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Conserved domains on  [gi|919404579|ref|WP_052822627|]
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DNA helicase RecQ [Bifidobacterium animalis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
8-511 0e+00

Superfamily II DNA helicase RecQ [Replication, recombination and repair];


:

Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 668.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579   8 NSALATLRKYFGYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSLLLHGITIVISPLISLMRDQVDGANEIGI 87
Cdd:COG0514    3 DDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  88 PAAFINTTQTPDEQQQVFDAANAGKVKLLYVAPERLETARFRAFATHADIALFAVDEAHCVSQWGQDFRSSYLAIGEFID 167
Cdd:COG0514   83 RAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGELRE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 168 SLPDRPtvaaftatatERVRRDIVNLLGLRNPLVMVTGFDRTNLYFDMLKLNTREKANWIAHYVAEHADESGIVYCATRK 247
Cdd:COG0514  163 RLPNVPvlalt-atatPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPPDDKLAQLLDFLKEHPGGSGIVYCLSRK 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 248 ETEALAQTLNimvpqlrkaqgsqmEDGPIAAAYHGGMPANVRERAQRDFVTDTVPLVVATNAFGMGIDKSNVRYVIHHNM 327
Cdd:COG0514  242 KVEELAEWLR--------------EAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDL 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 328 PESIEAYYQEAGRAGRDGEPSRCTLLWNESDIVTRRRLLDMADRNERltpeeqevVRRSKRQLLDAMIGYCRTTDCLHDY 407
Cdd:COG0514  308 PKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEE--------RKRVERAKLDAMLAYAETTGCRRQF 379
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 408 MTRYFGEsngterSADGHCiGGCVNCESTFETVDVSAVARAISMCVHDLGQHYGMGKVVQVLRGSKAQDLANRGLDAAPT 487
Cdd:COG0514  380 LLRYFGE------ELAEPC-GNCDNCLGPPETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLST 452
                        490       500
                 ....*....|....*....|....
gi 919404579 488 YGRLSEVNEAKIRDVLNQMVADGF 511
Cdd:COG0514  453 YGIGKDLSDKEWRSVIRQLLAQLF 476
HRDC pfam00570
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ...
578-645 8.53e-22

HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic acid binding. Mutations in the HRDC domain cause human disease. It is interesting to note that the RecQ helicase in Deinococcus radiodurans has three tandem HRDC domains.


:

Pssm-ID: 425755 [Multi-domain]  Cd Length: 68  Bit Score: 89.13  E-value: 8.53e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919404579  578 DAELFEHLRALRMQIAREIGKPPYIVFSDRALRDMAERHPHTSKEFLEVNGVGANKLERYGKRFMEVI 645
Cdd:pfam00570   1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
 
Name Accession Description Interval E-value
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
8-511 0e+00

Superfamily II DNA helicase RecQ [Replication, recombination and repair];


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 668.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579   8 NSALATLRKYFGYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSLLLHGITIVISPLISLMRDQVDGANEIGI 87
Cdd:COG0514    3 DDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  88 PAAFINTTQTPDEQQQVFDAANAGKVKLLYVAPERLETARFRAFATHADIALFAVDEAHCVSQWGQDFRSSYLAIGEFID 167
Cdd:COG0514   83 RAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGELRE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 168 SLPDRPtvaaftatatERVRRDIVNLLGLRNPLVMVTGFDRTNLYFDMLKLNTREKANWIAHYVAEHADESGIVYCATRK 247
Cdd:COG0514  163 RLPNVPvlalt-atatPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPPDDKLAQLLDFLKEHPGGSGIVYCLSRK 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 248 ETEALAQTLNimvpqlrkaqgsqmEDGPIAAAYHGGMPANVRERAQRDFVTDTVPLVVATNAFGMGIDKSNVRYVIHHNM 327
Cdd:COG0514  242 KVEELAEWLR--------------EAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDL 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 328 PESIEAYYQEAGRAGRDGEPSRCTLLWNESDIVTRRRLLDMADRNERltpeeqevVRRSKRQLLDAMIGYCRTTDCLHDY 407
Cdd:COG0514  308 PKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEE--------RKRVERAKLDAMLAYAETTGCRRQF 379
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 408 MTRYFGEsngterSADGHCiGGCVNCESTFETVDVSAVARAISMCVHDLGQHYGMGKVVQVLRGSKAQDLANRGLDAAPT 487
Cdd:COG0514  380 LLRYFGE------ELAEPC-GNCDNCLGPPETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLST 452
                        490       500
                 ....*....|....*....|....
gi 919404579 488 YGRLSEVNEAKIRDVLNQMVADGF 511
Cdd:COG0514  453 YGIGKDLSDKEWRSVIRQLLAQLF 476
recQ TIGR01389
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ...
13-646 0e+00

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: 649.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579   13 TLRKYFGYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSLLLHGITIVISPLISLMRDQVDGANEIGIPAAFI 92
Cdd:TIGR01389   4 VLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAAAYL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579   93 NTTQTPDEQQQVFDAANAGKVKLLYVAPERLETARFRAFATHADIALFAVDEAHCVSQWGQDFRSSYLAIGEFIDSLPDR 172
Cdd:TIGR01389  84 NSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERFPQV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  173 PTVAAFTATATErVRRDIVNLLGLRNPLVMVTGFDRTNLYFDMLKLNTREKanWIAHYVAEHADESGIVYCATRKETEAL 252
Cdd:TIGR01389 164 PRIALTATADAE-TRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQK--FLLDYLKKHRGQSGIIYASSRKKVEEL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  253 AQTLNimvpqlrkaqgsqmEDGPIAAAYHGGMPANVRERAQRDFVTDTVPLVVATNAFGMGIDKSNVRYVIHHNMPESIE 332
Cdd:TIGR01389 241 AERLE--------------SQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLE 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  333 AYYQEAGRAGRDGEPSRCTLLWNESDIVTRRRLLDmadrnerlTPEEQEVVRRSKRQLLDAMIGYCRTTDCLHDYMTRYF 412
Cdd:TIGR01389 307 SYYQEAGRAGRDGLPAEAILLYSPADIALLKRRIE--------QSEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYF 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  413 GESNGtersadGHCiGGCVNCESTFETVDVSAVARAISMCVHDLGQHYGMGKVVQVLRGSKAQDLANRGLDAAPTYGRLS 492
Cdd:TIGR01389 379 GENEV------EPC-GNCDNCLDPPKSYDATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGK 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  493 EVNEAKIRDVLNQMVADGFLVVSEGRLPlvqfGPRAAETVAPTFRYEIKKSERKsksrssggdaksTKLSAGERAAAGLG 572
Cdd:TIGR01389 452 DYTQKEWRSLIDQLIAEGLLTENDEIYI----GLQLTEAARKVLKNEVEVLLRP------------FKVVAKEKTRVQKN 515
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919404579  573 ANTGVDAELFEHLRALRMQIAREIGKPPYIVFSDRALRDMAERHPHTSKEFLEVNGVGANKLERYGKRFMEVIR 646
Cdd:TIGR01389 516 LSVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAEKRPATLNALLKIKGVGQNKLDRYGEAFLEVIR 589
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
7-646 1.31e-169

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 497.70  E-value: 1.31e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579   7 ENSALATLRKYFGYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSLLLHGITIVISPLISLMRDQVDGANEIG 86
Cdd:PRK11057  10 ESLAKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  87 IPAAFINTTQTPDEQQQVFDAANAGKVKLLYVAPERLETARFRAFATHADIALFAVDEAHCVSQWGQDFRSSYLAIGEFI 166
Cdd:PRK11057  90 VAAACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLR 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 167 DSLPDRPtVAAFTATATERVRRDIVNLLGLRNPLVMVTGFDRTNLYFDMLklntrEK---ANWIAHYVAEHADESGIVYC 243
Cdd:PRK11057 170 QRFPTLP-FMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLV-----EKfkpLDQLMRYVQEQRGKSGIIYC 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 244 ATRKETEALAQTLnimvpQLRkaqgsqmedGPIAAAYHGGMPANVRERAQRDFVTDTVPLVVATNAFGMGIDKSNVRYVI 323
Cdd:PRK11057 244 NSRAKVEDTAARL-----QSR---------GISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVV 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 324 HHNMPESIEAYYQEAGRAGRDGEPSRCTLLWNESDIVTRRRLLDMADrnerltPEEQEVVRRSKrqlLDAMIGYCRTTDC 403
Cdd:PRK11057 310 HFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWLRRCLEEKP------AGQQQDIERHK---LNAMGAFAEAQTC 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 404 LHDYMTRYFGESNGTErsadghCiGGCVNCESTFETVDVSAVARAISMCVHDLGQHYGMGKVVQVLRGSKAQDLANRGLD 483
Cdd:PRK11057 381 RRLVLLNYFGEGRQEP------C-GNCDICLDPPKQYDGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHD 453
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 484 AAPTYGRLSEVNEAKIRDVLNQMVADGFLVVSEGRLPLVQFgpraAETVAPTFRYEIKKSERKSKSRSSGGdAKSTKLSA 563
Cdd:PRK11057 454 KLKVYGIGRDKSHEHWVSVIRQLIHLGLVTQNIAQHSALQL----TEAARPVLRGEVSLQLAVPRIVALKP-RAMQKSFG 528
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 564 GEraaaglgantgVDAELFEHLRALRMQIAREIGKPPYIVFSDRALRDMAERHPHTSKEFLEVNGVGANKLERYGKRFME 643
Cdd:PRK11057 529 GN-----------YDRKLFAKLRKLRKSIADEENIPPYVVFNDATLIEMAEQMPITASEMLSVNGVGQRKLERFGKPFMA 597

