|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
680-1084 |
7.29e-107 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 348.67 E-value: 7.29e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 680 RETPQEVFRALseLGYSAFRPGQEVAVMRILSGLSTLVVLSTGMGKSLCYQLPAYLYGKrskcITLVISPLVSLMDDQVS 759
Cdd:COG0514 2 RDDALEVLKRV--FGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPG----LTLVVSPLIALMKDQVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 760 GLppH---LKAVCIHSNMSKSQREAAIERVKGGKVHVLLLSPEALvgggrAGSSCLPSADQLPPVAFAcIDEAHCVSEWS 836
Cdd:COG0514 76 AL--RaagIRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERL-----LNPRFLELLRRLKISLFA-IDEAHCISQWG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 837 HNFRPCYLRLcKVLRDRLG--------------VRcllgltatatlataQDVAQHLGIQEEEgiSVRSAAVPPNLHLSVS 902
Cdd:COG0514 148 HDFRPDYRRL-GELRERLPnvpvlaltatatprVR--------------ADIAEQLGLEDPR--VFVGSFDRPNLRLEVV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 903 --TDRDKDQALVSLLQgERFGGldSVIVYCTRREETARIAALIRtrlqgvtlresmtaeEQHHDdsagkrkkakakksir 980
Cdd:COG0514 211 pkPPDDKLAQLLDFLK-EHPGG--SGIVYCLSRKKVEELAEWLR---------------EAGIR---------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 981 cplkwvADSYHGGMSATERRRVQNNFMCGQLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGRDGKPAHC 1060
Cdd:COG0514 257 ------AAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEA 330
|
410 420
....*....|....*....|....
gi 1950408338 1061 HLFLDPEggDLHELRRHIYADTVD 1084
Cdd:COG0514 331 LLLYGPE--DVAIQRFFIEQSPPD 352
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
687-882 |
2.73e-87 |
|
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: 282.61 E-value: 2.73e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 687 FRALSEL-GYSAFRPGQEVAVMRILSGLSTLVVLSTGMGKSLCYQLPAYLYGKRSKCITLVISPLVSLMDDQVSGLPPHL 765
Cdd:cd18018 1 LKLLRRVfGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRRRGPGLTLVVSPLIALMKDQVDALPRAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 766 KAVCIHSNMSKSQREAAIERVKGGKVHVLLLSPEALVggGRAGSSCLPsadQLPPVAFACIDEAHCVSEWSHNFRPCYLR 845
Cdd:cd18018 81 KAAALNSSLTREERRRILEKLRAGEVKILYVSPERLV--NESFRELLR---QTPPISLLVVDEAHCISEWSHNFRPDYLR 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 1950408338 846 LCKVLRDRLGVRCLLGLTATATLATAQDVAQHLGIQE 882
Cdd:cd18018 156 LCRVLRELLGAPPVLALTATATKRVVEDIASHLGIPE 192
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
684-1076 |
6.92e-76 |
|
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: 260.47 E-value: 6.92e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 684 QEVFralselGYSAFRPGQEVAVMRILSGLSTLVVLSTGMGKSLCYQLPAYLYGKrskcITLVISPLVSLMDDQV----- 758
Cdd:TIGR00614 4 KKYF------GLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDG----ITLVISPLISLMEDQVlqlqa 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 759 SGLPphlkAVCIHSNMSKSQREAAIERVKGGKVHVLLLSPEALVGGgragSSCLPSADQLPPVAFACIDEAHCVSEWSHN 838
Cdd:TIGR00614 74 LGIP----ATFLNSAQTKEQQLNVLTDLKDGKIKLLYVTPEKISAS----NRLLQTLEERKGITLIAVDEAHCISQWGHD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 839 FRPCYLRLcKVLRDRLGVRCLLGLTATATLATAQDVAQHLGIQEEEgisVRSAAVP-PNLHLSVSTDRDK-DQALVSLLQ 916
Cdd:TIGR00614 146 FRPDYKAL-GSLKQKFPNVPVMALTATASPSVREDILRQLNLLNPQ---IFCTSFDrPNLYYEVRRKTPKiLEDLLRFIR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 917 GERFGglDSVIVYCTRREETARIAAlirtRLQGVTLResmtaeeqhhddsagkrkkakakksircplkwvADSYHGGMSA 996
Cdd:TIGR00614 222 KEFEG--KSGIIYCPSRKKVEQVAA----ELQKLGLA---------------------------------AGAYHAGLED 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 997 TERRRVQNNFMCGQLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGRDGKPAHCHLFLDPegGDLHELRR 1076
Cdd:TIGR00614 263 SARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECHLFYAP--ADMNRLRR 340
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
684-1076 |
7.28e-68 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 241.54 E-value: 7.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 684 QEVFralselGYSAFRPGQEVAVMRILSGLSTLVVLSTGMGKSLCYQLPAYLYGKrskcITLVISPLVSLMDDQVSGLPP 763
Cdd:PRK11057 18 QETF------GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDG----LTLVVSPLISLMKDQVDQLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 764 H-LKAVCIHSNMSKSQREAAIERVKGGKVHVLLLSPEALVgggraGSSCLPSADQLPPVAFAcIDEAHCVSEWSHNFRPC 842
Cdd:PRK11057 88 NgVAAACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLM-----MDNFLEHLAHWNPALLA-VDEAHCISQWGHDFRPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 843 YLRLCKvLRDRLGVRCLLGLTATATLATAQDVAQHLGIQEeegisvrsaavpPNLHLSvSTDRDK------------DQa 910
Cdd:PRK11057 162 YAALGQ-LRQRFPTLPFMALTATADDTTRQDIVRLLGLND------------PLIQIS-SFDRPNirytlvekfkplDQ- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 911 LVSLLQGERFgglDSVIVYCTRREETARIAAlirtRLQGVTLResmtaeeqhhddsagkrkkakakksircplkwvADSY 990
Cdd:PRK11057 227 LMRYVQEQRG---KSGIIYCNSRAKVEDTAA----RLQSRGIS---------------------------------AAAY 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 991 HGGMSATERRRVQNNFMCGQLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGRDGKPAHCHLFLDPegGD 1070
Cdd:PRK11057 267 HAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDP--AD 344
|
....*.
