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Conserved domains on  [gi|564360538|ref|XP_006241868|]
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ATP-dependent DNA helicase Q4 isoform X3 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RecQ super family cl33925
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
485-850 9.37e-115

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


The actual alignment was detected with superfamily member COG0514:

Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 366.77  E-value: 9.37e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  485 AEVFQVLEQL-GHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLyakrSPCLTLVVSPLLSLMDDQVSDLP 563
Cdd:COG0514     3 DDALEVLKRVfGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALL----LPGLTLVVSPLIALMKDQVDALR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  564 SC-LKAACLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVGcgakgPANLPPAAQLPPVAFAcIDEVHCLSQWSHNFRP 642
Cdd:COG0514    79 AAgIRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLN-----PRFLELLRRLKISLFA-IDEAHCISQWGHDFRP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  643 CYLRVcKVLREHMGVRCFLGLTATATRSTARDVAQHLGIAEELEVSGSASIPaNLHLSVS--MDRDSDQALVTLLQGdrf 720
Cdd:COG0514   153 DYRRL-GELRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRP-NLRLEVVpkPPDDKLAQLLDFLKE--- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  721 RTLDSIIIYCARRKDTERVAALLRTclstvrdskpRGRGpetlAEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMG 800
Cdd:COG0514   228 HPGGSGIVYCLSRKKVEELAEWLRE----------AGIR----AAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMG 293
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 564360538  801 LDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHPQGEDLWE 850
Cdd:COG0514   294 IDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQR 343
RecQL4_SLD2_NTD cd22289
N-terminal homeodomain-like domain of metazoan RecQ protein-like 4 (RecQL4), fungal DNA ...
2-50 5.19e-19

N-terminal homeodomain-like domain of metazoan RecQ protein-like 4 (RecQL4), fungal DNA replication regulator SLD2 and similar proteins; RecQL4, also called ATP-dependent DNA helicase Q4, or DNA helicase, RecQ-like type 4 (RecQ4), or RTS, is a DNA-dependent ATPase that may modulate chromosome segregation. This family also includes fungal DNA replication regulator SLD2, also known as DNA replication and checkpoint protein 1 (DRC1), which functions with DPB11 to control DNA replication and the S-phase checkpoint. It is also required for the proper activation of RAD53 in response to DNA damage and replication blocks. This model corresponds to the N-terminal domain of RecQL4 and SLD2, which is a homeodomain-like DNA interaction motif.


:

Pssm-ID: 412085  Cd Length: 49  Bit Score: 81.52  E-value: 5.19e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 564360538    2 ERLATVRARLQDWERAFVRLHGRRPAKEDVEAAPEETRALYREYRNLKQ 50
Cdd:cd22289     1 ERLQELKIALKTWERAFAKKHGRKPTKDDIKAAPEEIKDLYKEYAKLKK 49
Drc1-Sld2 super family cl44400
DNA replication and checkpoint protein; Genome duplication is precisely regulated by ...
4-170 6.67e-10

DNA replication and checkpoint protein; Genome duplication is precisely regulated by cyclin-dependent kinases CDKs, which bring about the onset of S phase by activating replication origins and then prevent re-licensing of origins until mitosis is completed. The optimum sequence motif for CDK phosphorylation is S/T-P-K/R-K/R, and Drc1-Sld2 is found to have at least 11 potential phosphorylation sites. Drc1 is required for DNA synthesis and S-M replication checkpoint control. Drc1 associates with Cdc2 and is phosphorylated at the onset of S phase when Cdc2 is activated. Thus Cdc2 promotes DNA replication by phosphorylating Drc1 and regulating its association with Cut5. Sld2 and Sld3 represent the minimal set of S-CDK substrates required for DNA replication.


The actual alignment was detected with superfamily member pfam11719:

Pssm-ID: 371692 [Multi-domain]  Cd Length: 391  Bit Score: 62.54  E-value: 6.67e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538     4 LATVRARLQDWERAFVRLHGRRPAKEDVEAAPeETRALYREYRNLKQAVSQADDGHRVQ---KQSLAKAAEEEQepscwg 80
Cdd:pfam11719    1 ISQLKAEIKEWERAFAAKNGRKPSKDDIKKNP-EIAKKYKLYSKLKKGESIKTKTPSKPvklEARPKKRKHEST------ 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538    81 shlNRAATQNTQSIPKQSplssiqdygKRLKANLkntlqgGPTLSRklqhQKRSLSIVPTSRPPGPRTESPcPEQANDAL 160
Cdd:pfam11719   74 ---NKSPEKNSQSTPRKS---------KNIKSEL------GPTPQA----NGKVLSLFDLLSTPPKSSPLK-SKEVKTDV 130
                          170
                   ....*....|
gi 564360538   161 PQVPVPQPRQ 170
Cdd:pfam11719  131 SGTAIFTPSK 140
ZnF_C2HC smart00343
zinc finger;
394-408 2.40e-03

zinc finger;


:

Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 36.27  E-value: 2.40e-03
                            10
                    ....*....|....*
gi 564360538    394 TCFRCGQFGHWASQC 408
Cdd:smart00343    1 KCYNCGKEGHIARDC 15
 
Name Accession Description Interval E-value
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
485-850 9.37e-115

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 366.77  E-value: 9.37e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  485 AEVFQVLEQL-GHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLyakrSPCLTLVVSPLLSLMDDQVSDLP 563
Cdd:COG0514     3 DDALEVLKRVfGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALL----LPGLTLVVSPLIALMKDQVDALR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  564 SC-LKAACLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVGcgakgPANLPPAAQLPPVAFAcIDEVHCLSQWSHNFRP 642
Cdd:COG0514    79 AAgIRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLN-----PRFLELLRRLKISLFA-IDEAHCISQWGHDFRP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  643 CYLRVcKVLREHMGVRCFLGLTATATRSTARDVAQHLGIAEELEVSGSASIPaNLHLSVS--MDRDSDQALVTLLQGdrf 720
Cdd:COG0514   153 DYRRL-GELRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRP-NLRLEVVpkPPDDKLAQLLDFLKE--- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  721 RTLDSIIIYCARRKDTERVAALLRTclstvrdskpRGRGpetlAEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMG 800
Cdd:COG0514   228 HPGGSGIVYCLSRKKVEELAEWLRE----------AGIR----AAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMG 293
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 564360538  801 LDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHPQGEDLWE 850
Cdd:COG0514   294 IDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQR 343
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
488-690 3.30e-99

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: 313.42  E-value: 3.30e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  488 FQVLEQL-GHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLYAKRSPCLTLVVSPLLSLMDDQVSDLPSCL 566
Cdd:cd18018     1 LKLLRRVfGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRRRGPGLTLVVSPLIALMKDQVDALPRAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  567 KAACLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVgcgakGPANLPPAAQLPPVAFACIDEVHCLSQWSHNFRPCYLR 646
Cdd:cd18018    81 KAAALNSSLTREERRRILEKLRAGEVKILYVSPERLV-----NESFRELLRQTPPISLLVVDEAHCISEWSHNFRPDYLR 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 564360538  647 VCKVLREHMGVRCFLGLTATATRSTARDVAQHLGIAEELEVSGS 690
Cdd:cd18018   156 LCRVLRELLGAPPVLALTATATKRVVEDIASHLGIPESGVVRGP 199
recQ_fam TIGR00614
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ...
495-843 1.67e-88

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: 294.76  E-value: 1.67e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538   495 GHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLyakrSPCLTLVVSPLLSLMDDQVSDLP-SCLKAACLHS 573
Cdd:TIGR00614    8 GLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALY----SDGITLVISPLISLMEDQVLQLQaLGIPATFLNS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538   574 GMTKKQRESVLKKVRAAQVHVLIVSPEALvgCGAKGPANLPPAAQLPpvAFACIDEVHCLSQWSHNFRPCYlRVCKVLRE 653
Cdd:TIGR00614   84 AQTKEQQLNVLTDLKDGKIKLLYVTPEKI--SASNRLLQTLEERKGI--TLIAVDEAHCISQWGHDFRPDY-KALGSLKQ 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538   654 HMGVRCFLGLTATATRSTARDVAQHLGIAEELEVSGSASIPaNLHLSVsMDRDSD--QALVTLLQGdRFRTlDSIIIYCA 731
Cdd:TIGR00614  159 KFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRP-NLYYEV-RRKTPKilEDLLRFIRK-EFEG-KSGIIYCP 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538   732 RRKDTERVAALLRTC-LStvrdskprgrgpetlAEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVL 810
Cdd:TIGR00614  235 SRKKVEQVAAELQKLgLA---------------AGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVI 299
                          330       340       350
                   ....*....|....*....|....*....|...
gi 564360538   811 HLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHP 843
Cdd:TIGR00614  300 HYSLPKSMESYYQESGRAGRDGLPSECHLFYAP 332
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
479-843 9.29e-79

