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Conserved domains on  [gi|672059437|ref|XP_008763788|]
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ATP-dependent DNA helicase Q4 isoform X1 [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];
491-856 8.53e-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: 8.53e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  491 AEVFQVLEQL-GHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLyakrSPCLTLVVSPLLSLMDDQVSDLP 569
Cdd:COG0514     3 DDALEVLKRVfGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALL----LPGLTLVVSPLIALMKDQVDALR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  570 SC-LKAACLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVGcgakgPANLPPAAQLPPVAFAcIDEVHCLSQWSHNFRP 648
Cdd:COG0514    79 AAgIRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLN-----PRFLELLRRLKISLFA-IDEAHCISQWGHDFRP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  649 CYLRVcKVLREHMGVRCFLGLTATATRSTARDVAQHLGIAEELEVSGSASIPaNLHLSVS--MDRDSDQALVTLLQGdrf 726
Cdd:COG0514   153 DYRRL-GELRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRP-NLRLEVVpkPPDDKLAQLLDFLKE--- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  727 RTLDSIIIYCARRKDTERVAALLRTclstvrdskpRGRGpetlAEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMG 806
Cdd:COG0514   228 HPGGSGIVYCLSRKKVEELAEWLRE----------AGIR----AAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMG 293
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 672059437  807 LDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHPQGEDLWE 856
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 5.22e-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: 5.22e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 672059437    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 6.83e-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: 6.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437     4 LATVRARLQDWERAFVRLHGRRPAKEDVEAAPeETRALYREYRNLKQAVSQADDGHRVQ---KQSLAKAAEEEQepscwg 80
Cdd:pfam11719    1 ISQLKAEIKEWERAFAAKNGRKPSKDDIKKNP-EIAKKYKLYSKLKKGESIKTKTPSKPvklEARPKKRKHEST------ 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437    81 shlNRAATQNTQSIPKQSplssiqdygKRLKANLkntlqgGPTLSRklqhQKRSLSIVPTSRPPGPRTESPcPEQANDAL 160
Cdd:pfam11719   74 ---NKSPEKNSQSTPRKS---------KNIKSEL------GPTPQA----NGKVLSLFDLLSTPPKSSPLK-SKEVKTDV 130
                          170
                   ....*....|
gi 672059437   161 PQVPVPQPRQ 170
Cdd:pfam11719  131 SGTAIFTPSK 140
ZnF_C2HC smart00343
zinc finger;
394-408 2.37e-03

zinc finger;


:

Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 36.27  E-value: 2.37e-03
                            10
                    ....*....|....*
gi 672059437    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];
491-856 8.53e-115

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 366.77  E-value: 8.53e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  491 AEVFQVLEQL-GHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLyakrSPCLTLVVSPLLSLMDDQVSDLP 569
Cdd:COG0514     3 DDALEVLKRVfGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALL----LPGLTLVVSPLIALMKDQVDALR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  570 SC-LKAACLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVGcgakgPANLPPAAQLPPVAFAcIDEVHCLSQWSHNFRP 648
Cdd:COG0514    79 AAgIRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLN-----PRFLELLRRLKISLFA-IDEAHCISQWGHDFRP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  649 CYLRVcKVLREHMGVRCFLGLTATATRSTARDVAQHLGIAEELEVSGSASIPaNLHLSVS--MDRDSDQALVTLLQGdrf 726
Cdd:COG0514   153 DYRRL-GELRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRP-NLRLEVVpkPPDDKLAQLLDFLKE--- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  727 RTLDSIIIYCARRKDTERVAALLRTclstvrdskpRGRGpetlAEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMG 806
Cdd:COG0514   228 HPGGSGIVYCLSRKKVEELAEWLRE----------AGIR----AAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMG 293
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 672059437  807 LDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHPQGEDLWE 856
Cdd:COG0514   294 IDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQR 343
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
494-696 3.22e-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: 313.81  E-value: 3.22e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  494 FQVLEQL-GHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLYAKRSPCLTLVVSPLLSLMDDQVSDLPSCL 572
Cdd:cd18018     1 LKLLRRVfGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRRRGPGLTLVVSPLIALMKDQVDALPRAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  573 KAACLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVgcgakGPANLPPAAQLPPVAFACIDEVHCLSQWSHNFRPCYLR 652
Cdd:cd18018    81 KAAALNSSLTREERRRILEKLRAGEVKILYVSPERLV-----NESFRELLRQTPPISLLVVDEAHCISEWSHNFRPDYLR 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 672059437  653 VCKVLREHMGVRCFLGLTATATRSTARDVAQHLGIAEELEVSGS 696
Cdd:cd18018   156 LCRVLRELLGAPPVLALTATATKRVVEDIASHLGIPESGVVRGP 199
recQ_fam TIGR00614
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ...
501-849 1.76e-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: 1.76e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437   501 GHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLyakrSPCLTLVVSPLLSLMDDQVSDLP-SCLKAACLHS 579
Cdd:TIGR00614    8 GLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALY----SDGITLVISPLISLMEDQVLQLQaLGIPATFLNS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437   580 GMTKKQRESVLKKVRAAQVHVLIVSPEALvgCGAKGPANLPPAAQLPpvAFACIDEVHCLSQWSHNFRPCYlRVCKVLRE 659
Cdd:TIGR00614   84 AQTKEQQLNVLTDLKDGKIKLLYVTPEKI--SASNRLLQTLEERKGI--TLIAVDEAHCISQWGHDFRPDY-KALGSLKQ 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437   660 HMGVRCFLGLTATATRSTARDVAQHLGIAEELEVSGSASIPaNLHLSVsMDRDSD--QALVTLLQGdRFRTlDSIIIYCA 737
Cdd:TIGR00614  159 KFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRP-NLYYEV-RRKTPKilEDLLRFIRK-EFEG-KSGIIYCP 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437   738 RRKDTERVAALLRTC-LStvrdskprgrgpetlAEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVL 816
Cdd:TIGR00614  235 SRKKVEQVAAELQKLgLA---------------AGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVI 299
                          330       340       350
                   ....*....|....*....|....*....|...
gi 672059437   817 HLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHP 849
Cdd:TIGR00614  300 HYSLPKSMESYYQESGRAGRDGLPSECHLFYAP 332
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
485-849 9.21e-79

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 271.97  E-value: 9.21e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  485 QVADTPAEVFQVL-EQLGHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLYakrsPCLTLVVSPLLSLMDD 563
Cdd:PRK11057    5 EVLNLESLAKQVLqETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVL----DGLTLVVSPLISLMKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  564 QVSDL-PSCLKAACLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVGCGAkgpanLPPAAQLPPVAFAcIDEVHCLSQW 642
Cdd:PRK11057   81 QVDQLlANGVAAACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNF-----LEHLAHWNPALLA-VDEAHCISQW 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  643 SHNFRPCYlRVCKVLREHMGVRCFLGLTATATRSTARDVAQHLGIAEELEVSGSASIPANLHLSVSMDRDSDQaLVTLLQ 722
Cdd:PRK11057  155 GHDFRPEY-AALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQ-LMRYVQ 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  723 GDRFRtldSIIIYCARRKDTERVAALLRtclstvrdskprGRGPEtlAEAYHAGMCSQERKRVQQAFMQGHLRMVVATVA 802
Cdd:PRK11057  233 EQRGK---SGIIYCNSRAKVEDTAARLQ------------SRGIS--AAAYHAGLDNDVRADVQEAFQRDDLQIVVATVA 295
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 672059437  803 FGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHP 849
Cdd:PRK11057  296 FGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDP 342
DpdF NF041063
protein DpdF;
500-850 1.87e-34

protein DpdF;


