEKDGNYHTKETHVNNLYSMVHYCEnITECRRIQLLAYFGEKGFN 1059
Cdd:COG0514 313 AYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFI-EQSPPDEERKRVERAKLDAMLAYAE-TTGCRRQFLLRYFGEELAE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 1060 PdfCKKypdvsCDNCCKTKdyKTKDVTDDVKNIIRFVqehssspgtRNIGPagRFTLNMLVDIFLGSKSAKVKSGIFGKG 1139
Cdd:COG0514 391 P--CGN-----CDNCLGPP--ETFDGTEAAQKALSCV---------YRTGQ--RFGAGHVIDVLRGSKNEKIRQFGHDKL 450
|
...
gi 110225360 1140 TTY 1142
Cdd:COG0514 451 STY 453
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
643-1284 |
5.88e-160 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 514.06 E-value: 5.88e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 643 SSKNPKhehFQSLNFPHTKEMMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTIVIS 722
Cdd:PLN03137 431 GSNDKK---WSSRNFPWTKKLEVNNKKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVIS 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 723 PLRSLIVDQVQKLTSFDIPATYLTGDKTDSEAANIYLQLSKKDPIIKLLYVTPEKVCASNRLISTLENLYERKLLARFVI 802
Cdd:PLN03137 508 PLVSLIQDQIMNLLQANIPAASLSAGMEWAEQLEILQELSSEYSKYKLLYVTPEKVAKSDSLLRHLENLNSRGLLARFVI 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 803 DEAHCVSQWGHDFRQDYKRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFNRHNLKYYVLPKKPKkv 882
Cdd:PLN03137 588 DEAHCVSQWGHDFRPDYQGLGILKQKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKK-- 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 883 afdCLE----WIRKHHPYDSGIIYCLSRRECDTMADTLQREGLAALAYHAGLSDSARDEVQHKWiNQDNCQVICATIAFG 958
Cdd:PLN03137 666 ---CLEdidkFIKENHFDECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQW-SKDEINIICATVAFG 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 959 MGIDKPDVRFVIHASLPKSMEGYYQESGRAGRDGEISHCVLFYTYHDVTRLKRLIMMEKDGNYHTK-------------E 1025
Cdd:PLN03137 742 MGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMISQGGVEQSPMAmgynrmassgrilE 821
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 1026 THVNNLYSMVHYCENITECRRIQLLAYFGEKgFNPDFCKKypdvSCDNCCKTKDYKTKDVTDDVKNIIRFVQEhssspgT 1105
Cdd:PLN03137 822 TNTENLLRMVSYCENEVDCRRFLQLVHFGEK-FDSTNCKK----TCDNCSSSKSLIDKDVTEIARQLVELVKL------T 890
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 1106 RNigpagRFTLNMLVDIFLGSKSAKVKS------GIFGKGTTYSRHNAERLFKKLILDKILDEDLYINANDQPIAYVML- 1178
Cdd:PLN03137 891 GE-----RFSSAHILEVYRGSLNQYVKKhrhetlSLHGAGKHLSKGEASRILHYLVTEDILAEDVKKSDLYGSVSSLLKv 965
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 1179 -GTKAHSVLSGHLKV--DFMETENSSSIKKQKALVAKVS--------------QREEVVKKCLGELTEVCKLLGKVF--- 1238
Cdd:PLN03137 966 nESKAYKLFSGGQTIimRFPSSVKASKPSKFEATPAKGPltsgkqstlpmatpAQPPVDLNLSAILYTALRKLRTALvke 1045
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 110225360 1239 ---GVHYFNIFNTATLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVI 1284
Cdd:PLN03137 1046 agdGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKAKVSKYGDRLL 1094
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
663-1290 |
4.93e-155 |
|
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: 481.49 E-value: 4.93e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 663 MMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTIVISPLRSLIVDQVQKLTSFDIPA 742
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 743 TYLTGDKTDSEAANIYLQLSKKDpiIKLLYVTPEKvcasnrlistLENLYERKLLAR-----FVIDEAHCVSQWGHDFRQ 817
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGE--LKLLYVAPER----------LEQDYFLNMLQRipialVAVDEAHCVSQWGHDFRP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 818 DYKRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFNRHNLKYYVLPKKPKKVafDCLEWIRKHHPyD 897
Cdd:TIGR01389 149 EYQRLGSLAERFPQVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQK--FLLDYLKKHRG-Q 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 898 SGIIYCLSRRECDTMADTLQREGLAALAYHAGLSDSARDEVQHKWINQDNcQVICATIAFGMGIDKPDVRFVIHASLPKS 977
Cdd:TIGR01389 226 SGIIYASSRKKVEELAERLESQGISALAYHAGLSNKVRAENQEDFLYDDV-KVMVATNAFGMGIDKPNVRFVIHYDMPGN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 978 MEGYYQESGRAGRDGEISHCVLFYTYHDVTRLKRLI-MMEKDGNYHTKETHvnNLYSMVHYCENITeCRRIQLLAYFGEK 1056
Cdd:TIGR01389 305 LESYYQEAGRAGRDGLPAEAILLYSPADIALLKRRIeQSEADDDYKQIERE--KLRAMIAYCETQT-CRRAYILRYFGEN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 1057 GFNPdfCKKypdvsCDNCckTKDYKTKDVTDDVKNIIRFVQEHSsspgtrnigpaGRFTLNMLVDIFLGSKSAKVKS--- 1133
Cdd:TIGR01389 382 EVEP--CGN-----CDNC--LDPPKSYDATVEAQKALSCVYRMG-----------QRFGVGYIIEVLRGSKNDKILQkgh 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 1134 ---GIFGKGTTYSRHNAERLFKKLILDKildedlYINANDQPIAYVMLGTKAHSVLSGHLKVdfMETEnsssiKKQKALV 1210
Cdd:TIGR01389 442 dqlSTYGIGKDYTQKEWRSLIDQLIAEG------LLTENDEIYIGLQLTEAARKVLKNEVEV--LLRP-----FKVVAKE 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 1211 AKVSQREEVV---KKCLGELTEVCKLLGKVFGVHYFNIFNTATLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVIPVL 1287
Cdd:TIGR01389 509 KTRVQKNLSVgvdNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAEKRPATLNALLKIKGVGQNKLDRYGEAFLEVI 588
|
...