gi 1950408338 1071 LHELRR 1076
Cdd:PRK11057 345 MAWLRR 350
|
|
| DpdF |
NF041063 |
protein DpdF; |
693-1062 |
3.99e-35 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 145.44 E-value: 3.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 693 LGYSAFR-PGQEVAVMRILS---GlSTLVV-LSTGMGKSLCYQLPAyLYGKRSKCITLVISPLVSLMDDQVSGL------ 761
Cdd:NF041063 135 LGFTHYRsPGQREAVRAALLappG-STLIVnLPTGSGKSLVAQAPA-LLASRQGGLTLVVVPTVALAIDQERRArellrr 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 762 --PPHLKAVCIHSNMSKSQREAAIERVKGGKVHVLLLSPEALVGGgragssclpsadqLPPVAFAC----------IDEA 829
Cdd:NF041063 213 agPDLGGPLAWHGGLSAEERAAIRQRIRDGTQRILFTSPESLTGS-------------LRPALFDAaeagllrylvVDEA 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 830 HCVSEWSHNFRPCYLRLcKVLRDRLGVRCLLGLtatatlataQ---------------DVAQHLGIQEEEGISVRSAAVP 894
Cdd:NF041063 280 HLVDQWGDGFRPEFQLL-AGLRRSLLRLAPSGR---------PfrtlllsatltestlDTLETLFGPPGPFIVVSAVQLR 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 895 P----NLHLSVSTDrDKDQALvsllqgerfggLDSV-------IVYCTRREETARIAALIRTrlQGVTlresmtaeeqhh 963
Cdd:NF041063 350 PepayWVAKCDSEE-ERRERV-----------LEALrhlprplILYVTKVEDAEAWLQRLRA--AGFR------------ 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 964 ddsagkrkkakakksiRCplkwvaDSYHGGMSATERRRVQNNFMCGQLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFES 1043
Cdd:NF041063 404 ----------------RV------ALFHGDTPDAERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDR 461
|
410
....*....|....*....
gi 1950408338 1044 YVQEIGRAGRDGKPAHCHL 1062
Cdd:NF041063 462 FYQEVGRGGRDGKASLSLL 480
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
987-1055 |
4.20e-20 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 85.73 E-value: 4.20e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1950408338 987 ADSYHGGMSATERRRVQNNFMCGQLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGRDG 1055
Cdd:smart00490 14 VARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
|
|
| RecQL4_SLD2_NTD |
cd22289 |
N-terminal homeodomain-like domain of metazoan RecQ protein-like 4 (RecQL4), fungal DNA ... |
2-50 |
6.05e-19 |
|
N-terminal homeodomain-like domain of metazoan RecQ protein-like 4 (RecQL4), fungal DNA replication regulator SLD2 and similar proteins; RecQL4, also called ATP-dependent DNA helicase Q4, or DNA helicase, RecQ-like type 4 (RecQ4), or RTS, is a DNA-dependent ATPase that may modulate chromosome segregation. This family also includes fungal DNA replication regulator SLD2, also known as DNA replication and checkpoint protein 1 (DRC1), which functions with DPB11 to control DNA replication and the S-phase checkpoint. It is also required for the proper activation of RAD53 in response to DNA damage and replication blocks. This model corresponds to the N-terminal domain of RecQL4 and SLD2, which is a homeodomain-like DNA interaction motif.
Pssm-ID: 412085 Cd Length: 49 Bit Score: 81.52 E-value: 6.05e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1950408338 2 DRYNEVKVLLKKWEMTFLQEHQRKPSKTDMEEAPEETKKLYREYKALKQ 50
Cdd:cd22289 1 ERLQELKIALKTWERAFAKKHGRKPTKDDIKAAPEEIKDLYKEYAKLKK 49
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
979-1055 |
1.84e-17 |
|
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: 79.18 E-value: 1.84e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1950408338 979 IRCPLKWVADSYHGGMSATERRRVQNNFMCGQLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGRDG 1055
Cdd:pfam00271 33 LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| Drc1-Sld2 |
pfam11719 |
DNA replication and checkpoint protein; Genome duplication is precisely regulated by ... |
5-67 |
4.64e-07 |
|
DNA replication and checkpoint protein; Genome duplication is precisely regulated by cyclin-dependent kinases CDKs, which bring about the onset of S phase by activating replication origins and then prevent re-licensing of origins until mitosis is completed. The optimum sequence motif for CDK phosphorylation is S/T-P-K/R-K/R, and Drc1-Sld2 is found to have at least 11 potential phosphorylation sites. Drc1 is required for DNA synthesis and S-M replication checkpoint control. Drc1 associates with Cdc2 and is phosphorylated at the onset of S phase when Cdc2 is activated. Thus Cdc2 promotes DNA replication by phosphorylating Drc1 and regulating its association with Cut5. Sld2 and Sld3 represent the minimal set of S-CDK substrates required for DNA replication.
Pssm-ID: 371692 [Multi-domain] Cd Length: 391 Bit Score: 54.07 E-value: 4.64e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1950408338 5 NEVKVLLKKWEMTFLQEHQRKPSKTDMEEAPeETKKLYREYKALKQAREHQGLPESSSVCQQA 67
Cdd:pfam11719 2 SQLKAEIKEWERAFAAKNGRKPSKDDIKKNP-EIAKKYKLYSKLKKGESIKTKTPSKPVKLEA 63
|
|
| ZnF_C2HC |
smart00343 |
zinc finger; |
573-588 |
2.71e-03 |
|
zinc finger;
Pssm-ID: 197667 [Multi-domain] Cd Length: 17 Bit Score: 36.65 E-value: 2.71e-03
|
| zf-CCHC |
pfam00098 |
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ... |
572-588 |
5.70e-03 |
|
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.