Pssm-ID: 468990 [Multi-domain]  Cd Length: 813  Bit Score: 142.74  E-value: 1.87e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  500 LGHHTFR-PGQERAVMRILS---GiSTLLV-LPTGAGKSLCYQLPALLYAKRSPcLTLVVSPLLSLMDDQVSDLPSCLKA 574
Cdd:NF041063  135 LGFTHYRsPGQREAVRAALLappG-STLIVnLPTGSGKSLVAQAPALLASRQGG-LTLVVVPTVALAIDQERRARELLRR 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  575 A--------CLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVGcgakgpANLPP---AAQLPPVAFACIDEVHCLSQWS 643
Cdd:NF041063  213 AgpdlggplAWHGGLSAEERAAIRQRIRDGTQRILFTSPESLTG------SLRPAlfdAAEAGLLRYLVVDEAHLVDQWG 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  644 HNFRPCY----------LRVCKvlrEHMGVRCFLgLTATATRSTaRDVAQHL-GIAEELE-VSGSasipanlHL----SV 707
Cdd:NF041063  287 DGFRPEFqllaglrrslLRLAP---SGRPFRTLL-LSATLTEST-LDTLETLfGPPGPFIvVSAV-------QLrpepAY 354
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  708 SMDRDSDQAlvtllqgDRFRT-LDSI-------IIYCARRKDTERVAALLRtclstvrdSKPRGRgpetlAEAYHAGMCS 779
Cdd:NF041063  355 WVAKCDSEE-------ERRERvLEALrhlprplILYVTKVEDAEAWLQRLR--------AAGFRR-----VALFHGDTPD 414
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672059437  780 QERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHPQ 850
Cdd:NF041063  415 AERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPD 485
DEXDc smart00487
DEAD-like helicases superfamily;
497-700 5.79e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 103.73  E-value: 5.79e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437    497 LEQLGHHTFRPGQERAVMRILSGI-STLLVLPTGAGKSLCYQLPALLYAKRSP-CLTLVVSPLLSLMDDQVSDL-----P 569
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRGKgGRVLVLVPTRELAEQWAEELkklgpS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437    570 SCLKAACLHSGMTKKQResvLKKVRAAQVHVLIVSPEALVGCGAKGPANlppaaqLPPVAFACIDEVHCLSQWshNFRPC 649
Cdd:smart00487   81 LGLKVVGLYGGDSKREQ---LRKLESGKTDILVTTPGRLLDLLENDKLS------LSNVDLVILDEAHRLLDG--GFGDQ 149
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|.
gi 672059437    650 YLRVCKVLREHmgvRCFLGLTATATRSTARDVAQHLGIAEELEVSGSASIP 700
Cdd:smart00487  150 LEKLLKLLPKN---VQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPLEP 197
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
506-679 1.61e-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: 1.61e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437   506 RPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPAL--LYAKRSPCLTLVVSPLLSLMDDQVSDL-----PSCLKAACLH 578
Cdd:pfam00270    1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALeaLDKLDNGPQALVLAPTRELAEQIYEELkklgkGLGLKVASLL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437   579 SGMTKKQRESVLKKvraaqVHVLIVSPEALVgcgakgpANLPPAAQLPPVAFACIDEVHCLSQWShnFRPCYLRVCKVLR 658
Cdd:pfam00270   81 GGDSRKEQLEKLKG-----PDILVGTPGRLL-------DLLQERKLLKNLKLLVLDEAHRLLDMG--FGPDLEEILRRLP 146
                          170       180
                   ....*....|....*....|.
gi 672059437   659 EHmgvRCFLGLTATATRSTAR 679
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 5.22e-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: 5.22e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 672059437    2 ERLATVRARLQDWERAFVRLHGRRPAKEDVEAAPEETRALYREYRNLKQ 50
Cdd:cd22289     1 ERLQELKIALKTWERAFAKKHGRKPTKDDIKAAPEEIKDLYKEYAKLKK 49
Drc1-Sld2 pfam11719
DNA replication and checkpoint protein; Genome duplication is precisely regulated by ...
4-170 6.83e-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: 6.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437     4 LATVRARLQDWERAFVRLHGRRPAKEDVEAAPeETRALYREYRNLKQAVSQADDGHRVQ---KQSLAKAAEEEQepscwg 80
Cdd:pfam11719    1 ISQLKAEIKEWERAFAAKNGRKPSKDDIKKNP-EIAKKYKLYSKLKKGESIKTKTPSKPvklEARPKKRKHEST------ 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437    81 shlNRAATQNTQSIPKQSplssiqdygKRLKANLkntlqgGPTLSRklqhQKRSLSIVPTSRPPGPRTESPcPEQANDAL 160
Cdd:pfam11719   74 ---NKSPEKNSQSTPRKS---------KNIKSEL------GPTPQA----NGKVLSLFDLLSTPPKSSPLK-SKEVKTDV 130
                          170
                   ....*....|
gi 672059437   161 PQVPVPQPRQ 170
Cdd:pfam11719  131 SGTAIFTPSK 140
ZnF_C2HC smart00343
zinc finger;
394-408 2.37e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 36.27  E-value: 2.37e-03
                            10
                    ....*....|....*
gi 672059437    394 TCFRCGQFGHWASQC 408
Cdd:smart00343    1 KCYNCGKEGHIARDC 15
zf-CCHC pfam00098
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ...
393-410 9.77e-03

Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.


Pssm-ID: 395050 [Multi-domain]  Cd Length: 18  Bit Score: 34.81  E-value: 9.77e-03
                           10
                   ....*....|....*...
gi 672059437   393 DTCFRCGQFGHWASQCSQ 410
Cdd:pfam00098    1 GKCYNCGEPGHIARDCPK 18
 
Name Accession Description Interval E-value
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
491-856 8.53e-115