gi 110225360 1288 QKY 1290
Cdd:TIGR01389 589 REY 591
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
659-866 |
2.11e-147 |
|
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: 446.20 E-value: 2.11e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 659 HTKEMMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTIVISPLRSLIVDQVQKLTSF 738
Cdd:cd18016 1 HSKEMMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 739 DIPATYLTGDKTDSEAANIYLQLSKKDPIIKLLYVTPEKVCASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRQD 818
Cdd:cd18016 81 DIPATYLTGDKTDAEATKIYLQLSKKDPIIKLLYVTPEKISASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 110225360 819 YKRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFN 866
Cdd:cd18016 161 YKRLNMLRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
664-1290 |
1.14e-118 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 384.84 E-value: 1.14e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 664 MKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTIVISPLRSLIVDQVQKLTSFDIPAT 743
Cdd:PRK11057 14 KQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 744 YLTGDKTDSEAANIYLQLSKKDpiIKLLYVTPEKVCASNrlisTLENLYERKlLARFVIDEAHCVSQWGHDFRQDYKRMN 823
Cdd:PRK11057 94 CLNSTQTREQQLEVMAGCRTGQ--IKLLYIAPERLMMDN----FLEHLAHWN-PALLAVDEAHCISQWGHDFRPEYAALG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 824 MLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFNRHNLKYYVLPK-KPkkvaFDCLEWIRKHHPYDSGIIY 902
Cdd:PRK11057 167 QLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKfKP----LDQLMRYVQEQRGKSGIIY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 903 CLSRRECDTMADTLQREGLAALAYHAGLSDSARDEVQHKWiNQDNCQVICATIAFGMGIDKPDVRFVIHASLPKSMEGYY 982
Cdd:PRK11057 243 CNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAF-QRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 983 QESGRAGRDGEISHCVLFYTYHDVTRLKRLIMMEKDGNYHTKETHvnNLYSMVHYCENITeCRRIQLLAYFGEkgfnpdf 1062
Cdd:PRK11057 322 QETGRAGRDGLPAEAMLFYDPADMAWLRRCLEEKPAGQQQDIERH--KLNAMGAFAEAQT-CRRLVLLNYFGE------- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 1063 ckkYPDVSCDNC--C--KTKDYK-TKDVTDDVKNIIRFVQehssspgtrnigpagRFTLNMLVDIFLGSKSAKV------ 1131
Cdd:PRK11057 392 ---GRQEPCGNCdiCldPPKQYDgLEDAQKALSCIYRVNQ---------------RFGMGYVVEVLRGANNQRIrdyghd 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 1132 KSGIFGKGTTYSRHNAERLFKKLILDKILDEDLYINANDQpiayvmLGTKAHSVLSGH--LKVDFMETENSSSIKKQKal 1209
Cdd:PRK11057 454 KLKVYGIGRDKSHEHWVSVIRQLIHLGLVTQNIAQHSALQ------LTEAARPVLRGEvsLQLAVPRIVALKPRAMQK-- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 1210 vakvSQREEVVKKCLGELTEVCKLLGKVFGVHYFNIFNTATLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVIPVLQK 1289
Cdd:PRK11057 526 ----SFGGNYDRKLFAKLRKLRKSIADEENIPPYVVFNDATLIEMAEQMPITASEMLSVNGVGQRKLERFGKPFMALIRA 601
|
.
gi 110225360 1290 Y 1290
Cdd:PRK11057 602 H 602
|
|
| BDHCT_assoc |
pfam16204 |
BDHCT-box associated domain on Bloom syndrome protein; This family is found on Bloom ... |
430-655 |
1.41e-109 |
|
BDHCT-box associated domain on Bloom syndrome protein; This family is found on Bloom syndrome-associated DEAD-box helicases in higher eukaryotes. It lies between the BDHCT, and DEAD-box families, pfam08072 and pfam00270.
Pssm-ID: 465065 Cd Length: 223 Bit Score: 345.25 E-value: 1.41e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 430 GSLWRHRPDSLDNTVQGDSCPVGHPNKELNSPYLLSHSPSTEECLPTTTPGKTGFSATPKNLFERPLLNSHLQKSFVSSN 509
Cdd:pfam16204 1 GSVWRCRPDSLGSPVKGDSCPTGNSVKELNFPHLPSNSLSTGECLLTTTPGKTGFSATTKNLSERPLFSSHLQKSFVSSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 510 WAETPRMENRNESTDFPGSVLTSTTVKAQSKQAASGWNVERHGQASYDIDNFNIDDFdddDDDDDWENIMHNFPASKSST 589
Cdd:pfam16204 81 WAETPRTEKRNESSYFPGNVLTSTAVKDQNKHTASVNDLEREIQASCDIDNFDIDDF---DDDDDWENIMHNLAASKSST 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110225360 590 ATYPPIKEGGPVKSLSERISSAKAKFLPVVSTAQNTNLSESIQNCSDKLAQNLSSKNPKHEHFQSL 655
Cdd:pfam16204 158 AAYQPIKEGGPVKSVSERISSAKTNCLPVASTAQNKNFSESIQNYTDKSAQNLASRNLKHEHFQSL 223
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
665-866 |
1.11e-95 |
|
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: 305.61 E-value: 1.11e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 665 KIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTIVISPLRSLIVDQVQKLTSFDIPATY 744
Cdd:cd17920 2 QILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 745 LTGDKTDSEAANIYLQLskKDPIIKLLYVTPEKvCASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRQDYKRMNM 824
Cdd:cd17920 82 LNSTLSPEEKREVLLRI--KNGQYKLLYVTPER-LLSPDFLELLQRLPERKRLALIVVDEAHCVSQWGHDFRPDYLRLGR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 110225360 825 LRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFN 866
Cdd:cd17920 159 LRRALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
658-866 |
1.72e-82 |
|
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: 269.24 E-value: 1.72e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 658 PHTKEMMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTIVISPLRSLIVDQVQKLTS 737
Cdd:cd18015 1 PWSGKVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 738 FDIPATYLTGdKTDSEAAN-IYLQLSKKDPIIKLLYVTPEKVCASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFR 816