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 271.97  E-value: 9.29e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  479 QVADTPAEVFQVL-EQLGHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLYakrsPCLTLVVSPLLSLMDD 557
Cdd:PRK11057    5 EVLNLESLAKQVLqETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVL----DGLTLVVSPLISLMKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  558 QVSDL-PSCLKAACLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVGCGAkgpanLPPAAQLPPVAFAcIDEVHCLSQW 636
Cdd:PRK11057   81 QVDQLlANGVAAACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNF-----LEHLAHWNPALLA-VDEAHCISQW 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  637 SHNFRPCYlRVCKVLREHMGVRCFLGLTATATRSTARDVAQHLGIAEELEVSGSASIPANLHLSVSMDRDSDQaLVTLLQ 716
Cdd:PRK11057  155 GHDFRPEY-AALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQ-LMRYVQ 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  717 GDRFRtldSIIIYCARRKDTERVAALLRtclstvrdskprGRGPEtlAEAYHAGMCSQERKRVQQAFMQGHLRMVVATVA 796
Cdd:PRK11057  233 EQRGK---SGIIYCNSRAKVEDTAARLQ------------SRGIS--AAAYHAGLDNDVRADVQEAFQRDDLQIVVATVA 295
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 564360538  797 FGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHP 843
Cdd:PRK11057  296 FGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDP 342
DpdF NF041063
protein DpdF;
494-844 1.90e-34

protein DpdF;


Pssm-ID: 468990 [Multi-domain]  Cd Length: 813  Bit Score: 142.74  E-value: 1.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  494 LGHHTFR-PGQERAVMRILS---GiSTLLV-LPTGAGKSLCYQLPALLYAKRSPcLTLVVSPLLSLMDDQVSDLPSCLKA 568
Cdd:NF041063  135 LGFTHYRsPGQREAVRAALLappG-STLIVnLPTGSGKSLVAQAPALLASRQGG-LTLVVVPTVALAIDQERRARELLRR 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  569 A--------CLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVGcgakgpANLPP---AAQLPPVAFACIDEVHCLSQWS 637
Cdd:NF041063  213 AgpdlggplAWHGGLSAEERAAIRQRIRDGTQRILFTSPESLTG------SLRPAlfdAAEAGLLRYLVVDEAHLVDQWG 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  638 HNFRPCY----------LRVCKvlrEHMGVRCFLgLTATATRSTaRDVAQHL-GIAEELE-VSGSasipanlHL----SV 701
Cdd:NF041063  287 DGFRPEFqllaglrrslLRLAP---SGRPFRTLL-LSATLTEST-LDTLETLfGPPGPFIvVSAV-------QLrpepAY 354
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  702 SMDRDSDQAlvtllqgDRFRT-LDSI-------IIYCARRKDTERVAALLRtclstvrdSKPRGRgpetlAEAYHAGMCS 773
Cdd:NF041063  355 WVAKCDSEE-------ERRERvLEALrhlprplILYVTKVEDAEAWLQRLR--------AAGFRR-----VALFHGDTPD 414
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564360538  774 QERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHPQ 844
Cdd:NF041063  415 AERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPD 485
DEXDc smart00487
DEAD-like helicases superfamily;
491-694 5.76e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 103.73  E-value: 5.76e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538    491 LEQLGHHTFRPGQERAVMRILSGI-STLLVLPTGAGKSLCYQLPALLYAKRSP-CLTLVVSPLLSLMDDQVSDL-----P 563
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRGKgGRVLVLVPTRELAEQWAEELkklgpS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538    564 SCLKAACLHSGMTKKQResvLKKVRAAQVHVLIVSPEALVGCGAKGPANlppaaqLPPVAFACIDEVHCLSQWshNFRPC 643
Cdd:smart00487   81 LGLKVVGLYGGDSKREQ---LRKLESGKTDILVTTPGRLLDLLENDKLS------LSNVDLVILDEAHRLLDG--GFGDQ 149
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|.
gi 564360538    644 YLRVCKVLREHmgvRCFLGLTATATRSTARDVAQHLGIAEELEVSGSASIP 694
Cdd:smart00487  150 LEKLLKLLPKN---VQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPLEP 197
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
500-673 1.60e-24

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: 101.17  E-value: 1.60e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538   500 RPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPAL--LYAKRSPCLTLVVSPLLSLMDDQVSDL-----PSCLKAACLH 572
Cdd:pfam00270    1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALeaLDKLDNGPQALVLAPTRELAEQIYEELkklgkGLGLKVASLL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538   573 SGMTKKQRESVLKKvraaqVHVLIVSPEALVgcgakgpANLPPAAQLPPVAFACIDEVHCLSQWShnFRPCYLRVCKVLR 652
Cdd:pfam00270   81 GGDSRKEQLEKLKG-----PDILVGTPGRLL-------DLLQERKLLKNLKLLVLDEAHRLLDMG--FGPDLEEILRRLP 146
                          170       180
                   ....*....|....*....|.
gi 564360538   653 EHmgvRCFLGLTATATRSTAR 673
Cdd:pfam00270  147 KK---RQILLLSATLPRNLED 164
RecQL4_SLD2_NTD cd22289
N-terminal homeodomain-like domain of metazoan RecQ protein-like 4 (RecQL4), fungal DNA ...
2-50 5.19e-19

N-terminal homeodomain-like domain of metazoan RecQ protein-like 4 (RecQL4), fungal DNA replication regulator SLD2 and similar proteins; RecQL4, also called ATP-dependent DNA helicase Q4, or DNA helicase, RecQ-like type 4 (RecQ4), or RTS, is a DNA-dependent ATPase that may modulate chromosome segregation. This family also includes fungal DNA replication regulator SLD2, also known as DNA replication and checkpoint protein 1 (DRC1), which functions with DPB11 to control DNA replication and the S-phase checkpoint. It is also required for the proper activation of RAD53 in response to DNA damage and replication blocks. This model corresponds to the N-terminal domain of RecQL4 and SLD2, which is a homeodomain-like DNA interaction motif.


Pssm-ID: 412085  Cd Length: 49  Bit Score: 81.52  E-value: 5.19e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 564360538    2 ERLATVRARLQDWERAFVRLHGRRPAKEDVEAAPEETRALYREYRNLKQ 50
Cdd:cd22289     1 ERLQELKIALKTWERAFAKKHGRKPTKDDIKAAPEEIKDLYKEYAKLKK 49
Drc1-Sld2 pfam11719
DNA replication and checkpoint protein; Genome duplication is precisely regulated by ...
4-170 6.67e-10

DNA replication and checkpoint protein; Genome duplication is precisely regulated by cyclin-dependent kinases CDKs, which bring about the onset of S phase by activating replication origins and then prevent re-licensing of origins until mitosis is completed. The optimum sequence motif for CDK phosphorylation is S/T-P-K/R-K/R, and Drc1-Sld2 is found to have at least 11 potential phosphorylation sites. Drc1 is required for DNA synthesis and S-M replication checkpoint control. Drc1 associates with Cdc2 and is phosphorylated at the onset of S phase when Cdc2 is activated. Thus Cdc2 promotes DNA replication by phosphorylating Drc1 and regulating its association with Cut5. Sld2 and Sld3 represent the minimal set of S-CDK substrates required for DNA replication.


Pssm-ID: 371692 [Multi-domain]  Cd Length: 391  Bit Score: 62.54  E-value: 6.67e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538     4 LATVRARLQDWERAFVRLHGRRPAKEDVEAAPeETRALYREYRNLKQAVSQADDGHRVQ---KQSLAKAAEEEQepscwg 80
Cdd:pfam11719    1 ISQLKAEIKEWERAFAAKNGRKPSKDDIKKNP-EIAKKYKLYSKLKKGESIKTKTPSKPvklEARPKKRKHEST------ 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538    81 shlNRAATQNTQSIPKQSplssiqdygKRLKANLkntlqgGPTLSRklqhQKRSLSIVPTSRPPGPRTESPcPEQANDAL 160
Cdd:pfam11719   74 ---NKSPEKNSQSTPRKS---------KNIKSEL------GPTPQA----NGKVLSLFDLLSTPPKSSPLK-SKEVKTDV 130
                          170
                   ....*....|
gi 564360538   161 PQVPVPQPRQ 170
Cdd:pfam11719  131 SGTAIFTPSK 140
ZnF_C2HC smart00343
zinc finger;
394-408 2.40e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 36.27  E-value: 2.40e-03
                            10
                    ....*....|....*
gi 564360538    394 TCFRCGQFGHWASQC 408
Cdd:smart00343    1 KCYNCGKEGHIARDC 15
 
Name Accession Description Interval E-value
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
485-850 9.37e-115

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 366.77  E-value: 9.37e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  485 AEVFQVLEQL-GHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLyakrSPCLTLVVSPLLSLMDDQVSDLP 563
Cdd:COG0514     3 DDALEVLKRVfGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALL----LPGLTLVVSPLIALMKDQVDALR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  564 SC-LKAACLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVGcgakgPANLPPAAQLPPVAFAcIDEVHCLSQWSHNFRP 642
Cdd:COG0514    79 AAgIRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLN-----PRFLELLRRLKISLFA-IDEAHCISQWGHDFRP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  643 CYLRVcKVLREHMGVRCFLGLTATATRSTARDVAQHLGIAEELEVSGSASIPaNLHLSVS--MDRDSDQALVTLLQGdrf 720
Cdd:COG0514   153 DYRRL-GELRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRP-NLRLEVVpkPPDDKLAQLLDFLKE--- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  721 RTLDSIIIYCARRKDTERVAALLRTclstvrdskpRGRGpetlAEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMG 800
Cdd:COG0514   228 HPGGSGIVYCLSRKKVEELAEWLRE----------AGIR----AAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMG 293
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 564360538  801 LDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHPQGEDLWE 850
Cdd:COG0514   294 IDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQR 343
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
488-690 3.30e-99