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 366.77  E-value: 8.53e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  491 AEVFQVLEQL-GHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLyakrSPCLTLVVSPLLSLMDDQVSDLP 569
Cdd:COG0514     3 DDALEVLKRVfGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALL----LPGLTLVVSPLIALMKDQVDALR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  570 SC-LKAACLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVGcgakgPANLPPAAQLPPVAFAcIDEVHCLSQWSHNFRP 648
Cdd:COG0514    79 AAgIRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLN-----PRFLELLRRLKISLFA-IDEAHCISQWGHDFRP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  649 CYLRVcKVLREHMGVRCFLGLTATATRSTARDVAQHLGIAEELEVSGSASIPaNLHLSVS--MDRDSDQALVTLLQGdrf 726
Cdd:COG0514   153 DYRRL-GELRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRP-NLRLEVVpkPPDDKLAQLLDFLKE--- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  727 RTLDSIIIYCARRKDTERVAALLRTclstvrdskpRGRGpetlAEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMG 806
Cdd:COG0514   228 HPGGSGIVYCLSRKKVEELAEWLRE----------AGIR----AAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMG 293
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 672059437  807 LDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHPQGEDLWE 856
Cdd:COG0514   294 IDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQR 343
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
494-696 3.22e-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: 313.81  E-value: 3.22e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  494 FQVLEQL-GHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLYAKRSPCLTLVVSPLLSLMDDQVSDLPSCL 572
Cdd:cd18018     1 LKLLRRVfGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRRRGPGLTLVVSPLIALMKDQVDALPRAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  573 KAACLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVgcgakGPANLPPAAQLPPVAFACIDEVHCLSQWSHNFRPCYLR 652
Cdd:cd18018    81 KAAALNSSLTREERRRILEKLRAGEVKILYVSPERLV-----NESFRELLRQTPPISLLVVDEAHCISEWSHNFRPDYLR 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 672059437  653 VCKVLREHMGVRCFLGLTATATRSTARDVAQHLGIAEELEVSGS 696
Cdd:cd18018   156 LCRVLRELLGAPPVLALTATATKRVVEDIASHLGIPESGVVRGP 199
recQ_fam TIGR00614
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ...
501-849 1.76e-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: 1.76e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437   501 GHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLyakrSPCLTLVVSPLLSLMDDQVSDLP-SCLKAACLHS 579
Cdd:TIGR00614    8 GLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALY----SDGITLVISPLISLMEDQVLQLQaLGIPATFLNS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437   580 GMTKKQRESVLKKVRAAQVHVLIVSPEALvgCGAKGPANLPPAAQLPpvAFACIDEVHCLSQWSHNFRPCYlRVCKVLRE 659
Cdd:TIGR00614   84 AQTKEQQLNVLTDLKDGKIKLLYVTPEKI--SASNRLLQTLEERKGI--TLIAVDEAHCISQWGHDFRPDY-KALGSLKQ 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437   660 HMGVRCFLGLTATATRSTARDVAQHLGIAEELEVSGSASIPaNLHLSVsMDRDSD--QALVTLLQGdRFRTlDSIIIYCA 737
Cdd:TIGR00614  159 KFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRP-NLYYEV-RRKTPKilEDLLRFIRK-EFEG-KSGIIYCP 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437   738 RRKDTERVAALLRTC-LStvrdskprgrgpetlAEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVL 816
Cdd:TIGR00614  235 SRKKVEQVAAELQKLgLA---------------AGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVI 299
                          330       340       350
                   ....*....|....*....|....*....|...
gi 672059437   817 HLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHP 849
Cdd:TIGR00614  300 HYSLPKSMESYYQESGRAGRDGLPSECHLFYAP 332
recQ TIGR01389
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ...
494-850 4.18e-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: 297.75  E-value: 4.18e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437   494 FQVL-EQLGHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLYakrsPCLTLVVSPLLSLMDDQVSDLPSC- 571
Cdd:TIGR01389    2 QQVLkRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLL----KGLTVVISPLISLMKDQVDQLRAAg 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437   572 LKAACLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVGcgakgPANLPPAAQLPPVAFAcIDEVHCLSQWSHNFRPCYL 651
Cdd:TIGR01389   78 VAAAYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQ-----DYFLNMLQRIPIALVA-VDEAHCVSQWGHDFRPEYQ 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437   652 RVCkVLREHMGVRCFLGLTATATRSTARDVAQHLGIAEELEVSGSASIPaNLHLSVSMDRDSDQALVTLLQGDRFRtldS 731
Cdd:TIGR01389  152 RLG-SLAERFPQVPRIALTATADAETRQDIRELLRLADANEFITSFDRP-NLRFSVVKKNNKQKFLLDYLKKHRGQ---S 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437   732 IIIYCARRKDTERVAALLRTclstvrdskprgRGPETLAeaYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPD 811
Cdd:TIGR01389  227 GIIYASSRKKVEELAERLES------------QGISALA--YHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPN 292
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 672059437   812 VRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHPQ 850
Cdd:TIGR01389  293 VRFVIHYDMPGNLESYYQEAGRAGRDGLPAEAILLYSPA 331
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
485-849 9.21e-79

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 271.97  E-value: 9.21e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  485 QVADTPAEVFQVL-EQLGHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLYakrsPCLTLVVSPLLSLMDD 563
Cdd:PRK11057    5 EVLNLESLAKQVLqETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVL----DGLTLVVSPLISLMKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  564 QVSDL-PSCLKAACLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVGCGAkgpanLPPAAQLPPVAFAcIDEVHCLSQW 642
Cdd:PRK11057   81 QVDQLlANGVAAACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNF-----LEHLAHWNPALLA-VDEAHCISQW 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  643 SHNFRPCYlRVCKVLREHMGVRCFLGLTATATRSTARDVAQHLGIAEELEVSGSASIPANLHLSVSMDRDSDQaLVTLLQ 722
Cdd:PRK11057  155 GHDFRPEY-AALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQ-LMRYVQ 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  723 GDRFRtldSIIIYCARRKDTERVAALLRtclstvrdskprGRGPEtlAEAYHAGMCSQERKRVQQAFMQGHLRMVVATVA 802
Cdd:PRK11057  233 EQRGK---SGIIYCNSRAKVEDTAARLQ------------SRGIS--AAAYHAGLDNDVRADVQEAFQRDDLQIVVATVA 295
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 672059437  803 FGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHP 849
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 ...
498-696 5.31e-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: 5.31e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  498 EQLGHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLyakrSPCLTLVVSPLLSLMDDQVSDLPS-CLKAAC 576
Cdd:cd17920     6 EVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALL----LDGVTLVVSPLISLMQDQVDRLQQlGIRAAA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  577 LHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVgcgakGPANLPPAAQLP---PVAFACIDEVHCLSQWSHNFRPCYLRV 653
Cdd:cd17920    82 LNSTLSPEEKREVLLRIKNGQYKLLYVTPERLL-----SPDFLELLQRLPerkRLALIVVDEAHCVSQWGHDFRPDYLRL 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 672059437  654 CKVLREHMGVrCFLGLTATATRSTARDVAQHLGIAEELEVSGS 696
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 ...
702-846 6.27e-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: 190.11  E-value: 6.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  702 NLHLSVSMDRDSDQALVTLLQGDRFRTLDSIIIYCARRKDTERVAALLRTCLSTvrdskprgrgpetlAEAYHAGMCSQE 781
Cdd:cd18794     3 NLFYSVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGIS--------------AAAYHAGLEPSD 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672059437  782 RKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLF 846
Cdd:cd18794    69 RRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
501-846 3.27e-52

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 200.89  E-value: 3.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  501 GHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLyakrSPCLTLVVSPLLSLMDDQVSD-LPSCLKAACLHS 579
Cdd:PLN03137  457 GNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALI----CPGITLVISPLVSLIQDQIMNlLQANIPAASLSA 532
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  580 GMTKKQRESVLKKVRA--AQVHVLIVSPEALvgcgAKGPA---NLPPAAQLPPVAFACIDEVHCLSQWSHNFRPCYlRVC 654
Cdd:PLN03137  533 GMEWAEQLEILQELSSeySKYKLLYVTPEKV----AKSDSllrHLENLNSRGLLARFVIDEAHCVSQWGHDFRPDY-QGL 607
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  655 KVLREHMGVRCFLGLTATATRSTARDVAQHLGIAEELEVSGSASIPaNLHLSVSmdRDSDQALVTLLQGDRFRTLDSI-I 733
Cdd:PLN03137  608 GILKQKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRP-NLWYSVV--PKTKKCLEDIDKFIKENHFDECgI 684
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  734 IYCARRKDTERVAALLRTClstvrdskprgrGPEtlAEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVR 813
Cdd:PLN03137  685 IYCLSRMDCEKVAERLQEF------------GHK--AAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVR 750
                         330       340       350
                  ....*....|....*....|....*....|...
gi 672059437  814 AVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLF 846
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 ...
484-696 5.07e-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: 5.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  484 GQVADTPAEVFQVleqlghHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLyakrSPCLTLVVSPLLSLMDD 563
Cdd:cd18015     4 GKVKDTLKNVFKL------EKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALC----SDGFTLVVSPLISLMED 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  564 QVSDLPSC-LKAACLHSGMTKKQRESVLKKVR--AAQVHVLIVSPEALvgcgAKGP---ANLPPAAQLPPVAFACIDEVH 637
Cdd:cd18015    74 QLMALKKLgISATMLNASSSKEHVKWVHAALTdkNSELKLLYVTPEKI----AKSKrfmSKLEKAYNAGRLARIAIDEVH 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672059437  638 CLSQWSHNFRPCYlrvckvlrEHMGV--RCF-----LGLTATATRSTARDVAQHLGIAEELEVSGS 696
Cdd:cd18015   150 CCSQWGHDFRPDY--------KKLGIlkRQFpnvpiLGLTATATSKVLKDVQKILCIQKCLTFTAS 207
DpdF NF041063
protein DpdF;
500-850 1.87e-34

protein DpdF;