Cdd:cd18015 81 LGISATMLNA-SSSKEHVKwVHAALTDKNSELKLLYVTPEKIAKSKRFMSKLEKAYNAGRLARIAIDEVHCCSQWGHDFR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 110225360 817 QDYKRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFN 866
Cdd:cd18015 160 PDYKKLGILKRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
867-1001 |
8.35e-78 |
|
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: 252.51 E-value: 8.35e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 867 RHNLKYYVLPKKPKKVAFDCLEWIRKHHPYDSGIIYCLSRRECDTMADTLQREGLAALAYHAGLSDSARDEVQHKWINQD 946
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 110225360 947 nCQVICATIAFGMGIDKPDVRFVIHASLPKSMEGYYQESGRAGRDGEISHCVLFY 1001
Cdd:cd18794 81 -IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
664-866 |
6.79e-62 |
|
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: 210.19 E-value: 6.79e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 664 MKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACV----SPGVTIVISPLRSLIVDQVQKLTSFd 739
Cdd:cd18018 1 LKLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLlrrrGPGLTLVVSPLIALMKDQVDALPRA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 740 IPATYLTGDKTDSEAANIYLQLSKKDpiIKLLYVTPEKVCASnrliSTLENLYERKLLARFVIDEAHCVSQWGHDFRQDY 819
Cdd:cd18018 80 IKAAALNSSLTREERRRILEKLRAGE--VKILYVSPERLVNE----SFRELLRQTPPISLLVVDEAHCISEWSHNFRPDY 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 110225360 820 KRM-NMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFN 866
Cdd:cd18018 154 LRLcRVLRELLGAPPVLALTATATKRVVEDIASHLGIPESGVVRGPLY 201
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
665-858 |
7.77e-61 |
|
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: 207.32 E-value: 7.77e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 665 KIFHKKFGLHNFRTN-QLEAINAALLGE-DCFILMPTGGGKSLCYQLPACVSPGVTIVISPLRSLIVDQVQKLTSFDIPA 742
Cdd:cd18014 2 STLKKVFGHSDFKSPlQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 743 TYLTGDKTDSEAANIYLQLSKKDPIIKLLYVTPEKVcASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRQDYKRM 822
Cdd:cd18014 82 DSLNSKLSAQERKRIIADLESEKPQTKFLYITPEMA-ATSSFQPLLSSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 110225360 823 NMLRQKFPSVPVMALTATANPRVQKDILTQLKILRP 858
Cdd:cd18014 161 GALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKP 196
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
671-866 |
1.93e-50 |
|
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: 176.89 E-value: 1.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 671 FGLHNFRTNQLEAINAAL-LGEDCFILMPTGGGKSLCYQLPACVSPGVTIVISPLRSLIVDQVQKLTSFDIPATYLTGDK 749
Cdd:cd18017 8 FGHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFLGSAQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 750 TDSEAANIylqlskKDPIIKLLYVTPEKVCASNRLISTLENlyERKLLArfvIDEAHCVSQWGHDFRQDYKRMNMLRQKF 829
Cdd:cd18017 88 SQNVLDDI------KMGKIRVIYVTPEFVSKGLELLQQLRN--GITLIA---IDEAHCVSQWGHDFRSSYRHLGSIRNRL 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 110225360 830 PSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFN 866
Cdd:cd18017 157 PNVPIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| DpdF |
NF041063 |
protein DpdF; |
680-1017 |
1.96e-49 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 190.12 E-value: 1.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 680 QLEAINAALL---GEDCFILMPTGGGKSLCYQLPACVSP---GVTIVISPLRSLIVDQVQKLTSF-------DIPATYLT 746
Cdd:NF041063 145 QREAVRAALLappGSTLIVNLPTGSGKSLVAQAPALLASrqgGLTLVVVPTVALAIDQERRARELlrragpdLGGPLAWH 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 747 GDKTDSEAANIYLQLskKDPIIKLLYVTPEKVCASnrLISTLENLYERKLLARFVIDEAHCVSQWGHDFRQDYKRMNMLR 826
Cdd:NF041063 225 GGLSAEERAAIRQRI--RDGTQRILFTSPESLTGS--LRPALFDAAEAGLLRYLVVDEAHLVDQWGDGFRPEFQLLAGLR 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 827 QKFPSVP-------VMALTATanprvqkdiLTQ-----LKIL-----RPQVFSMSFNRHNLKYYVLPKKPKKVAFDC-LE 888
Cdd:NF041063 301 RSLLRLApsgrpfrTLLLSAT---------LTEstldtLETLfgppgPFIVVSAVQLRPEPAYWVAKCDSEEERRERvLE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 889 WIRkhH---PYdsgIIYCLSRRECDTMADTLQREGLAALA-YHAGLSDSARDEVQHKWiNQDNCQVICATIAFGMGIDKP 964
Cdd:NF041063 372 ALR--HlprPL---ILYVTKVEDAEAWLQRLRAAGFRRVAlFHGDTPDAERERLIEQW-RENELDIVVATSAFGLGMDKS 445
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 110225360 965 DVRFVIHASLPKSMEGYYQESGRAGRDGEISHCVLFYTYHDVT---RL--KRLIMMEK 1017
Cdd:NF041063 446 DVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDiakSLnrPKLISVEK 503
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
677-849 |
3.86e-30 |
|
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: 117.73 E-value: 3.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 677 RTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPAC------VSPGVTIVISPLRSLIVDQVQKLTSFDIPATY-----L 745
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGLkvaslL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 746 TGDKTDSEAANIylqlsKKdpiIKLLYVTPEKVCASNRLISTLENLyerKLLarfVIDEAHCVSQWGhdFRQDYKRmnML 825
Cdd:pfam00270 81 GGDSRKEQLEKL-----KG---PDILVGTPGRLLDLLQERKLLKNL---KLL---VLDEAHRLLDMG--FGPDLEE--IL 142
|
170 180
....*....|....*....|....