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: 313.42  E-value: 3.30e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  488 FQVLEQL-GHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLYAKRSPCLTLVVSPLLSLMDDQVSDLPSCL 566
Cdd:cd18018     1 LKLLRRVfGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRRRGPGLTLVVSPLIALMKDQVDALPRAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  567 KAACLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVgcgakGPANLPPAAQLPPVAFACIDEVHCLSQWSHNFRPCYLR 646
Cdd:cd18018    81 KAAALNSSLTREERRRILEKLRAGEVKILYVSPERLV-----NESFRELLRQTPPISLLVVDEAHCISEWSHNFRPDYLR 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 564360538  647 VCKVLREHMGVRCFLGLTATATRSTARDVAQHLGIAEELEVSGS 690
Cdd:cd18018   156 LCRVLRELLGAPPVLALTATATKRVVEDIASHLGIPESGVVRGP 199
recQ_fam TIGR00614
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ...
495-843 1.67e-88

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: 294.76  E-value: 1.67e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538   495 GHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLyakrSPCLTLVVSPLLSLMDDQVSDLP-SCLKAACLHS 573
Cdd:TIGR00614    8 GLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALY----SDGITLVISPLISLMEDQVLQLQaLGIPATFLNS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538   574 GMTKKQRESVLKKVRAAQVHVLIVSPEALvgCGAKGPANLPPAAQLPpvAFACIDEVHCLSQWSHNFRPCYlRVCKVLRE 653
Cdd:TIGR00614   84 AQTKEQQLNVLTDLKDGKIKLLYVTPEKI--SASNRLLQTLEERKGI--TLIAVDEAHCISQWGHDFRPDY-KALGSLKQ 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538   654 HMGVRCFLGLTATATRSTARDVAQHLGIAEELEVSGSASIPaNLHLSVsMDRDSD--QALVTLLQGdRFRTlDSIIIYCA 731
Cdd:TIGR00614  159 KFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRP-NLYYEV-RRKTPKilEDLLRFIRK-EFEG-KSGIIYCP 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538   732 RRKDTERVAALLRTC-LStvrdskprgrgpetlAEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVL 810
Cdd:TIGR00614  235 SRKKVEQVAAELQKLgLA---------------AGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVI 299
                          330       340       350
                   ....*....|....*....|....*....|...
gi 564360538   811 HLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHP 843
Cdd:TIGR00614  300 HYSLPKSMESYYQESGRAGRDGLPSECHLFYAP 332
recQ TIGR01389
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ...
488-844 4.58e-88

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: 297.37  E-value: 4.58e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538   488 FQVL-EQLGHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLYakrsPCLTLVVSPLLSLMDDQVSDLPSC- 565
Cdd:TIGR01389    2 QQVLkRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLL----KGLTVVISPLISLMKDQVDQLRAAg 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538   566 LKAACLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVGcgakgPANLPPAAQLPPVAFAcIDEVHCLSQWSHNFRPCYL 645
Cdd:TIGR01389   78 VAAAYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQ-----DYFLNMLQRIPIALVA-VDEAHCVSQWGHDFRPEYQ 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538   646 RVCkVLREHMGVRCFLGLTATATRSTARDVAQHLGIAEELEVSGSASIPaNLHLSVSMDRDSDQALVTLLQGDRFRtldS 725
Cdd:TIGR01389  152 RLG-SLAERFPQVPRIALTATADAETRQDIRELLRLADANEFITSFDRP-NLRFSVVKKNNKQKFLLDYLKKHRGQ---S 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538   726 IIIYCARRKDTERVAALLRTclstvrdskprgRGPETLAeaYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPD 805
Cdd:TIGR01389  227 GIIYASSRKKVEELAERLES------------QGISALA--YHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPN 292
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 564360538   806 VRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHPQ 844
Cdd:TIGR01389  293 VRFVIHYDMPGNLESYYQEAGRAGRDGLPAEAILLYSPA 331
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
479-843 9.29e-79

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 271.97  E-value: 9.29e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  479 QVADTPAEVFQVL-EQLGHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLYakrsPCLTLVVSPLLSLMDD 557
Cdd:PRK11057    5 EVLNLESLAKQVLqETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVL----DGLTLVVSPLISLMKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  558 QVSDL-PSCLKAACLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVGCGAkgpanLPPAAQLPPVAFAcIDEVHCLSQW 636
Cdd:PRK11057   81 QVDQLlANGVAAACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNF-----LEHLAHWNPALLA-VDEAHCISQW 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  637 SHNFRPCYlRVCKVLREHMGVRCFLGLTATATRSTARDVAQHLGIAEELEVSGSASIPANLHLSVSMDRDSDQaLVTLLQ 716
Cdd:PRK11057  155 GHDFRPEY-AALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQ-LMRYVQ 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  717 GDRFRtldSIIIYCARRKDTERVAALLRtclstvrdskprGRGPEtlAEAYHAGMCSQERKRVQQAFMQGHLRMVVATVA 796
Cdd:PRK11057  233 EQRGK---SGIIYCNSRAKVEDTAARLQ------------SRGIS--AAAYHAGLDNDVRADVQEAFQRDDLQIVVATVA 295
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 564360538  797 FGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHP 843
Cdd:PRK11057  296 FGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDP 342
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
492-690 5.50e-66

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: 221.25  E-value: 5.50e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  492 EQLGHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLyakrSPCLTLVVSPLLSLMDDQVSDLPS-CLKAAC 570
Cdd:cd17920     6 EVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALL----LDGVTLVVSPLISLMQDQVDRLQQlGIRAAA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  571 LHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVgcgakGPANLPPAAQLP---PVAFACIDEVHCLSQWSHNFRPCYLRV 647
Cdd:cd17920    82 LNSTLSPEEKREVLLRIKNGQYKLLYVTPERLL-----SPDFLELLQRLPerkRLALIVVDEAHCVSQWGHDFRPDYLRL 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 564360538  648 CKVLREHMGVrCFLGLTATATRSTARDVAQHLGIAEELEVSGS 690
Cdd:cd17920   157 GRLRRALPGV-PILALTATATPEVREDILKRLGLRNPVIFRAS 198
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
696-840 7.35e-56

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: 189.73  E-value: 7.35e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  696 NLHLSVSMDRDSDQALVTLLQGDRFRTLDSIIIYCARRKDTERVAALLRTCLSTvrdskprgrgpetlAEAYHAGMCSQE 775
Cdd:cd18794     3 NLFYSVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGIS--------------AAAYHAGLEPSD 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564360538  776 RKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLF 840
Cdd:cd18794    69 RRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
495-840 3.16e-52

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 200.89  E-value: 3.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  495 GHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLyakrSPCLTLVVSPLLSLMDDQVSD-LPSCLKAACLHS 573
Cdd:PLN03137  457 GNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALI----CPGITLVISPLVSLIQDQIMNlLQANIPAASLSA 532
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  574 GMTKKQRESVLKKVRA--AQVHVLIVSPEALvgcgAKGPA---NLPPAAQLPPVAFACIDEVHCLSQWSHNFRPCYlRVC 648
Cdd:PLN03137  533 GMEWAEQLEILQELSSeySKYKLLYVTPEKV----AKSDSllrHLENLNSRGLLARFVIDEAHCVSQWGHDFRPDY-QGL 607
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  649 KVLREHMGVRCFLGLTATATRSTARDVAQHLGIAEELEVSGSASIPaNLHLSVSmdRDSDQALVTLLQGDRFRTLDSI-I 727
Cdd:PLN03137  608 GILKQKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRP-NLWYSVV--PKTKKCLEDIDKFIKENHFDECgI 684
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  728 IYCARRKDTERVAALLRTClstvrdskprgrGPEtlAEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVR 807
Cdd:PLN03137  685 IYCLSRMDCEKVAERLQEF------------GHK--AAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVR 750
                         330       340       350
                  ....*....|....*....|....*....|...
gi 564360538  808 AVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLF 840
Cdd:PLN03137  751 FVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLY 783
DEXHc_RecQ1 cd18015
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ...
478-690 5.19e-38

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: 141.73  E-value: 5.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  478 GQVADTPAEVFQVleqlghHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLyakrSPCLTLVVSPLLSLMDD 557
Cdd:cd18015     4 GKVKDTLKNVFKL------EKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALC----SDGFTLVVSPLISLMED 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  558 QVSDLPSC-LKAACLHSGMTKKQRESVLKKVR--AAQVHVLIVSPEALvgcgAKGP---ANLPPAAQLPPVAFACIDEVH 631
Cdd:cd18015    74 QLMALKKLgISATMLNASSSKEHVKWVHAALTdkNSELKLLYVTPEKI----AKSKrfmSKLEKAYNAGRLARIAIDEVH 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564360538  632 CLSQWSHNFRPCYlrvckvlrEHMGV--RCF-----LGLTATATRSTARDVAQHLGIAEELEVSGS 690
Cdd:cd18015   150 CCSQWGHDFRPDY--------KKLGIlkRQFpnvpiLGLTATATSKVLKDVQKILCIQKCLTFTAS 207
DpdF NF041063
protein DpdF;
494-844 1.90e-34

protein DpdF;


