|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
486-900 |
6.13e-106 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 343.66 E-value: 6.13e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 486 EEVLEALRNL-GYDSFRPGQAEAVMRILSGLSTLVVLPTGMGKSLCYQLPAFLyhkNSGsVSLVISPLVSLMDDQVSGLp 564
Cdd:COG0514 3 DDALEVLKRVfGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALL---LPG-LTLVVSPLIALMKDQVDALr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 565 p-cLKAVCIHSNLSQSQREAAMekvttipnfpsfrtaqrrnlgfsrffRQVRNGQAQILLLSPEALVASGssslfFRDRL 643
Cdd:COG0514 79 aagIRAAFLNSSLSAEERREVL--------------------------RALRAGELKLLYVAPERLLNPR-----FLELL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 644 P--PVAFACLDEAHCISQWSHNFRPAYLRVcKVLRQRLG--------------VRcflgltatataataRDVAQHLGIPP 707
Cdd:COG0514 128 RrlKISLFAIDEAHCISQWGHDFRPDYRRL-GELRERLPnvpvlaltatatprVR--------------ADIAEQLGLED 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 708 EQ---GGGVRSaavpaNLLLSVS--MDADREQALLSLLRADPFGSChplIVFCTRREDTERLAALLRSQfpqfpphpkpl 782
Cdd:COG0514 193 PRvfvGSFDRP-----NLRLEVVpkPPDDKLAQLLDFLKEHPGGSG---IVYCLSRKKVEELAEWLREA----------- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 783 gknpgkgktaGIpgfcSATAYHAGLSGPERRRIQRDFMGGRIRVLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVG 862
Cdd:COG0514 254 ----------GI----RAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIG 319
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1799935007 863 RAGRDGSAARCHLFLEPQDLE------PESSGILEFREREKRRL 900
Cdd:COG0514 320 RAGRDGLPAEALLLYGPEDVAiqrffiEQSPPDEERKRVERAKL 363
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
489-707 |
6.32e-83 |
|
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: 269.13 E-value: 6.32e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 489 LEALRNL-GYDSFRPGQAEAVMRILSGLSTLVVLPTGMGKSLCYQLPAFLYHKNSGSVSLVISPLVSLMDDQVSGLPPCL 567
Cdd:cd18018 1 LKLLRRVfGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRRRGPGLTLVVSPLIALMKDQVDALPRAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 568 KAVCIHSNLSQSQREAAMEkvttipnfpsfrtaqrrnlgfsrffrQVRNGQAQILLLSPEALVASGSSSLFFrdRLPPVA 647
Cdd:cd18018 81 KAAALNSSLTREERRRILE--------------------------KLRAGEVKILYVSPERLVNESFRELLR--QTPPIS 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 648 FACLDEAHCISQWSHNFRPAYLRVCKVLRQRLGVRCFLGLTATATAATARDVAQHLGIPP 707
Cdd:cd18018 133 LLVVDEAHCISEWSHNFRPDYLRLCRVLRELLGAPPVLALTATATKRVVEDIASHLGIPE 192
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
493-899 |
3.61e-82 |
|
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: 281.19 E-value: 3.61e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 493 RNLGYDSFRPGQAEAVMRILSGLSTLVVLPTGMGKSLCYQLPAFLYhknsGSVSLVISPLVSLMDDQVSGLPPC-LKAVC 571
Cdd:TIGR01389 7 RTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLL----KGLTVVISPLISLMKDQVDQLRAAgVAAAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 572 IHSNLSQSQReaamekvttipnfpsfrtaqrrnlgfSRFFRQVRNGQAQILLLSPEALVasgssSLFFRDRL---PPVAF 648
Cdd:TIGR01389 83 LNSTLSAKEQ--------------------------QDIEKALVNGELKLLYVAPERLE-----QDYFLNMLqriPIALV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 649 AcLDEAHCISQWSHNFRPAYLRVCkVLRQRLGVRCFLGLTATATAATARDVAQHLGI--PPEQgggVRSAAVPaNLLLSV 726
Cdd:TIGR01389 132 A-VDEAHCVSQWGHDFRPEYQRLG-SLAERFPQVPRIALTATADAETRQDIRELLRLadANEF---ITSFDRP-NLRFSV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 727 SMDADREQALLSLLRADPFGSChplIVFCTRREDTERLAALLRSQfpqfpphpkplgknpgkgktaGIPgfcsATAYHAG 806
Cdd:TIGR01389 206 VKKNNKQKFLLDYLKKHRGQSG---IIYASSRKKVEELAERLESQ---------------------GIS----ALAYHAG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 807 LSGPERRRIQRDFMGGRIRVLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGRDGSAARCHLFLEPQDL---- 882
Cdd:TIGR01389 258 LSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDGLPAEAILLYSPADIallk 337
|
410 420
....*....|....*....|.
gi 1799935007 883 ----EPESSGILEFREREKRR 899
Cdd:TIGR01389 338 rrieQSEADDDYKQIEREKLR 358
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
484-897 |
5.69e-65 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 232.30 E-value: 5.69e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 484 PPEEVLEalRNLGYDSFRPGQAEAVMRILSGLSTLVVLPTGMGKSLCYQLPAFLYhknsGSVSLVISPLVSLMDDQVSGL 563
Cdd:PRK11057 12 LAKQVLQ--ETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVL----DGLTLVVSPLISLMKDQVDQL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 564 PP-CLKAVCIHSNLSQSQREAAMekvttipnfpsfrtaqrrnlgfsrffRQVRNGQAQILLLSPEALVASGssslfFRDR 642
Cdd:PRK11057 86 LAnGVAAACLNSTQTREQQLEVM--------------------------AGCRTGQIKLLYIAPERLMMDN-----FLEH 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 643 LP--PVAFACLDEAHCISQWSHNFRPAYlRVCKVLRQRLGVRCFLGLTATATAATARDVAQHLGI--PPEQGGGVRSAAV 718
Cdd:PRK11057 135 LAhwNPALLAVDEAHCISQWGHDFRPEY-AALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLndPLIQISSFDRPNI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 719 PANLLlsvsmdaDREQALLSLLR--ADPFGSCHplIVFCTRREDTERLAALLRSQfpqfpphpkplgknpgkgktaGIpg 796
Cdd:PRK11057 214 RYTLV-------EKFKPLDQLMRyvQEQRGKSG--IIYCNSRAKVEDTAARLQSR---------------------GI-- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 797 fcSATAYHAGLSGPERRRIQRDFMGGRIRVLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGRDGSAARCHLF 876
Cdd:PRK11057 262 --SAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLF 339
|
410 420
....*....|....*....|....*...