                 ...
gi 919404579 644 VIR 646
Cdd:PRK11057 598 LIR 600
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
11-207 1.89e-92

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: 284.43  E-value: 1.89e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  11 LATLRKYFGYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSLLLHGITIVISPLISLMRDQVDGANEIGIPAA 90
Cdd:cd17920    1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  91 FINTTQTPDEQQQVFDAANAGKVKLLYVAPERLETARFRAFATHAD----IALFAVDEAHCVSQWGQDFRSSYLAIGEFI 166
Cdd:cd17920   81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLRLGRLR 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 919404579 167 DSLPDRPtvaaftatatERVRRDIVNLLGLRNPLVMVTGFD 207
Cdd:cd17920  161 RALPGVPilalt-atatPEVREDILKRLGLRNPVIFRASFD 200
DpdF NF041063
protein DpdF;
14-365 5.69e-46

protein DpdF;


Pssm-ID: 468990 [Multi-domain]  Cd Length: 813  Bit Score: 174.71  E-value: 5.69e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  14 LRKYFGYESFR-PGQAELINAIL---EGRDVLGVMPTGSGKSVCYQIPSLLL---HGITIVISPLISLMRDQVDGANEIg 86
Cdd:NF041063 131 LAEALGFTHYRsPGQREAVRAALlapPGSTLIVNLPTGSGKSLVAQAPALLAsrqGGLTLVVVPTVALAIDQERRAREL- 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  87 IPAAFINTT--------QTPDEQQQVFDAANAGKVKLLYVAPE----RLETARFRAfATHADIALFAVDEAHCVSQWGQD 154
Cdd:NF041063 210 LRRAGPDLGgplawhggLSAEERAAIRQRIRDGTQRILFTSPEsltgSLRPALFDA-AEAGLLRYLVVDEAHLVDQWGDG 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 155 FRSSYLAIGEFIDSLPDRPTVAAFTATA------TERVRRDIVNLLGLRNPLVMVTG-FDRTnlyfdmlklntrEkanwI 227
Cdd:NF041063 289 FRPEFQLLAGLRRSLLRLAPSGRPFRTLllsatlTESTLDTLETLFGPPGPFIVVSAvQLRP------------E----P 352
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 228 AHYVAEHADESG----------------IVYCATRKETEALAQTLnimvpqlrKAQGSQMedgpiAAAYHGGMPANVRER 291
Cdd:NF041063 353 AYWVAKCDSEEErrervlealrhlprplILYVTKVEDAEAWLQRL--------RAAGFRR-----VALFHGDTPDAERER 419
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919404579 292 AQRDFVTDTVPLVVATNAFGMGIDKSNVRYVIHHNMPESIEAYYQEAGRAGRDGEPSRCTLLWNESDIVTRRRL 365
Cdd:NF041063 420 LIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDIAKSL 493
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
24-162 1.59e-25

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: 103.09  E-value: 1.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579   24 RPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSL------LLHGITIVISPLISLMRDQVDGANEIGIPAAF-INTTQ 96
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGLkVASLL 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919404579   97 TPDEQQQVFDAANagKVKLLYVAPERLETARFRAFATHaDIALFAVDEAHCVSQWGqdFRSSYLAI 162
Cdd:pfam00270  81 GGDSRKEQLEKLK--GPDILVGTPGRLLDLLQERKLLK-NLKLLVLDEAHRLLDMG--FGPDLEEI 141
HRDC pfam00570
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ...
578-645 8.53e-22

HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic acid binding. Mutations in the HRDC domain cause human disease. It is interesting to note that the RecQ helicase in Deinococcus radiodurans has three tandem HRDC domains.


Pssm-ID: 425755 [Multi-domain]  Cd Length: 68  Bit Score: 89.13  E-value: 8.53e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919404579  578 DAELFEHLRALRMQIAREIGKPPYIVFSDRALRDMAERHPHTSKEFLEVNGVGANKLERYGKRFMEVI 645
Cdd:pfam00570   1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
DEXDc smart00487
DEAD-like helicases superfamily;
16-166 2.11e-21

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 92.55  E-value: 2.11e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579    16 KYFGYESFRPGQAELINAILEG-RDVLGVMPTGSGKSVCYQIPSLLL-----HGITIVISPLISLMRDQVDGANEIGIPA 89
Cdd:smart00487   2 EKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLGPSL 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919404579    90 AFINTT-QTPDEQQQVFDAANAGKVKLLYVAPERLETARFRAFATHADIALFAVDEAHCVSQWGqdFRSSYLAIGEFI 166
Cdd:smart00487  82 GLKVVGlYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKLLKLL 157
HRDC smart00341
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ...
580-648 1.65e-17

Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the HRDC domain cause human disease.


Pssm-ID: 128635 [Multi-domain]  Cd Length: 81  Bit Score: 77.34  E-value: 1.65e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919404579   580 ELFEHLRALRMQIAREIGKPPYIVFSDRALRDMAERHPHTSKEFLEVNGVGANKLERYGKRFMEVIRIF 648
Cdd:smart00341   6 RLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEA 74
Rnd COG0349
Ribonuclease D [Translation, ribosomal structure and biogenesis];
585-646 5.36e-07

Ribonuclease D [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440118 [Multi-domain]  Cd Length: 365  Bit Score: 52.18  E-value: 5.36e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919404579 585 LRAL---RMQIAREIGKPPYIVFSDRALRDMAERHPHTSKEFLEVNGVGANKLERYGKRFMEVIR 646
Cdd:COG0349  213 LRELaawREREARKRDVPRNRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAVA 277
 
Name Accession Description Interval E-value
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
8-511 0e+00

Superfamily II DNA helicase RecQ [Replication, recombination and repair];


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 668.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579   8 NSALATLRKYFGYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSLLLHGITIVISPLISLMRDQVDGANEIGI 87
Cdd:COG0514    3 DDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  88 PAAFINTTQTPDEQQQVFDAANAGKVKLLYVAPERLETARFRAFATHADIALFAVDEAHCVSQWGQDFRSSYLAIGEFID 167
Cdd:COG0514   83 RAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGELRE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 168 SLPDRPtvaaftatatERVRRDIVNLLGLRNPLVMVTGFDRTNLYFDMLKLNTREKANWIAHYVAEHADESGIVYCATRK 247
Cdd:COG0514  163 RLPNVPvlalt-atatPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPPDDKLAQLLDFLKEHPGGSGIVYCLSRK 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 248 ETEALAQTLNimvpqlrkaqgsqmEDGPIAAAYHGGMPANVRERAQRDFVTDTVPLVVATNAFGMGIDKSNVRYVIHHNM 327
Cdd:COG0514  242 KVEELAEWLR--------------EAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDL 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 328 PESIEAYYQEAGRAGRDGEPSRCTLLWNESDIVTRRRLLDMADRNERltpeeqevVRRSKRQLLDAMIGYCRTTDCLHDY 407
Cdd:COG0514  308 PKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEE--------RKRVERAKLDAMLAYAETTGCRRQF 379
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 408 MTRYFGEsngterSADGHCiGGCVNCESTFETVDVSAVARAISMCVHDLGQHYGMGKVVQVLRGSKAQDLANRGLDAAPT 487
Cdd:COG0514  380 LLRYFGE------ELAEPC-GNCDNCLGPPETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLST 452
                        490       500
                 ....*....|....*....|....
gi 919404579 488 YGRLSEVNEAKIRDVLNQMVADGF 511
Cdd:COG0514  453 YGIGKDLSDKEWRSVIRQLLAQLF 476
recQ TIGR01389
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ...
13-646 0e+00