Pssm-ID: 468990 [Multi-domain]  Cd Length: 813  Bit Score: 142.74  E-value: 1.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  494 LGHHTFR-PGQERAVMRILS---GiSTLLV-LPTGAGKSLCYQLPALLYAKRSPcLTLVVSPLLSLMDDQVSDLPSCLKA 568
Cdd:NF041063  135 LGFTHYRsPGQREAVRAALLappG-STLIVnLPTGSGKSLVAQAPALLASRQGG-LTLVVVPTVALAIDQERRARELLRR 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  569 A--------CLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVGcgakgpANLPP---AAQLPPVAFACIDEVHCLSQWS 637
Cdd:NF041063  213 AgpdlggplAWHGGLSAEERAAIRQRIRDGTQRILFTSPESLTG------SLRPAlfdAAEAGLLRYLVVDEAHLVDQWG 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  638 HNFRPCY----------LRVCKvlrEHMGVRCFLgLTATATRSTaRDVAQHL-GIAEELE-VSGSasipanlHL----SV 701
Cdd:NF041063  287 DGFRPEFqllaglrrslLRLAP---SGRPFRTLL-LSATLTEST-LDTLETLfGPPGPFIvVSAV-------QLrpepAY 354
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  702 SMDRDSDQAlvtllqgDRFRT-LDSI-------IIYCARRKDTERVAALLRtclstvrdSKPRGRgpetlAEAYHAGMCS 773
Cdd:NF041063  355 WVAKCDSEE-------ERRERvLEALrhlprplILYVTKVEDAEAWLQRLR--------AAGFRR-----VALFHGDTPD 414
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564360538  774 QERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHPQ 844
Cdd:NF041063  415 AERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPD 485
DEXHc_RecQ5 cd18014
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ...
495-681 4.27e-32

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: 124.51  E-value: 4.27e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  495 GHHTFR-PGQERAVMRILSGISTLLV-LPTGAGKSLCYQLPALLYAKrspcLTLVVSPLLSLMDDQVSDLPSC-LKAACL 571
Cdd:cd18014     9 GHSDFKsPLQEKATMAVVKGNKDVFVcMPTGAGKSLCYQLPALLAKG----ITIVISPLIALIQDQVDHLKTLkIRVDSL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  572 HSGMTKKQRESVLKKVRAA--QVHVLIVSPEAlvgcgAKGPANLPPAAQLPP---VAFACIDEVHCLSQWSHNFRPCYLR 646
Cdd:cd18014    85 NSKLSAQERKRIIADLESEkpQTKFLYITPEM-----AATSSFQPLLSSLVSrnlLSYLVVDEAHCVSQWGHDFRPDYLR 159
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 564360538  647 VCKVLREHMGVRCfLGLTATATRSTARDVAQHLGI 681
Cdd:cd18014   160 LGALRSRYGHVPW-VALTATATPQVQEDIFAQLRL 193
DEXHc_RecQ3 cd18017
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ...
492-681 4.48e-32

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: 124.12  E-value: 4.48e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  492 EQLGHHTFRPGQERAVMRIL-SGISTLLVLPTGAGKSLCYQLPALLYAKrspcLTLVVSPLLSLMDDQVSDLPSCLKAAC 570
Cdd:cd18017     6 EYFGHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVLLNS----LTLVISPLISLMEDQVLQLVMSNIPAC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  571 LhsgMTKKQRESVLKKVRAAQVHVLIVSPEAlvgcGAKGPANLPP-AAQLPPVAfacIDEVHCLSQWSHNFRPCYlRVCK 649
Cdd:cd18017    82 F---LGSAQSQNVLDDIKMGKIRVIYVTPEF----VSKGLELLQQlRNGITLIA---IDEAHCVSQWGHDFRSSY-RHLG 150
                         170       180       190
                  ....*....|....*....|....*....|..
gi 564360538  650 VLREHMGVRCFLGLTATATRSTARDVAQHLGI 681
Cdd:cd18017   151 SIRNRLPNVPIVALTATATPSVRDDIIKNLNL 182
DEXHc_RecQ2_BLM cd18016
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ...
493-681 3.90e-28

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: 113.00  E-value: 3.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  493 QLGHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLyakrSPCLTLVVSPLLSLMDDQVSDLPSC-LKAACL 571
Cdd:cd18016    12 KFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACV----SPGVTVVISPLRSLIVDQVQKLTSLdIPATYL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  572 HSGMTKKQRESVLKKVRAAQ--VHVLIVSPEALVGCGAKGPA--NLPPAAQLppvAFACIDEVHCLSQWSHNFRPCYLRV 647
Cdd:cd18016    88 TGDKTDAEATKIYLQLSKKDpiIKLLYVTPEKISASNRLISTleNLYERKLL---ARFVIDEAHCVSQWGHDFRPDYKRL 164
                         170       180       190
                  ....*....|....*....|....*....|....
gi 564360538  648 cKVLREHMGVRCFLGLTATATRSTARDVAQHLGI 681
Cdd:cd18016   165 -NMLRQKFPSVPMMALTATATPRVQKDILNQLKM 197
DEXDc smart00487
DEAD-like helicases superfamily;
491-694 5.76e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 103.73  E-value: 5.76e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538    491 LEQLGHHTFRPGQERAVMRILSGI-STLLVLPTGAGKSLCYQLPALLYAKRSP-CLTLVVSPLLSLMDDQVSDL-----P 563
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRGKgGRVLVLVPTRELAEQWAEELkklgpS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538    564 SCLKAACLHSGMTKKQResvLKKVRAAQVHVLIVSPEALVGCGAKGPANlppaaqLPPVAFACIDEVHCLSQWshNFRPC 643
Cdd:smart00487   81 LGLKVVGLYGGDSKREQ---LRKLESGKTDILVTTPGRLLDLLENDKLS------LSNVDLVILDEAHRLLDG--GFGDQ 149
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|.
gi 564360538    644 YLRVCKVLREHmgvRCFLGLTATATRSTARDVAQHLGIAEELEVSGSASIP 694
Cdd:smart00487  150 LEKLLKLLPKN---VQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPLEP 197
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
500-673 1.60e-24

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: 101.17  E-value: 1.60e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538   500 RPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPAL--LYAKRSPCLTLVVSPLLSLMDDQVSDL-----PSCLKAACLH 572
Cdd:pfam00270    1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALeaLDKLDNGPQALVLAPTRELAEQIYEELkklgkGLGLKVASLL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538   573 SGMTKKQRESVLKKvraaqVHVLIVSPEALVgcgakgpANLPPAAQLPPVAFACIDEVHCLSQWShnFRPCYLRVCKVLR 652
Cdd:pfam00270   81 GGDSRKEQLEKLKG-----PDILVGTPGRLL-------DLLQERKLLKNLKLLVLDEAHRLLDMG--FGPDLEEILRRLP 146
                          170       180
                   ....*....|....*....|.
gi 564360538   653 EHmgvRCFLGLTATATRSTAR 673
Cdd:pfam00270  147 KK---RQILLLSATLPRNLED 164
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
474-835 3.81e-20

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: 96.83  E-value: 3.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  474 PGPLGQVADTPA----EVFQVLEQLGHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPAL--LYAKRSPClTLV 547
Cdd:COG1205    28 PAREARYAPWPDwlppELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLeaLLEDPGAT-ALY 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  548 VSPLLSLMDDQVS-------DLPSCLKAACLHSGMTKKQRESVLKkvraaQVHVLIVSPEAL-VGcgakgpanLPPA--- 616
Cdd:COG1205   107 LYPTKALARDQLRrlrelaeALGLGVRVATYDGDTPPEERRWIRE-----HPDIVLTNPDMLhYG--------LLPHhtr 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  617 -AQLppvaFAC-----IDEVHCL-----SQWSHNFRPcYLRVCkvlrEHMGVRC-FLGLTAT-------ATRSTARDVaq 677
Cdd:COG1205   174 wARF----FRNlryvvIDEAHTYrgvfgSHVANVLRR-LRRIC----RHYGSDPqFILASATignpaehAERLTGRPV-- 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  678 hlgiaEELEVSGSAS------------IPANLHLSVSmdRDSDQALVTLLQGDRfRTldsiIIYCARRKDTERVAallrt 745
Cdd:COG1205   243 -----TVVDEDGSPRgertfvlwnpplVDDGIRRSAL--AEAARLLADLVREGL-RT----LVFTRSRRGAELLA----- 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  746 clSTVRDSKPRGRGPETLAeAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAI 825
Cdd:COG1205   306 --RYARRALREPDLADRVA-AYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQA 382
                         410
                  ....*....|
gi 564360538  826 GRAGRDGKPA 835
Cdd:COG1205   383 GRAGRRGQDS 392
HELICc smart00490
helicase superfamily c-terminal domain;
764-832 7.73e-20

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 84.96  E-value: 7.73e-20
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564360538    764 AEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDG 832
Cdd:smart00490   14 VARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
RecQL4_SLD2_NTD cd22289
N-terminal homeodomain-like domain of metazoan RecQ protein-like 4 (RecQL4), fungal DNA ...
2-50 5.19e-19

N-terminal homeodomain-like domain of metazoan RecQ protein-like 4 (RecQL4), fungal DNA replication regulator SLD2 and similar proteins; RecQL4, also called ATP-dependent DNA helicase Q4, or DNA helicase, RecQ-like type 4 (RecQ4), or RTS, is a DNA-dependent ATPase that may modulate chromosome segregation. This family also includes fungal DNA replication regulator SLD2, also known as DNA replication and checkpoint protein 1 (DRC1), which functions with DPB11 to control DNA replication and the S-phase checkpoint. It is also required for the proper activation of RAD53 in response to DNA damage and replication blocks. This model corresponds to the N-terminal domain of RecQL4 and SLD2, which is a homeodomain-like DNA interaction motif.