gi 1799935007 877 LEPQD-------LEPESSGILEFREREK 897
Cdd:PRK11057 340 YDPADmawlrrcLEEKPAGQQQDIERHK 367
|
|
| DpdF |
NF041063 |
protein DpdF; |
455-883 |
1.04e-43 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 172.02 E-value: 1.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 455 FPW-PEFSPSPPPAAVD-PLYSPAPDGTIPDPP-EEVLEALrnLGYDSFR-PGQAEAVMRILS---GlSTLVV-LPTGMG 526
Cdd:NF041063 94 RPWrPEWLDAAADDPPFeDVFAERLRRTLEPVPgDPFLAEA--LGFTHYRsPGQREAVRAALLappG-STLIVnLPTGSG 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 527 KSLCYQLPAfLYHKNSGSVSLVISPLVSLMDDQ-------VSGLPPCLKAVCI-HSNLSQSQREAamekvttIpnfpsfr 598
Cdd:NF041063 171 KSLVAQAPA-LLASRQGGLTLVVVPTVALAIDQerrarelLRRAGPDLGGPLAwHGGLSAEERAA-------I------- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 599 taqrrnlgfsrfFRQVRNGQAQILLLSPEALVASGSSSLF-------FRdrlppvAFAcLDEAHCISQWSHNFRPAYlrv 671
Cdd:NF041063 236 ------------RQRIRDGTQRILFTSPESLTGSLRPALFdaaeaglLR------YLV-VDEAHLVDQWGDGFRPEF--- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 672 ckvlrQRLG--VRCFLGLTATATA-----------ATARDVAQHLGIPPEQGGGVRSAAV---PANLLLSVSMDADREQA 735
Cdd:NF041063 294 -----QLLAglRRSLLRLAPSGRPfrtlllsatltESTLDTLETLFGPPGPFIVVSAVQLrpePAYWVAKCDSEEERRER 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 736 LLSLLRADPfgscHPLIVFCTRREDTERLAALLRSQfpqfpphpkplgknpgkgktagipGFCSATAYHAGLSGPERRRI 815
Cdd:NF041063 369 VLEALRHLP----RPLILYVTKVEDAEAWLQRLRAA------------------------GFRRVALFHGDTPDAERERL 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799935007 816 QRDFMGGRIRVLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGRDGSAARCHLFLEPQDLE 883
Cdd:NF041063 421 IEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLD 488
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
799-868 |
1.48e-19 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 84.19 E-value: 1.48e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 799 SATAYHAGLSGPERRRIQRDFMGGRIRVLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGRDG 868
Cdd:smart00490 13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
|
|
| RecQL4_SLD2_NTD |
cd22289 |
N-terminal homeodomain-like domain of metazoan RecQ protein-like 4 (RecQL4), fungal DNA ... |
2-50 |
8.27e-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: 80.75 E-value: 8.27e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1799935007 2 ERQQELKVLLKRWEAEFLRERRRKPSQADIEEAPEETRKLYKEYRMLKQ 50
Cdd:cd22289 1 ERLQELKIALKTWERAFAKKHGRKPTKDDIKAAPEEIKDLYKEYAKLKK 49
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
731-868 |
1.04e-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: 79.95 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 731 DREQALLSLLRADPFGSChplIVFCTRREDTErlAALLRsqfpqfpphpkplgknpgkgKTAGIpgfcSATAYHAGLSGP 810
Cdd:pfam00271 1 EKLEALLELLKKERGGKV---LIFSQTKKTLE--AELLL--------------------EKEGI----KVARLHGDLSQE 51
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799935007 811 ERRRIQRDFMGGRIRVLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGRDG 868
Cdd:pfam00271 52 EREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| Drc1-Sld2 |
pfam11719 |
DNA replication and checkpoint protein; Genome duplication is precisely regulated by ... |
5-60 |
2.00e-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: 54.84 E-value: 2.00e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1799935007 5 QELKVLLKRWEAEFLRERRRKPSQADIEEAPeETRKLYKEYRMLKQQGKASDSSEK 60
Cdd:pfam11719 2 SQLKAEIKEWERAFAAKNGRKPSKDDIKKNP-EIAKKYKLYSKLKKGESIKTKTPS 56
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
21-282 |
5.10e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 47.76 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 21 ERRRKPSQADIEEAPEETRKLYKEYRMLKQQGKASDSSektgSQEIPNVEQvEDSGFWGSHLNRAPKIPGKSRSG-SARP 99
Cdd:PTZ00449 531 EGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHK----PSKIPTLSK-KPEFPKDPKHPKDPEEPKKPKRPrSAQR 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 100 GISAEFYGMKLKAKLGMTGKEP--PLTPRRTPNPRR--IPKIPQSQKNPEREAEASSPEPPRNEGESEKSGD-----AGK 170
Cdd:PTZ00449 606 PTRPKSPKLPELLDIPKSPKRPesPKSPKRPPPPQRpsSPERPEGPKIIKSPKPPKSPKPPFDPKFKEKFYDdyldaAAK 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 171 SGDPEKS----GEFSGLGPLTLPAgmNPGFP-----PVPDKFQRLKQSVAQTLRSLDpgwlqrcQESPENQEFPAGSVRE 241
Cdd:PTZ00449 686 SKETKTTvvldESFESILKETLPE--TPGTPfttprPLPPKLPRDEEFPFEPIGDPD-------AEQPDDIEFFTPPEEE 756
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799935007 242 KGEIHTASIG----------------NSVRKRPREGGGAAEAPAKLQRGPQGSDPGI 282
Cdd:PTZ00449 757 RTFFHETPADtplpdilaeefkeediHAETGEPDEAMKRPDSPSEHEDKPPGDHPSL 813
|
|
| ZnF_C2HC |
smart00343 |
zinc finger; |
383-398 |
1.04e-03 |
|
zinc finger;
Pssm-ID: 197667 [Multi-domain] Cd Length: 17 Bit Score: 37.42 E-value: 1.04e-03
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
803-1046 |
1.23e-03 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 43.02 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 803 YHAG-LSG--PERRR--IQRDFMGGRIRVLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGRDG--------- 868
Cdd:PRK04537 282 YRVGvLSGdvPQKKResLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGeegdaisfa 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 869 ------SAARCHLFLEPQ-DLEPESSGILEFREREKRRLCRGHERCVPVAELV-----QALDLREEGENsgmRPGIRESP 936
Cdd:PRK04537 362 ceryamSLPDIEAYIEQKiPVEPVTAELLTPLPRPPRVPVEGEEADDEAGDSVgtifrEAREQRAAEEQ---RRGGGRSG 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 937 PGpgipgavpafpsRSDRDPPVLPGAASRQLPAAASCHRFPLPHPLLRRRPAAPGAGAELPSR--GRGPGSGALGRGRLP 1014
Cdd:PRK04537 439 PG------------GGSRSGSVGGGGRRDGAGADGKPRPRRKPRVEGEADAAAAGAETPVVAAaaAQAPGVVAADGERAP 506
|
250 260 270
....*....|....*....|....*....|...