gi 110225360 826 RQKFPSVPVMALTATAnPRVQKDI 849
Cdd:pfam00270 143 RRLPKKRQILLLSATL-PRNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
669-849 |
1.23e-23 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 100.26 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 669 KKFGLHNFRTNQLEAINAALLGE-DCFILMPTGGGKSLCYQLPA-----CVSPGVTIVISPLRSLIVDQVQKLTSF---- 738
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPAlealkRGKGGRVLVLVPTRELAEQWAEELKKLgpsl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 739 -DIPATYLTGDKTDSEAANIylqlskKDPIIKLLYVTPEKVcasnrLISTLENLYERKLLARFVIDEAHCVSQWGhdFRQ 817
Cdd:smart00487 82 gLKVVGLYGGDSKREQLRKL------ESGKTDILVTTPGRL-----LDLLENDKLSLSNVDLVILDEAHRLLDGG--FGD 148
|
170 180 190
....*....|....*....|....*....|..
gi 110225360 818 DYKRmnMLRQKFPSVPVMALTATANPRVQKDI 849
Cdd:smart00487 149 QLEK--LLKLLPKNVQLLLLSATPPEEIENLL 178
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
1003-1075 |
5.07e-22 |
|
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: 90.81 E-value: 5.07e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110225360 1003 YHDVTRLKRLIMMEkDGNYHTKETHVNNLYSMVHYCENITECRRIQLLAYFGEKgFNPDFCKKypdvsCDNCC 1075
Cdd:pfam16124 1 YQDVVRLRFLIEQS-EADEERKEVELQKLQAMVAYCENTTDCRRKQLLRYFGEE-FDSEPCGN-----CDNCL 66
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
910-992 |
1.71e-20 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 86.88 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 910 DTMADTLQREGLAALAYHAGLSDSARDEVQHKWiNQDNCQVICATIAFGMGIDKPDVRFVIHASLPKSMEGYYQESGRAG 989
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKF-NNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAG 79
|
...
gi 110225360 990 RDG 992
Cdd:smart00490 80 RAG 82
|
|
| BDHCT |
pfam08072 |
BDHCT (NUC031) domain; This is a C-terminal domain in Bloom's syndrome DEAD helicase subfamily. |
379-417 |
8.60e-20 |
|
BDHCT (NUC031) domain; This is a C-terminal domain in Bloom's syndrome DEAD helicase subfamily.
Pssm-ID: 462356 Cd Length: 41 Bit Score: 83.48 E-value: 8.60e-20
10 20 30
....*....|....*....|....*....|....*....
gi 110225360 379 HVMEHICKLVDTVPTDELEALNCGTELLQQRNIRRKLLA 417
Cdd:pfam08072 3 SVMEEICKLVDTIPIHELKALSCGNELLQQRDIRRKLLA 41
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
884-992 |
1.48e-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: 82.26 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 884 FDCLEWIRKHHPYDSGIIYCLSRRECDTMAdTLQREGLAALAYHAGLSDSARDEVQHKWiNQDNCQVICATIAFGMGIDK 963
Cdd:pfam00271 3 LEALLELLKKERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDF-RKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*....
gi 110225360 964 PDVRFVIHASLPKSMEGYYQESGRAGRDG 992
Cdd:pfam00271 81 PDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
1218-1294 |
6.18e-18 |
|
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the HRDC domain cause human disease.
Pssm-ID: 128635 [Multi-domain] Cd Length: 81 Bit Score: 79.65 E-value: 6.18e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110225360 1218 EVVKKCLGELTEVCKLLGKVFGVHYFNIFNTATLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVIPVLQKYSEWT 1294
Cdd:smart00341 2 ERQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEASDSP 78
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
680-1012 |
6.07e-16 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 82.12 E-value: 6.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 680 QLEAINAALLGEDCFILMPTGGGKSLCYQLPAC--VSPGV-----TIVISPLRSL---IVDQVQKLTSF-DIPATYLTGd 748
Cdd:COG0513 29 QAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLqrLDPSRprapqALILAPTRELalqVAEELRKLAKYlGLRVATVYG- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 749 ktdseAANIYLQ---LSKKDPIIkllyV-TPekvcasNRLIstleNLYERKLLA-----RFVIDEAhcvsqwghD----- 814
Cdd:COG0513 108 -----GVSIGRQiraLKRGVDIV----VaTP------GRLL----DLIERGALDlsgveTLVLDEA--------Drmldm 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 815 -FRQDYKR-MNML---RQkfpsvpVMALTATANPRVQKdiLTQlKILR-PQVfsMSFNRHNLK------YYVLPKKPKKv 882
Cdd:COG0513 161 gFIEDIERiLKLLpkeRQ------TLLFSATMPPEIRK--LAK-RYLKnPVR--IEVAPENATaetieqRYYLVDKRDK- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 883 aFDCLEWIRKHHPYDSGIIYCLSRRECDTMADTLQREGLAALAYHAGLSDSARDEVQHKwINQDNCQVICAT-IAfGMGI 961
Cdd:COG0513 229 -LELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDA-FRNGKIRVLVATdVA-ARGI 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 110225360 962 DKPDVRFVIHASLPKSMEGYYQESG---RAGRDGEishCVLFYTYHDVTRLKRL 1012
Cdd:COG0513 306 DIDDVSHVINYDLPEDPEDYVHRIGrtgRAGAEGT---AISLVTPDERRLLRAI 356
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
670-1006 |
7.55e-16 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 82.77 E-value: 7.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 670 KFGLHNFrtnQLEAINAALL----GEDCFIL-MPTGGGKS-----LCYQLPAcvsPGVTIVISPLRSLiVDQ-VQKLTSF 738
Cdd:COG1061 78 SFELRPY---QQEALEALLAalerGGGRGLVvAPTGTGKTvlalaLAAELLR---GKRVLVLVPRREL-LEQwAEELRRF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 739 DiPATYLTGDKTDSEAaniylqlskkdPIIkllyvtpekvcasnrlISTLENLYERKLLARF-------VIDEAHcvsqw 811
Cdd:COG1061 151 L-GDPLAGGGKKDSDA-----------PIT----------------VATYQSLARRAHLDELgdrfglvIIDEAH----- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 812 gHDFRQDYKRmnmLRQKFPSVPVMALTATANPRVQKDILTQL----------------KILRPQVF---SMSFNRHNLKY 872
Cdd:COG1061 198 -HAGAPSYRR---ILEAFPAAYRLGLTATPFRSDGREILLFLfdgivyeyslkeaiedGYLAPPEYygiRVDLTDERAEY 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 873 YVL------------PKKPKKVAfdclEWIRKHHPYDSGIIYCLSRRECDTMADTLQREGLAALAYHAGLSDSARDEVQh 940
Cdd:COG1061 274 DALserlrealaadaERKDKILR----ELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEIL- 348
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110225360 941 KWINQDNCQVICATIAFGMGIDKPDVRFVIHASLPKSMEGYYQESGRAGRDGEISHCVLFYTYHDV 1006
Cdd:COG1061 349 EAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKEDALVYDFVGN 414
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
1084-1186 |
2.49e-15 |
|
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: 214936 [Multi-domain] Cd Length: 92 Bit Score: 72.51 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 1084 DVTDDVKNIIRFVQEHSsspgtrnigpaGRFTLNMLVDIFLGSKSAKVKS------GIFGKGTTYSRHNAERLFKKLILD 1157
Cdd:smart00956 1 DVTEEAQKLLSCVYRTG-----------QRFGAGHVIDVLRGSKNKKIRQkghdrlSTFGIGKDLSKKEWRRLIRQLIAE 69
|
90 100
....*....|....*....|....*....