Pssm-ID: 412085  Cd Length: 49  Bit Score: 81.52  E-value: 5.19e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 564360538    2 ERLATVRARLQDWERAFVRLHGRRPAKEDVEAAPEETRALYREYRNLKQ 50
Cdd:cd22289     1 ERLQELKIALKTWERAFAKKHGRKPTKDDIKAAPEEIKDLYKEYAKLKK 49
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
727-835 4.25e-17

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: 79.22  E-value: 4.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  727 IIYCARRKDTERVAALLRTCLstvrdsKPRGRGPETLAeAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPDV 806
Cdd:cd18797    39 IVFCRSRKLAELLLRYLKARL------VEEGPLASKVA-SYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGL 111
                          90       100
                  ....*....|....*....|....*....
gi 564360538  807 RAVLHLGLPPSFESYVQAIGRAGRDGKPA 835
Cdd:cd18797   112 DAVVLAGYPGSLASLWQQAGRAGRRGKDS 140
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
709-832 3.76e-16

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: 75.32  E-value: 3.76e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538   709 QALVTLLQGDRFrtlDSIIIYCARRKDTERVAALLRTCLSTVRdskprgrgpetlaeaYHAGMCSQERKRVQQAFMQGHL 788
Cdd:pfam00271    4 EALLELLKKERG---GKVLIFSQTKKTLEAELLLEKEGIKVAR---------------LHGDLSQEEREEILEDFRKGKI 65
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 564360538   789 RMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDG 832
Cdd:pfam00271   66 DVLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
500-840 2.03e-14

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 77.76  E-value: 2.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  500 RPGQERAVMRILSGIST-----LLVLPTGAGKSLCyqlpALLYAKR--SPCLTLVVSPLLSLMDDQVSDLPSCLKAACLH 572
Cdd:COG1061    82 RPYQQEALEALLAALERgggrgLVVAPTGTGKTVL----ALALAAEllRGKRVLVLVPRRELLEQWAEELRRFLGDPLAG 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  573 SGmtKKQRESvlkkvraaqvHVLIVSPEALvgcgakgpANLPPAAQLPP-VAFACIDEVHclsqwsHNFRPCYLRVckvl 651
Cdd:COG1061   158 GG--KKDSDA----------PITVATYQSL--------ARRAHLDELGDrFGLVIIDEAH------HAGAPSYRRI---- 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  652 REHMGVRCFLGLTATATRSTARDVAQHL--GIA-----EELEVSGsasIPANLH-LSVSMDRDSDQALVTLLQGDRFRTL 723
Cdd:COG1061   208 LEAFPAAYRLGLTATPFRSDGREILLFLfdGIVyeyslKEAIEDG---YLAPPEyYGIRVDLTDERAEYDALSERLREAL 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  724 DS---------------------IIIYCARRKDTERVAALLRTclstvrdskprgRGPEtlAEAYHAGMCSQERKRVQQA 782
Cdd:COG1061   285 AAdaerkdkilrellrehpddrkTLVFCSSVDHAEALAELLNE------------AGIR--AAVVTGDTPKKEREEILEA 350
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564360538  783 FMQGHLRMVVATVAFGMGLDRPDVRAVLHLGlppSFES---YVQAIGRA--GRDGKPaHCHLF 840
Cdd:COG1061   351 FRDGELRILVTVDVLNEGVDVPRLDVAILLR---PTGSpreFIQRLGRGlrPAPGKE-DALVY 409
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
705-841 2.20e-14

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 71.00  E-value: 2.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  705 RDSDQALVTLLQGDRFRTLDSIIIYCARRKDTERVAALLRTClstvrdskprgrgpETLAEAYHAGMCSQERKRVQQAFM 784
Cdd:cd18787     9 EEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEEL--------------GIKVAALHGDLSQEERERALKKFR 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 564360538  785 QGHLRMVVAT-VAfGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFL 841
Cdd:cd18787    75 SGKVRVLVATdVA-ARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
484-833 2.75e-14

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 76.34  E-value: 2.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  484 PAEVFQVLEQLGHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPA---LLYAKRSPCLTLVVSPL--LSLmddQ 558
Cdd:COG0513    10 SPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLlqrLDPSRPRAPQALILAPTreLAL---Q 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  559 VSD--------LPscLKAACLHSGMT-KKQRESvLKKvraaQVHVLIVSP---EALVGcgaKGPANLppaaqlppvafac 626
Cdd:COG0513    87 VAEelrklakyLG--LRVATVYGGVSiGRQIRA-LKR----GVDIVVATPgrlLDLIE---RGALDL------------- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  627 iDEVHCLsqwshnfrpcylrvckVLRE-----HMG----VRCFLGLT----------ATATRSTARDVAQHLGIAEELEV 687
Cdd:COG0513   144 -SGVETL----------------VLDEadrmlDMGfiedIERILKLLpkerqtllfsATMPPEIRKLAKRYLKNPVRIEV 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  688 SGSASIPANLHLSVSM--DRDSDQALVTLLQGDRFrtlDSIIIYCARRKDTERVAALLRtclstvrdskprGRGPEtlAE 765
Cdd:COG0513   207 APENATAETIEQRYYLvdKRDKLELLRRLLRDEDP---ERAIVFCNTKRGADRLAEKLQ------------KRGIS--AA 269
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564360538  766 AYHAGMcSQ-ERKRVQQAFMQGHLRMVVAT-VAfGMGLDRPDVRAVLHLGLPPSFESYVQAIG---RAGRDGK 833
Cdd:COG0513   270 ALHGDL-SQgQRERALDAFRNGKIRVLVATdVA-ARGIDIDDVSHVINYDLPEDPEDYVHRIGrtgRAGAEGT 340
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
516-666 3.85e-14

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: 70.90  E-value: 3.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  516 TLLVLPTGAGKSLCYQLPALLYAKRSPCLTLVVSPLLSLMDDQVSDL----PSCLKAACLHSGMTKKQREsvlkKVRAAQ 591
Cdd:cd00046     4 VLITAPTGSGKTLAALLAALLLLLKKGKKVLVLVPTKALALQTAERLrelfGPGIRVAVLVGGSSAEERE----KNKLGD 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564360538  592 VHVLIVSPEALVGCgakgpanLPPAAQL--PPVAFACIDEVHCLSQWSHNFRPCYLRVCKVLREHMGVrcfLGLTAT 666
Cdd:cd00046    80 ADIIIATPDMLLNL-------LLREDRLflKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQV---ILLSAT 146
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
479-846 2.43e-12

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 71.08  E-value: 2.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  479 QVADTP-AEVFQVLEQLGHHTFRPGQERAVMR-ILSGISTLLVLPTGAGKSLCYQLpALLYAKRSPCLTLVVSPLLSLMD 556
Cdd:COG1204     2 KVAELPlEKVIEFLKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAEL-AILKALLNGGKALYIVPLRALAS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  557 DQVSDLPSCLKAACLHSGMTKKQRESVLKkvRAAQVHVLIVSPE---ALVGCGAKgpanlppaaQLPPVAFACIDEVH-- 631
Cdd:COG1204    81 EKYREFKRDFEELGIKVGVSTGDYDSDDE--WLGRYDILVATPEkldSLLRNGPS---------WLRDVDLVVVDEAHli 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  632 -----------CLSqwshnfrpcylrvcKVLREHMGVRcFLGLTATA--------------TRSTARDVAQHLGIA--EE 684
Cdd:COG1204   150 ddesrgptlevLLA--------------RLRRLNPEAQ-IVALSATIgnaeeiaewldaelVKSDWRPVPLNEGVLydGV 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  685 LEVSGSASIPANLHLSVSMDrdsdqalvTLLQGDrfrtldSIIIYCARRKDTERVAALLRTCLSTVRDSKPRGR------ 758
Cdd:COG1204   215 LRFDDGSRRSKDPTLALALD--------LLEEGG------QVLVFVSSRRDAESLAKKLADELKRRLTPEEREEleelae 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  759 ---------GP-ETLAE------AYH-AGMCSQERKRVQQAFMQGHLRMVVAT--VAFGMGLdrPdVRAVL-----HLGL 814
Cdd:COG1204   281 ellevseetHTnEKLADclekgvAFHhAGLPSELRRLVEDAFREGLIKVLVATptLAAGVNL--P-ARRVIirdtkRGGM 357
                         410       420       430
                  ....*....|....*....|....*....|....
gi 564360538  815 PP--SFEsYVQAIGRAGRDGKpahchlflHPQGE 846
Cdd:COG1204   358 VPipVLE-FKQMAGRAGRPGY--------DPYGE 382
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
733-835 3.92e-11