gi 1799935007 1015 GIRRRlpeRFHGLGISAGQ-AQPEAAPVGFPKR 1046
Cdd:PRK04537 507 RKRRR---RRNGRPVEGAEpVSTPVPAPAAPRK 536
|
|
| zf-CCHC |
pfam00098 |
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ... |
382-397 |
4.74e-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: 4.74e-03
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
486-900 |
6.13e-106 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 343.66 E-value: 6.13e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 486 EEVLEALRNL-GYDSFRPGQAEAVMRILSGLSTLVVLPTGMGKSLCYQLPAFLyhkNSGsVSLVISPLVSLMDDQVSGLp 564
Cdd:COG0514 3 DDALEVLKRVfGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALL---LPG-LTLVVSPLIALMKDQVDALr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 565 p-cLKAVCIHSNLSQSQREAAMekvttipnfpsfrtaqrrnlgfsrffRQVRNGQAQILLLSPEALVASGssslfFRDRL 643
Cdd:COG0514 79 aagIRAAFLNSSLSAEERREVL--------------------------RALRAGELKLLYVAPERLLNPR-----FLELL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 644 P--PVAFACLDEAHCISQWSHNFRPAYLRVcKVLRQRLG--------------VRcflgltatataataRDVAQHLGIPP 707
Cdd:COG0514 128 RrlKISLFAIDEAHCISQWGHDFRPDYRRL-GELRERLPnvpvlaltatatprVR--------------ADIAEQLGLED 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 708 EQ---GGGVRSaavpaNLLLSVS--MDADREQALLSLLRADPFGSChplIVFCTRREDTERLAALLRSQfpqfpphpkpl 782
Cdd:COG0514 193 PRvfvGSFDRP-----NLRLEVVpkPPDDKLAQLLDFLKEHPGGSG---IVYCLSRKKVEELAEWLREA----------- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 783 gknpgkgktaGIpgfcSATAYHAGLSGPERRRIQRDFMGGRIRVLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVG 862
Cdd:COG0514 254 ----------GI----RAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIG 319
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1799935007 863 RAGRDGSAARCHLFLEPQDLE------PESSGILEFREREKRRL 900
Cdd:COG0514 320 RAGRDGLPAEALLLYGPEDVAiqrffiEQSPPDEERKRVERAKL 363
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
489-707 |
6.32e-83 |
|
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: 269.13 E-value: 6.32e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 489 LEALRNL-GYDSFRPGQAEAVMRILSGLSTLVVLPTGMGKSLCYQLPAFLYHKNSGSVSLVISPLVSLMDDQVSGLPPCL 567
Cdd:cd18018 1 LKLLRRVfGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRRRGPGLTLVVSPLIALMKDQVDALPRAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 568 KAVCIHSNLSQSQREAAMEkvttipnfpsfrtaqrrnlgfsrffrQVRNGQAQILLLSPEALVASGSSSLFFrdRLPPVA 647
Cdd:cd18018 81 KAAALNSSLTREERRRILE--------------------------KLRAGEVKILYVSPERLVNESFRELLR--QTPPIS 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 648 FACLDEAHCISQWSHNFRPAYLRVCKVLRQRLGVRCFLGLTATATAATARDVAQHLGIPP 707
Cdd:cd18018 133 LLVVDEAHCISEWSHNFRPDYLRLCRVLRELLGAPPVLALTATATKRVVEDIASHLGIPE 192
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
493-899 |
3.61e-82 |
|
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: 281.19 E-value: 3.61e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 493 RNLGYDSFRPGQAEAVMRILSGLSTLVVLPTGMGKSLCYQLPAFLYhknsGSVSLVISPLVSLMDDQVSGLPPC-LKAVC 571
Cdd:TIGR01389 7 RTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLL----KGLTVVISPLISLMKDQVDQLRAAgVAAAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 572 IHSNLSQSQReaamekvttipnfpsfrtaqrrnlgfSRFFRQVRNGQAQILLLSPEALVasgssSLFFRDRL---PPVAF 648
Cdd:TIGR01389 83 LNSTLSAKEQ--------------------------QDIEKALVNGELKLLYVAPERLE-----QDYFLNMLqriPIALV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 649 AcLDEAHCISQWSHNFRPAYLRVCkVLRQRLGVRCFLGLTATATAATARDVAQHLGI--PPEQgggVRSAAVPaNLLLSV 726
Cdd:TIGR01389 132 A-VDEAHCVSQWGHDFRPEYQRLG-SLAERFPQVPRIALTATADAETRQDIRELLRLadANEF---ITSFDRP-NLRFSV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 727 SMDADREQALLSLLRADPFGSChplIVFCTRREDTERLAALLRSQfpqfpphpkplgknpgkgktaGIPgfcsATAYHAG 806
Cdd:TIGR01389 206 VKKNNKQKFLLDYLKKHRGQSG---IIYASSRKKVEELAERLESQ---------------------GIS----ALAYHAG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 807 LSGPERRRIQRDFMGGRIRVLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGRDGSAARCHLFLEPQDL---- 882
Cdd:TIGR01389 258 LSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDGLPAEAILLYSPADIallk 337
|
410 420
....*....|....*....|.
gi 1799935007 883 ----EPESSGILEFREREKRR 899
Cdd:TIGR01389 338 rrieQSEADDDYKQIEREKLR 358
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
496-898 |
2.78e-74 |
|
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: 255.08 E-value: 2.78e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 496 GYDSFRPGQAEAVMRILSGLSTLVVLPTGMGKSLCYQLPAFLyhknSGSVSLVISPLVSLMDDQV-----SGLPPCLkav 570
Cdd:TIGR00614 8 GLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALY----SDGITLVISPLISLMEDQVlqlqaLGIPATF--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 571 cihsnLSQSQREAAMEKVTTipnfpsfrtaqrrnlgfsrffrQVRNGQAQILLLSPEALvaSGSSSLFFR--DRLPPVAF 648
Cdd:TIGR00614 81 -----LNSAQTKEQQLNVLT----------------------DLKDGKIKLLYVTPEKI--SASNRLLQTleERKGITLI 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 649 AcLDEAHCISQWSHNFRPAYlRVCKVLRQRLGVRCFLGLTATATAATARDVAQHLGIppeqgggvrsaavpaNLLLSVSM 728
Cdd:TIGR00614 132 A-VDEAHCISQWGHDFRPDY-KALGSLKQKFPNVPVMALTATASPSVREDILRQLNL---------------LNPQIFCT 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 729 DADREQALLSLLR--ADPFGSCHPL----------IVFCTRREDTERLAALLRSQfpqfpphpkplgknpgkgktaGIpg 796
Cdd:TIGR00614 195 SFDRPNLYYEVRRktPKILEDLLRFirkefegksgIIYCPSRKKVEQVAAELQKL---------------------GL-- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 797 fcSATAYHAGLSGPERRRIQRDFMGGRIRVLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGRDGSAARCHLF 876
Cdd:TIGR00614 252 --AAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECHLF 329
|
410 420
....*....|....*....|..
gi 1799935007 877 LEPQDLEPESSGILEFREREKR 898
Cdd:TIGR00614 330 YAPADMNRLRRLLMEEPDGNFR 351
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
484-897 |
5.69e-65 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 232.30 E-value: 5.69e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 484 PPEEVLEalRNLGYDSFRPGQAEAVMRILSGLSTLVVLPTGMGKSLCYQLPAFLYhknsGSVSLVISPLVSLMDDQVSGL 563
Cdd:PRK11057 12 LAKQVLQ--ETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVL----DGLTLVVSPLISLMKDQVDQL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 564 PP-CLKAVCIHSNLSQSQREAAMekvttipnfpsfrtaqrrnlgfsrffRQVRNGQAQILLLSPEALVASGssslfFRDR 642
Cdd:PRK11057 86 LAnGVAAACLNSTQTREQQLEVM--------------------------AGCRTGQIKLLYIAPERLMMDN-----FLEH 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 643 LP--PVAFACLDEAHCISQWSHNFRPAYlRVCKVLRQRLGVRCFLGLTATATAATARDVAQHLGI--PPEQGGGVRSAAV 718
Cdd:PRK11057 135 LAhwNPALLAVDEAHCISQWGHDFRPEY-AALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLndPLIQISSFDRPNI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 719 PANLLlsvsmdaDREQALLSLLR--ADPFGSCHplIVFCTRREDTERLAALLRSQfpqfpphpkplgknpgkgktaGIpg 796
Cdd:PRK11057 214 RYTLV-------EKFKPLDQLMRyvQEQRGKSG--IIYCNSRAKVEDTAARLQSR---------------------GI-- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 797 fcSATAYHAGLSGPERRRIQRDFMGGRIRVLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGRDGSAARCHLF 876
Cdd:PRK11057 262 --SAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLF 339
|
410 420
....*....|....*....|....*...