Pssm-ID: 468990 [Multi-domain]  Cd Length: 813  Bit Score: 142.74  E-value: 1.87e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  500 LGHHTFR-PGQERAVMRILS---GiSTLLV-LPTGAGKSLCYQLPALLYAKRSPcLTLVVSPLLSLMDDQVSDLPSCLKA 574
Cdd:NF041063  135 LGFTHYRsPGQREAVRAALLappG-STLIVnLPTGSGKSLVAQAPALLASRQGG-LTLVVVPTVALAIDQERRARELLRR 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  575 A--------CLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVGcgakgpANLPP---AAQLPPVAFACIDEVHCLSQWS 643
Cdd:NF041063  213 AgpdlggplAWHGGLSAEERAAIRQRIRDGTQRILFTSPESLTG------SLRPAlfdAAEAGLLRYLVVDEAHLVDQWG 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  644 HNFRPCY----------LRVCKvlrEHMGVRCFLgLTATATRSTaRDVAQHL-GIAEELE-VSGSasipanlHL----SV 707
Cdd:NF041063  287 DGFRPEFqllaglrrslLRLAP---SGRPFRTLL-LSATLTEST-LDTLETLfGPPGPFIvVSAV-------QLrpepAY 354
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  708 SMDRDSDQAlvtllqgDRFRT-LDSI-------IIYCARRKDTERVAALLRtclstvrdSKPRGRgpetlAEAYHAGMCS 779
Cdd:NF041063  355 WVAKCDSEE-------ERRERvLEALrhlprplILYVTKVEDAEAWLQRLR--------AAGFRR-----VALFHGDTPD 414
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672059437  780 QERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHPQ 850
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 ...
501-687 4.01e-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: 4.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  501 GHHTFR-PGQERAVMRILSGISTLLV-LPTGAGKSLCYQLPALLYAKrspcLTLVVSPLLSLMDDQVSDLPSC-LKAACL 577
Cdd:cd18014     9 GHSDFKsPLQEKATMAVVKGNKDVFVcMPTGAGKSLCYQLPALLAKG----ITIVISPLIALIQDQVDHLKTLkIRVDSL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  578 HSGMTKKQRESVLKKVRAA--QVHVLIVSPEAlvgcgAKGPANLPPAAQLPP---VAFACIDEVHCLSQWSHNFRPCYLR 652
Cdd:cd18014    85 NSKLSAQERKRIIADLESEkpQTKFLYITPEM-----AATSSFQPLLSSLVSrnlLSYLVVDEAHCVSQWGHDFRPDYLR 159
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 672059437  653 VCKVLREHMGVRCfLGLTATATRSTARDVAQHLGI 687
Cdd:cd18014   160 LGALRSRYGHVPW-VALTATATPQVQEDIFAQLRL 193
DEXHc_RecQ3 cd18017
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ...
498-687 4.46e-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: 4.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  498 EQLGHHTFRPGQERAVMRIL-SGISTLLVLPTGAGKSLCYQLPALLYAKrspcLTLVVSPLLSLMDDQVSDLPSCLKAAC 576
Cdd:cd18017     6 EYFGHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVLLNS----LTLVISPLISLMEDQVLQLVMSNIPAC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  577 LhsgMTKKQRESVLKKVRAAQVHVLIVSPEAlvgcGAKGPANLPP-AAQLPPVAfacIDEVHCLSQWSHNFRPCYlRVCK 655
Cdd:cd18017    82 F---LGSAQSQNVLDDIKMGKIRVIYVTPEF----VSKGLELLQQlRNGITLIA---IDEAHCVSQWGHDFRSSY-RHLG 150
                         170       180       190
                  ....*....|....*....|....*....|..
gi 672059437  656 VLREHMGVRCFLGLTATATRSTARDVAQHLGI 687
Cdd:cd18017   151 SIRNRLPNVPIVALTATATPSVRDDIIKNLNL 182
DEXHc_RecQ2_BLM cd18016
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ...
499-687 3.92e-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: 3.92e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  499 QLGHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLyakrSPCLTLVVSPLLSLMDDQVSDLPSC-LKAACL 577
Cdd:cd18016    12 KFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACV----SPGVTVVISPLRSLIVDQVQKLTSLdIPATYL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  578 HSGMTKKQRESVLKKVRAAQ--VHVLIVSPEALVGCGAKGPA--NLPPAAQLppvAFACIDEVHCLSQWSHNFRPCYLRV 653
Cdd:cd18016    88 TGDKTDAEATKIYLQLSKKDpiIKLLYVTPEKISASNRLISTleNLYERKLL---ARFVIDEAHCVSQWGHDFRPDYKRL 164
                         170       180       190
                  ....*....|....*....|....*....|....
gi 672059437  654 cKVLREHMGVRCFLGLTATATRSTARDVAQHLGI 687
Cdd:cd18016   165 -NMLRQKFPSVPMMALTATATPRVQKDILNQLKM 197
DEXDc smart00487
DEAD-like helicases superfamily;
497-700 5.79e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 103.73  E-value: 5.79e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437    497 LEQLGHHTFRPGQERAVMRILSGI-STLLVLPTGAGKSLCYQLPALLYAKRSP-CLTLVVSPLLSLMDDQVSDL-----P 569
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRGKgGRVLVLVPTRELAEQWAEELkklgpS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437    570 SCLKAACLHSGMTKKQResvLKKVRAAQVHVLIVSPEALVGCGAKGPANlppaaqLPPVAFACIDEVHCLSQWshNFRPC 649
Cdd:smart00487   81 LGLKVVGLYGGDSKREQ---LRKLESGKTDILVTTPGRLLDLLENDKLS------LSNVDLVILDEAHRLLDG--GFGDQ 149
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|.
gi 672059437    650 YLRVCKVLREHmgvRCFLGLTATATRSTARDVAQHLGIAEELEVSGSASIP 700
Cdd:smart00487  150 LEKLLKLLPKN---VQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPLEP 197
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
506-679 1.61e-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: 1.61e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437   506 RPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPAL--LYAKRSPCLTLVVSPLLSLMDDQVSDL-----PSCLKAACLH 578
Cdd:pfam00270    1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALeaLDKLDNGPQALVLAPTRELAEQIYEELkklgkGLGLKVASLL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437   579 SGMTKKQRESVLKKvraaqVHVLIVSPEALVgcgakgpANLPPAAQLPPVAFACIDEVHCLSQWShnFRPCYLRVCKVLR 658
Cdd:pfam00270   81 GGDSRKEQLEKLKG-----PDILVGTPGRLL-------DLLQERKLLKNLKLLVLDEAHRLLDMG--FGPDLEEILRRLP 146
                          170       180
                   ....*....|....*....|.
gi 672059437   659 EHmgvRCFLGLTATATRSTAR 679
Cdd:pfam00270  147 KK---RQILLLSATLPRNLED 164
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
480-841 3.84e-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: 3.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  480 PGPLGQVADTPA----EVFQVLEQLGHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPAL--LYAKRSPClTLV 553
Cdd:COG1205    28 PAREARYAPWPDwlppELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLeaLLEDPGAT-ALY 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  554 VSPLLSLMDDQVS-------DLPSCLKAACLHSGMTKKQRESVLKkvraaQVHVLIVSPEAL-VGcgakgpanLPPA--- 622
Cdd:COG1205   107 LYPTKALARDQLRrlrelaeALGLGVRVATYDGDTPPEERRWIRE-----HPDIVLTNPDMLhYG--------LLPHhtr 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  623 -AQLppvaFAC-----IDEVHCL-----SQWSHNFRPcYLRVCkvlrEHMGVRC-FLGLTAT-------ATRSTARDVaq 683
Cdd:COG1205   174 wARF----FRNlryvvIDEAHTYrgvfgSHVANVLRR-LRRIC----RHYGSDPqFILASATignpaehAERLTGRPV-- 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  684 hlgiaEELEVSGSAS------------IPANLHLSVSmdRDSDQALVTLLQGDRfRTldsiIIYCARRKDTERVAallrt 751
Cdd:COG1205   243 -----TVVDEDGSPRgertfvlwnpplVDDGIRRSAL--AEAARLLADLVREGL-RT----LVFTRSRRGAELLA----- 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  752 clSTVRDSKPRGRGPETLAeAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAI 831
Cdd:COG1205   306 --RYARRALREPDLADRVA-AYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQA 382
                         410
                  ....*....|
gi 672059437  832 GRAGRDGKPA 841
Cdd:COG1205   383 GRAGRRGQDS 392
HELICc smart00490
helicase superfamily c-terminal domain;
770-838 7.77e-20