Pssm-ID: 395050 [Multi-domain] Cd Length: 18 Bit Score: 35.58 E-value: 5.70e-03
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
680-1084 |
7.29e-107 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 348.67 E-value: 7.29e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 680 RETPQEVFRALseLGYSAFRPGQEVAVMRILSGLSTLVVLSTGMGKSLCYQLPAYLYGKrskcITLVISPLVSLMDDQVS 759
Cdd:COG0514 2 RDDALEVLKRV--FGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPG----LTLVVSPLIALMKDQVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 760 GLppH---LKAVCIHSNMSKSQREAAIERVKGGKVHVLLLSPEALvgggrAGSSCLPSADQLPPVAFAcIDEAHCVSEWS 836
Cdd:COG0514 76 AL--RaagIRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERL-----LNPRFLELLRRLKISLFA-IDEAHCISQWG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 837 HNFRPCYLRLcKVLRDRLG--------------VRcllgltatatlataQDVAQHLGIQEEEgiSVRSAAVPPNLHLSVS 902
Cdd:COG0514 148 HDFRPDYRRL-GELRERLPnvpvlaltatatprVR--------------ADIAEQLGLEDPR--VFVGSFDRPNLRLEVV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 903 --TDRDKDQALVSLLQgERFGGldSVIVYCTRREETARIAALIRtrlqgvtlresmtaeEQHHDdsagkrkkakakksir 980
Cdd:COG0514 211 pkPPDDKLAQLLDFLK-EHPGG--SGIVYCLSRKKVEELAEWLR---------------EAGIR---------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 981 cplkwvADSYHGGMSATERRRVQNNFMCGQLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGRDGKPAHC 1060
Cdd:COG0514 257 ------AAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEA 330
|
410 420
....*....|....*....|....
gi 1950408338 1061 HLFLDPEggDLHELRRHIYADTVD 1084
Cdd:COG0514 331 LLLYGPE--DVAIQRFFIEQSPPD 352
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
687-882 |
2.73e-87 |
|
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: 282.61 E-value: 2.73e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 687 FRALSEL-GYSAFRPGQEVAVMRILSGLSTLVVLSTGMGKSLCYQLPAYLYGKRSKCITLVISPLVSLMDDQVSGLPPHL 765
Cdd:cd18018 1 LKLLRRVfGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRRRGPGLTLVVSPLIALMKDQVDALPRAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 766 KAVCIHSNMSKSQREAAIERVKGGKVHVLLLSPEALVggGRAGSSCLPsadQLPPVAFACIDEAHCVSEWSHNFRPCYLR 845
Cdd:cd18018 81 KAAALNSSLTREERRRILEKLRAGEVKILYVSPERLV--NESFRELLR---QTPPISLLVVDEAHCISEWSHNFRPDYLR 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 1950408338 846 LCKVLRDRLGVRCLLGLTATATLATAQDVAQHLGIQE 882
Cdd:cd18018 156 LCRVLRELLGAPPVLALTATATKRVVEDIASHLGIPE 192
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
684-1076 |
6.92e-76 |
|
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: 260.47 E-value: 6.92e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 684 QEVFralselGYSAFRPGQEVAVMRILSGLSTLVVLSTGMGKSLCYQLPAYLYGKrskcITLVISPLVSLMDDQV----- 758
Cdd:TIGR00614 4 KKYF------GLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDG----ITLVISPLISLMEDQVlqlqa 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 759 SGLPphlkAVCIHSNMSKSQREAAIERVKGGKVHVLLLSPEALVGGgragSSCLPSADQLPPVAFACIDEAHCVSEWSHN 838
Cdd:TIGR00614 74 LGIP----ATFLNSAQTKEQQLNVLTDLKDGKIKLLYVTPEKISAS----NRLLQTLEERKGITLIAVDEAHCISQWGHD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 839 FRPCYLRLcKVLRDRLGVRCLLGLTATATLATAQDVAQHLGIQEEEgisVRSAAVP-PNLHLSVSTDRDK-DQALVSLLQ 916
Cdd:TIGR00614 146 FRPDYKAL-GSLKQKFPNVPVMALTATASPSVREDILRQLNLLNPQ---IFCTSFDrPNLYYEVRRKTPKiLEDLLRFIR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 917 GERFGglDSVIVYCTRREETARIAAlirtRLQGVTLResmtaeeqhhddsagkrkkakakksircplkwvADSYHGGMSA 996
Cdd:TIGR00614 222 KEFEG--KSGIIYCPSRKKVEQVAA----ELQKLGLA---------------------------------AGAYHAGLED 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 997 TERRRVQNNFMCGQLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGRDGKPAHCHLFLDPegGDLHELRR 1076
Cdd:TIGR00614 263 SARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECHLFYAP--ADMNRLRR 340
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
684-1076 |
7.28e-68 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 241.54 E-value: 7.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 684 QEVFralselGYSAFRPGQEVAVMRILSGLSTLVVLSTGMGKSLCYQLPAYLYGKrskcITLVISPLVSLMDDQVSGLPP 763
Cdd:PRK11057 18 QETF------GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDG----LTLVVSPLISLMKDQVDQLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 764 H-LKAVCIHSNMSKSQREAAIERVKGGKVHVLLLSPEALVgggraGSSCLPSADQLPPVAFAcIDEAHCVSEWSHNFRPC 842
Cdd:PRK11057 88 NgVAAACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLM-----MDNFLEHLAHWNPALLA-VDEAHCISQWGHDFRPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 843 YLRLCKvLRDRLGVRCLLGLTATATLATAQDVAQHLGIQEeegisvrsaavpPNLHLSvSTDRDK------------DQa 910
Cdd:PRK11057 162 YAALGQ-LRQRFPTLPFMALTATADDTTRQDIVRLLGLND------------PLIQIS-SFDRPNirytlvekfkplDQ- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 911 LVSLLQGERFgglDSVIVYCTRREETARIAAlirtRLQGVTLResmtaeeqhhddsagkrkkakakksircplkwvADSY 990
Cdd:PRK11057 227 LMRYVQEQRG---KSGIIYCNSRAKVEDTAA----RLQSRGIS---------------------------------AAAY 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 991 HGGMSATERRRVQNNFMCGQLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGRDGKPAHCHLFLDPegGD 1070
Cdd:PRK11057 267 HAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDP--AD 344
|
....*.