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: 649.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579   13 TLRKYFGYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSLLLHGITIVISPLISLMRDQVDGANEIGIPAAFI 92
Cdd:TIGR01389   4 VLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAAAYL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579   93 NTTQTPDEQQQVFDAANAGKVKLLYVAPERLETARFRAFATHADIALFAVDEAHCVSQWGQDFRSSYLAIGEFIDSLPDR 172
Cdd:TIGR01389  84 NSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERFPQV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  173 PTVAAFTATATErVRRDIVNLLGLRNPLVMVTGFDRTNLYFDMLKLNTREKanWIAHYVAEHADESGIVYCATRKETEAL 252
Cdd:TIGR01389 164 PRIALTATADAE-TRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQK--FLLDYLKKHRGQSGIIYASSRKKVEEL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  253 AQTLNimvpqlrkaqgsqmEDGPIAAAYHGGMPANVRERAQRDFVTDTVPLVVATNAFGMGIDKSNVRYVIHHNMPESIE 332
Cdd:TIGR01389 241 AERLE--------------SQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLE 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  333 AYYQEAGRAGRDGEPSRCTLLWNESDIVTRRRLLDmadrnerlTPEEQEVVRRSKRQLLDAMIGYCRTTDCLHDYMTRYF 412
Cdd:TIGR01389 307 SYYQEAGRAGRDGLPAEAILLYSPADIALLKRRIE--------QSEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYF 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  413 GESNGtersadGHCiGGCVNCESTFETVDVSAVARAISMCVHDLGQHYGMGKVVQVLRGSKAQDLANRGLDAAPTYGRLS 492
Cdd:TIGR01389 379 GENEV------EPC-GNCDNCLDPPKSYDATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGK 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  493 EVNEAKIRDVLNQMVADGFLVVSEGRLPlvqfGPRAAETVAPTFRYEIKKSERKsksrssggdaksTKLSAGERAAAGLG 572
Cdd:TIGR01389 452 DYTQKEWRSLIDQLIAEGLLTENDEIYI----GLQLTEAARKVLKNEVEVLLRP------------FKVVAKEKTRVQKN 515
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919404579  573 ANTGVDAELFEHLRALRMQIAREIGKPPYIVFSDRALRDMAERHPHTSKEFLEVNGVGANKLERYGKRFMEVIR 646
Cdd:TIGR01389 516 LSVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAEKRPATLNALLKIKGVGQNKLDRYGEAFLEVIR 589
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
7-646 1.31e-169

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 497.70  E-value: 1.31e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579   7 ENSALATLRKYFGYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSLLLHGITIVISPLISLMRDQVDGANEIG 86
Cdd:PRK11057  10 ESLAKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  87 IPAAFINTTQTPDEQQQVFDAANAGKVKLLYVAPERLETARFRAFATHADIALFAVDEAHCVSQWGQDFRSSYLAIGEFI 166
Cdd:PRK11057  90 VAAACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLR 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 167 DSLPDRPtVAAFTATATERVRRDIVNLLGLRNPLVMVTGFDRTNLYFDMLklntrEK---ANWIAHYVAEHADESGIVYC 243
Cdd:PRK11057 170 QRFPTLP-FMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLV-----EKfkpLDQLMRYVQEQRGKSGIIYC 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 244 ATRKETEALAQTLnimvpQLRkaqgsqmedGPIAAAYHGGMPANVRERAQRDFVTDTVPLVVATNAFGMGIDKSNVRYVI 323
Cdd:PRK11057 244 NSRAKVEDTAARL-----QSR---------GISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVV 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 324 HHNMPESIEAYYQEAGRAGRDGEPSRCTLLWNESDIVTRRRLLDMADrnerltPEEQEVVRRSKrqlLDAMIGYCRTTDC 403
Cdd:PRK11057 310 HFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWLRRCLEEKP------AGQQQDIERHK---LNAMGAFAEAQTC 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 404 LHDYMTRYFGESNGTErsadghCiGGCVNCESTFETVDVSAVARAISMCVHDLGQHYGMGKVVQVLRGSKAQDLANRGLD 483
Cdd:PRK11057 381 RRLVLLNYFGEGRQEP------C-GNCDICLDPPKQYDGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHD 453
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 484 AAPTYGRLSEVNEAKIRDVLNQMVADGFLVVSEGRLPLVQFgpraAETVAPTFRYEIKKSERKSKSRSSGGdAKSTKLSA 563
Cdd:PRK11057 454 KLKVYGIGRDKSHEHWVSVIRQLIHLGLVTQNIAQHSALQL----TEAARPVLRGEVSLQLAVPRIVALKP-RAMQKSFG 528
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 564 GEraaaglgantgVDAELFEHLRALRMQIAREIGKPPYIVFSDRALRDMAERHPHTSKEFLEVNGVGANKLERYGKRFME 643
Cdd:PRK11057 529 GN-----------YDRKLFAKLRKLRKSIADEENIPPYVVFNDATLIEMAEQMPITASEMLSVNGVGQRKLERFGKPFMA 597

                 ...
gi 919404579 644 VIR 646
Cdd:PRK11057 598 LIR 600
recQ_fam TIGR00614
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ...
14-490 8.46e-149

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: 439.21  E-value: 8.46e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579   14 LRKYFGYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSLLLHGITIVISPLISLMRDQVDGANEIGIPAAFIN 93
Cdd:TIGR00614   3 LKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATFLN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579   94 TTQTPDEQQQVFDAANAGKVKLLYVAPERLETAR--FRAFATHADIALFAVDEAHCVSQWGQDFRSSYLAIGEFIDSLPD 171
Cdd:TIGR00614  83 SAQTKEQQLNVLTDLKDGKIKLLYVTPEKISASNrlLQTLEERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKFPN 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  172 RPTVAAFTATATeRVRRDIVNLLGLRNPLVMVTGFDRTNLYFDMLKLNTREKANWIAHYVAEHADESGIVYCATRKETEA 251
Cdd:TIGR00614 163 VPVMALTATASP-SVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTPKILEDLLRFIRKEFEGKSGIIYCPSRKKVEQ 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  252 LAQTLNimvpqlrkaqgsqmEDGPIAAAYHGGMPANVRERAQRDFVTDTVPLVVATNAFGMGIDKSNVRYVIHHNMPESI 331
Cdd:TIGR00614 242 VAAELQ--------------KLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSM 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  332 EAYYQEAGRAGRDGEPSRCTLLWNESDIVTRRRLLDMadrnerltpEEQEVVRRSKRQLLDAMIGYCRTTDCLHDYMTRY 411
Cdd:TIGR00614 308 ESYYQESGRAGRDGLPSECHLFYAPADMNRLRRLLME---------EPDGNFRTYKLKLYEMMEYCLNSSTCRRLILLSY 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  412 FGESNGTERSADGHCIGGCVNCEST--FETVDV-------SAVARAISMCVHDLGQHYGMGKVVQVLRGSKAQDLANRGL 482
Cdd:TIGR00614 379 FGEKGFNKSFCIMGTEKCCDNCCKRldYKTKDVtdkvydfGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGF 458

                  ....*...
gi 919404579  483 DAAPTYGR 490
Cdd:TIGR00614 459 RKHSLYGR 466
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
15-645 6.31e-103

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 339.18  E-value: 6.31e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579   15 RKYFGYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSLLLHGITIVISPLISLMRDQVDGANEIGIPAAFINT 94
Cdd:PLN03137  453 KKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSA 532
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579   95 TQTPDEQQQVFDAANAG--KVKLLYVAPERLetARFRAFATHADI-------ALFAVDEAHCVSQWGQDFRSSYLAIGEF 165
Cdd:PLN03137  533 GMEWAEQLEILQELSSEysKYKLLYVTPEKV--AKSDSLLRHLENlnsrgllARFVIDEAHCVSQWGHDFRPDYQGLGIL 610
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  166 IDSLPDRPTVAAFTATATErVRRDIVNLLGLRNPLVMVTGFDRTNLYFDMLKlNTREKANWIAHYVAE-HADESGIVYCA 244
Cdd:PLN03137  611 KQKFPNIPVLALTATATAS-VKEDVVQALGLVNCVVFRQSFNRPNLWYSVVP-KTKKCLEDIDKFIKEnHFDECGIIYCL 688
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  245 TRKETEALAQTLNimvpqlrkaqgsqmEDGPIAAAYHGGMPANVRERAQRDFVTDTVPLVVATNAFGMGIDKSNVRYVIH 324
Cdd:PLN03137  689 SRMDCEKVAERLQ--------------EFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIH 754
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  325 HNMPESIEAYYQEAGRAGRDGEPSRCTLLWNESDIVTRRRLLDMADRNERLTPEEQEVVRRSKRQL------LDAMIGYC 398
Cdd:PLN03137  755 HSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMISQGGVEQSPMAMGYNRMASSGRILetntenLLRMVSYC 834
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  399 RT-TDCLHDYMTRYFGesngtERSADGHCIGGCVNCES--TFETVDVSAVARAISMCVHDLGQHYGMGKVVQVLRGSKAQ 475
Cdd:PLN03137  835 ENeVDCRRFLQLVHFG-----EKFDSTNCKKTCDNCSSskSLIDKDVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQ 909
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  476 DLANRGLDAAPTYGRLSEVNEAKIRDVLNQMVADGFLV-----------------VSEGRLPLVQFGpraAETVAPTFRY 538
Cdd:PLN03137  910 YVKKHRHETLSLHGAGKHLSKGEASRILHYLVTEDILAedvkksdlygsvssllkVNESKAYKLFSG---GQTIIMRFPS 986
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  539 EIKKSERKSKSRSSG-GDAKSTKLSAGERA-AAGLGANTGVDAELFEHLRALRMQIAREIGKP--PYIVFSDRALRDMAE 614
Cdd:PLN03137  987 SVKASKPSKFEATPAkGPLTSGKQSTLPMAtPAQPPVDLNLSAILYTALRKLRTALVKEAGDGvmAYHIFGNATLQQISK 1066
                         650       660       670
                  ....*....|....*....|....*....|.
gi 919404579  615 RHPHTSKEFLEVNGVGANKLERYGKRFMEVI 645
Cdd:PLN03137 1067 RIPRTKEELLEINGLGKAKVSKYGDRLLETI 1097
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
11-207 1.89e-92