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 84.96  E-value: 7.77e-20
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672059437    770 AEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDG 838
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 5.22e-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: 5.22e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 672059437    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 ...
733-841 4.19e-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: 4.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  733 IIYCARRKDTERVAALLRTCLstvrdsKPRGRGPETLAeAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPDV 812
Cdd:cd18797    39 IVFCRSRKLAELLLRYLKARL------VEEGPLASKVA-SYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGL 111
                          90       100
                  ....*....|....*....|....*....
gi 672059437  813 RAVLHLGLPPSFESYVQAIGRAGRDGKPA 841
Cdd:cd18797   112 DAVVLAGYPGSLASLWQQAGRAGRRGKDS 140
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
715-838 3.78e-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: 3.78e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437   715 QALVTLLQGDRFrtlDSIIIYCARRKDTERVAALLRTCLSTVRdskprgrgpetlaeaYHAGMCSQERKRVQQAFMQGHL 794
Cdd:pfam00271    4 EALLELLKKERG---GKVLIFSQTKKTLEAELLLEKEGIKVAR---------------LHGDLSQEEREEILEDFRKGKI 65
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 672059437   795 RMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDG 838
Cdd:pfam00271   66 DVLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
506-846 2.04e-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: 2.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  506 RPGQERAVMRILSGIST-----LLVLPTGAGKSLCyqlpALLYAKR--SPCLTLVVSPLLSLMDDQVSDLPSCLKAACLH 578
Cdd:COG1061    82 RPYQQEALEALLAALERgggrgLVVAPTGTGKTVL----ALALAAEllRGKRVLVLVPRRELLEQWAEELRRFLGDPLAG 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  579 SGmtKKQRESvlkkvraaqvHVLIVSPEALvgcgakgpANLPPAAQLPP-VAFACIDEVHclsqwsHNFRPCYLRVckvl 657
Cdd:COG1061   158 GG--KKDSDA----------PITVATYQSL--------ARRAHLDELGDrFGLVIIDEAH------HAGAPSYRRI---- 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  658 REHMGVRCFLGLTATATRSTARDVAQHL--GIA-----EELEVSGsasIPANLH-LSVSMDRDSDQALVTLLQGDRFRTL 729
Cdd:COG1061   208 LEAFPAAYRLGLTATPFRSDGREILLFLfdGIVyeyslKEAIEDG---YLAPPEyYGIRVDLTDERAEYDALSERLREAL 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  730 DS---------------------IIIYCARRKDTERVAALLRTclstvrdskprgRGPEtlAEAYHAGMCSQERKRVQQA 788
Cdd:COG1061   285 AAdaerkdkilrellrehpddrkTLVFCSSVDHAEALAELLNE------------AGIR--AAVVTGDTPKKEREEILEA 350
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672059437  789 FMQGHLRMVVATVAFGMGLDRPDVRAVLHLGlppSFES---YVQAIGRA--GRDGKPaHCHLF 846
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 ...
711-847 2.21e-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: 2.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  711 RDSDQALVTLLQGDRFRTLDSIIIYCARRKDTERVAALLRTClstvrdskprgrgpETLAEAYHAGMCSQERKRVQQAFM 790
Cdd:cd18787     9 EEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEEL--------------GIKVAALHGDLSQEERERALKKFR 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 672059437  791 QGHLRMVVAT-VAfGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFL 847
Cdd:cd18787    75 SGKVRVLVATdVA-ARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
490-839 2.60e-14

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 76.72  E-value: 2.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  490 PAEVFQVLEQLGHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPA---LLYAKRSPCLTLVVSPL--LSLmddQ 564
Cdd:COG0513    10 SPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLlqrLDPSRPRAPQALILAPTreLAL---Q 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  565 VSD--------LPscLKAACLHSGMT-KKQRESvLKKvraaQVHVLIVSP---EALVGcgaKGPANLppaaqlppvafac 632
Cdd:COG0513    87 VAEelrklakyLG--LRVATVYGGVSiGRQIRA-LKR----GVDIVVATPgrlLDLIE---RGALDL------------- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  633 iDEVHCLsqwshnfrpcylrvckVLRE-----HMG----VRCFLGLT----------ATATRSTARDVAQHLGIAEELEV 693
Cdd:COG0513   144 -SGVETL----------------VLDEadrmlDMGfiedIERILKLLpkerqtllfsATMPPEIRKLAKRYLKNPVRIEV 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  694 SGSASIPANLHLSVSM--DRDSDQALVTLLQGDRFrtlDSIIIYCARRKDTERVAALLRtclstvrdskprGRGPEtlAE 771
Cdd:COG0513   207 APENATAETIEQRYYLvdKRDKLELLRRLLRDEDP---ERAIVFCNTKRGADRLAEKLQ------------KRGIS--AA 269
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672059437  772 AYHAGMcSQ-ERKRVQQAFMQGHLRMVVAT-VAfGMGLDRPDVRAVLHLGLPPSFESYVQAIG---RAGRDGK 839
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 ...
522-672 3.87e-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: 3.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  522 TLLVLPTGAGKSLCYQLPALLYAKRSPCLTLVVSPLLSLMDDQVSDL----PSCLKAACLHSGMTKKQREsvlkKVRAAQ 597
Cdd:cd00046     4 VLITAPTGSGKTLAALLAALLLLLKKGKKVLVLVPTKALALQTAERLrelfGPGIRVAVLVGGSSAEERE----KNKLGD 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672059437  598 VHVLIVSPEALVGCgakgpanLPPAAQL--PPVAFACIDEVHCLSQWSHNFRPCYLRVCKVLREHMGVrcfLGLTAT 672
Cdd:cd00046    80 ADIIIATPDMLLNL-------LLREDRLflKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQV---ILLSAT 146
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
485-852 2.44e-12