gi 1950408338 1071 LHELRR 1076
Cdd:PRK11057 345 MAWLRR 350
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
684-855 |
2.05e-57 |
|
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: 196.99 E-value: 2.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 684 QEVFralselGYSAFRPGQEVAVMRILSGLSTLVVLSTGMGKSLCYQLPAYLygkrSKCITLVISPLVSLMDDQVSGLPP 763
Cdd:cd17920 5 KEVF------GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALL----LDGVTLVVSPLISLMQDQVDRLQQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 764 H-LKAVCIHSNMSKSQREAAIERVKGGKVHVLLLSPEALVgggraGSSCLPSADQLP---PVAFACIDEAHCVSEWSHNF 839
Cdd:cd17920 75 LgIRAAALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLL-----SPDFLELLQRLPerkRLALIVVDEAHCVSQWGHDF 149
|
170
....*....|....*.
gi 1950408338 840 RPCYLRLCKvLRDRLG 855
Cdd:cd17920 150 RPDYLRLGR-LRRALP 164
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
894-1063 |
1.14e-48 |
|
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: 169.31 E-value: 1.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 894 PPNLHLSVSTDRDKDQALVSLLQGERFGGLDSVIVYCTRREETARIAALIRTRlqGVTlresmtaeeqhhddsagkrkka 973
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSK--GIS---------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 974 kakksircplkwvADSYHGGMSATERRRVQNNFMCGQLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGR 1053
Cdd:cd18794 57 -------------AAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGR 123
|
170
....*....|
gi 1950408338 1054 DGKPAHCHLF 1063
Cdd:cd18794 124 DGLPSECILF 133
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
694-1063 |
1.34e-38 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 157.75 E-value: 1.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 694 GYSAFRPGQEVAVMRILSGLSTLVVLSTGMGKSLCYQLPAYLYGKrskcITLVISPLVSLMDDQVSGL-PPHLKAVCIHS 772
Cdd:PLN03137 457 GNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPG----ITLVISPLVSLIQDQIMNLlQANIPAASLSA 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 773 NMSKSQREAAIERVKGG--KVHVLLLSPEALVgggrAGSSCLPSADQLPP---VAFACIDEAHCVSEWSHNFRPCYLRLc 847
Cdd:PLN03137 533 GMEWAEQLEILQELSSEysKYKLLYVTPEKVA----KSDSLLRHLENLNSrglLARFVIDEAHCVSQWGHDFRPDYQGL- 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 848 KVLRDRLGVRCLLGLTATATLATAQDVAQHLGIQeeEGISVRSAAVPPNLHLSVSTDRDKdqALVSLLQGERFGGLDSV- 926
Cdd:PLN03137 608 GILKQKFPNIPVLALTATATASVKEDVVQALGLV--NCVVFRQSFNRPNLWYSVVPKTKK--CLEDIDKFIKENHFDECg 683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 927 IVYCTRREETARIAalirTRLQgvtlresmtaeeqhhddsagkrkkakakksiRCPLKwvADSYHGGMSATERRRVQNNF 1006
Cdd:PLN03137 684 IIYCLSRMDCEKVA----ERLQ-------------------------------EFGHK--AAFYHGSMDPAQRAFVQKQW 726
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1950408338 1007 MCGQLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGRDGKPAHCHLF 1063
Cdd:PLN03137 727 SKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLY 783
|
|
| DpdF |
NF041063 |
protein DpdF; |
693-1062 |
3.99e-35 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 145.44 E-value: 3.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 693 LGYSAFR-PGQEVAVMRILS---GlSTLVV-LSTGMGKSLCYQLPAyLYGKRSKCITLVISPLVSLMDDQVSGL------ 761
Cdd:NF041063 135 LGFTHYRsPGQREAVRAALLappG-STLIVnLPTGSGKSLVAQAPA-LLASRQGGLTLVVVPTVALAIDQERRArellrr 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 762 --PPHLKAVCIHSNMSKSQREAAIERVKGGKVHVLLLSPEALVGGgragssclpsadqLPPVAFAC----------IDEA 829
Cdd:NF041063 213 agPDLGGPLAWHGGLSAEERAAIRQRIRDGTQRILFTSPESLTGS-------------LRPALFDAaeagllrylvVDEA 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 830 HCVSEWSHNFRPCYLRLcKVLRDRLGVRCLLGLtatatlataQ---------------DVAQHLGIQEEEGISVRSAAVP 894
Cdd:NF041063 280 HLVDQWGDGFRPEFQLL-AGLRRSLLRLAPSGR---------PfrtlllsatltestlDTLETLFGPPGPFIVVSAVQLR 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 895 P----NLHLSVSTDrDKDQALvsllqgerfggLDSV-------IVYCTRREETARIAALIRTrlQGVTlresmtaeeqhh 963
Cdd:NF041063 350 PepayWVAKCDSEE-ERRERV-----------LEALrhlprplILYVTKVEDAEAWLQRLRA--AGFR------------ 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 964 ddsagkrkkakakksiRCplkwvaDSYHGGMSATERRRVQNNFMCGQLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFES 1043
Cdd:NF041063 404 ----------------RV------ALFHGDTPDAERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDR 461
|
410
....*....|....*....