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: 284.43  E-value: 1.89e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  11 LATLRKYFGYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSLLLHGITIVISPLISLMRDQVDGANEIGIPAA 90
Cdd:cd17920    1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  91 FINTTQTPDEQQQVFDAANAGKVKLLYVAPERLETARFRAFATHAD----IALFAVDEAHCVSQWGQDFRSSYLAIGEFI 166
Cdd:cd17920   81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLRLGRLR 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 919404579 167 DSLPDRPtvaaftatatERVRRDIVNLLGLRNPLVMVTGFD 207
Cdd:cd17920  161 RALPGVPilalt-atatPEVREDILKRLGLRNPVIFRASFD 200
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
11-207 3.20e-68

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: 220.98  E-value: 3.20e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  11 LATLRKYFGYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSLLLH----GITIVISPLISLMRDQVDGANEIg 86
Cdd:cd18018    1 LKLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRrrgpGLTLVVSPLIALMKDQVDALPRA- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  87 IPAAFINTTQTPDEQQQVFDAANAGKVKLLYVAPERLETARFRAFATHAD-IALFAVDEAHCVSQWGQDFRSSYLAIGEF 165
Cdd:cd18018   80 IKAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTPpISLLVVDEAHCISEWSHNFRPDYLRLCRV 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 919404579 166 IDSLPDRPTVAAFTATATERVRRDIVNLLGLRNPLVMVTGFD 207
Cdd:cd18018  160 LRELLGAPPVLALTATATKRVVEDIASHLGIPESGVVRGPLY 201
DEXHc_RecQ3 cd18017
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ...
11-207 1.84e-60

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: 200.39  E-value: 1.84e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  11 LATLRKYFGYESFRPGQAELINAILE-GRDVLGVMPTGSGKSVCYQIPSLLLHGITIVISPLISLMRDQVDGANEIGIPA 89
Cdd:cd18017    1 LNALNEYFGHSSFRPVQWKVIRSVLEeRRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  90 AFINTTQtpdeQQQVFDAANAGKVKLLYVAPERLETARFRAFATHADIALFAVDEAHCVSQWGQDFRSSYLAIGEFIDSL 169
Cdd:cd18017   81 CFLGSAQ----SQNVLDDIKMGKIRVIYVTPEFVSKGLELLQQLRNGITLIAIDEAHCVSQWGHDFRSSYRHLGSIRNRL 156
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 919404579 170 PDRPTVAAFTATATeRVRRDIVNLLGLRNPLVMVTGFD 207
Cdd:cd18017  157 PNVPIVALTATATP-SVRDDIIKNLNLRNPQITCTSFD 193
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
208-354 1.96e-52

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: 176.63  E-value: 1.96e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 208 RTNLYFD-MLKLNTREKANWIAHYVAEHADESGIVYCATRKETEALAQTLNimvpqlrkaqgsqmEDGPIAAAYHGGMPA 286
Cdd:cd18794    1 RPNLFYSvRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQ--------------SKGISAAAYHAGLEP 66
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919404579 287 NVRERAQRDFVTDTVPLVVATNAFGMGIDKSNVRYVIHHNMPESIEAYYQEAGRAGRDGEPSRCTLLW 354
Cdd:cd18794   67 SDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
DEXHc_RecQ1 cd18015
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ...
12-207 2.16e-52

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: 179.48  E-value: 2.16e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  12 ATLRKYFGYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSLLLHGITIVISPLISLMRDQVDGANEIGIPAAF 91
Cdd:cd18015    8 DTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISATM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  92 INTTQTPDEQQQVFDAANAGK--VKLLYVAPERL-ETARFRAFATHAD----IALFAVDEAHCVSQWGQDFRSSYLAIGE 164
Cdd:cd18015   88 LNASSSKEHVKWVHAALTDKNseLKLLYVTPEKIaKSKRFMSKLEKAYnagrLARIAIDEVHCCSQWGHDFRPDYKKLGI 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 919404579 165 FIDSLPDRPTVAAFTATATeRVRRDIVNLLGLRNPLVMVTGFD 207
Cdd:cd18015  168 LKRQFPNVPILGLTATATS-KVLKDVQKILCIQKCLTFTASFN 209
DEXHc_RecQ5 cd18014
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ...
11-202 2.67e-47

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: 165.34  E-value: 2.67e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  11 LATLRKYFGYESFR-PGQAELINAILEGR-DVLGVMPTGSGKSVCYQIPSLLLHGITIVISPLISLMRDQVDGANEIGIP 88
Cdd:cd18014    1 RSTLKKVFGHSDFKsPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  89 AAFINTTQTPDEQQQVFD--AANAGKVKLLYVAPERLETARF-RAFAT---HADIALFAVDEAHCVSQWGQDFRSSYLAI 162
Cdd:cd18014   81 VDSLNSKLSAQERKRIIAdlESEKPQTKFLYITPEMAATSSFqPLLSSlvsRNLLSYLVVDEAHCVSQWGHDFRPDYLRL 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 919404579 163 GEFIDSLPDRPTVAAFTATATErVRRDIVNLLGLRNPLVM 202
Cdd:cd18014  161 GALRSRYGHVPWVALTATATPQ-VQEDIFAQLRLKKPVAI 199
DEXHc_RecQ2_BLM cd18016
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ...
11-207 3.16e-46

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: 162.69  E-value: 3.16e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  11 LATLRKYFGYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSLLLHGITIVISPLISLMRDQVDGANEIGIPAA 90
Cdd:cd18016    6 MKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPAT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  91 FINTTQTPDEQQQVFDAANAGK--VKLLYVAPERLeTARFRAFATHAD------IALFAVDEAHCVSQWGQDFRSSYLAI 162
Cdd:cd18016   86 YLTGDKTDAEATKIYLQLSKKDpiIKLLYVTPEKI-SASNRLISTLENlyerklLARFVIDEAHCVSQWGHDFRPDYKRL 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 919404579 163 GEFIDSLPDRPtVAAFTATATERVRRDIVNLLGLRNPLVMVTGFD 207
Cdd:cd18016  165 NMLRQKFPSVP-MMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
DpdF NF041063
protein DpdF;
14-365 5.69e-46

protein DpdF;


Pssm-ID: 468990 [Multi-domain]  Cd Length: 813  Bit Score: 174.71  E-value: 5.69e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  14 LRKYFGYESFR-PGQAELINAIL---EGRDVLGVMPTGSGKSVCYQIPSLLL---HGITIVISPLISLMRDQVDGANEIg 86
Cdd:NF041063 131 LAEALGFTHYRsPGQREAVRAALlapPGSTLIVNLPTGSGKSLVAQAPALLAsrqGGLTLVVVPTVALAIDQERRAREL- 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  87 IPAAFINTT--------QTPDEQQQVFDAANAGKVKLLYVAPE----RLETARFRAfATHADIALFAVDEAHCVSQWGQD 154
Cdd:NF041063 210 LRRAGPDLGgplawhggLSAEERAAIRQRIRDGTQRILFTSPEsltgSLRPALFDA-AEAGLLRYLVVDEAHLVDQWGDG 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 155 FRSSYLAIGEFIDSLPDRPTVAAFTATA------TERVRRDIVNLLGLRNPLVMVTG-FDRTnlyfdmlklntrEkanwI 227
Cdd:NF041063 289 FRPEFQLLAGLRRSLLRLAPSGRPFRTLllsatlTESTLDTLETLFGPPGPFIVVSAvQLRP------------E----P 352
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 228 AHYVAEHADESG----------------IVYCATRKETEALAQTLnimvpqlrKAQGSQMedgpiAAAYHGGMPANVRER 291
Cdd:NF041063 353 AYWVAKCDSEEErrervlealrhlprplILYVTKVEDAEAWLQRL--------RAAGFRR-----VALFHGDTPDAERER 419
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919404579 292 AQRDFVTDTVPLVVATNAFGMGIDKSNVRYVIHHNMPESIEAYYQEAGRAGRDGEPSRCTLLWNESDIVTRRRL 365
Cdd:NF041063 420 LIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDIAKSL 493
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
24-162 1.59e-25

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: 103.09  E-value: 1.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579   24 RPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSL------LLHGITIVISPLISLMRDQVDGANEIGIPAAF-INTTQ 96
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGLkVASLL 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919404579   97 TPDEQQQVFDAANagKVKLLYVAPERLETARFRAFATHaDIALFAVDEAHCVSQWGqdFRSSYLAI 162
Cdd:pfam00270  81 GGDSRKEQLEKLK--GPDILVGTPGRLLDLLQERKLLK-NLKLLVLDEAHRLLDMG--FGPDLEEI 141
RQC pfam09382
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ...
436-530 6.44e-22

RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix structure. The RQC domain, found only in RecQ family enzymes, is a high affinity G4 DNA binding domain.