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: 62.28  E-value: 3.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  733 RKDTERVAALLRtclstvrdSKPRGRGPETLAEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVLHL 812
Cdd:cd18796    48 RSQAERLAQRLR--------ELCPDRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQI 119
                          90       100
                  ....*....|....*....|...
gi 564360538  813 GLPPSFESYVQAIGRAGRDGKPA 835
Cdd:cd18796   120 GSPKSVARLLQRLGRSGHRPGAA 142
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
791-840 6.02e-10

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: 56.56  E-value: 6.02e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564360538  791 VVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGK-PAHCHLF 840
Cdd:cd18785    26 LVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKdEGEVILF 76
Drc1-Sld2 pfam11719
DNA replication and checkpoint protein; Genome duplication is precisely regulated by ...
4-170 6.67e-10

DNA replication and checkpoint protein; Genome duplication is precisely regulated by cyclin-dependent kinases CDKs, which bring about the onset of S phase by activating replication origins and then prevent re-licensing of origins until mitosis is completed. The optimum sequence motif for CDK phosphorylation is S/T-P-K/R-K/R, and Drc1-Sld2 is found to have at least 11 potential phosphorylation sites. Drc1 is required for DNA synthesis and S-M replication checkpoint control. Drc1 associates with Cdc2 and is phosphorylated at the onset of S phase when Cdc2 is activated. Thus Cdc2 promotes DNA replication by phosphorylating Drc1 and regulating its association with Cut5. Sld2 and Sld3 represent the minimal set of S-CDK substrates required for DNA replication.


Pssm-ID: 371692 [Multi-domain]  Cd Length: 391  Bit Score: 62.54  E-value: 6.67e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538     4 LATVRARLQDWERAFVRLHGRRPAKEDVEAAPeETRALYREYRNLKQAVSQADDGHRVQ---KQSLAKAAEEEQepscwg 80
Cdd:pfam11719    1 ISQLKAEIKEWERAFAAKNGRKPSKDDIKKNP-EIAKKYKLYSKLKKGESIKTKTPSKPvklEARPKKRKHEST------ 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538    81 shlNRAATQNTQSIPKQSplssiqdygKRLKANLkntlqgGPTLSRklqhQKRSLSIVPTSRPPGPRTESPcPEQANDAL 160
Cdd:pfam11719   74 ---NKSPEKNSQSTPRKS---------KNIKSEL------GPTPQA----NGKVLSLFDLLSTPPKSSPLK-SKEVKTDV 130
                          170
                   ....*....|
gi 564360538   161 PQVPVPQPRQ 170
Cdd:pfam11719  131 SGTAIFTPSK 140
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
725-832 7.63e-09

C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350182 [Multi-domain]  Cd Length: 154  Bit Score: 56.02  E-value: 7.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  725 SIIIYCARRKDTERVAALLRtclstvrdskprGRGpetlaeAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRP 804
Cdd:cd18795    45 PVLVFCSSRKECEKTAKDLA------------GIA------FHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLP 106
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 564360538  805 DVRAVLhLGLP----------PSFEsYVQAIGRAGRDG 832
Cdd:cd18795   107 ARTVII-KGTQrydgkgyrelSPLE-YLQMIGRAGRPG 142
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
728-829 9.11e-09

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 59.94  E-value: 9.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  728 IYCARRKDTERVAALLRTCLSTVRDSKPRGRG-PETLAEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPDV 806
Cdd:PRK09751  267 LYAARLQRSPSIAVDAAHFESTSGATSNRVQSsDVFIARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAV 346
                          90       100
                  ....*....|....*....|...
gi 564360538  807 RAVLHLGLPPSFESYVQAIGRAG 829
Cdd:PRK09751  347 DLVIQVATPLSVASGLQRIGRAG 369
PTZ00110 PTZ00110
helicase; Provisional
484-843 3.06e-08

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 57.86  E-value: 3.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  484 PAEVFQVLEQLGHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLYAKRSPCL-------TLVVSPLLSLMD 556
Cdd:PTZ00110  138 PDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLrygdgpiVLVLAPTRELAE 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  557 dQVSD------LPSCLKAACLHSGMTKKQRESVLKKvraaQVHVLIVSPEALVGCGAKGPANLPPaaqlppVAFACIDEV 630
Cdd:PTZ00110  218 -QIREqcnkfgASSKIRNTVAYGGVPKRGQIYALRR----GVEILIACPGRLIDFLESNVTNLRR------VTYLVLDEA 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  631 HclSQWSHNFRPCYLRVCKVLREHmgvRCFLGLTATATR---STARDVAQHLGI---AEELEVSGSASIPANLHLsvsMD 704
Cdd:PTZ00110  287 D--RMLDMGFEPQIRKIVSQIRPD---RQTLMWSATWPKevqSLARDLCKEEPVhvnVGSLDLTACHNIKQEVFV---VE 358
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  705 RDSDQALVTLLQGDRFRTLDSIIIYCARRKDTERVAALLRTclstvrDSKPrgrgpetlAEAYHAGMCSQERKRVQQAFM 784
Cdd:PTZ00110  359 EHEKRGKLKMLLQRIMRDGDKILIFVETKKGADFLTKELRL------DGWP--------ALCIHGDKKQEERTWVLNEFK 424
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564360538  785 QGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHP 843
Cdd:PTZ00110  425 TGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTP 483
PRK13767 PRK13767
ATP-dependent helicase; Provisional
498-829 4.51e-08

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 57.59  E-value: 4.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  498 TFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPAL---------------LYAkrspcltLVVSPLLSLMDD----- 557
Cdd:PRK13767   32 TFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIdelfrlgregeledkVYC-------LYVSPLRALNNDihrnl 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  558 --------QVS-----DLPScLKAACLHSGMTKKQRESVLKKvraaQVHVLIVSPEALvgcgakgpA---NLPPAAQ-LP 620
Cdd:PRK13767  105 eeplteirEIAkergeELPE-IRVAIRTGDTSSYEKQKMLKK----PPHILITTPESL--------AillNSPKFREkLR 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  621 PVAFACIDEVHCLSQwshNFRPCYLRVC-KVLREHMG---VRcfLGLTATAtrSTARDVAQHLGIAEELEVSGSASIpan 696
Cdd:PRK13767  172 TVKWVIVDEIHSLAE---NKRGVHLSLSlERLEELAGgefVR--IGLSATI--EPLEEVAKFLVGYEDDGEPRDCEI--- 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  697 lhLSVSMDRDSDQALVT----LLQGDR-------FRTLDSII-------IYCARRKDTERVAALLRTCLSTVRDskprgr 758
Cdd:PRK13767  242 --VDARFVKPFDIKVISpvddLIHTPAeeisealYETLHELIkehrttlIFTNTRSGAERVLYNLRKRFPEEYD------ 313
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564360538  759 gpETLAEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAG 829
Cdd:PRK13767  314 --EDNIGAHHSSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGRAG 382
PTZ00424 PTZ00424
helicase 45; Provisional
722-854 1.65e-07

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 55.22  E-value: 1.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  722 TLDSIIIYCARRKDTERVAALLRTCLSTVrdskprgrgpetlaEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGL 801
Cdd:PTZ00424  266 TITQAIIYCNTRRKVDYLTKKMHERDFTV--------------SCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGI 331
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564360538  802 DRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHPQG-EDLWELSRH 854
Cdd:PTZ00424  332 DVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDiEQLKEIERH 385
COG1202 COG1202
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
764-830 6.78e-07

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


Pssm-ID: 440815 [Multi-domain]  Cd Length: 790  Bit Score: 53.74  E-value: 6.78e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564360538  764 AEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVlhlglppsFES------------YVQAIGRAGR 830
Cdd:COG1202   451 AAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVI--------FDSlamgiewlsvqeFHQMLGRAGR 521
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
503-562 1.28e-06

DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 49.89  E-value: 1.28e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564360538  503 QERAVMRILSGISTLLVLPTGAGKSLCYQLPAL--LYAKRSPClTLVVSPLLSLMDDQVSDL 562
Cdd:cd17923     5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILeaLLRDPGSR-ALYLYPTKALAQDQLRSL 65
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
498-829 2.96e-06