gi 1799935007 877 LEPQD-------LEPESSGILEFREREK 897
Cdd:PRK11057 340 YDPADmawlrrcLEEKPAGQQQDIERHK 367
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
489-707 |
8.16e-55 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 189.67 E-value: 8.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 489 LEALRNL-GYDSFRPGQAEAVMRILSGLSTLVVLPTGMGKSLCYQLPAFLYHKnsgsVSLVISPLVSLMDDQVSGLPP-C 566
Cdd:cd17920 1 EQILKEVfGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDG----VTLVVSPLISLMQDQVDRLQQlG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 567 LKAVCIHSNLSQSQREAAMEKvttipnfpsfrtaqrrnlgfsrffrqVRNGQAQILLLSPEALVASGSSSLFFRD-RLPP 645
Cdd:cd17920 77 IRAAALNSTLSPEEKREVLLR--------------------------IKNGQYKLLYVTPERLLSPDFLELLQRLpERKR 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799935007 646 VAFACLDEAHCISQWSHNFRPAYLRVCKvLRQRLGVRCFLGLTATATAATARDVAQHLGIPP 707
Cdd:cd17920 131 LALIVVDEAHCVSQWGHDFRPDYLRLGR-LRRALPGVPILALTATATPEVREDILKRLGLRN 191
|
|
| DpdF |
NF041063 |
protein DpdF; |
455-883 |
1.04e-43 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 172.02 E-value: 1.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 455 FPW-PEFSPSPPPAAVD-PLYSPAPDGTIPDPP-EEVLEALrnLGYDSFR-PGQAEAVMRILS---GlSTLVV-LPTGMG 526
Cdd:NF041063 94 RPWrPEWLDAAADDPPFeDVFAERLRRTLEPVPgDPFLAEA--LGFTHYRsPGQREAVRAALLappG-STLIVnLPTGSG 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 527 KSLCYQLPAfLYHKNSGSVSLVISPLVSLMDDQ-------VSGLPPCLKAVCI-HSNLSQSQREAamekvttIpnfpsfr 598
Cdd:NF041063 171 KSLVAQAPA-LLASRQGGLTLVVVPTVALAIDQerrarelLRRAGPDLGGPLAwHGGLSAEERAA-------I------- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 599 taqrrnlgfsrfFRQVRNGQAQILLLSPEALVASGSSSLF-------FRdrlppvAFAcLDEAHCISQWSHNFRPAYlrv 671
Cdd:NF041063 236 ------------RQRIRDGTQRILFTSPESLTGSLRPALFdaaeaglLR------YLV-VDEAHLVDQWGDGFRPEF--- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 672 ckvlrQRLG--VRCFLGLTATATA-----------ATARDVAQHLGIPPEQGGGVRSAAV---PANLLLSVSMDADREQA 735
Cdd:NF041063 294 -----QLLAglRRSLLRLAPSGRPfrtlllsatltESTLDTLETLFGPPGPFIVVSAVQLrpePAYWVAKCDSEEERRER 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 736 LLSLLRADPfgscHPLIVFCTRREDTERLAALLRSQfpqfpphpkplgknpgkgktagipGFCSATAYHAGLSGPERRRI 815
Cdd:NF041063 369 VLEALRHLP----RPLILYVTKVEDAEAWLQRLRAA------------------------GFRRVALFHGDTPDAERERL 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799935007 816 QRDFMGGRIRVLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGRDGSAARCHLFLEPQDLE 883
Cdd:NF041063 421 IEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLD 488
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
721-876 |
1.10e-43 |
|
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: 155.06 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 721 NLLLSVSMDADREQALLSLLRADPFGSCHPLIVFCTRREDTERLAALLRSQfpqfpphpkplgknpgkgktaGIpgfcSA 800
Cdd:cd18794 3 NLFYSVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSK---------------------GI----SA 57
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799935007 801 TAYHAGLSGPERRRIQRDFMGGRIRVLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGRDGSAARCHLF 876
Cdd:cd18794 58 AAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
496-876 |
1.89e-42 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 169.69 E-value: 1.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 496 GYDSFRPGQAEAVMRILSGLSTLVVLPTGMGKSLCYQLPAFLyhknSGSVSLVISPLVSLMDDQVSGLppclkavcIHSN 575
Cdd:PLN03137 457 GNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALI----CPGITLVISPLVSLIQDQIMNL--------LQAN 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 576 LSQSQREAAMEKVTTIPNFpsfrtaQRRNLGFSRFfrqvrngqaQILLLSPEALVASGS-----SSLFFRDRLppvAFAC 650
Cdd:PLN03137 525 IPAASLSAGMEWAEQLEIL------QELSSEYSKY---------KLLYVTPEKVAKSDSllrhlENLNSRGLL---ARFV 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 651 LDEAHCISQWSHNFRPAYlRVCKVLRQRLGVRCFLGLTATATAATARDVAQHLGIppeqgggV-----RSAAVPANLLLS 725
Cdd:PLN03137 587 IDEAHCVSQWGHDFRPDY-QGLGILKQKFPNIPVLALTATATASVKEDVVQALGL-------VncvvfRQSFNRPNLWYS 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 726 VS-------MDADReqallsLLRADPFGSCHplIVFCTRREDTERLAALLRSqfpqfpphpkplgknpgkgktagipgFC 798
Cdd:PLN03137 659 VVpktkkclEDIDK------FIKENHFDECG--IIYCLSRMDCEKVAERLQE--------------------------FG 704
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799935007 799 SATAYHAGLSGPERRR-IQRDFMGGRIRVLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGRDGSAARCHLF 876
Cdd:PLN03137 705 HKAAFYHGSMDPAQRAfVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLY 783
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
486-668 |
1.80e-27 |
|
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: 111.30 E-value: 1.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 486 EEVLEALRN-LGYDSFRPGQAEAVMRILSGLSTLVVLPTGMGKSLCYQLPAFLyhknSGSVSLVISPLVSLMDDQVSGLP 564
Cdd:cd18015 4 GKVKDTLKNvFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALC----SDGFTLVVSPLISLMEDQLMALK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 565 PC-LKAVCIHSNlsqSQREAAmekvttipnfpsfrtaqrrnlgfSRFFRQVRNGQAQILLL--SPEALvasgSSSLFFRD 641
Cdd:cd18015 80 KLgISATMLNAS---SSKEHV-----------------------KWVHAALTDKNSELKLLyvTPEKI----AKSKRFMS 129
|
170 180 190
....*....|....*....|....*....|...