Pssm-ID: 462780 [Multi-domain]  Cd Length: 108  Bit Score: 91.06  E-value: 6.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  436 TFETVDVSAVARAISMCVHDLGQHYGMGKVVQVLRGSKAQDLANRGLDAAPTYGRLSEVNEAKIRDVLNQMVADGFLVVS 515
Cdd:pfam09382   1 PPETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVD 80
                          90
                  ....*....|....*
gi 919404579  516 EGRLPLVQFGPRAAE 530
Cdd:pfam09382  81 IEFYSVLKLTPKARE 95
HRDC pfam00570
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ...
578-645 8.53e-22

HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic acid binding. Mutations in the HRDC domain cause human disease. It is interesting to note that the RecQ helicase in Deinococcus radiodurans has three tandem HRDC domains.


Pssm-ID: 425755 [Multi-domain]  Cd Length: 68  Bit Score: 89.13  E-value: 8.53e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919404579  578 DAELFEHLRALRMQIAREIGKPPYIVFSDRALRDMAERHPHTSKEFLEVNGVGANKLERYGKRFMEVI 645
Cdd:pfam00570   1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
DEXDc smart00487
DEAD-like helicases superfamily;
16-166 2.11e-21

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 92.55  E-value: 2.11e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579    16 KYFGYESFRPGQAELINAILEG-RDVLGVMPTGSGKSVCYQIPSLLL-----HGITIVISPLISLMRDQVDGANEIGIPA 89
Cdd:smart00487   2 EKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLGPSL 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919404579    90 AFINTT-QTPDEQQQVFDAANAGKVKLLYVAPERLETARFRAFATHADIALFAVDEAHCVSQWGqdFRSSYLAIGEFI 166
Cdd:smart00487  82 GLKVVGlYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKLLKLL 157
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
222-345 3.96e-21

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: 88.81  E-value: 3.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  222 EKANWIAHYVAEHADESGIVYCATRK--ETEALAQTLNIMVpqlrkaqgsqmedgpiaAAYHGGMPANVRERAQRDFVTD 299
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKtlEAELLLEKEGIKV-----------------ARLHGDLSQEEREEILEDFRKG 63
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 919404579  300 TVPLVVATNAFGMGIDKSNVRYVIHHNMPESIEAYYQEAGRAGRDG 345
Cdd:pfam00271  64 KIDVLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
RQC smart00956
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ...
441-530 4.41e-20

This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix structure; The RQC domain, found only in RecQ family enzymes, is a high affinity G4 DNA binding domain.


Pssm-ID: 214936 [Multi-domain]  Cd Length: 92  Bit Score: 85.22  E-value: 4.41e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579   441 DVSAVARAISMCVHDLGQHYGMGKVVQVLRGSKAQDLANRGLDAAPTYGRLSEVNEAKIRDVLNQMVADGFLVVSEGRLP 520
Cdd:smart00956   1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYP 80
                           90
                   ....*....|
gi 919404579   521 LVQFGPRAAE 530
Cdd:smart00956  81 YLKLTEKARP 90
HELICc smart00490
helicase superfamily c-terminal domain;
277-345 2.76e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 82.64  E-value: 2.76e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919404579   277 AAAYHGGMPANVRERAQRDFVTDTVPLVVATNAFGMGIDKSNVRYVIHHNMPESIEAYYQEAGRAGRDG 345
Cdd:smart00490  14 VARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
HRDC smart00341
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ...
580-648 1.65e-17

Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the HRDC domain cause human disease.


Pssm-ID: 128635 [Multi-domain]  Cd Length: 81  Bit Score: 77.34  E-value: 1.65e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919404579   580 ELFEHLRALRMQIAREIGKPPYIVFSDRALRDMAERHPHTSKEFLEVNGVGANKLERYGKRFMEVIRIF 648
Cdd:smart00341   6 RLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEA 74
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
223-353 3.30e-16

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: 75.62  E-value: 3.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 223 KANWIAHYVAEHADESGIVYCATRKETEALAQTLNimvpqlrkaqgsqmEDGPIAAAYHGGMPANVRERAQRDFVTDTVP 302
Cdd:cd18787   14 KLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLE--------------ELGIKVAALHGDLSQEERERALKKFRSGKVR 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 919404579 303 LVVATNAFGMGIDKSNVRYVIHHNMPESIEAYYQEAGRAGRDGEPSRCTLL 353
Cdd:cd18787   80 VLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITF 130
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
10-346 6.35e-16

Superfamily II DNA and RNA helicase [Replication, recombination and repair];


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 80.19  E-value: 6.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  10 ALATLrkyfGYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPslLLHGI---------TIVISP---LIslmrD 77
Cdd:COG0513   16 ALAEL----GYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLP--LLQRLdpsrprapqALILAPtreLA----L 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  78 QVdgANEIGIPAAFINTTQTP-------DEQQQ---------------VFDAANAGKVKLlyvapERLETarfrafatha 135
Cdd:COG0513   86 QV--AEELRKLAKYLGLRVATvyggvsiGRQIRalkrgvdivvatpgrLLDLIERGALDL-----SGVET---------- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 136 dialFAVDEAhcvsqwgqD------FRSsylAIGEFIDSLPDRptvaaftatatervRR----------DIVNLLG--LR 197
Cdd:COG0513  149 ----LVLDEA--------DrmldmgFIE---DIERILKLLPKE--------------RQtllfsatmppEIRKLAKryLK 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 198 NPL-VMVTGFDRTN------LYFdmlkLNTREKANWIAHYVAEHADESGIVYCATRKETEALAQTLNimvpqlrkaqgsq 270
Cdd:COG0513  200 NPVrIEVAPENATAetieqrYYL----VDKRDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQ------------- 262
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919404579 271 mEDGPIAAAYHGGMPANVRERAQRDFVTDTVPLVVATNAFGMGIDKSNVRYVIHHNMPESIEAYYQEAG---RAGRDGE 346
Cdd:COG0513  263 -KRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGrtgRAGAEGT 340
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
27-348 1.46e-15

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: 80.26  E-value: 1.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  27 QAELINAILEGRDVLGVMPTGSGKSVCYQIPSL--LLHGIT---IVISPLISLMRDQVDGANE------IGIPAAFINTT 95
Cdd:COG1205   61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLeaLLEDPGataLYLYPTKALARDQLRRLRElaealgLGVRVATYDGD 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  96 QTPDEQQQVFDAANagkvkLLYVAPERLETA------RFRAFatHADIALFAVDEAHC--------VSQ----------- 150
Cdd:COG1205  141 TPPEERRWIREHPD-----IVLTNPDMLHYGllphhtRWARF--FRNLRYVVIDEAHTyrgvfgshVANvlrrlrricrh 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 151 WGQDFRssYLA----IG---EFIDSLPDRPTVAAFTATATeRVRRDIVnllgLRNPLVMVTGFDRTNlyfdmlklnTREK 223
Cdd:COG1205  214 YGSDPQ--FILasatIGnpaEHAERLTGRPVTVVDEDGSP-RGERTFV----LWNPPLVDDGIRRSA---------LAEA 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 224 ANWIAHYVAEHAdeSGIVYCATRKETEALAQtlnimvpQLRKAQGSQMEDGPIAAaYHGGMPANVRERAQRDFVTDTVPL 303
Cdd:COG1205  278 ARLLADLVREGL--RTLVFTRSRRGAELLAR-------YARRALREPDLADRVAA-YRAGYLPEERREIERGLRSGELLG 347
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 919404579 304 VVATNAFGMGIDKSNVRYVIHHNMPESIEAYYQEAGRAGRDGEPS 348
Cdd:COG1205  348 VVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDS 392
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
217-348 7.09e-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: 72.29  E-value: 7.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 217 KLNTREKANWIAHYVAEHADESG---IVYCATRKETEALaqtlnimvpqLRKAQGSQMEDGPIA---AAYHGGMPANVRE 290
Cdd:cd18797   13 KDGERGSARREAARLFADLVRAGvktIVFCRSRKLAELL----------LRYLKARLVEEGPLAskvASYRAGYLAEDRR 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 919404579 291 RAQRDFVTDTVPLVVATNAFGMGIDKSNVRYVIHHNMPESIEAYYQEAGRAGRDGEPS 348
Cdd:cd18797   83 EIEAELFNGELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDS 140
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
19-358 3.55e-14