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 71.08  E-value: 2.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  485 QVADTP-AEVFQVLEQLGHHTFRPGQERAVMR-ILSGISTLLVLPTGAGKSLCYQLpALLYAKRSPCLTLVVSPLLSLMD 562
Cdd:COG1204     2 KVAELPlEKVIEFLKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAEL-AILKALLNGGKALYIVPLRALAS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  563 DQVSDLPSCLKAACLHSGMTKKQRESVLKkvRAAQVHVLIVSPE---ALVGCGAKgpanlppaaQLPPVAFACIDEVH-- 637
Cdd:COG1204    81 EKYREFKRDFEELGIKVGVSTGDYDSDDE--WLGRYDILVATPEkldSLLRNGPS---------WLRDVDLVVVDEAHli 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  638 -----------CLSqwshnfrpcylrvcKVLREHMGVRcFLGLTATA--------------TRSTARDVAQHLGIA--EE 690
Cdd:COG1204   150 ddesrgptlevLLA--------------RLRRLNPEAQ-IVALSATIgnaeeiaewldaelVKSDWRPVPLNEGVLydGV 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  691 LEVSGSASIPANLHLSVSMDrdsdqalvTLLQGDrfrtldSIIIYCARRKDTERVAALLRTCLSTVRDSKPRGR------ 764
Cdd:COG1204   215 LRFDDGSRRSKDPTLALALD--------LLEEGG------QVLVFVSSRRDAESLAKKLADELKRRLTPEEREEleelae 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  765 ---------GP-ETLAE------AYH-AGMCSQERKRVQQAFMQGHLRMVVAT--VAFGMGLdrPdVRAVL-----HLGL 820
Cdd:COG1204   281 ellevseetHTnEKLADclekgvAFHhAGLPSELRRLVEDAFREGLIKVLVATptLAAGVNL--P-ARRVIirdtkRGGM 357
                         410       420       430
                  ....*....|....*....|....*....|....
gi 672059437  821 PP--SFEsYVQAIGRAGRDGKpahchlflHPQGE 852
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 ...
739-841 3.76e-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: 3.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  739 RKDTERVAALLRtclstvrdSKPRGRGPETLAEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVLHL 818
Cdd:cd18796    48 RSQAERLAQRLR--------ELCPDRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQI 119
                          90       100
                  ....*....|....*....|...
gi 672059437  819 GLPPSFESYVQAIGRAGRDGKPA 841
Cdd:cd18796   120 GSPKSVARLLQRLGRSGHRPGAA 142
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
797-846 6.05e-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: 6.05e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 672059437  797 VVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGK-PAHCHLF 846
Cdd:cd18785    26 LVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKdEGEVILF 76
Drc1-Sld2 pfam11719
DNA replication and checkpoint protein; Genome duplication is precisely regulated by ...
4-170 6.83e-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: 6.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437     4 LATVRARLQDWERAFVRLHGRRPAKEDVEAAPeETRALYREYRNLKQAVSQADDGHRVQ---KQSLAKAAEEEQepscwg 80
Cdd:pfam11719    1 ISQLKAEIKEWERAFAAKNGRKPSKDDIKKNP-EIAKKYKLYSKLKKGESIKTKTPSKPvklEARPKKRKHEST------ 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437    81 shlNRAATQNTQSIPKQSplssiqdygKRLKANLkntlqgGPTLSRklqhQKRSLSIVPTSRPPGPRTESPcPEQANDAL 160
Cdd:pfam11719   74 ---NKSPEKNSQSTPRKS---------KNIKSEL------GPTPQA----NGKVLSLFDLLSTPPKSSPLK-SKEVKTDV 130
                          170
                   ....*....|
gi 672059437   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 ...
731-838 7.67e-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: 7.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  731 SIIIYCARRKDTERVAALLRtclstvrdskprGRGpetlaeAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRP 810
Cdd:cd18795    45 PVLVFCSSRKECEKTAKDLA------------GIA------FHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLP 106
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 672059437  811 DVRAVLhLGLP----------PSFEsYVQAIGRAGRDG 838
Cdd:cd18795   107 ARTVII-KGTQrydgkgyrelSPLE-YLQMIGRAGRPG 142
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
734-835 9.32e-09

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 59.94  E-value: 9.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  734 IYCARRKDTERVAALLRTCLSTVRDSKPRGRG-PETLAEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPDV 812
Cdd:PRK09751  267 LYAARLQRSPSIAVDAAHFESTSGATSNRVQSsDVFIARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAV 346
                          90       100
                  ....*....|....*....|...
gi 672059437  813 RAVLHLGLPPSFESYVQAIGRAG 835
Cdd:PRK09751  347 DLVIQVATPLSVASGLQRIGRAG 369
PTZ00110 PTZ00110
helicase; Provisional
490-849 3.10e-08

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 57.86  E-value: 3.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  490 PAEVFQVLEQLGHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLYAKRSPCL-------TLVVSPLLSLMD 562
Cdd:PTZ00110  138 PDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLrygdgpiVLVLAPTRELAE 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  563 dQVSD------LPSCLKAACLHSGMTKKQRESVLKKvraaQVHVLIVSPEALVGCGAKGPANLPPaaqlppVAFACIDEV 636
Cdd:PTZ00110  218 -QIREqcnkfgASSKIRNTVAYGGVPKRGQIYALRR----GVEILIACPGRLIDFLESNVTNLRR------VTYLVLDEA 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  637 HclSQWSHNFRPCYLRVCKVLREHmgvRCFLGLTATATR---STARDVAQHLGI---AEELEVSGSASIPANLHLsvsMD 710
Cdd:PTZ00110  287 D--RMLDMGFEPQIRKIVSQIRPD---RQTLMWSATWPKevqSLARDLCKEEPVhvnVGSLDLTACHNIKQEVFV---VE 358
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  711 RDSDQALVTLLQGDRFRTLDSIIIYCARRKDTERVAALLRTclstvrDSKPrgrgpetlAEAYHAGMCSQERKRVQQAFM 790
Cdd:PTZ00110  359 EHEKRGKLKMLLQRIMRDGDKILIFVETKKGADFLTKELRL------DGWP--------ALCIHGDKKQEERTWVLNEFK 424
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 672059437  791 QGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHP 849
Cdd:PTZ00110  425 TGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTP 483
PRK13767 PRK13767
ATP-dependent helicase; Provisional
504-835 4.53e-08

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 57.59  E-value: 4.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  504 TFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPAL---------------LYAkrspcltLVVSPLLSLMDD----- 563
Cdd:PRK13767   32 TFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIdelfrlgregeledkVYC-------LYVSPLRALNNDihrnl 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  564 --------QVS-----DLPScLKAACLHSGMTKKQRESVLKKvraaQVHVLIVSPEALvgcgakgpA---NLPPAAQ-LP 626
Cdd:PRK13767  105 eeplteirEIAkergeELPE-IRVAIRTGDTSSYEKQKMLKK----PPHILITTPESL--------AillNSPKFREkLR 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  627 PVAFACIDEVHCLSQwshNFRPCYLRVC-KVLREHMG---VRcfLGLTATAtrSTARDVAQHLGIAEELEVSGSASIpan 702
Cdd:PRK13767  172 TVKWVIVDEIHSLAE---NKRGVHLSLSlERLEELAGgefVR--IGLSATI--EPLEEVAKFLVGYEDDGEPRDCEI--- 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  703 lhLSVSMDRDSDQALVT----LLQGDR-------FRTLDSII-------IYCARRKDTERVAALLRTCLSTVRDskprgr 764
Cdd:PRK13767  242 --VDARFVKPFDIKVISpvddLIHTPAeeisealYETLHELIkehrttlIFTNTRSGAERVLYNLRKRFPEEYD------ 313
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672059437  765 gpETLAEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAG 835
Cdd:PRK13767  314 --EDNIGAHHSSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGRAG 382
PTZ00424 PTZ00424
helicase 45; Provisional
728-860 1.66e-07

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 55.22  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  728 TLDSIIIYCARRKDTERVAALLRTCLSTVrdskprgrgpetlaEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGL 807
Cdd:PTZ00424  266 TITQAIIYCNTRRKVDYLTKKMHERDFTV--------------SCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGI 331
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 672059437  808 DRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHPQG-EDLWELSRH 860
Cdd:PTZ00424  332 DVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDiEQLKEIERH 385
COG1202 COG1202
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
770-836 6.83e-07

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


Pssm-ID: 440815 [Multi-domain]  Cd Length: 790  Bit Score: 53.74  E-value: 6.83e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672059437  770 AEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVlhlglppsFES------------YVQAIGRAGR 836
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 ...
509-568 1.27e-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: 1.27e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672059437  509 QERAVMRILSGISTLLVLPTGAGKSLCYQLPAL--LYAKRSPClTLVVSPLLSLMDDQVSDL 568
Cdd:cd17923     5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILeaLLRDPGSR-ALYLYPTKALAQDQLRSL 65
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
504-835 2.95e-06