gi 1950408338 1044 YVQEIGRAGRDGKPAHCHL 1062
Cdd:NF041063 462 FYQEVGRGGRDGKASLSLL 480
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
676-846 |
1.75e-31 |
|
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: 123.24 E-value: 1.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 676 DGKVRETPQEVFralselGYSAFRPGQEVAVMRILSGLSTLVVLSTGMGKSLCYQLPAYLygkrSKCITLVISPLVSLMD 755
Cdd:cd18015 3 SGKVKDTLKNVF------KLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALC----SDGFTLVVSPLISLME 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 756 DQVSGLPP-HLKAVCIHSNMSKSQREAAIERVKGGK--VHVLLLSPEALVGGGRAGSScLPSADQLPPVAFACIDEAHCV 832
Cdd:cd18015 73 DQLMALKKlGISATMLNASSSKEHVKWVHAALTDKNseLKLLYVTPEKIAKSKRFMSK-LEKAYNAGRLARIAIDEVHCC 151
|
170
....*....|....
gi 1950408338 833 SEWSHNFRPCYLRL 846
Cdd:cd18015 152 SQWGHDFRPDYKKL 165
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
694-855 |
3.90e-30 |
|
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: 118.72 E-value: 3.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 694 GYSAFRPGQEVAVMRIL-SGLSTLVVLSTGMGKSLCYQLPAYLYGKrskcITLVISPLVSLMDDQV-----SGLPphlkA 767
Cdd:cd18017 9 GHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVLLNS----LTLVISPLISLMEDQVlqlvmSNIP----A 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 768 VCIHSNMSKSQREAaierVKGGKVHVLLLSPEALVGGGRAGSSClpsADQLPPVAfacIDEAHCVSEWSHNFRPCYlRLC 847
Cdd:cd18017 81 CFLGSAQSQNVLDD----IKMGKIRVIYVTPEFVSKGLELLQQL---RNGITLIA---IDEAHCVSQWGHDFRSSY-RHL 149
|
....*...
gi 1950408338 848 KVLRDRLG 855
Cdd:cd18017 150 GSIRNRLP 157
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
694-858 |
1.69e-27 |
|
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: 111.41 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 694 GYSAFR-PGQEVAVMRILSG-LSTLVVLSTGMGKSLCYQLPAYLYgkrsKCITLVISPLVSLMDDQVSglppHLKAVCIH 771
Cdd:cd18014 9 GHSDFKsPLQEKATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLA----KGITIVISPLIALIQDQVD----HLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 772 -----SNMSKSQREAAIERVKGG--KVHVLLLSPEAlvgggRAGSSCLPSADQLPP---VAFACIDEAHCVSEWSHNFRP 841
Cdd:cd18014 81 vdslnSKLSAQERKRIIADLESEkpQTKFLYITPEM-----AATSSFQPLLSSLVSrnlLSYLVVDEAHCVSQWGHDFRP 155
|
170
....*....|....*...
gi 1950408338 842 CYLRLcKVLRDRLG-VRC 858
Cdd:cd18014 156 DYLRL-GALRSRYGhVPW 172
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
691-853 |
7.86e-24 |
|
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: 101.06 E-value: 7.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 691 SELGYSAFRPGQEVAVMRILSGLSTLVVLSTGMGKSLCYQLPAYLygkrSKCITLVISPLVSLMDDQVSglppHLKAVCI 770
Cdd:cd18016 11 KKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACV----SPGVTVVISPLRSLIVDQVQ----KLTSLDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 771 HSN-MSKSQREAAIERV------KGGKVHVLLLSPEALVGGGRAGSScLPSADQLPPVAFACIDEAHCVSEWSHNFRPCY 843
Cdd:cd18016 83 PATyLTGDKTDAEATKIylqlskKDPIIKLLYVTPEKISASNRLIST-LENLYERKLLARFVIDEAHCVSQWGHDFRPDY 161
|
170
....*....|
gi 1950408338 844 LRLcKVLRDR 853
Cdd:cd18016 162 KRL-NMLRQK 170
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
987-1055 |
4.20e-20 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 85.73 E-value: 4.20e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1950408338 987 ADSYHGGMSATERRRVQNNFMCGQLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGRDG 1055
Cdd:smart00490 14 VARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
|
|
| RecQL4_SLD2_NTD |
cd22289 |
N-terminal homeodomain-like domain of metazoan RecQ protein-like 4 (RecQL4), fungal DNA ... |
2-50 |
6.05e-19 |
|
N-terminal homeodomain-like domain of metazoan RecQ protein-like 4 (RecQL4), fungal DNA replication regulator SLD2 and similar proteins; RecQL4, also called ATP-dependent DNA helicase Q4, or DNA helicase, RecQ-like type 4 (RecQ4), or RTS, is a DNA-dependent ATPase that may modulate chromosome segregation. This family also includes fungal DNA replication regulator SLD2, also known as DNA replication and checkpoint protein 1 (DRC1), which functions with DPB11 to control DNA replication and the S-phase checkpoint. It is also required for the proper activation of RAD53 in response to DNA damage and replication blocks. This model corresponds to the N-terminal domain of RecQL4 and SLD2, which is a homeodomain-like DNA interaction motif.
Pssm-ID: 412085 Cd Length: 49 Bit Score: 81.52 E-value: 6.05e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1950408338 2 DRYNEVKVLLKKWEMTFLQEHQRKPSKTDMEEAPEETKKLYREYKALKQ 50
Cdd:cd22289 1 ERLQELKIALKTWERAFAKKHGRKPTKDDIKAAPEEIKDLYKEYAKLKK 49
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
690-851 |
7.10e-18 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 83.70 E-value: 7.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 690 LSELGYSAFRPGQEVAVMRILSGL-STLVVLSTGMGKSLCYQLPAYLYGKRSKCI-TLVISPLVSLMDDQVS-----GLP 762
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRGKGGrVLVLVPTRELAEQWAEelkklGPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 763 PHLKAVCIHSNMSKSQREAAIERvkgGKVHVLLLSPEALVgggragSSCLPSADQLPPVAFACIDEAHCVSEWshNFRPC 842
Cdd:smart00487 81 LGLKVVGLYGGDSKREQLRKLES---GKTDILVTTPGRLL------DLLENDKLSLSNVDLVILDEAHRLLDG--GFGDQ 149
|
....*....