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 75.59  E-value: 3.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  19 GYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIP------SLLLHGIT-------IVISPLISLMRdQVDGANEI 85
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPiisrccTIRSGHPSeqrnplaMVLTPTRELCV-QVEDQAKV 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  86 ---GIP---AAFINTTQTPdeqQQVFDAANAgkVKLLYVAPERLETARFRAFATHADIALFAVDEAHCVSQWGqdFRSSY 159
Cdd:PLN00206 219 lgkGLPfktALVVGGDAMP---QQLYRIQQG--VELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERG--FRDQV 291
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 160 LAIGEFIdSLPDRPTVAAFTATATERVRRDIvnllgLRNPLVMVTGF-DRTNLYFDMLKL--NTREKANWIAHYV--AEH 234
Cdd:PLN00206 292 MQIFQAL-SQPQVLLFSATVSPEVEKFASSL-----AKDIILISIGNpNRPNKAVKQLAIwvETKQKKQKLFDILksKQH 365
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 235 ADESGIVYCATRKETEALAQTLnimvpqlRKAQGSQmedgpiAAAYHGGMPANVRERAQRDFVTDTVPLVVATNAFGMGI 314
Cdd:PLN00206 366 FKPPAVVFVSSRLGADLLANAI-------TVVTGLK------ALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGV 432
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 919404579 315 DKSNVRYVIHHNMPESIEAYYQEAGRAGRDGEPSRCTLLWNESD 358
Cdd:PLN00206 433 DLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEED 476
RecQ_Zn_bind pfam16124
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ.
357-433 3.09e-12

RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ.


Pssm-ID: 465031 [Multi-domain]  Cd Length: 66  Bit Score: 61.92  E-value: 3.09e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919404579  357 SDIVTRRRLLDMADRNERltpeeqevVRRSKRQLLDAMIGYCR-TTDCLHDYMTRYFGESNGTErsadgHCiGGCVNC 433
Cdd:pfam16124   2 QDVVRLRFLIEQSEADEE--------RKEVELQKLQAMVAYCEnTTDCRRKQLLRYFGEEFDSE-----PC-GNCDNC 65
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
37-172 1.37e-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: 59.72  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  37 GRDVLGVMPTGSGKSVCYQIPSLLL----HGITIVISPLISLMRDQ---VDGANEIGIPAAfINTTQTPDEQQQVFDAAN 109
Cdd:cd00046    1 GENVLITAPTGSGKTLAALLAALLLllkkGKKVLVLVPTKALALQTaerLRELFGPGIRVA-VLVGGSSAEEREKNKLGD 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919404579 110 AgkvKLLYVAPERLETARFRAFATHA-DIALFAVDEAHCVSQWGQDFRSSYLAIGEFIDSLPDR 172
Cdd:cd00046   80 A---DIIIATPDMLLNLLLREDRLFLkDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQV 140
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
24-395 2.61e-10

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 63.51  E-value: 2.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  24 RPGQAELINAIL-----EGRDVLGVMPTGSGKSV----CYQipSLLLHGITIVISPLISLMRdqvdganeigipaafint 94
Cdd:COG1061   82 RPYQQEALEALLaalerGGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLE------------------ 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  95 tQTPDEQQQVFDAANAGkvkllyvAPERLETARFrAFATHADIA-------------LFAVDEAHCVSqwgqdfRSSYLA 161
Cdd:COG1061  142 -QWAEELRRFLGDPLAG-------GGKKDSDAPI-TVATYQSLArrahldelgdrfgLVIIDEAHHAG------APSYRR 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 162 IGEFIDSL--------PDRPTVAAFTATATERVR-----RDIVNLLGLRNPLVM---VTGFDRTNLY-------FDMLKL 218
Cdd:COG1061  207 ILEAFPAAyrlgltatPFRSDGREILLFLFDGIVyeyslKEAIEDGYLAPPEYYgirVDLTDERAEYdalserlREALAA 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 219 NTREKANWIAHYVAEHADES-GIVYCATRKETEALAQTLNimvpqlrkaqgsqmEDGPIAAAYHGGMPANVRERAQRDFV 297
Cdd:COG1061  287 DAERKDKILRELLREHPDDRkTLVFCSSVDHAEALAELLN--------------EAGIRAAVVTGDTPKKEREEILEAFR 352
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 298 TDTVPLVVATNAFGMGIDKSNVRYVIHHNMPESIEAYYQEAGRAGRDGEP-SRCTLLwnesDIVTRRR--LLDMADRNER 374
Cdd:COG1061  353 DGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGkEDALVY----DFVGNDVpvLEELAKDLRD 428
                        410       420
                 ....*....|....*....|.
gi 919404579 375 LTPEEQEVVRRSKRQLLDAMI 395
Cdd:COG1061  429 LAGYRVEFLDEEESEELALLI 449
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
227-349 5.30e-09

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: 55.35  E-value: 5.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 227 IAHYVAE-HADESGIVYCATRKETEALAQTLnimvpqlRKAQGSQMEDGPIAAaYHGGMPANVRERAQRDFVTDTVPLVV 305
Cdd:cd18796   28 YAEVIFLlERHKSTLVFTNTRSQAERLAQRL-------RELCPDRVPPDFIAL-HHGSLSRELREEVEAALKRGDLKVVV 99
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 919404579 306 ATNAFGMGIDKSNVRYVIHHNMPESIEAYYQEAGRAG-RDGEPSR 349
Cdd:cd18796  100 ATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGhRPGAASK 144
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
18-408 6.57e-09

Replicative superfamily II helicase [Replication, recombination and repair];


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 58.75  E-value: 6.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  18 FGYESFRPGQAELINA-ILEGRDVLGVMPTGSGKSVCYQIP---SLLLHGITIVISPLISLmrdqvdgANEI------GI 87
Cdd:COG1204   18 RGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAELAilkALLNGGKALYIVPLRAL-------ASEKyrefkrDF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  88 PAAFINTTQTPDEqqQVFDAANAGKVKLLYVAPERLETA-RFRAfATHADIALFAVDEAHCVsqwGQDFRSS--YLAIGE 164
Cdd:COG1204   91 EELGIKVGVSTGD--YDSDDEWLGRYDILVATPEKLDSLlRNGP-SWLRDVDLVVVDEAHLI---DDESRGPtlEVLLAR 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 165 FIDSLPDrptvaaftatatervrrdiVNLLGL----RNP----------LVMVT--------GF--DRTNLYFDMLKLNT 220
Cdd:COG1204  165 LRRLNPE-------------------AQIVALsatiGNAeeiaewldaeLVKSDwrpvplneGVlyDGVLRFDDGSRRSK 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 221 REKANWIAHYVAEhaDESGIVYCATRKETEALAQTL----------------NIMVPQLRKAQGSQMEDGPIA------A 278
Cdd:COG1204  226 DPTLALALDLLEE--GGQVLVFVSSRRDAESLAKKLadelkrrltpeereelEELAEELLEVSEETHTNEKLAdclekgV 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 279 AYH-GGMPANVRERAQRDFVTDTVPLVVATNAFGMGIdksN--VRYVIHH------NMPESIEAYYQEAGRAGRDG-EPs 348
Cdd:COG1204  304 AFHhAGLPSELRRLVEDAFREGLIKVLVATPTLAAGV---NlpARRVIIRdtkrggMVPIPVLEFKQMAGRAGRPGyDP- 379
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919404579 349 rctllWNESDIVTRRRLLDMADRNERLTPEEQEVvrRSK--------RQLLDA-MIGYCRTTDCLHDYM 408
Cdd:COG1204  380 -----YGEAILVAKSSDEADELFERYILGEPEPI--RSKlanesalrTHLLALiASGFANSREELLDFL 441
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
27-146 7.45e-09

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: 55.67  E-value: 7.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  27 QAELINAILEGRDVLGVMPTGSGKSVCYQIPSL--LL--HGIT-IVISPLISLMRDQVDGANEIGIP-----AAFINTTQ 96
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILeaLLrdPGSRaLYLYPTKALAQDQLRSLRELLEQlglgiRVATYDGD 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 919404579  97 TPDEQQQVFDAANAgkvKLLYVAPERLETARFRAFATHADIA----LFAVDEAH 146
Cdd:cd17923   85 TPREERRAIIRNPP---RILLTNPDMLHYALLPHHDRWARFLrnlrYVVLDEAH 135
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
19-382 1.71e-07