gi 1799935007 642 RLPP------VAFACLDEAHCISQWSHNFRPAY 668
Cdd:cd18015 130 KLEKaynagrLARIAIDEVHCCSQWGHDFRPDY 162
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
486-678 |
1.84e-27 |
|
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: 111.46 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 486 EEVLEAL-RNLGYDSFRPGQAEAVMRILSGLSTLVVLPTGMGKSLCYQLPAFLyhknSGSVSLVISPLVSLMDDQVsglp 564
Cdd:cd18016 3 KEMMKIFhKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACV----SPGVTVVISPLRSLIVDQV---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 565 pclkavcihsnlsqsqreaamEKVTTIPNFPSFRTAQRRNLGFSRFFRQVRNGQAQILLL--SPEALVASGS--SSLFFR 640
Cdd:cd18016 75 ---------------------QKLTSLDIPATYLTGDKTDAEATKIYLQLSKKDPIIKLLyvTPEKISASNRliSTLENL 133
|
170 180 190
....*....|....*....|....*....|....*...
gi 1799935007 641 DRLPPVAFACLDEAHCISQWSHNFRPAYLRVcKVLRQR 678
Cdd:cd18016 134 YERKLLARFVIDEAHCVSQWGHDFRPDYKRL-NMLRQK 170
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
496-680 |
5.93e-25 |
|
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: 103.70 E-value: 5.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 496 GYDSFRPGQAEAVMRIL-SGLSTLVVLPTGMGKSLCYQLPAFLyhknSGSVSLVISPLVSLMDDQV-----SGLPPClka 569
Cdd:cd18017 9 GHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVL----LNSLTLVISPLISLMEDQVlqlvmSNIPAC--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 570 vCIHSnlsqsqreaamekvttipnfpsfrtAQRRNLgfsrfFRQVRNGQAQILLLSPEaLVASGSSSLffRDRLPPVAFA 649
Cdd:cd18017 82 -FLGS-------------------------AQSQNV-----LDDIKMGKIRVIYVTPE-FVSKGLELL--QQLRNGITLI 127
|
170 180 190
....*....|....*....|....*....|.
gi 1799935007 650 CLDEAHCISQWSHNFRPAYlRVCKVLRQRLG 680
Cdd:cd18017 128 AIDEAHCVSQWGHDFRSSY-RHLGSIRNRLP 157
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
489-683 |
3.23e-24 |
|
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: 101.78 E-value: 3.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 489 LEALRN-LGYDSFR-PGQAEAVMRILSG-LSTLVVLPTGMGKSLCYQLPAFLYHKnsgsVSLVISPLVSLMDDQVSGLpp 565
Cdd:cd18014 1 RSTLKKvFGHSDFKsPLQEKATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLAKG----ITIVISPLIALIQDQVDHL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 566 clKAVCIHSNlSQSQREAAMEKVTTIPNFPSFRTaqrrnlgfsrffrqvrngQAQILLLSPEaLVASGS-----SSLFFR 640
Cdd:cd18014 75 --KTLKIRVD-SLNSKLSAQERKRIIADLESEKP------------------QTKFLYITPE-MAATSSfqpllSSLVSR 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1799935007 641 DRLppvAFACLDEAHCISQWSHNFRPAYLRVcKVLRQRLG-VRC 683
Cdd:cd18014 133 NLL---SYLVVDEAHCVSQWGHDFRPDYLRL-GALRSRYGhVPW 172
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
799-868 |
1.48e-19 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 84.19 E-value: 1.48e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 799 SATAYHAGLSGPERRRIQRDFMGGRIRVLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGRDG 868
Cdd:smart00490 13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
464-871 |
1.68e-19 |
|
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: 94.52 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 464 PPPAAVdplYSPAPDGTipdpPEEVLEALRNLGYDSFRPGQAEAVMRILSGLSTLVVLPTGMGKSLCYQLPAFL-YHKNS 542
Cdd:COG1205 28 PAREAR---YAPWPDWL----PPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEaLLEDP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 543 GSVSLVISPLVSLMDDQVS-------GLPPCLKAVCIHSNLSQSQREAAMEK----VTT--------IPNFPSFRtaqrr 603
Cdd:COG1205 101 GATALYLYPTKALARDQLRrlrelaeALGLGVRVATYDGDTPPEERRWIREHpdivLTNpdmlhyglLPHHTRWA----- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 604 nlgfsRFFRQVRngqaqilllspeALVasgssslffrdrlppvafacLDEAHcisqwshnfrpAY--------------- 668
Cdd:COG1205 176 -----RFFRNLR------------YVV--------------------IDEAH-----------TYrgvfgshvanvlrrl 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 669 LRVCKVLR-------------------QRL-GVRCFLgLTATATAATARDVAqhLGIPPEQGGGVR-SAAVPANLLLSvs 727
Cdd:COG1205 208 RRICRHYGsdpqfilasatignpaehaERLtGRPVTV-VDEDGSPRGERTFV--LWNPPLVDDGIRrSALAEAARLLA-- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 728 mdadreqallSLLRADpfgscHPLIVFCTRREDTERLAALLRSQfpqfpphpkpLGKNPGKGKTAgipgfcsatAYHAGL 807
Cdd:COG1205 283 ----------DLVREG-----LRTLVFTRSRRGAELLARYARRA----------LREPDLADRVA---------AYRAGY 328
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799935007 808 SGPERRRIQRDFMGGRIRVLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGRDGSAA 871
Cdd:COG1205 329 LPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDS 392
|
|
| RecQL4_SLD2_NTD |
cd22289 |
N-terminal homeodomain-like domain of metazoan RecQ protein-like 4 (RecQL4), fungal DNA ... |
2-50 |
8.27e-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: 80.75 E-value: 8.27e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1799935007 2 ERQQELKVLLKRWEAEFLRERRRKPSQADIEEAPEETRKLYKEYRMLKQ 50
Cdd:cd22289 1 ERLQELKIALKTWERAFAKKHGRKPTKDDIKAAPEEIKDLYKEYAKLKK 49
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
731-868 |
1.04e-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: 79.95 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 731 DREQALLSLLRADPFGSChplIVFCTRREDTErlAALLRsqfpqfpphpkplgknpgkgKTAGIpgfcSATAYHAGLSGP 810
Cdd:pfam00271 1 EKLEALLELLKKERGGKV---LIFSQTKKTLE--AELLL--------------------EKEGI----KVARLHGDLSQE 51
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799935007 811 ERRRIQRDFMGGRIRVLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGRDG 868
Cdd:pfam00271 52 EREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
726-877 |
1.62e-17 |
|
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: 80.24 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 726 VSMDADREQALLSLLRADPFGSChplIVFCTRREDTERLAALLRSqfpqfpphpkplgknpgkgktAGIPgfcsATAYHA 805
Cdd:cd18787 8 VEEEEKKLLLLLLLLEKLKPGKA---IIFVNTKKRVDRLAELLEE---------------------LGIK----VAALHG 59
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799935007 806 GLSGPERRRIQRDFMGGRIRVLVAT-VAfGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGRDGSAARCHLFL 877
Cdd:cd18787 60 DLSQEERERALKKFRSGKVRVLVATdVA-ARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
729-882 |
8.37e-17 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 84.43 E-value: 8.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 729 DADREQALLSLLRADPFGSChplIVFCTRREDTERLAALLRSQfpqfpphpkplgknpgkgktagipGFcSATAYHAGLS 808
Cdd:COG0513 225 KRDKLELLRRLLRDEDPERA---IVFCNTKRGADRLAEKLQKR------------------------GI-SAAALHGDLS 276
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799935007 809 GPERRRIQRDFMGGRIRVLVAT-VAfGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGRDGSAARCHLFLEPQDL 882