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 51.64  E-value: 2.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  498 TFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALL-YAKRSP-------CLTLVVSPLLSL--------------M 555
Cdd:COG1201    24 APTPPQREAWPAIAAGESTLLIAPTGSGKTLAAFLPALDeLARRPRpgelpdgLRVLYISPLKALandiernlrapleeI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  556 DDQVSDLPSCLKAAcLHSGMTKkQREsvlkkvRAAQV----HVLIVSPE--ALVGCGAKGPANLppaAQLPPVAfacIDE 629
Cdd:COG1201   104 GEAAGLPLPEIRVG-VRTGDTP-ASE------RQRQRrrppHILITTPEslALLLTSPDARELL---RGVRTVI---VDE 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  630 VHCL------SQWS------HNFRPCYLRVckvlrehmgvrcfLGLTATAtrstaRD---VAQHLGIAEELE----VSgs 690
Cdd:COG1201   170 IHALagskrgVHLAlslerlRALAPRPLQR-------------IGLSATV-----GPleeVARFLVGYEDPRpvtiVD-- 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  691 ASIPANLHLSV-SMDRDSD--------------QALVTLLQGDRfrtldSIIIYCARRKDTERVAALLRTclstvrdskp 755
Cdd:COG1201   230 AGAGKKPDLEVlVPVEDLIerfpwaghlwphlyPRVLDLIEAHR-----TTLVFTNTRSQAERLFQRLNE---------- 294
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564360538  756 RGRGPETLAEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAG 829
Cdd:COG1201   295 LNPEDALPIAAHHGSLSREQRLEVEEALKAGELRAVVATSSLELGIDIGDVDLVIQVGSPKSVARLLQRIGRAG 368
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
509-598 3.50e-06

DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350682 [Multi-domain]  Cd Length: 189  Bit Score: 48.86  E-value: 3.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  509 RILSGISTLLVLPTGAGKS---LCYQLPALLYAKRSpcltLVVSPLLSLMDdQVSD--------LPSCLKAACLHSGMTK 577
Cdd:cd17924    28 RLLRGKSFAIIAPTGVGKTtfgLATSLYLASKGKRS----YLIFPTKSLVK-QAYErlskyaekAGVEVKILVYHSRLKK 102
                          90       100
                  ....*....|....*....|.
gi 564360538  578 KQRESVLKKVRAAQVHVLIVS 598
Cdd:cd17924   103 KEKEELLEKIEKGDFDILVTT 123
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
499-666 4.19e-06

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 47.69  E-value: 4.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  499 FRPGQERAVMRILSGIST---LLVLPTGAGKSLC-YQLPALLYAKRspclTLVVSPLLSLMDDQVSDLpsclkAACLHSG 574
Cdd:cd17926     1 LRPYQEEALEAWLAHKNNrrgILVLPTGSGKTLTaLALIAYLKELR----TLIVVPTDALLDQWKERF-----EDFLGDS 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  575 MTKKQRESVLKKVRAAQvhVLIVSPEALvgcgakgpANLPPAAQLPPVAFACI--DEVHCLS--QWSHnfrpcylrvckv 650
Cdd:cd17926    72 SIGLIGGGKKKDFDDAN--VVVATYQSL--------SNLAEEEKDLFDQFGLLivDEAHHLPakTFSE------------ 129
                         170
                  ....*....|....*.
gi 564360538  651 LREHMGVRCFLGLTAT 666
Cdd:cd17926   130 ILKELNAKYRLGLTAT 145
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
774-849 7.30e-06

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 50.17  E-value: 7.30e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564360538  774 QERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHPQGEDLW 849
Cdd:PLN00206  405 KERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLF 480
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
464-613 1.15e-05

DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 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: 350807 [Multi-domain]  Cd Length: 234  Bit Score: 48.08  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  464 CPTPVLPLYPpgplgqvADTPAEVFQVLEQLGHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLYAKRSPC 543
Cdd:cd18049    19 CPKPVLNFYE-------ANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPF 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  544 LT-------LVVSPLLSLMdDQVSDLP-----SC-LKAACLHSGMTKKQRESVLKKvraaQVHVLIVSPEALVGCGAKGP 610
Cdd:cd18049    92 LErgdgpicLVLAPTRELA-QQVQQVAaeygrACrLKSTCIYGGAPKGPQIRDLER----GVEICIATPGRLIDFLEAGK 166

                  ...
gi 564360538  611 ANL 613
Cdd:cd18049   167 TNL 169
ResIII pfam04851
Type III restriction enzyme, res subunit;
497-666 1.31e-05

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 46.51  E-value: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538   497 HTFRPGQERAVMRILSGIST-----LLVLPTGAGKSLCY-QLPALLYAKRSPCLTLVVSPLLSLMDDQVSDLPSCLKAAC 570
Cdd:pfam04851    2 LELRPYQIEAIENLLESIKNgqkrgLIVMATGSGKTLTAaKLIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538   571 LHSGMTKKQResvlKKVRAAQVHVLIVSPEALvgcgakGPANLPPAAQLPPVAFACI--DEVHCL--SQWSH---NFRPC 643
Cdd:pfam04851   82 EIGEIISGDK----KDESVDDNKIVVTTIQSL------YKALELASLELLPDFFDVIiiDEAHRSgaSSYRNileYFKPA 151
                          170       180
                   ....*....|....*....|...
gi 564360538   644 YLrvckvlrehmgvrcfLGLTAT 666
Cdd:pfam04851  152 FL---------------LGLTAT 159
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
498-686 2.82e-05

DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 46.10  E-value: 2.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  498 TFRPGQERAVMRI-LSGISTLLVLPTGAGKSLCYQLPALLYAKRSPCLTLVVSPLLSLMDDQVSDLPSCLKAACLHSGMt 576
Cdd:cd17921     1 LLNPIQREALRALyLSGDSVLVSAPTSSGKTLIAELAILRALATSGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGL- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  577 kKQRESVLKKVRAAQVHVLIVSPEALVGCGAKGPANLppaaqLPPVAFACIDEVHCLSQWShnfRPCYLRVC--KVLREH 654
Cdd:cd17921    80 -LTGDPSVNKLLLAEADILVATPEKLDLLLRNGGERL-----IQDVRLVVVDEAHLIGDGE---RGVVLELLlsRLLRIN 150
                         170       180       190
                  ....*....|....*....|....*....|..
gi 564360538  655 MGVRcFLGLTATAtrSTARDVAQHLGIAEELE 686
Cdd:cd17921   151 KNAR-FVGLSATL--PNAEDLAEWLGVEDLIR 179
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
776-836 3.56e-05

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 47.66  E-value: 3.56e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564360538  776 RKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAH 836
Cdd:PRK04837  294 RLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGH 354
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
513-602 6.56e-05

DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350680 [Multi-domain]  Cd Length: 166  Bit Score: 44.88  E-value: 6.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  513 GISTLLVLPTGAGKSLCYQLPALL-YAKR--SPCLTLVVSPLLSLMDDQVSDLPSCLKAACL-------HSGMTKKQRES 582
Cdd:cd17922     1 GRNVLIAAPTGSGKTEAAFLPALSsLADEpeKGVQVLYISPLKALINDQERRLEEPLDEIDLeipvavrHGDTSQSEKAK 80
                          90       100
                  ....*....|....*....|
gi 564360538  583 VLKKVRaaqvHVLIVSPEAL 602
Cdd:cd17922    81 QLKNPP----GILITTPESL 96
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
464-613 1.18e-04

DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 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: 350808 [Multi-domain]  Cd Length: 271  Bit Score: 45.39  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  464 CPTPVLPLYPpgplgqvADTPAEVFQVLEQLGHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLYAKRSP- 542
Cdd:cd18050    57 CPKPVFAFHQ-------ANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPy 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  543 --------CLTLVVSPLLSLMDDQVSD---LPSCLKAACLHSGMTKKQRESVLKKvraaQVHVLIVSPEALVGCGAKGPA 611
Cdd:cd18050   130 lergdgpiCLVLAPTRELAQQVQQVADdygKSSRLKSTCIYGGAPKGPQIRDLER----GVEICIATPGRLIDFLEAGKT 205

                  ..
gi 564360538  612 NL 613
Cdd:cd18050   206 NL 207
PRK01172 PRK01172
ATP-dependent DNA helicase;
661-832 2.89e-04

ATP-dependent DNA helicase;


Pssm-ID: 100801 [Multi-domain]  Cd Length: 674  Bit Score: 45.26  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  661 LGLTATAtrSTARDVAQHLGIAeeLEVSGSASIPANL------HLSVSMDRDSDQALVTLLQgDRFRTLDSIIIYCARRK 734
Cdd:PRK01172  173 LALSATV--SNANELAQWLNAS--LIKSNFRPVPLKLgilyrkRLILDGYERSQVDINSLIK-ETVNDGGQVLVFVSSRK 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  735 DTERVAALLRTCLSTVRDSKPRGRG----PETLAEA-------YHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDR 803
Cdd:PRK01172  248 NAEDYAEMLIQHFPEFNDFKVSSENnnvyDDSLNEMlphgvafHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNL 327
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 564360538  804 P-------DVRAVLHLGLPP-SFESYVQAIGRAGRDG 832
Cdd:PRK01172  328 ParlvivrDITRYGNGGIRYlSNMEIKQMIGRAGRPG 364
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
709-841 3.15e-04