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 54.47  E-value: 1.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  19 GYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPslLLHGI--------TIVISPLISLMRDQVDGANEI----- 85
Cdd:PRK11634  25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLP--LLHNLdpelkapqILVLAPTRELAVQVAEAMTDFskhmr 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  86 GIPAAFINTTQTPDEQQQvfdAANAGKvKLLYVAPERLETARFRAFATHADIALFAVDEAHcvsqwgQDFRSSYLAIGEF 165
Cdd:PRK11634 103 GVNVVALYGGQRYDVQLR---ALRQGP-QIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEAD------EMLRMGFIEDVET 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 166 IDS-LPDRPTVAAFTATATERVRRDIVNLLG----LRNPLVMVTGFDRTNLYFDMLKLntREKANWIAHYVAEHADeSGI 240
Cdd:PRK11634 173 IMAqIPEGHQTALFSATMPEAIRRITRRFMKepqeVRIQSSVTTRPDISQSYWTVWGM--RKNEALVRFLEAEDFD-AAI 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 241 VYCATRKETEALAQTLNimvpqlrkaqgsqmEDGPIAAAYHGGMPANVRERAQRDFVTDTVPLVVATNAFGMGIDKSNVR 320
Cdd:PRK11634 250 IFVRTKNATLEVAEALE--------------RNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERIS 315
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919404579 321 YVIHHNMPESIEAYYQEAGRAGRDGEPSRcTLLWNESdivTRRRLLDMADRNERLTPEEQEV 382
Cdd:PRK11634 316 LVVNYDIPMDSESYVHRIGRTGRAGRAGR-ALLFVEN---RERRLLRNIERTMKLTIPEVEL 373
PTZ00424 PTZ00424
helicase 45; Provisional
240-345 1.83e-07

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 53.68  E-value: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 240 IVYCATRKETEALAQTLnimvpQLRKAQGSQMedgpiaaayHGGMPANVRERAQRDFVTDTVPLVVATNAFGMGIDKSNV 319
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKM-----HERDFTVSCM---------HGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQV 336
                         90       100
                 ....*....|....*....|....*.
gi 919404579 320 RYVIHHNMPESIEAYYQEAGRAGRDG 345
Cdd:PTZ00424 337 SLVINYDLPASPENYIHRIGRSGRFG 362
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
303-353 3.21e-07

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: 48.08  E-value: 3.21e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 919404579 303 LVVATNAFGMGIDKSNVRYVIHHNMPESIEAYYQEAGRAGRDG-EPSRCTLL 353
Cdd:cd18785   25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILF 76
PTZ00110 PTZ00110
helicase; Provisional
240-345 4.50e-07

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 52.85  E-value: 4.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 240 IVYCATRKETEALAQTLNImvpqlrkaqgsqmeDGPIAAAYHGGMPANVRERAQRDFVTDTVPLVVATNAFGMGIDKSNV 319
Cdd:PTZ00110 381 LIFVETKKGADFLTKELRL--------------DGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDV 446
                         90       100
                 ....*....|....*....|....*.
gi 919404579 320 RYVIHHNMPESIEAYYQEAGRAGRDG 345
Cdd:PTZ00110 447 KYVINFDFPNQIEDYVHRIGRTGRAG 472
Rnd COG0349
Ribonuclease D [Translation, ribosomal structure and biogenesis];
585-646 5.36e-07

Ribonuclease D [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440118 [Multi-domain]  Cd Length: 365  Bit Score: 52.18  E-value: 5.36e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919404579 585 LRAL---RMQIAREIGKPPYIVFSDRALRDMAERHPHTSKEFLEVNGVGANKLERYGKRFMEVIR 646
Cdd:COG0349  213 LRELaawREREARKRDVPRNRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAVA 277
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
16-59 1.85e-06

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: 49.30  E-value: 1.85e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 919404579  16 KYFGYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSL 59
Cdd:cd17953   28 KKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMF 71
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
11-59 1.96e-06

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: 48.98  E-value: 1.96e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 919404579  11 LATLRKYfGYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSL 59
Cdd:cd00268    2 LKALKKL-GFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPIL 49
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
237-345 2.26e-06

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 50.33  E-value: 2.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 237 ESGIVYCATRKETEALAQtlnimvpQLRKAQgsqmedgpIAAAY-HGGMPANVRERAQRDFVTDTVPLVVATNAFGMGID 315
Cdd:PRK11192 246 TRSIVFVRTRERVHELAG-------WLRKAG--------INCCYlEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGID 310
                         90       100       110
                 ....*....|....*....|....*....|
gi 919404579 316 KSNVRYVIHHNMPESIEAYYQEAGRAGRDG 345
Cdd:PRK11192 311 IDDVSHVINFDMPRSADTYLHRIGRTGRAG 340
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
199-345 2.61e-06

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: 47.55  E-value: 2.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 199 PL-VMVTGFDRTNLYFDMLKLNTREKANWIAHYVAEHADESG-IVYCATRKETEALAQTLNimvpqlrkaqGsqmedgpi 276
Cdd:cd18795    4 PLeEYVLGFNGLGIKLRVDVMNKFDSDIIVLLKIETVSEGKPvLVFCSSRKECEKTAKDLA----------G-------- 65
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919404579 277 AAAYHGGMPANVRERAQRDFVTDTVPLVVATNAFGMGID--------KSNVRYVIHHNMPESIEAYYQEAGRAGRDG 345
Cdd:cd18795   66 IAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpartviiKGTQRYDGKGYRELSPLEYLQMIGRAGRPG 142
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
8-64 8.92e-06

DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) 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: 350713 [Multi-domain]  Cd Length: 204  Bit Score: 46.83  E-value: 8.92e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 919404579   8 NSALATLRKYFGYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPslLLHGI 64
Cdd:cd17955    7 SSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALP--ILQRL 61
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
16-70 1.62e-05

DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 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: 350700 [Multi-domain]  Cd Length: 198  Bit Score: 46.20  E-value: 1.62e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919404579  16 KYFGYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSL-LLHGI---------TIVISP 70
Cdd:cd17942    6 EEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIeLLYKLkfkprngtgVIIISP 70
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
240-343 2.64e-05

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 47.11  E-value: 2.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 240 IVYCATRKETEALAQTLNimvpqlrkaqgsqmEDGPIAAAYHGGMPANVRERAQRDFVTDTVPLVVATNAFGMGIDKSNV 319
Cdd:PRK10590 249 LVFTRTKHGANHLAEQLN--------------KDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEEL 314
                         90       100
                 ....*....|....*....|....
gi 919404579 320 RYVIHHNMPESIEAYYQEAGRAGR 343
Cdd:PRK10590 315 PHVVNYELPNVPEDYVHRIGRTGR 338
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
25-70 3.16e-05

DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 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: 350715 [Multi-domain]  Cd Length: 198  Bit Score: 45.27  E-value: 3.16e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 919404579  25 PGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSLLL-------HGI-TIVISP 70
Cdd:cd17957   15 PIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKlgkprkkKGLrALILAP 68
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
11-59 9.39e-05

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 45.32  E-value: 9.39e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 919404579  11 LATLRKyFGYEsfRPG--QAELINAILEGRDVLGVMPTGSGKSVCYQIPSL 59
Cdd:PRK11192  13 LEALQD-KGYT--RPTaiQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPAL 60
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
19-59 1.04e-04

DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor 3B-Associated 125 kDa Protein, RHELP, or RNAHP) is an NTPase with a preference for ATP, the hydrolysis of which is enhanced by various RNA substrates. It acts as a non-processive RNA helicase with protein displacement and RNA annealing activities. DDX42 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: 350710 [Multi-domain]  Cd Length: 197  Bit Score: 43.94  E-value: 1.04e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 919404579  19 GYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSL 59
Cdd:cd17952    9 EYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPML 49
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
19-57 1.57e-04

DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 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: 350717 [Multi-domain]  Cd Length: 205  Bit Score: 43.45  E-value: 1.57e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 919404579  19 GYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIP 57
Cdd:cd17959   20 GYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIP 58
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
19-70 1.69e-04

DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 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: 350699 [Multi-domain]  Cd Length: 198  Bit Score: 43.05  E-value: 1.69e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919404579  19 GYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSL-LLH--------GI-TIVISP 70
Cdd:cd17941    9 GFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLeKLYrerwtpedGLgALIISP 70
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
262-345 1.75e-04

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 44.52  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 262 QLRKAQGSQMEDGPIAAAYHGGMPANVRERAQRDFVTDTVPLVVATNAFGMGIDKSNVRYVIHHNMPESIEAYYQEAGRA 341
Cdd:PRK01297 347 EVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRT 426

                 ....
gi 919404579 342 GRDG 345
Cdd:PRK01297 427 GRAG 430
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
228-370 2.97e-04

C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 41.87  E-value: 2.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 228 AHYVAEHADESGIVycaTRKETEALAQTLNIMVPQLRkaqgsqmedgpIAAAyHGGMPANVRERAQRDFVTDTVPLVVAT 307
Cdd:cd18792   29 VYYVYPRIEESEKL---DLKSIEALAEELKELVPEAR-----------VALL-HGKMTEDEKEAVMLEFREGEYDILVST 93
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919404579 308 NAFGMGIDKSNVR-YVIHHNMPESIEAYYQEAGRAGRDGEPSRCTLLWNESDIVT---RRRLLDMAD 370
Cdd:cd18792   94 TVIEVGIDVPNANtMIIEDADRFGLSQLHQLRGRVGRGKHQSYCYLLYPDPKKLTetaKKRLRAIAE 160
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
281-370 3.90e-04