gi 1950408338 843 YLRLCKVLR 851
Cdd:smart00487 150 LEKLLKLLP 158
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
979-1055 |
1.84e-17 |
|
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: 79.18 E-value: 1.84e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1950408338 979 IRCPLKWVADSYHGGMSATERRRVQNNFMCGQLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGRDG 1055
Cdd:pfam00271 33 LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
699-851 |
2.07e-16 |
|
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: 78.05 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 699 RPGQEVAVMRILSGLSTLVVLSTGMGKSLCYQLPAY--LYGKRSKCITLVISPLVSLMDDQVS-----GLPPHLKAVCIH 771
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALeaLDKLDNGPQALVLAPTRELAEQIYEelkklGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 772 SNMSKSQREAAIErvkggKVHVLLLSPEALVgggragsSCLPSADQLPPVAFACIDEAHCVSEWShnFRPCYLRLCKVLR 851
Cdd:pfam00270 81 GGDSRKEQLEKLK-----GPDILVGTPGRLL-------DLLQERKLLKNLKLLVLDEAHRLLDMG--FGPDLEEILRRLP 146
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
904-1064 |
1.08e-14 |
|
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: 72.15 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 904 DRDKDQALVSLLQGERFGGldSVIVYCTRREETARIAALIRTrlqgvtlresmtaeeqhhddsagkrkkakakksircpL 983
Cdd:cd18787 10 EEEKKLLLLLLLLEKLKPG--KAIIFVNTKKRVDRLAELLEE-------------------------------------L 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 984 KWVADSYHGGMSATERRRVQNNFMCGQLRIVVAT-VAfGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGRDGKPAHCHL 1062
Cdd:cd18787 51 GIKVAALHGDLSQEERERALKKFRSGKVRVLVATdVA-ARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAIT 129
|
..
gi 1950408338 1063 FL 1064
Cdd:cd18787 130 FV 131
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
904-1098 |
3.98e-14 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 76.34 E-value: 3.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 904 DRDKDQALVSLLQGERFgglDSVIVYCTRREETARIAAlirtRLQ--GVTlresmtaeeqhhddsagkrkkakakksirc 981
Cdd:COG0513 225 KRDKLELLRRLLRDEDP---ERAIVFCNTKRGADRLAE----KLQkrGIS------------------------------ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 982 plkwvADSYHGGMSATERRRVQNNFMCGQLRIVVAT-VAfGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGRDGKPAHC 1060
Cdd:COG0513 268 -----AAALHGDLSQGQRERALDAFRNGKIRVLVATdVA-ARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTA 341
|
170 180 190
....*....|....*....|....*....|....*...
gi 1950408338 1061 HLFLDPEggDLHELRRhiyadtvdfftIKKLVQKVFPR 1098
Cdd:COG0513 342 ISLVTPD--ERRLLRA-----------IEKLIGQKIEE 366
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
989-1058 |
8.97e-12 |
|
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: 64.20 E-value: 8.97e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 989 SYHGGMSATERRRVQNNFMCGQLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGRDGKPA 1058
Cdd:cd18797 71 SYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDS 140
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
978-1071 |
5.70e-11 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 66.74 E-value: 5.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 978 SIRCPLKWVADSYHGGMSATERRRVQNNFMCGQLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGRDGKP 1057
Cdd:PLN00206 386 AITVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEK 465
|
90
....*....|....
gi 1950408338 1058 AHCHLFLDPEGGDL 1071
Cdd:PLN00206 466 GTAIVFVNEEDRNL 479
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
683-1058 |
6.95e-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: 67.17 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 683 PQEVFRALSELGYSAFRPGQEVAVMRILSGLSTLVVLSTGMGKSLCYQLP---AYLYGKRSKciTLVISPLVSLMDDQVS 759
Cdd:COG1205 42 PPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPvleALLEDPGAT--ALYLYPTKALARDQLR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 760 -------GLPPHLKAVCIHSNMSKSQREAAIERVkggkvHVLLLSPEALvgggraGSSCLPSADQLPPVaFAC-----ID 827
Cdd:COG1205 120 rlrelaeALGLGVRVATYDGDTPPEERRWIREHP-----DIVLTNPDML------HYGLLPHHTRWARF-FRNlryvvID 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 828 EAHcvsEW-----SHnfrpcyLRLckVLRdRLgvrcllgltatatlataQDVAQHLGiqeeegisvrsaAVP-------- 894
Cdd:COG1205 188 EAH---TYrgvfgSH------VAN--VLR-RL-----------------RRICRHYG------------SDPqfilasat 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 895 ---PNLHLSVSTDR-----DKDQALvsllQGER-FGGLDSVIVYCTRRE----ETARIAA-LIRTRLQgvTL-----R-- 953
Cdd:COG1205 227 ignPAEHAERLTGRpvtvvDEDGSP----RGERtFVLWNPPLVDDGIRRsalaEAARLLAdLVREGLR--TLvftrsRrg 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 954 -ESMT--AEEQHHDdsagkrkkAKAKKSIRcplkwvadSYHGGMSATERRRVQNNFMCGQLRIVVATVAFGMGLDKSDVR 1030
Cdd:COG1205 301 aELLAryARRALRE--------PDLADRVA--------AYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLD 364
|
410 420 430
....*....|....*....|....*....|
gi 1950408338 1031 G--IVHYnmPKNFESYVQEIGRAGRDGKPA 1058
Cdd:COG1205 365 AvvLAGY--PGTRASFWQQAGRAGRRGQDS 392
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
715-856 |
2.68e-10 |
|
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: 60.11 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 715 TLVVLSTGMGKSLCYQLPAYLYGKRSKCITLVISPLVSLMDDQVSGL----PPHLKAVCIHSNMSKSQREAAIERvkggK 790
Cdd:cd00046 4 VLITAPTGSGKTLAALLAALLLLLKKGKKVLVLVPTKALALQTAERLrelfGPGIRVAVLVGGSSAEEREKNKLG----D 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1950408338 791 VHVLLLSPEALVgggragSSCLPSA-DQLPPVAFACIDEAHCVSEWSHNFRPCYLRLCKVLRDRLGV 856
Cdd:cd00046 80 ADIIIATPDMLL------NLLLREDrLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQV 140
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
985-1067 |
3.91e-10 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 64.41 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 985 WVADSYHGGMSATERRRVQNNFMCGQLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGRDGKPAHCHLFL 1064
Cdd:PTZ00110 402 WPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFL 481
|
...