gi 110225360 1158 KILDEDlyinanDQPIAYVMLGTKAHSVL 1186
Cdd:smart00956 70 GYLRED------GGRYPYLKLTEKARPVL 92
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
690-840 |
2.77e-15 |
|
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: 74.36 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 690 GEDCFILMPTGGGKSLCYQLPA-CVS---PGVTIVISPLRSLIVDQ---VQKLTSFDIPATYLTGDKTDSEAANIYLQLS 762
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAAlLLLlkkGKKVLVLVPTKALALQTaerLRELFGPGIRVAVLVGGSSAEEREKNKLGDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110225360 763 kkdpiiKLLYVTPEKVcasNRLISTLENLYERKlLARFVIDEAHCVSQWGHDFRQDYKRmnMLRQKFPSVPVMALTAT 840
Cdd:cd00046 81 ------DIIIATPDML---LNLLLREDRLFLKD-LKLIIVDEAHALLIDSRGALILDLA--VRKAGLKNAQVILLSAT 146
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
871-1001 |
4.06e-15 |
|
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: 73.31 E-value: 4.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 871 KYYVLPKKPKKVAfdCLEWIRKHHPYDSGIIYCLSRRECDTMADTLQREGLAALAYHAGLSDSARDEVQHKwINQDNCQV 950
Cdd:cd18787 4 LYVVVEEEEKKLL--LLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKK-FRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 110225360 951 ICATIAFGMGIDKPDVRFVIHASLPKSMEGYYQESGRAGRDGEISHCVLFY 1001
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
669-999 |
2.00e-14 |
|
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: 78.34 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 669 KKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPA----CVSPGVT-IVISPLRSLIVDQVQKLTSF----- 738
Cdd:COG1205 50 KKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVlealLEDPGATaLYLYPTKALARDQLRRLRELaealg 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 739 -DI-PATYlTGDkTDSEAaniylqlskKDPIIK---LLYVTPEKVCAS-----NRLISTLENLyerkllaRF-VIDEAHC 807
Cdd:COG1205 130 lGVrVATY-DGD-TPPEE---------RRWIREhpdIVLTNPDMLHYGllphhTRWARFFRNL-------RYvVIDEAHT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 808 ---V--SQWGHDFRqdykRMNMLRQKFPSVPVMALT-AT-ANPrvqKDILTQLkILRP-QVFSMSFNRHNLKYYVL---P 876
Cdd:COG1205 192 yrgVfgSHVANVLR----RLRRICRHYGSDPQFILAsATiGNP---AEHAERL-TGRPvTVVDEDGSPRGERTFVLwnpP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 877 KKPKKVAFDCL--------EWIRKHHpydSGIIYCLSRRECDTMADTLQRE------GLAALAYHAGLSDSARDEVQHKw 942
Cdd:COG1205 264 LVDDGIRRSALaeaarllaDLVREGL---RTLVFTRSRRGAELLARYARRAlrepdlADRVAAYRAGYLPEERREIERG- 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 110225360 943 INQDNCQVICATIAFGMGIDKPDVRFVIHASLPKSMEGYYQESGRAGRDGEISHCVL 999
Cdd:COG1205 340 LRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVL 396
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
1080-1192 |
7.93e-14 |
|
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: 68.72 E-value: 7.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 1080 YKTKDVTDDVKNIIRFVQEhssspgTRnigpaGRFTLNMLVDIFLGSKSAKV------KSGIFGKGTTYSRHNAERLFKK 1153
Cdd:pfam09382 2 PETVDVTEEAQKILSCVYR------TG-----QRFGAGHLIDVLRGSKNKKIrqlghdKLSTFGIGKDLSKKEWRRIIRQ 70
|
90 100 110
....*....|....*....|....*....|....*....