C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 42.19  E-value: 3.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  709 QALVTLLQGDRFRTLDSI-IIYCARRkDTERV-AALLRTCLSTVRDSKPR---GRGPETlaEAYHAGMCSQERKRVQQAF 783
Cdd:cd18802    10 QKLIEILREYFPKTPDFRgIIFVERR-ATAVVlSRLLKEHPSTLAFIRCGfliGRGNSS--QRKRSLMTQRKQKETLDKF 86
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 564360538  784 MQGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGkpAHCHLFL 841
Cdd:cd18802    87 RDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN--SKYILMV 142
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
489-603 5.28e-04

DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350669 [Multi-domain]  Cd Length: 196  Bit Score: 42.43  E-value: 5.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  489 QVLEQLGHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPAL------LYAKRSPCLTLVVSPL--LSLmddQVS 560
Cdd:cd00268     3 KALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILekllpePKKKGRGPQALVLAPTreLAM---QIA 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 564360538  561 DL------PSCLKAACLHSGMTKKQRESVLKKvraaQVHVLIVSPEALV 603
Cdd:cd00268    80 EVarklgkGTGLKVAAIYGGAPIKKQIEALKK----GPDIVVGTPGRLL 124
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
566-596 5.75e-04

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: 41.34  E-value: 5.75e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 564360538  566 LKAACLHSGMTKKQRESVLKKVRAAQVHVLI 596
Cdd:cd18787    52 IKVAALHGDLSQEERERALKKFRSGKVRVLV 82
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
684-832 6.57e-04

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 43.75  E-value: 6.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  684 ELEVSGSASIPANLHLSVSMDRDSDQALVTLLQGDRFrtlDSIIIYCARRKDTERVAALLrtclstVRDskprgrgpetl 763
Cdd:PRK01297  299 EIEPENVASDTVEQHVYAVAGSDKYKLLYNLVTQNPW---ERVMVFANRKDEVRRIEERL------VKD----------- 358
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564360538  764 aeAYHAGMCSQE-----RKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDG 832
Cdd:PRK01297  359 --GINAAQLSGDvpqhkRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAG 430
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
532-598 7.79e-04

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: 40.27  E-value: 7.79e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564360538   532 LPALLYAKRSPClTLVVSPLLSLMDDQVSDLPSCLKAACLHSGMTKKQRESVLKKVRAAQVHVLIVS 598
Cdd:pfam00271    6 LLELLKKERGGK-VLIFSQTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVAT 71
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
708-841 7.97e-04

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 43.68  E-value: 7.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  708 DQALVTLLQGDRFrtlDSIIIYCARRKDTERVA-ALLRTCLSTVrdskprgrgpetlaeAYHAGMCSQERKRVQQAFMQG 786
Cdd:PRK11634  233 NEALVRFLEAEDF---DAAIIFVRTKNATLEVAeALERNGYNSA---------------ALNGDMNQALREQTLERLKDG 294
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564360538  787 HLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFL 841
Cdd:PRK11634  295 RLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFV 349
PRK00254 PRK00254
ski2-like helicase; Provisional
727-830 1.58e-03

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 42.88  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  727 IIYCARRKDTERVAALLRTCLSTVRDsKPRGRGPETLAEA--------------------YHAGMCSQERKRVQQAFMQG 786
Cdd:PRK00254  242 LVFVNTRRSAEKEALELAKKIKRFLT-KPELRALKELADSleenptneklkkalrggvafHHAGLGRTERVLIEDAFREG 320
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564360538  787 HLRMVVATVAFGMGLDRPDVRAVL-------HLGLP--PSFESYvQAIGRAGR 830
Cdd:PRK00254  321 LIKVITATPTLSAGINLPAFRVIIrdtkrysNFGWEdiPVLEIQ-QMMGRAGR 372
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
487-599 1.75e-03

DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350716 [Multi-domain]  Cd Length: 197  Bit Score: 40.91  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  487 VFQVLEQLGHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALL--------YAKRSPCLTLVVSPLLSL---M 555
Cdd:cd17958     1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIhldlqpipREQRNGPGVLVLTPTRELalqI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 564360538  556 DDQVSD-LPSCLKAACLHSGMTKKQRESVLKKvraaQVHVLIVSP 599
Cdd:cd17958    81 EAECSKySYKGLKSVCVYGGGNRNEQIEDLSK----GVDIIIATP 121
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
503-602 2.33e-03

DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 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: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 41.20  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  503 QERAVMRILSGISTLLVLPTGAGKSLCYQLP---ALLYAK-------RSPcLTLVVSPLLSLMdDQVS--------DLPs 564
Cdd:cd17948    17 QKQGIPSILRGRNTLCAAETGSGKTLTYLLPiiqRLLRYKllaegpfNAP-RGLVITPSRELA-EQIGsvaqslteGLG- 93
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 564360538  565 cLKAACLHSGMTKKQresvLKKVRAAQVHVLIVSPEAL 602
Cdd:cd17948    94 -LKVKVITGGRTKRQ----IRNPHFEEVDILVATPGAL 126
ZnF_C2HC smart00343
zinc finger;
394-408 2.40e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 36.27  E-value: 2.40e-03
                            10
                    ....*....|....*
gi 564360538    394 TCFRCGQFGHWASQC 408
Cdd:smart00343    1 KCYNCGKEGHIARDC 15
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
492-541 2.46e-03

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


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 42.22  E-value: 2.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564360538  492 EQLGHHTFRPGQER---AVMRILSGISTLLVL-PTGAGKSLCYQLPALLYAKRS 541
Cdd:COG1199     8 LAFPGFEPRPGQREmaeAVARALAEGRHLLIEaGTGTGKTLAYLVPALLAARET 61
PRK02362 PRK02362
ATP-dependent DNA helicase;
761-846 2.89e-03

ATP-dependent DNA helicase;


Pssm-ID: 235032 [Multi-domain]  Cd Length: 737  Bit Score: 41.87  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  761 ETLAEA-------YHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVLH--------LGLPP-SFESYVQA 824
Cdd:PRK02362  296 KDLADCvakgaafHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRdyrrydggAGMQPiPVLEYHQM 375
                          90       100
                  ....*....|....*....|..
gi 564360538  825 IGRAGRDGkpahchlfLHPQGE 846
Cdd:PRK02362  376 AGRAGRPG--------LDPYGE 389
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
704-833 3.57e-03

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 41.33  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  704 DRDSDQALVTLLQgdRFRTlDSIIIYCARRKDTERVAALLRtclstvrdskprGRGPETLAeaYHAGMCSQERKRVQQAF 783
Cdd:PRK11776  226 PDERLPALQRLLL--HHQP-ESCVVFCNTKKECQEVADALN------------AQGFSALA--LHGDLEQRDRDQVLVRF 288
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564360538  784 MQGHLRMVVAT-VAfGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGK 833
Cdd:PRK11776  289 ANRSCSVLVATdVA-ARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGS 338
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
767-841 6.24e-03

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. 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: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 38.23  E-value: 6.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  767 YHAGMCSQERKRVQQAFM--QGHLRMVVATVAFGMGL-----DRpdvraVLHLGLP--PSFESyvQAIGRAGRDG--KPA 835
Cdd:cd18793    57 LDGSTSSKERQKLVDRFNedPDIRVFLLSTKAGGVGLnltaaNR-----VILYDPWwnPAVEE--QAIDRAHRIGqkKPV 129

                  ....*.
gi 564360538  836 HCHLFL 841
Cdd:cd18793   130 VVYRLI 135
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
523-666 6.62e-03

DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 39.09  E-value: 6.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564360538  523 GAGK-----SLCYQLpalLYAKRSPCLTLVVSPlLSLMDDQVSDL----PScLKAACLHSgmTKKQRESVLKKVRAAQVH 593
Cdd:cd17919    29 GLGKtlqaiAFLAYL---LKEGKERGPVLVVCP-LSVLENWEREFekwtPD-LRVVVYHG--SQRERAQIRAKEKLDKFD 101
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564360538  594 VLIVSPEALVGCgakgpanlppAAQLPPVAFACI--DEVHCL----SQWShnfrpcylRVCKVLREHMgvRcfLGLTAT 666
Cdd:cd17919   102 VVLTTYETLRRD----------KASLRKFRWDLVvvDEAHRLknpkSQLS--------KALKALRAKR--R--LLLTGT 158
HELICc smart00490
helicase superfamily c-terminal domain;
566-598 7.10e-03

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 36.81  E-value: 7.10e-03
                            10        20        30
                    ....*....|....*....|....*....|...
gi 564360538    566 LKAACLHSGMTKKQRESVLKKVRAAQVHVLIVS 598
Cdd:smart00490   12 IKVARLHGGLSQEEREEILDKFNNGKIKVLVAT 44
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
768-839 8.01e-03

C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 38.48  E-value: 8.01e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564360538  768 HAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPD--VRAVLH---LGLppsfESYVQAIGRAGRDGKPAHCHL 839
Cdd:cd18811    68 HGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatVMVIEDaerFGL----SQLHQLRGRVGRGDHQSYCLL 140
 
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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