gi 1950408338 1065 DPE 1067
Cdd:PTZ00110 482 TPD 484
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
1010-1063 |
4.47e-09 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 54.25 E-value: 4.47e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1950408338 1010 QLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGRDGK-PAHCHLF 1063
Cdd:cd18785 22 SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKdEGEVILF 76
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
991-1058 |
3.14e-07 |
|
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: 51.50 E-value: 3.14e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1950408338 991 HGGMSATERRRVQNNFMCGQLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGRDGKPA 1058
Cdd:cd18796 75 HGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPGAA 142
|
|
| Drc1-Sld2 |
pfam11719 |
DNA replication and checkpoint protein; Genome duplication is precisely regulated by ... |
5-67 |
4.64e-07 |
|
DNA replication and checkpoint protein; Genome duplication is precisely regulated by cyclin-dependent kinases CDKs, which bring about the onset of S phase by activating replication origins and then prevent re-licensing of origins until mitosis is completed. The optimum sequence motif for CDK phosphorylation is S/T-P-K/R-K/R, and Drc1-Sld2 is found to have at least 11 potential phosphorylation sites. Drc1 is required for DNA synthesis and S-M replication checkpoint control. Drc1 associates with Cdc2 and is phosphorylated at the onset of S phase when Cdc2 is activated. Thus Cdc2 promotes DNA replication by phosphorylating Drc1 and regulating its association with Cut5. Sld2 and Sld3 represent the minimal set of S-CDK substrates required for DNA replication.
Pssm-ID: 371692 [Multi-domain] Cd Length: 391 Bit Score: 54.07 E-value: 4.64e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1950408338 5 NEVKVLLKKWEMTFLQEHQRKPSKTDMEEAPeETKKLYREYKALKQAREHQGLPESSSVCQQA 67
Cdd:pfam11719 2 SQLKAEIKEWERAFAAKNGRKPSKDDIKKNP-EIAKKYKLYSKLKKGESIKTKTPSKPVKLEA 63
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
989-1077 |
9.04e-07 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 52.91 E-value: 9.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 989 SYHGGMSATERRRVQNNFMCGQLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGRDGKPAHCHLFLDPEG 1068
Cdd:PTZ00424 296 CMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDD 375
|
90
....*....|
gi 1950408338 1069 GD-LHELRRH 1077
Cdd:PTZ00424 376 IEqLKEIERH 385
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
702-830 |
1.13e-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: 50.28 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 702 QEVAVMRILSGLSTLVVLSTGMGKSLCYQLP---AYLYGKRSKciTLVISPLVSLMDDQVSGL-------PPHLKAVCIH 771
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPileALLRDPGSR--ALYLYPTKALAQDQLRSLrelleqlGLGIRVATYD 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1950408338 772 SNMSKSQREAAIERvkggKVHVLLLSPEALvgggraGSSCLPSADQLPP----VAFACIDEAH 830
Cdd:cd17923 83 GDTPREERRAIIRN----PPRILLTNPDML------HYALLPHHDRWARflrnLRYVVLDEAH 135
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
925-1052 |
1.17e-06 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 53.39 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 925 SVIVYCTRR----EETARIAALIRTRLQgvtlRESMTAEEQHHDDSAGKRKKAKAKKSIrcplKWVADSYHGGMSATERR 1000
Cdd:PRK09751 246 STIVFTNSRglaeKLTARLNELYAARLQ----RSPSIAVDAAHFESTSGATSNRVQSSD----VFIARSHHGSVSKEQRA 317
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1950408338 1001 RVQNNFMCGQLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAG 1052
Cdd:PRK09751 318 ITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
991-1065 |
5.15e-06 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 51.00 E-value: 5.15e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1950408338 991 HGGMSATERRRVQNNFMCGQLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGRDGKPAHCHLFLD 1065
Cdd:PRK11634 276 NGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVE 350
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
685-797 |
8.54e-06 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350682 [Multi-domain] Cd Length: 189 Bit Score: 48.09 E-value: 8.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 685 EVFRALseLGYSAFRPgQEVAVMRILSGLSTLVVLSTGMGKS---LCYQLPAYLYGKRSkcitLVISPLVSLMD---DQV 758
Cdd:cd17924 8 EFFKKK--TGFPPWGA-QRTWAKRLLRGKSFAIIAPTGVGKTtfgLATSLYLASKGKRS----YLIFPTKSLVKqayERL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1950408338 759 SGLPPHL----KAVCIHSNMSKSQREAAIERVKGGKVHVLLLS 797
Cdd:cd17924 81 SKYAEKAgvevKILVYHSRLKKKEKEELLEKIEKGDFDILVTT 123
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
987-1053 |
1.76e-05 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 49.50 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 987 ADSYHGGMSATERRRVQNNFMCGQLRIVVATVAFGMGLD--KSDVrgIvhynmpknFESY--------VQE----IGRAG 1052
Cdd:COG1202 451 AAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDfpASQV--I--------FDSLamgiewlsVQEfhqmLGRAG 520
|
.
gi 1950408338 1053 R 1053
Cdd:COG1202 521 R 521
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
987-1053 |
2.44e-05 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 48.65 E-value: 2.44e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1950408338 987 ADSYHGGMSATERRRVQNNFMCGQLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGR 1053
Cdd:PRK10590 272 SAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGR 338
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
990-1068 |
3.03e-05 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 45.62 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 990 YHGGMSATERRRVQNNFMCGQLRIVVATVAFGMGLD---KSDV-RGIVHYNmPKNFE-----SYVQEIGRAGRDGkpahc 1060
Cdd:cd18795 69 HHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpaRTVIiKGTQRYD-GKGYRelsplEYLQMIGRAGRPG----- 142
|
....*...