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 51.64  E-value: 2.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  504 TFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALL-YAKRSP-------CLTLVVSPLLSL--------------M 561
Cdd:COG1201    24 APTPPQREAWPAIAAGESTLLIAPTGSGKTLAAFLPALDeLARRPRpgelpdgLRVLYISPLKALandiernlrapleeI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  562 DDQVSDLPSCLKAAcLHSGMTKkQREsvlkkvRAAQV----HVLIVSPE--ALVGCGAKGPANLppaAQLPPVAfacIDE 635
Cdd:COG1201   104 GEAAGLPLPEIRVG-VRTGDTP-ASE------RQRQRrrppHILITTPEslALLLTSPDARELL---RGVRTVI---VDE 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  636 VHCL------SQWS------HNFRPCYLRVckvlrehmgvrcfLGLTATAtrstaRD---VAQHLGIAEELE----VSgs 696
Cdd:COG1201   170 IHALagskrgVHLAlslerlRALAPRPLQR-------------IGLSATV-----GPleeVARFLVGYEDPRpvtiVD-- 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  697 ASIPANLHLSV-SMDRDSD--------------QALVTLLQGDRfrtldSIIIYCARRKDTERVAALLRTclstvrdskp 761
Cdd:COG1201   230 AGAGKKPDLEVlVPVEDLIerfpwaghlwphlyPRVLDLIEAHR-----TTLVFTNTRSQAERLFQRLNE---------- 294
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672059437  762 RGRGPETLAEAYHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAG 835
Cdd:COG1201   295 LNPEDALPIAAHHGSLSREQRLEVEEALKAGELRAVVATSSLELGIDIGDVDLVIQVGSPKSVARLLQRIGRAG 368
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
515-604 3.51e-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: 3.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  515 RILSGISTLLVLPTGAGKS---LCYQLPALLYAKRSpcltLVVSPLLSLMDdQVSD--------LPSCLKAACLHSGMTK 583
Cdd:cd17924    28 RLLRGKSFAIIAPTGVGKTtfgLATSLYLASKGKRS----YLIFPTKSLVK-QAYErlskyaekAGVEVKILVYHSRLKK 102
                          90       100
                  ....*....|....*....|.
gi 672059437  584 KQRESVLKKVRAAQVHVLIVS 604
Cdd:cd17924   103 KEKEELLEKIEKGDFDILVTT 123
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
505-672 4.21e-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: 4.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  505 FRPGQERAVMRILSGIST---LLVLPTGAGKSLC-YQLPALLYAKRspclTLVVSPLLSLMDDQVSDLpsclkAACLHSG 580
Cdd:cd17926     1 LRPYQEEALEAWLAHKNNrrgILVLPTGSGKTLTaLALIAYLKELR----TLIVVPTDALLDQWKERF-----EDFLGDS 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  581 MTKKQRESVLKKVRAAQvhVLIVSPEALvgcgakgpANLPPAAQLPPVAFACI--DEVHCLS--QWSHnfrpcylrvckv 656
Cdd:cd17926    72 SIGLIGGGKKKDFDDAN--VVVATYQSL--------SNLAEEEKDLFDQFGLLivDEAHHLPakTFSE------------ 129
                         170
                  ....*....|....*.
gi 672059437  657 LREHMGVRCFLGLTAT 672
Cdd:cd17926   130 ILKELNAKYRLGLTAT 145
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
780-855 7.34e-06

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 50.17  E-value: 7.34e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672059437  780 QERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFLHPQGEDLW 855
Cdd:PLN00206  405 KERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLF 480
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
470-619 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 672059437  470 CPTPVLPLYPpgplgqvADTPAEVFQVLEQLGHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLYAKRSPC 549
Cdd:cd18049    19 CPKPVLNFYE-------ANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPF 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  550 LT-------LVVSPLLSLMdDQVSDLP-----SC-LKAACLHSGMTKKQRESVLKKvraaQVHVLIVSPEALVGCGAKGP 616
Cdd:cd18049    92 LErgdgpicLVLAPTRELA-QQVQQVAaeygrACrLKSTCIYGGAPKGPQIRDLER----GVEICIATPGRLIDFLEAGK 166

                  ...
gi 672059437  617 ANL 619
Cdd:cd18049   167 TNL 169
ResIII pfam04851
Type III restriction enzyme, res subunit;
503-672 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 672059437   503 HTFRPGQERAVMRILSGIST-----LLVLPTGAGKSLCY-QLPALLYAKRSPCLTLVVSPLLSLMDDQVSDLPSCLKAAC 576
Cdd:pfam04851    2 LELRPYQIEAIENLLESIKNgqkrgLIVMATGSGKTLTAaKLIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437   577 LHSGMTKKQResvlKKVRAAQVHVLIVSPEALvgcgakGPANLPPAAQLPPVAFACI--DEVHCL--SQWSH---NFRPC 649
Cdd:pfam04851   82 EIGEIISGDK----KDESVDDNKIVVTTIQSL------YKALELASLELLPDFFDVIiiDEAHRSgaSSYRNileYFKPA 151
                          170       180
                   ....*....|....*....|...
gi 672059437   650 YLrvckvlrehmgvrcfLGLTAT 672
Cdd:pfam04851  152 FL---------------LGLTAT 159
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
504-692 2.84e-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: 2.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  504 TFRPGQERAVMRI-LSGISTLLVLPTGAGKSLCYQLPALLYAKRSPCLTLVVSPLLSLMDDQVSDLPSCLKAACLHSGMt 582
Cdd:cd17921     1 LLNPIQREALRALyLSGDSVLVSAPTSSGKTLIAELAILRALATSGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGL- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  583 kKQRESVLKKVRAAQVHVLIVSPEALVGCGAKGPANLppaaqLPPVAFACIDEVHCLSQWShnfRPCYLRVC--KVLREH 660
Cdd:cd17921    80 -LTGDPSVNKLLLAEADILVATPEKLDLLLRNGGERL-----IQDVRLVVVDEAHLIGDGE---RGVVLELLlsRLLRIN 150
                         170       180       190
                  ....*....|....*....|....*....|..
gi 672059437  661 MGVRcFLGLTATAtrSTARDVAQHLGIAEELE 692
Cdd:cd17921   151 KNAR-FVGLSATL--PNAEDLAEWLGVEDLIR 179
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
782-842 3.58e-05

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 47.66  E-value: 3.58e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672059437  782 RKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAH 842
Cdd:PRK04837  294 RLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGH 354
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
519-608 6.79e-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: 44.50  E-value: 6.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  519 GISTLLVLPTGAGKSLCYQLPALL-YAKR--SPCLTLVVSPLLSLMDDQVSDLPSCLKAACL-------HSGMTKKQRES 588
Cdd:cd17922     1 GRNVLIAAPTGSGKTEAAFLPALSsLADEpeKGVQVLYISPLKALINDQERRLEEPLDEIDLeipvavrHGDTSQSEKAK 80
                          90       100
                  ....*....|....*....|
gi 672059437  589 VLKKVRaaqvHVLIVSPEAL 608
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 ...
470-619 1.24e-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: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  470 CPTPVLPLYPpgplgqvADTPAEVFQVLEQLGHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLYAKRSP- 548
Cdd:cd18050    57 CPKPVFAFHQ-------ANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPy 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  549 --------CLTLVVSPLLSLMDDQVSD---LPSCLKAACLHSGMTKKQRESVLKKvraaQVHVLIVSPEALVGCGAKGPA 617
Cdd:cd18050   130 lergdgpiCLVLAPTRELAQQVQQVADdygKSSRLKSTCIYGGAPKGPQIRDLER----GVEICIATPGRLIDFLEAGKT 205

                  ..
gi 672059437  618 NL 619
Cdd:cd18050   206 NL 207
PRK01172 PRK01172
ATP-dependent DNA helicase;
667-838 2.91e-04

ATP-dependent DNA helicase;