Cdd:COG0513 277 QGQRERALDAFRNGKIRVLVATdVA-ARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDER 350
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
492-681 |
1.68e-16 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 79.46 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 492 LRNLGYDSFRPGQAEAVMRILSGL-STLVVLPTGMGKSLCYQLPAFLY-HKNSGSVSLVISPLVSLMDDQVS-----GLP 564
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEAlKRGKGGRVLVLVPTRELAEQWAEelkklGPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 565 PCLKAVCIHSNLSqsqreaamekvttipnfpsfrtaqrrnlgFSRFFRQVRNGQAQILLLSPEALVASGSSSLFFRDRlp 644
Cdd:smart00487 81 LGLKVVGLYGGDS-----------------------------KREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSN-- 129
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1799935007 645 pVAFACLDEAHCISQWshNFRPAYLRVCKVL---RQRLGV 681
Cdd:smart00487 130 -VDLVILDEAHRLLDG--GFGDQLEKLLKLLpknVQLLLL 166
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
501-677 |
2.06e-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: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 501 RPGQAEAVMRILSGLSTLVVLPTGMGKSLCYQLPAF--LYHKNSGSVSLVISPLVSLMDDQVS-----GLPPCLKAVCIH 573
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALeaLDKLDNGPQALVLAPTRELAEQIYEelkklGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 574 SNLSQSQREAAMEKVttipnfpsfrtaqrrnlgfsrffrqvrngqaQILLLSPEALVasgsSSLFFRDRLPPVAFACLDE 653
Cdd:pfam00270 81 GGDSRKEQLEKLKGP-------------------------------DILVGTPGRLL----DLLQERKLLKNLKLLVLDE 125
|
170 180
....*....|....*....|....
gi 1799935007 654 AHCISQWShnFRPAYLRVCKVLRQ 677
Cdd:pfam00270 126 AHRLLDMG--FGPDLEEILRRLPK 147
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
752-871 |
3.42e-15 |
|
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: 73.83 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 752 IVFCTRREDTERLAALLRSQFPqfpphpkplGKNPGKGKTAgipgfcsatAYHAGLSGPERRRIQRDFMGGRIRVLVATV 831
Cdd:cd18797 39 IVFCRSRKLAELLLRYLKARLV---------EEGPLASKVA---------SYRAGYLAEDRREIEAELFNGELLGVVATN 100
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1799935007 832 AFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGRDGSAA 871
Cdd:cd18797 101 ALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDS 140
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
504-563 |
2.65e-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: 2.65e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799935007 504 QAEAVMRILSGLSTLVVLPTGMGKSLCYQLPAF--LYhKNSGSVSLVISPLVSLMDDQVSGL 563
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILeaLL-RDPGSRALYLYPTKALAQDQLRSL 65
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
749-868 |
4.59e-09 |
|
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: 56.41 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 749 HPLIVFC-TRREdTERLAALLrsqfpqfpphpkplgknpgkgktAGIpGFcsataYHAGLSGPERRRIQRDFMGGRIRVL 827
Cdd:cd18795 44 KPVLVFCsSRKE-CEKTAKDL-----------------------AGI-AF-----HHAGLTREDRELVEELFREGLIKVL 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1799935007 828 VATVAFGMGLD----KADVRGIVHYNIPGNLE----SYVQEVGRAGRDG 868
Cdd:cd18795 94 VATSTLAAGVNlparTVIIKGTQRYDGKGYRElsplEYLQMIGRAGRPG 142
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
517-681 |
5.35e-09 |
|
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: 56.26 E-value: 5.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 517 TLVVLPTGMGKSLCYQLPAFLYHKNSGSVSLVISPLVSLMDDQvsglppclkavciHSNLsqsQREAAMEKVTTIpnFPS 596
Cdd:cd00046 4 VLITAPTGSGKTLAALLAALLLLLKKGKKVLVLVPTKALALQT-------------AERL---RELFGPGIRVAV--LVG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 597 FRTAQRRnlgfsrffRQVRNGQAQILLLSPEALVASGSSSLffRDRLPPVAFACLDEAHCISQWSHNFRPAYLRVCKVLR 676
Cdd:cd00046 66 GSSAEER--------EKNKLGDADIIIATPDMLLNLLLRED--RLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGL 135
|
....*
gi 1799935007 677 QRLGV 681
Cdd:cd00046 136 KNAQV 140
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
484-866 |
5.90e-09 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 60.29 E-value: 5.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 484 PPEEVLEALRNLGYDSFRPGQAEAVMR-ILSGLSTLVVLPTGMGKSLCYQLpAFLYHKNSGSVSLVISPLVSLmddqvsg 562
Cdd:COG1204 7 PLEKVIEFLKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAEL-AILKALLNGGKALYIVPLRAL------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 563 lppclkavcihsnlsqsqreaAMEKVTTipnfpsfrtaqrrnlgFSRFFRQV----------------RNGQAQILLLSP 626
Cdd:COG1204 79 ---------------------ASEKYRE----------------FKRDFEELgikvgvstgdydsddeWLGRYDILVATP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 627 E---ALVASGSSslFFRDrlppvaFACL--DEAHCISQWShnfRPAYLRVC--KVLRQRLGVRcFLGLtaTATAATARDV 699
Cdd:COG1204 122 EkldSLLRNGPS--WLRD------VDLVvvDEAHLIDDES---RGPTLEVLlaRLRRLNPEAQ-IVAL--SATIGNAEEI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 700 AQHLGIPPeqgggVRSAAVPANLLLSVSMDA------------DREQAL-LSLLRADpfGSChplIVFCTRREDTERLAA 766
Cdd:COG1204 188 AEWLDAEL-----VKSDWRPVPLNEGVLYDGvlrfddgsrrskDPTLALaLDLLEEG--GQV---LVFVSSRRDAESLAK 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 767 LLRSQFPQFPPHPKplgknpgKGKTAGIPGFCSAT------------------AYH-AGLSGPERRRIQRDFMGGRIRVL 827
Cdd:COG1204 258 KLADELKRRLTPEE-------REELEELAEELLEVseethtnekladclekgvAFHhAGLPSELRRLVEDAFREGLIKVL 330
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1799935007 828 VAT--VAFGMGLDK-----ADVRGIVHYNIPgNLEsYVQEVGRAGR 866
Cdd:COG1204 331 VATptLAAGVNLPArrviiRDTKRGGMVPIP-VLE-FKQMAGRAGR 374
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
826-876 |
9.10e-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: 53.48 E-value: 9.10e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1799935007 826 VLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGRDGS-AARCHLF 876
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKdEGEVILF 76
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
713-885 |
2.21e-08 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 58.26 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 713 VRSAAVPANLLLSVSMDADREQALLSLLRA----------DPFGSCHPLIVFCTRREDTERLAALLRSQFPQFPPHPKPL 782
Cdd:PLN00206 295 FQALSQPQVLLFSATVSPEVEKFASSLAKDiilisignpnRPNKAVKQLAIWVETKQKKQKLFDILKSKQHFKPPAVVFV 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 783 GKNPGK-------GKTAGIpgfcSATAYHAGLSGPERRRIQRDFMGGRIRVLVATVAFGMGLDKADVRGIVHYNIPGNLE 855
Cdd:PLN00206 375 SSRLGAdllanaiTVVTGL----KALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIK 450
|
170 180 190
....*....|....*....|....*....|..