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: 41.56  E-value: 3.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 281 HGGMPANVRERAQRDFVTDTVPLVVATNAFGMGIDKSNVR-YVIHHNMPESIEAYYQEAGRAGRDGEPSRCTLL-WNESD 358
Cdd:cd18811   68 HGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATvMVIEDAERFGLSQLHQLRGRVGRGDHQSYCLLVyKDPLT 147
                         90
                 ....*....|..
gi 919404579 359 IVTRRRLLDMAD 370
Cdd:cd18811  148 ETAKQRLRVMTE 159
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
22-74 4.27e-04

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: 41.55  E-value: 4.27e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 919404579  22 SFRPGQAELINA-ILEGRDVLGVMPTGSGKSVCYQ---IPSLLLHGITIVISPLISL 74
Cdd:cd18028    1 ELYPPQAEAVRAgLLKGENLLISIPTASGKTLIAEmamVNTLLEGGKALYLVPLRAL 57
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
16-62 5.55e-04

DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 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: 350712 [Multi-domain]  Cd Length: 203  Bit Score: 41.53  E-value: 5.55e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 919404579  16 KYFGYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSL--LLH 62
Cdd:cd17954   16 EKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILqaLLE 64
COG1202 COG1202
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
221-343 5.82e-04

Superfamily II helicase, archaea-specific [Replication, recombination and repair];


Pssm-ID: 440815 [Multi-domain]  Cd Length: 790  Bit Score: 42.96  E-value: 5.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 221 REKANWIAHYVAEHAD-ESG-------IVYCATRKETEALAQTLnimvpqlrkaqgsqmedGPIAAAYHGGMPANVRERA 292
Cdd:COG1202  404 REKIRIINKLVKREFDtKSSkgyrgqtIIFTNSRRRCHEIARAL-----------------GYKAAPYHAGLDYGERKKV 466
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919404579 293 QRDFVTDTVPLVVATNAFG----------------MGIDKSNVRyvihhnmpesieAYYQEAGRAGR 343
Cdd:COG1202  467 ERRFADQELAAVVTTAALAagvdfpasqvifdslaMGIEWLSVQ------------EFHQMLGRAGR 521
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
19-59 8.14e-04

DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 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: 350703 [Multi-domain]  Cd Length: 220  Bit Score: 41.15  E-value: 8.14e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 919404579  19 GYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSL 59
Cdd:cd17945    9 GYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLL 49
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
11-57 9.05e-04

DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It 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: 350714 [Multi-domain]  Cd Length: 231  Bit Score: 41.46  E-value: 9.05e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 919404579  11 LATLRKyFGYESFRPGQAELINAILEG---------RDVLGVMPTGSGKSVCYQIP 57
Cdd:cd17956    2 LKNLQN-NGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLP 56
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
1-77 1.28e-03

Lhr-like helicase [Replication, recombination and repair];


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 42.01  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579   1 MTNEHEENSALATLRKYFG--YESFRPGQAELINAILEGRDVLGVMPTGSGKS-----------VCYQIPSLLLHGITIV 67
Cdd:COG1201    1 MSAEDVLSLLHPAVRAWFAarFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlaaflpaldelARRPRPGELPDGLRVL 80
                         90
                 ....*....|.
gi 919404579  68 -ISPLISLMRD 77
Cdd:COG1201   81 yISPLKALAND 91
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
9-69 1.54e-03

Rad3-related DNA helicase DinG [Replication, recombination and repair];


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 41.45  E-value: 1.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579   9 SALATLRKYF-GYEsFRPGQAELINAI---LEGRDVLgVM--PTGSGKSVCYQIPSLLL---HGITIVIS 69
Cdd:COG1199    1 ADDGLLALAFpGFE-PRPGQREMAEAVaraLAEGRHL-LIeaGTGTGKTLAYLVPALLAareTGKKVVIS 68
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
269-377 1.70e-03

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 41.83  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579  269 SQMEDGPIAAAYHGGMPANVRERAQRDFVTDTVPLVVATNAFGMGIDKSNVRYVIHHNMPESIEAYYQEAGRAGRDGEPS 348
Cdd:PRK09751  296 VQSSDVFIARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGHQVGGV 375
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 919404579  349 RCTLLWNEsdivTRRRLLD--------MADRNERLTP 377
Cdd:PRK09751  376 SKGLFFPR----TRRDLVDsavivecmFAGRLENLTP 408
Dob10 COG4581
Superfamily II RNA helicase [Replication, recombination and repair];
244-345 2.28e-03

Superfamily II RNA helicase [Replication, recombination and repair];


Pssm-ID: 443638 [Multi-domain]  Cd Length: 751  Bit Score: 41.08  E-value: 2.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579 244 ATRKETEALAQTLNIMVPQLRKAQGSQMEDGPIA--AAYHGGMPANVRERAQRDFVTDTVPLVVATNAFGMGIdksnvry 321
Cdd:COG4581  267 TTKEERAEIREAIDEFAEDFSVLFGKTLSRLLRRgiAVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGI------- 339
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 919404579 322 vihhNMP-----------------ESIEA--YYQEAGRAGRDG 345
Cdd:COG4581  340 ----NMPartvvftklskfdgerhRPLTAreFHQIAGRAGRRG 378
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
9-64 2.35e-03

DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350719 [Multi-domain]  Cd Length: 206  Bit Score: 39.87  E-value: 2.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 919404579   9 SALATLrkyfGYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPslLLHGI 64
Cdd:cd17961    7 KAIAKL----GWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALP--IIQKI 56
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
27-64 2.35e-03

DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 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: 350704 [Multi-domain]  Cd Length: 235  Bit Score: 39.91  E-value: 2.35e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 919404579  27 QAELI-NAILEGRDVLGVMPTGSGKSVCYQIPslLLHGI 64
Cdd:cd17946   17 QALALpAAIRDGKDVIGAAETGSGKTLAFGIP--ILERL 53
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
10-59 3.15e-03

DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 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: 350705 [Multi-domain]  Cd Length: 196  Bit Score: 39.16  E-value: 3.15e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 919404579  10 ALATLrkyfGYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSL 59
Cdd:cd17947    4 ALSSL----GFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPIL 49
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
25-60 3.52e-03

DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 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: 350709 [Multi-domain]  Cd Length: 206  Bit Score: 39.24  E-value: 3.52e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 919404579  25 PGQAELINAILEGRDVLGVMPTGSGKSVCYQIPSLL 60
Cdd:cd17951   15 PIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIM 50
ResIII pfam04851
Type III restriction enzyme, res subunit;
22-146 5.40e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 38.04  E-value: 5.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579   22 SFRPGQAELINAILEGRD-----VLGVMPTGSGKSVCYQIPSLLLHGI-----TIVISPLISLMRDQVDGANEIGIPAAF 91
Cdd:pfam04851   3 ELRPYQIEAIENLLESIKngqkrGLIVMATGSGKTLTAAKLIARLFKKgpikkVLFLVPRKDLLEQALEEFKKFLPNYVE 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 919404579   92 INTTQTPDEQQQVFDAAnagKVKL-----LYVAperLETARFRAFATHADiaLFAVDEAH 146
Cdd:pfam04851  83 IGEIISGDKKDESVDDN---KIVVttiqsLYKA---LELASLELLPDFFD--VIIIDEAH 134
DUF3106 pfam11304
Protein of unknown function (DUF3106); Some members in this family of proteins are annotated ...
354-385 5.61e-03

Protein of unknown function (DUF3106); Some members in this family of proteins are annotated as transmembrane proteins however this cannot be confirmed. Currently no function is known.


Pssm-ID: 463257 [Multi-domain]  Cd Length: 104  Bit Score: 36.81  E-value: 5.61e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 919404579  354 WNESDIVTRRRLLDMADRNERLTPEEQEVVRR 385
Cdd:pfam11304  19 WNSLPPEQRRKWLEIAERYPKMTPEEQQRLQE 50
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
27-59 8.69e-03

DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 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: 350696 [Multi-domain]  Cd Length: 204  Bit Score: 38.07  E-value: 8.69e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 919404579  27 QAELINAILEGRDVLGVMPTGSGKSVCYQIPSL 59
Cdd:cd17938   26 QAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL 58
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
11-65 8.93e-03

DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are 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: 350810 [Multi-domain]  Cd Length: 264  Bit Score: 38.41  E-value: 8.93e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 919404579  11 LATLRKYfGYESFRPGQAELINAILEGRDVLGVMPTGSGKSVCYQIP---SLLLHGIT 65
Cdd:cd18052   55 LKNIRKA-GYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPvltGMMKEGLT 111
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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