gi 110225360 1154 LILDKILDEDLyinanDQPIaYVMLGTKAHSVLSGHLKV 1192
Cdd:pfam09382 71 LIAEGYLEVDI-----EFYS-VLKLTPKAREVLKGEEKV 103
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
669-990 |
3.94e-13 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 73.78 E-value: 3.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 669 KKFGLHNFRTNQLEAINAALLGEDCFIL-MPTGGGKSLCYQLPAC--VSPGVTIV-ISPLRSLIvDQV-----QKLTSFD 739
Cdd:COG1204 16 KERGIEELYPPQAEALEAGLLEGKNLVVsAPTASGKTLIAELAILkaLLNGGKALyIVPLRALA-SEKyrefkRDFEELG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 740 IPATYLTGDKTDSEAAniylqLSKKDPIIkllyVTPEKvcasnrLISTLENlyERKLLARF---VIDEAHCVsqwghdfr 816
Cdd:COG1204 95 IKVGVSTGDYDSDDEW-----LGRYDILV----ATPEK------LDSLLRN--GPSWLRDVdlvVVDEAHLI-------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 817 QDYKR---MNM----LRQKFPSVPVMALTAT-ANPrvqKDIltqLKILRPQVFSMSFNRHNLKYYVLpkKPKKVAFDC-- 886
Cdd:COG1204 150 DDESRgptLEVllarLRRLNPEAQIVALSATiGNA---EEI---AEWLDAELVKSDWRPVPLNEGVL--YDGVLRFDDgs 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 887 ------LEWIRKHHPYDSG--IIYCLSRRECDTMAD-------------------------------TLQREGLAAL--- 924
Cdd:COG1204 222 rrskdpTLALALDLLEEGGqvLVFVSSRRDAESLAKkladelkrrltpeereeleelaeellevseeTHTNEKLADClek 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110225360 925 --AYH-AGLSDSARDEVQhKWINQDNCQVICAT--IAfgMGIDKPdVRFVIHASL-------PKSMEgYYQESGRAGR 990
Cdd:COG1204 302 gvAFHhAGLPSELRRLVE-DAFREGLIKVLVATptLA--AGVNLP-ARRVIIRDTkrggmvpIPVLE-FKQMAGRAGR 374
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
680-1017 |
2.83e-12 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 70.97 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 680 QLEAINAALLGEDCFILMPTGGGKSLCYQLP---ACVS----------PGVTIVISPLRSLIVdQVQ---KLTSFDIP-- 741
Cdd:PLN00206 148 QMQAIPAALSGRSLLVSADTGSGKTASFLVPiisRCCTirsghpseqrNPLAMVLTPTRELCV-QVEdqaKVLGKGLPfk 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 742 -ATYLTGDKTDSeaaniylQLSKKDPIIKLLYVTPekvcasNRLISTL-ENLYERKLLARFVIDEAHCVSQWGhdFRQdy 819
Cdd:PLN00206 227 tALVVGGDAMPQ-------QLYRIQQGVELIVGTP------GRLIDLLsKHDIELDNVSVLVLDEVDCMLERG--FRD-- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 820 kRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKilrpQVFSMSF---NR-----HNLKYYVLPKKPKKVAFDCLEwiR 891
Cdd:PLN00206 290 -QVMQIFQALSQPQVLLFSATVSPEVEKFASSLAK----DIILISIgnpNRpnkavKQLAIWVETKQKKQKLFDILK--S 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 892 KHHPYDSGIIYCLSRRECDTMADTLQR-EGLAALAYHAGLSDSARDEVQHKWINQDnCQVICATIAFGMGIDKPDVRFVI 970
Cdd:PLN00206 363 KQHFKPPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGE-VPVIVATGVLGRGVDLLRVRQVI 441
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 110225360 971 HASLPKSMEGYYQESGRAGRDGEISHCVLFYTYHDVTRLKRLIMMEK 1017
Cdd:PLN00206 442 IFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLK 488
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
1221-1287 |
8.23e-12 |
|
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic acid binding. Mutations in the HRDC domain cause human disease. It is interesting to note that the RecQ helicase in Deinococcus radiodurans has three tandem HRDC domains.
Pssm-ID: 425755 [Multi-domain] Cd Length: 68 Bit Score: 61.78 E-value: 8.23e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110225360 1221 KKCLGELTEVCKLLGKVFGVHYFNIFNTATLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVIPVL 1287
Cdd:pfam00570 2 LALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
680-806 |
3.96e-10 |
|
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: 60.68 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 680 QLEAINAALLGEDCFILMPTGGGKSLCYQLP----ACVSPGVT-IVISPLRSLIVDQVQKLTSF------DI-PATYlTG 747
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPileaLLRDPGSRaLYLYPTKALAQDQLRSLRELleqlglGIrVATY-DG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110225360 748 DKTDSEAANIYLQLSKkdpII-----KLLY-VTPekvcASNRLISTLENLyerkllaRF-VIDEAH 806
Cdd:cd17923 84 DTPREERRAIIRNPPR---ILltnpdMLHYaLLP----HHDRWARFLRNL-------RYvVLDEAH 135
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
690-806 |
2.46e-09 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 57.98 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 690 GEDCFILMPTGGGKSLCYQLPACVS------PGVTIV-ISPLRSLIVDQVQKLT------SFDIPATYLTGDKTDSEAAn 756
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSladepeKGVQVLyISPLKALINDQERRLEepldeiDLEIPVAVRHGDTSQSEKA- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 110225360 757 iylQLSKKDPIIklLYVTPEKVCA---SNRLISTLENLyerkllaRFVI-DEAH 806
Cdd:cd17922 80 ---KQLKNPPGI--LITTPESLELllvNKKLRELFAGL-------RYVVvDEIH 121
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
900-993 |
4.22e-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: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 900 IIYCLSRRECDTMA----DTLQREGLAA---LAYHAGLSDSARDEVQHKWINQDNCQVIcATIAFGMGIDKPDVRFVIHA 972
Cdd:cd18797 39 IVFCRSRKLAELLLrylkARLVEEGPLAskvASYRAGYLAEDRREIEAELFNGELLGVV-ATNALELGIDIGGLDAVVLA 117
|
90 100
....*....|....*....|.
gi 110225360 973 SLPKSMEGYYQESGRAGRDGE 993
Cdd:cd18797 118 GYPGSLASLWQQAGRAGRRGK 138
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
900-1022 |
9.88e-09 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 59.90 E-value: 9.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 900 IIYCLSRRECDTMADTLqreGLAALAYHAGLSDSARDEVQHKWINQDnCQVICATIAFGMGIDKPDVRfVIHASLPK--- 976
Cdd:COG1202 431 IIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQE-LAAVVTTAALAAGVDFPASQ-VIFDSLAMgie 505
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 110225360 977 --SMEGYYQESGRAGRDGeishcvlfytYHDvtRLKRLIMMEKDGNYH 1022
Cdd:COG1202 506 wlSVQEFHQMLGRAGRPD----------YHD--RGKVYLLVEPGKSYH 541
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
896-1007 |
4.44e-08 |
|
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: 51.55 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 896 YDSGIIYCLSRRECDTMADTLQreglaalayhaglsdsardevqhkwinqdncqVICATIAFGMGIDKPDVRFVIHASLP 975
Cdd:cd18785 3 VVKIIVFTNSIEHAEEIASSLE--------------------------------ILVATNVLGEGIDVPSLDTVIFFDPP 50
|
90 100 110
....*....|....*....|....*....|..