gi 1799935007 856 SYVQEVGRAGRDGSAARCHLFL--EPQDLEPE 885
Cdd:PLN00206 451 EYIHQIGRASRMGEKGTAIVFVneEDRNLFPE 482
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
804-883 |
2.63e-08 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 57.53 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 804 HAGLSGPERRRIQRDFMGGRIRVLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGRDGSAARCHLFLEPQDLE 883
Cdd:PTZ00424 298 HGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIE 377
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
822-916 |
1.39e-07 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 56.01 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 822 GRIRVLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGRDGSAARCHLFLEpqdlepessgilefrEREkRRLC 901
Cdd:PRK11634 294 GRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVE---------------NRE-RRLL 357
|
90
....*....|....*....
gi 1799935007 902 RGHER----CVPVAELVQA 916
Cdd:PRK11634 358 RNIERtmklTIPEVELPNA 376
|
|
| Drc1-Sld2 |
pfam11719 |
DNA replication and checkpoint protein; Genome duplication is precisely regulated by ... |
5-60 |
2.00e-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: 54.84 E-value: 2.00e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1799935007 5 QELKVLLKRWEAEFLRERRRKPSQADIEEAPeETRKLYKEYRMLKQQGKASDSSEK 60
Cdd:pfam11719 2 SQLKAEIKEWERAFAAKNGRKPSKDDIKKNP-EIAKKYKLYSKLKKGESIKTKTPS 56
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
793-879 |
2.53e-07 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 54.78 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 793 GIPGFCsataYHAGLSGPERRRIQRDFMGGRIRVLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGRDGSAAR 872
Cdd:PTZ00110 401 GWPALC----IHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGA 476
|
....*..
gi 1799935007 873 CHLFLEP 879
Cdd:PTZ00110 477 SYTFLTP 483
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
752-869 |
2.16e-06 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 48.36 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 752 IVFCTRReDTERLAALLRSQFPQFPPHPKP---LGKNPGKGKTAgipgfcsatayhAGLSGPERRRIQRDFMGGRIRVLV 828
Cdd:cd18802 29 IIFVERR-ATAVVLSRLLKEHPSTLAFIRCgflIGRGNSSQRKR------------SLMTQRKQKETLDKFRDGELNLLI 95
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1799935007 829 ATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGRDGS 869
Cdd:cd18802 96 ATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPNS 136
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
799-866 |
3.28e-06 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 51.35 E-value: 3.28e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799935007 799 SATAYHAGLSGPERRRIQRDFMGGRIRVLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGR 866
Cdd:PRK10590 271 RSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGR 338
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
713-878 |
4.08e-06 |
|
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: 48.03 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 713 VRSAAVPANLLLSVSMDADREQALLSLLRADpfGSChplIVFCTRREDTERLAALLRSQFPQ-FPPHPKPlgknpgkgkt 791
Cdd:cd18796 8 VILPVAPEIFPWAGESGADAYAEVIFLLERH--KST---LVFTNTRSQAERLAQRLRELCPDrVPPDFIA---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 792 agipgfcsatAYHAGLSGPERRRIQRDFMGGRIRVLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAG-RDGSA 870
Cdd:cd18796 73 ----------LHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGhRPGAA 142
|
....*...
gi 1799935007 871 ARCHLFLE 878
Cdd:cd18796 143 SKGRLVPT 150
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
799-838 |
1.01e-05 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 49.89 E-value: 1.01e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1799935007 799 SATAYHAGLSGPERRRIQRDFMGGRIRVLVATVAFGMGLD 838
Cdd:COG1202 450 KAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVD 489
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
752-865 |
1.67e-05 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 49.54 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 752 IVFCTRREDTERLAALLR----SQFPQFPPHPKPLGK-----NPGKGKTAGIPGFCsATAYHAGLSGPERRRIQRDFMGG 822
Cdd:PRK09751 248 IVFTNSRGLAEKLTARLNelyaARLQRSPSIAVDAAHfestsGATSNRVQSSDVFI-ARSHHGSVSKEQRAITEQALKSG 326
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1799935007 823 RIRVLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAG 865
Cdd:PRK09751 327 ELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
21-282 |
5.10e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 47.76 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 21 ERRRKPSQADIEEAPEETRKLYKEYRMLKQQGKASDSSektgSQEIPNVEQvEDSGFWGSHLNRAPKIPGKSRSG-SARP 99
Cdd:PTZ00449 531 EGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHK----PSKIPTLSK-KPEFPKDPKHPKDPEEPKKPKRPrSAQR 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 100 GISAEFYGMKLKAKLGMTGKEP--PLTPRRTPNPRR--IPKIPQSQKNPEREAEASSPEPPRNEGESEKSGD-----AGK 170
Cdd:PTZ00449 606 PTRPKSPKLPELLDIPKSPKRPesPKSPKRPPPPQRpsSPERPEGPKIIKSPKPPKSPKPPFDPKFKEKFYDdyldaAAK 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 171 SGDPEKS----GEFSGLGPLTLPAgmNPGFP-----PVPDKFQRLKQSVAQTLRSLDpgwlqrcQESPENQEFPAGSVRE 241
Cdd:PTZ00449 686 SKETKTTvvldESFESILKETLPE--TPGTPfttprPLPPKLPRDEEFPFEPIGDPD-------AEQPDDIEFFTPPEEE 756
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799935007 242 KGEIHTASIG----------------NSVRKRPREGGGAAEAPAKLQRGPQGSDPGI 282
Cdd:PTZ00449 757 RTFFHETPADtplpdilaeefkeediHAETGEPDEAMKRPDSPSEHEDKPPGDHPSL 813
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
488-587 |
5.54e-05 |
|
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: 45.53 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 488 VLEALRNLGYDSFRPGQAEAVMRILSGLSTLVVLPTGMGKSLCYQLPAFL--------YHKNSGSVSLVISP---LVSLM 556
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIhldlqpipREQRNGPGVLVLTPtreLALQI 80
|
90 100 110
....*....|....*....|....*....|..