gi 1950408338 1061 hlfLDPEG 1068
Cdd:cd18795 143 ---FDTRG 147
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
999-1059 |
5.99e-05 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 47.27 E-value: 5.99e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1950408338 999 RRRVQNNFMCGQLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGRDGKPAH 1059
Cdd:PRK04837 294 RLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGH 354
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
744-795 |
7.63e-05 |
|
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: 43.35 E-value: 7.63e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1950408338 744 TLVISPLVSLMDDQVSGLPPHLKAVCIHSNMSKSQREAAIERVKGGKVHVLL 795
Cdd:pfam00271 18 VLIFSQTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLV 69
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
686-829 |
1.07e-04 |
|
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members 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: 350716 [Multi-domain] Cd Length: 197 Bit Score: 44.76 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 686 VFRALSELGYSAFRPGQEVAVMRILSGLSTLVVLSTGMGKSLCYQLPAYL--------YGKRSKCITLVISP---LVSLM 754
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIhldlqpipREQRNGPGVLVLTPtreLALQI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1950408338 755 DDQVSG-LPPHLKAVCIHSNMSKSQREAAIERvkggKVHVLLLSPealvggGRAGSSCLPSADQLPPVAFACIDEA 829
Cdd:cd17958 81 EAECSKySYKGLKSVCVYGGGNRNEQIEDLSK----GVDIIIATP------GRLNDLQMNNVINLKSITYLVLDEA 146
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
992-1056 |
1.76e-04 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 46.10 E-value: 1.76e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1950408338 992 GGMSATERRRVQNNFMCGQLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGRDGK 1056
Cdd:PRK04537 289 GDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGE 353
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
992-1064 |
1.86e-04 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 45.70 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 992 GGMSATERRRVQNNFMCGQLRIVVAT-VAfGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGRDGKP--------AHCHL 1062
Cdd:PRK11192 277 GEMVQAKRNEAIKRLTDGRVNVLVATdVA-ARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKgtaislveAHDHL 355
|
..
gi 1950408338 1063 FL 1064
Cdd:PRK11192 356 LL 357
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
984-1055 |
1.00e-03 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 43.36 E-value: 1.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1950408338 984 KWVADSYHGGMSATE-----RRRVQNNFMCGQLRIVVATVAFGMGLDKSDVRGIVHYNMPKNFESYVQEIGRAGRDG 1055
Cdd:PRK01297 354 RLVKDGINAAQLSGDvpqhkRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAG 430
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
765-795 |
1.13e-03 |
|
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: 40.57 E-value: 1.13e-03
10 20 30
....*....|....*....|....*....|.
gi 1950408338 765 LKAVCIHSNMSKSQREAAIERVKGGKVHVLL 795
Cdd:cd18787 52 IKVAALHGDLSQEERERALKKFRSGKVRVLV 82
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
984-1070 |
1.44e-03 |
|
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: 40.79 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 984 KWVADSYHGGMSATERRRVQNNFMCGQLRIVVATVAFGMGLDKSDVRGIVHYNmPKNFE-SYVQEI-GRAGRDGKPAHCH 1061
Cdd:cd18811 61 ELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED-AERFGlSQLHQLrGRVGRGDHQSYCL 139
|
....*....
gi 1950408338 1062 LFLDPEGGD 1070
Cdd:cd18811 140 LVYKDPLTE 148
|
|
| ZnF_C2HC |
smart00343 |
zinc finger; |
573-588 |
2.71e-03 |
|
zinc finger;
Pssm-ID: 197667 [Multi-domain] Cd Length: 17 Bit Score: 36.65 E-value: 2.71e-03
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
688-794 |
4.05e-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: 40.12 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 688 RALSELGYSAFRPGQEVAVMRILSGLSTLVVLSTGMGKSLCYQLPA------YLYGKRSKCITLVISP---LVSlmddQV 758
Cdd:cd00268 3 KALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPIlekllpEPKKKGRGPQALVLAPtreLAM----QI 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1950408338 759 S------GLPPHLKAVCIHSNMSKSQREAAIERvkggKVHVL 794
Cdd:cd00268 79 AevarklGKGTGLKVAAIYGGAPIKKQIEALKK----GPDIV 116
|
|
| zf-CCHC |
pfam00098 |
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ... |
572-588 |
5.70e-03 |
|
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.
Pssm-ID: 395050 [Multi-domain] Cd Length: 18 Bit Score: 35.58 E-value: 5.70e-03
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
765-794 |
5.74e-03 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 40.90 E-value: 5.74e-03
10 20 30
....*....|....*....|....*....|
gi 1950408338 765 LKAVCIHSNMSKSQREAAIERVKGGKVHVL 794
Cdd:COG0513 266 ISAAALHGDLSQGQRERALDAFRNGKIRVL 295
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
764-795 |
6.97e-03 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 37.19 E-value: 6.97e-03
10 20 30
....*....|....*....|....*....|..
gi 1950408338 764 HLKAVCIHSNMSKSQREAAIERVKGGKVHVLL 795
Cdd:smart00490 11 GIKVARLHGGLSQEEREEILDKFNNGKIKVLV 42
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
712-801 |
9.71e-03 |
|
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: 38.72 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408338 712 GLSTLVVLSTGMGKSLCYQLPAY--LYGKRSKCI-TLVISPLVSLMDDQ-------VSGLPPHLKAVCIHSNMSKSQREA 781
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALssLADEPEKGVqVLYISPLKALINDQerrleepLDEIDLEIPVAVRHGDTSQSEKAK 80
|
90 100
....*....|....*....|
gi 1950408338 782 AIERVKggkvHVLLLSPEAL 801
Cdd:cd17922 81 QLKNPP----GILITTPESL 96
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