gi 110225360 976 KSMEGYYQESGRAGRDGEIShcvlfYTYHDVT 1007
Cdd:cd18785 51 SSAASYIQRVGRAGRGGKDE-----GEVILFV 77
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
900-1012 |
1.45e-07 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 55.60 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 900 IIYCLSRRECDTMADTLQREGLAALAYHAGLSDSARDEVQHKWiNQDNCQVICATIAFGMGIDKPDVRFVIHASLPKSME 979
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREF-RSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPE 349
|
90 100 110
....*....|....*....|....*....|...
gi 110225360 980 GYYQESGRAGRDGEISHCVLFYTYHDVTRLKRL 1012
Cdd:PTZ00424 350 NYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEI 382
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
680-845 |
3.74e-07 |
|
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: 51.88 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 680 QLEAINAALLGEDCFIL-MPTGGGKSLCYQLPA----CVSPGVTIVISPLRSLiVDQV-----QKLTSFDIPATYLTGDK 749
Cdd:cd17921 6 QREALRALYLSGDSVLVsAPTSSGKTLIAELAIlralATSGGKAVYIAPTRAL-VNQKeadlrERFGPLGKNVGLLTGDP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 750 TDSeaaniYLQLSKKDPIIkllyVTPEKVCAsnrLISTLENLYERKLLArFVIDEAHCVSqwghdfrqDYKR-------M 822
Cdd:cd17921 85 SVN-----KLLLAEADILV----ATPEKLDL---LLRNGGERLIQDVRL-VVVDEAHLIG--------DGERgvvlellL 143
|
170 180
....*....|....*....|....
gi 110225360 823 NMLRQKFPSVPVMALTAT-ANPRV 845
Cdd:cd17921 144 SRLLRINKNARFVGLSATlPNAED 167
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
881-1000 |
5.74e-07 |
|
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: 50.63 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 881 KVAFDCLEWIRKHHPYdsgIIYCLSRRECDTMADTLqrEGLAalAYHAGLSDSARDEVQhkwINQDNC--QVICATIAFG 958
Cdd:cd18795 31 IIVLLKIETVSEGKPV---LVFCSSRKECEKTAKDL--AGIA--FHHAGLTREDRELVE---ELFREGliKVLVATSTLA 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 110225360 959 MGIDKPdVRFVIHASLPK----------SMEgYYQESGRAGRDG--EISHCVLF 1000
Cdd:cd18795 101 AGVNLP-ARTVIIKGTQRydgkgyrelsPLE-YLQMIGRAGRPGfdTRGEAIIM 152
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
680-1011 |
5.75e-07 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 54.01 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 680 QLEAINAALLGEDCFILMPTGGGKSLCYQLPACV--------SPG---VTIVISPLRSLiVDQV-QKLTSFdipatyltG 747
Cdd:PTZ00110 157 QVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVhinaqpllRYGdgpIVLVLAPTREL-AEQIrEQCNKF--------G 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 748 DKTDSEAANIYLQLSKKDPIIKLLYVTPEKVCASNRLISTLE-NLYERKLLARFVIDEAHCVSQWGHDFrQDYKRMNMLR 826
Cdd:PTZ00110 228 ASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLEsNVTNLRRVTYLVLDEADRMLDMGFEP-QIRKIVSQIR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 827 qkfPSVPVMALTATANPRVQK---DILTQLKIlRPQVFSMSFNR-HNLK--YYVLPKKPKKVAFDCLeWIRKHHPYDSGI 900
Cdd:PTZ00110 307 ---PDRQTLMWSATWPKEVQSlarDLCKEEPV-HVNVGSLDLTAcHNIKqeVFVVEEHEKRGKLKML-LQRIMRDGDKIL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 901 IYCLSRRECDTMADTLQREGLAALAYHAGLSDSARDEVQHKWINQDNcQVICATIAFGMGIDKPDVRFVIHASLPKSMEG 980
Cdd:PTZ00110 382 IFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKS-PIMIATDVASRGLDVKDVKYVINFDFPNQIED 460
|
330 340 350
....*....|....*....|....*....|.
gi 110225360 981 YYQESGRAGRDGEISHCVLFYTyHDVTRLKR 1011
Cdd:PTZ00110 461 YVHRIGRTGRAGAKGASYTFLT-PDKYRLAR 490
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
675-864 |
3.98e-06 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 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: 350781 [Multi-domain] Cd Length: 206 Bit Score: 49.28 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 675 NFRTNQLEAINAALLGEDCFIL-MPTGGGKSLCYQL--------PACVSPG--VTIVISPLRSLIVDQV----QKLTSFD 739
Cdd:cd18023 1 YFNRIQSEVFPDLLYSDKNFVVsAPTGSGKTVLFELailrllkeRNPLPWGnrKVVYIAPIKALCSEKYddwkEKFGPLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 740 IPATYLTGDKTDSEAANIylqlSKKDPIIkllyVTPEKVCASNRLISTLENLYErkLLARFVIDEAHCVSQW-GHDFRQD 818
Cdd:cd18023 81 LSCAELTGDTEMDDTFEI----QDADIIL----TTPEKWDSMTRRWRDNGNLVQ--LVALVLIDEVHIIKENrGATLEVV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 110225360 819 YKRMNML-------RQKFPSVPVMALTATAnPRVQkDILTQLKILRPQVFSMS 864
Cdd:cd18023 151 VSRMKTLsssselrGSTVRPMRFVAVSATI-PNIE-DLAEWLGDNPAGCFSFG 201
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
886-1000 |
2.50e-05 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 45.72 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 886 CLEWIRKHhpyDSGIIYCLSRRECDTMADTL------QREGLAALAYHAGLSDSARDEVQHKwINQDNCQVICATIAFGM 959
Cdd:cd18796 31 VIFLLERH---KSTLVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAA-LKRGDLKVVVATSSLEL 106
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 110225360 960 GIDKPDVRFVIHASLPKSMEGYYQESGRAG-RDGEISHCVLF 1000
Cdd:cd18796 107 GIDIGDVDLVIQIGSPKSVARLLQRLGRSGhRPGAASKGRLV 148
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
680-843 |
3.77e-05 |
|
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: 45.79 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 680 QLEAINAALL-GEDCFILMPTGGGKSLCYQL---PACVSPGVTIVISPLRSLivdQVQKLTSFDIPATYL------TGDk 749
Cdd:cd18028 6 QAEAVRAGLLkGENLLISIPTASGKTLIAEMamvNTLLEGGKALYLVPLRAL---ASEKYEEFKKLEEIGlkvgisTGD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 750 TDSEAANiylqLSKKDPIIkllyVTPEKVCASNRLISTLENlyerkLLARFVIDEAHCVSqwghdfrqDYKR-------M 822
Cdd:cd18028 82 YDEDDEW----LGDYDIIV----ATYEKFDSLLRHSPSWLR-----DVGVVVVDEIHLIS--------DEERgptlesiV 140
|
170 180
....*....|....*....|..