gi 1799935007 557 DDQVSG-LPPCLKAVCIHSNLSQSQREAAMEK 587
Cdd:cd17958 81 EAECSKySYKGLKSVCVYGGGNRNEQIEDLSK 112
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
729-864 |
5.58e-05 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 47.33 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 729 DADREQALLSLLRADpFGSCHPLIVFCTRREDTERLAALLRSqfpqfpphpkplgknpgkgktAGIPgfcsATAYHAGLS 808
Cdd:COG1061 287 DAERKDKILRELLRE-HPDDRKTLVFCSSVDHAEALAELLNE---------------------AGIR----AAVVTGDTP 340
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799935007 809 GPERRRIQRDFMGGRIRVLVATVAFGMGLD--KADVrGIVHYNIpGNLESYVQEVGRA 864
Cdd:COG1061 341 KKEREEILEAFRDGELRILVTVDVLNEGVDvpRLDV-AILLRPT-GSPREFIQRLGRG 396
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
752-868 |
7.15e-05 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 47.19 E-value: 7.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 752 IVFCTRREDTERLAALLRSQFPQFPPHPKPLGKNPGKGKTAG--IPgfcSATAYH-AGLSGPERRRIQRDFMGGRIRVLV 828
Cdd:PRK01172 240 LVFVSSRKNAEDYAEMLIQHFPEFNDFKVSSENNNVYDDSLNemLP---HGVAFHhAGLSNEQRRFIEEMFRNRYIKVIV 316
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1799935007 829 ATVAFGMGLDKAD----VRGIVHYNIPG-----NLEsYVQEVGRAGRDG 868
Cdd:PRK01172 317 ATPTLAAGVNLPArlviVRDITRYGNGGirylsNME-IKQMIGRAGRPG 364
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
805-870 |
8.79e-05 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 46.44 E-value: 8.79e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 805 AGLSG--PERRRIQ--RDFMGGRIRVLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGRDGSA 870
Cdd:PRK01297 363 AQLSGdvPQHKRIKtlEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGAS 432
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
488-551 |
1.17e-04 |
|
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: 44.35 E-value: 1.17e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 488 VLEALRNLGYDSFRPGQAEAVMRILSGLSTLVVLPTGMGKSLCYQLPAF--LYHKNSGSVS----LVISP 551
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILekLLPEPKKKGRgpqaLVLAP 70
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
510-588 |
1.99e-04 |
|
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: 43.86 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 510 RILSGLSTLVVLPTGMGKSlCYQLPAFLYHKNSGSVSLVISPLVSLM-------DDQVSGLPPCLKAVCIHSNLSQSQRE 582
Cdd:cd17924 28 RLLRGKSFAIIAPTGVGKT-TFGLATSLYLASKGKRSYLIFPTKSLVkqayerlSKYAEKAGVEVKILVYHSRLKKKEKE 106
|
....*.
gi 1799935007 583 AAMEKV 588
Cdd:cd17924 107 ELLEKI 112
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
485-555 |
2.05e-04 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 45.72 E-value: 2.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799935007 485 PEEVLEALRNLGYDSFRPGQAEAVMR-ILSGLSTLVVLPTGMGKSLCYQLpAFLYHKNSGSVSLVISPLVSL 555
Cdd:PRK02362 9 PEGVIEFYEAEGIEELYPPQAEAVEAgLLDGKNLLAAIPTASGKTLIAEL-AMLKAIARGGKALYIVPLRAL 79
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
485-551 |
2.80e-04 |
|
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350711 [Multi-domain] Cd Length: 222 Bit Score: 43.91 E-value: 2.80e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799935007 485 PEEVLEALRNLGYDSFRPGQAEAVMRILSGLSTLVVLPTGMGKSLCYQLPAFLYHKN-------SGSVSLVISP 551
Cdd:cd17953 20 SEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDqrpvkpgEGPIGLIMAP 93
|
|
| ZnF_C2HC |
smart00343 |
zinc finger; |
383-398 |
1.04e-03 |
|
zinc finger;
Pssm-ID: 197667 [Multi-domain] Cd Length: 17 Bit Score: 37.42 E-value: 1.04e-03
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
803-1046 |
1.23e-03 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 43.02 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 803 YHAG-LSG--PERRR--IQRDFMGGRIRVLVATVAFGMGLDKADVRGIVHYNIPGNLESYVQEVGRAGRDG--------- 868
Cdd:PRK04537 282 YRVGvLSGdvPQKKResLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGeegdaisfa 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 869 ------SAARCHLFLEPQ-DLEPESSGILEFREREKRRLCRGHERCVPVAELV-----QALDLREEGENsgmRPGIRESP 936
Cdd:PRK04537 362 ceryamSLPDIEAYIEQKiPVEPVTAELLTPLPRPPRVPVEGEEADDEAGDSVgtifrEAREQRAAEEQ---RRGGGRSG 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 937 PGpgipgavpafpsRSDRDPPVLPGAASRQLPAAASCHRFPLPHPLLRRRPAAPGAGAELPSR--GRGPGSGALGRGRLP 1014
Cdd:PRK04537 439 PG------------GGSRSGSVGGGGRRDGAGADGKPRPRRKPRVEGEADAAAAGAETPVVAAaaAQAPGVVAADGERAP 506
|
250 260 270
....*....|....*....|....*....|...
gi 1799935007 1015 GIRRRlpeRFHGLGISAGQ-AQPEAAPVGFPKR 1046
Cdd:PRK04537 507 RKRRR---RRNGRPVEGAEpVSTPVPAPAAPRK 536
|
|
| zf-CCHC |
pfam00098 |
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ... |
382-397 |
4.74e-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: 4.74e-03
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
499-659 |
5.30e-03 |
|
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: 39.55 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 499 SFRPGQAEAVMRI-LSGLSTLVVLPTGMGKSLCYQLPAFLYHKNSGSVSLVISPLVSLMDDQVSGLppclkavcihsnls 577
Cdd:cd17921 1 LLNPIQREALRALyLSGDSVLVSAPTSSGKTLIAELAILRALATSGGKAVYIAPTRALVNQKEADL-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 578 QSQREAAMEKVTtipnfpsfrtaqrrNLGFSRFFRQVRNGQAQILLLSPEAL--VASGSSSLFFRDrlppVAFACLDEAH 655
Cdd:cd17921 67 RERFGPLGKNVG--------------LLTGDPSVNKLLLAEADILVATPEKLdlLLRNGGERLIQD----VRLVVVDEAH 128
|
....
gi 1799935007 656 CISQ 659
Cdd:cd17921 129 LIGD 132
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
488-572 |
5.79e-03 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 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: 350718 [Multi-domain] Cd Length: 202 Bit Score: 39.48 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935007 488 VLEALRNLGYDSFRPGQAEAVMRILSGLSTLVVLPTGMGKSLCYQLPAF--LY-----HKNSGSVSLVISP-------LV 553
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLeiLLkrkanLKKGQVGALIISPtrelatqIY 80
|
90
....*....|....*....
gi 1799935007 554 SLMDDQVSGLPPCLKAVCI 572
Cdd:cd17960 81 EVLQSFLEHHLPKLKCQLL 99
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
499-555 |
7.80e-03 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 38.85 E-value: 7.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799935007 499 SFRPGQAEAVMR-ILSGLSTLVVLPTGMGKSLCYQLpAFLYHKNSGSVSLVISPLVSL 555
Cdd:cd18028 1 ELYPPQAEAVRAgLLKGENLLISIPTASGKTLIAEM-AMVNTLLEGGKALYLVPLRAL 57
|
|
| |