gi 110225360 823 NMLRQKFPSVPVMALTATA-NP 843
Cdd:cd18028 141 ARLRRLNPNTQIIGLSATIgNP 162
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
676-840 |
1.14e-04 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is 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: 350685 [Multi-domain] Cd Length: 201 Bit Score: 44.73 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 676 FRTNQLEAINAALLGEDCFILMPTGGGKS-----LC----YQLPaCVSPGVTIVISPLRSLIVDQVQKL-TSFDIPA--- 742
Cdd:cd17927 3 PRNYQLELAQPALKGKNTIICLPTGSGKTfvavlICehhlKKFP-AGRKGKVVFLANKVPLVEQQKEVFrKHFERPGykv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 743 TYLTGDKTDSEAANIYLQLSkkdpiiKLLYVTPEKvcasnrLISTLENLYERKlLARF---VIDEAHCVSQwGHDFRQDY 819
Cdd:cd17927 82 TGLSGDTSENVSVEQIVESS------DVIIVTPQI------LVNDLKSGTIVS-LSDFsllVFDECHNTTK-NHPYNEIM 147
|
170 180
....*....|....*....|....*
gi 110225360 820 KRmnMLRQKFPSV---P-VMALTAT 840
Cdd:cd17927 148 FR--YLDQKLGSSgplPqILGLTAS 170
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
680-857 |
6.40e-04 |
|
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 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: 350719 [Multi-domain] Cd Length: 206 Bit Score: 42.57 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 680 QLEAINAALLGEDCFILMPTGGGKSLCYQLP-----------ACVSPGVT-IVISPLRSLiVDQVQK----LTSF---DI 740
Cdd:cd17961 21 QSKAIPLALEGKDILARARTGSGKTAAYALPiiqkilkakaeSGEEQGTRaLILVPTREL-AQQVSKvleqLTAYcrkDV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 741 PATYLTGDKTDSEAANIylqLSKKDPIIkllyV-TPEKV---CASNRLI--STLENLyerkllarfVIDEAHCVSQWGHD 814
Cdd:cd17961 100 RVVNLSASSSDSVQRAL---LAEKPDIV----VsTPARLlshLESGSLLllSTLKYL---------VIDEADLVLSYGYE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 110225360 815 frQDYKRmnmLRQKFPSVPVMALT-ATANPRVQKdiLTQLkILR 857
Cdd:cd17961 164 --EDLKS---LLSYLPKNYQTFLMsATLSEDVEA--LKKL-VLH 199
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
680-847 |
1.17e-03 |
|
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 41.66 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 680 QLEAINAALLGEDCFILMPTGGGKSLCYQLPACV-----------SPGVtIVISPLRSL---IVDQVQKLTSF-DIPATY 744
Cdd:cd00268 17 QAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEkllpepkkkgrGPQA-LVLAPTRELamqIAEVARKLGKGtGLKVAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 745 LTGdktdseAANIYLQLSKKDPIIKLLYVTPEkvcasnRListLENLYERKLLAR----FVIDEAhcvsqwghD------ 814
Cdd:cd00268 96 IYG------GAPIKKQIEALKKGPDIVVGTPG------RL---LDLIERGKLDLSnvkyLVLDEA--------Drmldmg 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 110225360 815 FRQD----YKRMNMLRQkfpsvpVMALTATANPRVQK 847
Cdd:cd00268 153 FEEDvekiLSALPKDRQ------TLLFSATLPEEVKE 183
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
896-1000 |
1.28e-03 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins 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: 350186 [Multi-domain] Cd Length: 116 Bit Score: 39.85 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 896 YDSGIIYCLSRRECDTMADTLQREGLAALAYHAGLSDSARDE--VQHKWINQDNCQVICATIAFGMGIDKPDVRFVIHAS 973
Cdd:cd18799 6 EIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDeaLILLFFGELKPPILVTVDLLTTGVDIPEVDNVVFLR 85
|
90 100
....*....|....*....|....*...
gi 110225360 974 LPKSMEGYYQESGRAGR-DGEISHCVLF 1000
Cdd:cd18799 86 PTESRTLFLQMLGRGLRlHEGKDFFTIL 113
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
665-747 |
8.11e-03 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 40.68 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225360 665 KIFHKKFGLHNFRTNQLEAINA---ALL-GEDCFILMPTGGGKSLCYQLPA---CVSPGVTIVIS----PLRSLIVDQ-- 731
Cdd:COG1199 4 GLLALAFPGFEPRPGQREMAEAvarALAeGRHLLIEAGTGTGKTLAYLVPAllaARETGKKVVIStatkALQEQLVEKdl 83
|
90
....*....|....*...
gi 110225360 732 --VQKLTSFDIPATYLTG 747
Cdd:COG1199 84 plLRKALGLPLRVALLKG 101
|
|
| |