Pssm-ID: 100801 [Multi-domain]  Cd Length: 674  Bit Score: 45.26  E-value: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  667 LGLTATAtrSTARDVAQHLGIAeeLEVSGSASIPANL------HLSVSMDRDSDQALVTLLQgDRFRTLDSIIIYCARRK 740
Cdd:PRK01172  173 LALSATV--SNANELAQWLNAS--LIKSNFRPVPLKLgilyrkRLILDGYERSQVDINSLIK-ETVNDGGQVLVFVSSRK 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  741 DTERVAALLRTCLSTVRDSKPRGRG----PETLAEA-------YHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDR 809
Cdd:PRK01172  248 NAEDYAEMLIQHFPEFNDFKVSSENnnvyDDSLNEMlphgvafHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNL 327
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 672059437  810 P-------DVRAVLHLGLPP-SFESYVQAIGRAGRDG 838
Cdd:PRK01172  328 ParlvivrDITRYGNGGIRYlSNMEIKQMIGRAGRPG 364
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
715-847 3.17e-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: 3.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  715 QALVTLLQGDRFRTLDSI-IIYCARRkDTERV-AALLRTCLSTVRDSKPR---GRGPETlaEAYHAGMCSQERKRVQQAF 789
Cdd:cd18802    10 QKLIEILREYFPKTPDFRgIIFVERR-ATAVVlSRLLKEHPSTLAFIRCGfliGRGNSS--QRKRSLMTQRKQKETLDKF 86
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 672059437  790 MQGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGkpAHCHLFL 847
Cdd:cd18802    87 RDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN--SKYILMV 142
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
495-609 5.31e-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: 5.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  495 QVLEQLGHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPAL------LYAKRSPCLTLVVSPL--LSLmddQVS 566
Cdd:cd00268     3 KALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILekllpePKKKGRGPQALVLAPTreLAM---QIA 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 672059437  567 DL------PSCLKAACLHSGMTKKQRESVLKKvraaQVHVLIVSPEALV 609
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 ...
572-602 5.78e-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: 5.78e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 672059437  572 LKAACLHSGMTKKQRESVLKKVRAAQVHVLI 602
Cdd:cd18787    52 IKVAALHGDLSQEERERALKKFRSGKVRVLV 82
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
690-838 6.44e-04

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 43.75  E-value: 6.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  690 ELEVSGSASIPANLHLSVSMDRDSDQALVTLLQGDRFrtlDSIIIYCARRKDTERVAALLrtclstVRDskprgrgpetl 769
Cdd:PRK01297  299 EIEPENVASDTVEQHVYAVAGSDKYKLLYNLVTQNPW---ERVMVFANRKDEVRRIEERL------VKD----------- 358
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672059437  770 aeAYHAGMCSQE-----RKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDG 838
Cdd:PRK01297  359 --GINAAQLSGDvpqhkRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAG 430
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
538-604 7.83e-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: 7.83e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672059437   538 LPALLYAKRSPClTLVVSPLLSLMDDQVSDLPSCLKAACLHSGMTKKQRESVLKKVRAAQVHVLIVS 604
Cdd:pfam00271    6 LLELLKKERGGK-VLIFSQTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVAT 71
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
714-847 8.15e-04

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 43.68  E-value: 8.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  714 DQALVTLLQGDRFrtlDSIIIYCARRKDTERVA-ALLRTCLSTVrdskprgrgpetlaeAYHAGMCSQERKRVQQAFMQG 792
Cdd:PRK11634  233 NEALVRFLEAEDF---DAAIIFVRTKNATLEVAeALERNGYNSA---------------ALNGDMNQALREQTLERLKDG 294
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 672059437  793 HLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFL 847
Cdd:PRK11634  295 RLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFV 349
PRK00254 PRK00254
ski2-like helicase; Provisional
733-836 1.59e-03

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 42.88  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  733 IIYCARRKDTERVAALLRTCLSTVRDsKPRGRGPETLAEA--------------------YHAGMCSQERKRVQQAFMQG 792
Cdd:PRK00254  242 LVFVNTRRSAEKEALELAKKIKRFLT-KPELRALKELADSleenptneklkkalrggvafHHAGLGRTERVLIEDAFREG 320
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 672059437  793 HLRMVVATVAFGMGLDRPDVRAVL-------HLGLP--PSFESYvQAIGRAGR 836
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 ...
493-605 1.76e-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: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  493 VFQVLEQLGHHTFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALL--------YAKRSPCLTLVVSPLLSL---M 561
Cdd:cd17958     1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIhldlqpipREQRNGPGVLVLTPTRELalqI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 672059437  562 DDQVSD-LPSCLKAACLHSGMTKKQRESVLKKvraaQVHVLIVSP 605
Cdd:cd17958    81 EAECSKySYKGLKSVCVYGGGNRNEQIEDLSK----GVDIIIATP 121
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
509-608 2.35e-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: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  509 QERAVMRILSGISTLLVLPTGAGKSLCYQLP---ALLYAK-------RSPcLTLVVSPLLSLMdDQVS--------DLPs 570
Cdd:cd17948    17 QKQGIPSILRGRNTLCAAETGSGKTLTYLLPiiqRLLRYKllaegpfNAP-RGLVITPSRELA-EQIGsvaqslteGLG- 93
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 672059437  571 cLKAACLHSGMTKKQresvLKKVRAAQVHVLIVSPEAL 608
Cdd:cd17948    94 -LKVKVITGGRTKRQ----IRNPHFEEVDILVATPGAL 126
ZnF_C2HC smart00343
zinc finger;
394-408 2.37e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 36.27  E-value: 2.37e-03
                            10
                    ....*....|....*
gi 672059437    394 TCFRCGQFGHWASQC 408
Cdd:smart00343    1 KCYNCGKEGHIARDC 15
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
498-547 2.45e-03

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


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 42.22  E-value: 2.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 672059437  498 EQLGHHTFRPGQER---AVMRILSGISTLLVL-PTGAGKSLCYQLPALLYAKRS 547
Cdd:COG1199     8 LAFPGFEPRPGQREmaeAVARALAEGRHLLIEaGTGTGKTLAYLVPALLAARET 61
PRK02362 PRK02362
ATP-dependent DNA helicase;
767-852 2.93e-03

ATP-dependent DNA helicase;


Pssm-ID: 235032 [Multi-domain]  Cd Length: 737  Bit Score: 41.87  E-value: 2.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  767 ETLAEA-------YHAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPDVRAVLH--------LGLPP-SFESYVQA 830
Cdd:PRK02362  296 KDLADCvakgaafHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRdyrrydggAGMQPiPVLEYHQM 375
                          90       100
                  ....*....|....*....|..
gi 672059437  831 IGRAGRDGkpahchlfLHPQGE 852
Cdd:PRK02362  376 AGRAGRPG--------LDPYGE 389
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
710-839 3.53e-03

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 41.33  E-value: 3.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  710 DRDSDQALVTLLQgdRFRTlDSIIIYCARRKDTERVAALLRtclstvrdskprGRGPETLAeaYHAGMCSQERKRVQQAF 789
Cdd:PRK11776  226 PDERLPALQRLLL--HHQP-ESCVVFCNTKKECQEVADALN------------AQGFSALA--LHGDLEQRDRDQVLVRF 288
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 672059437  790 MQGHLRMVVAT-VAfGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGK 839
Cdd:PRK11776  289 ANRSCSVLVATdVA-ARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGS 338
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
773-847 6.27e-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: 6.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  773 YHAGMCSQERKRVQQAFM--QGHLRMVVATVAFGMGL-----DRpdvraVLHLGLP--PSFESyvQAIGRAGRDG--KPA 841
Cdd:cd18793    57 LDGSTSSKERQKLVDRFNedPDIRVFLLSTKAGGVGLnltaaNR-----VILYDPWwnPAVEE--QAIDRAHRIGqkKPV 129

                  ....*.
gi 672059437  842 HCHLFL 847
Cdd:cd18793   130 VVYRLI 135
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
529-672 6.65e-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: 6.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059437  529 GAGK-----SLCYQLpalLYAKRSPCLTLVVSPlLSLMDDQVSDL----PScLKAACLHSgmTKKQRESVLKKVRAAQVH 599
Cdd:cd17919    29 GLGKtlqaiAFLAYL---LKEGKERGPVLVVCP-LSVLENWEREFekwtPD-LRVVVYHG--SQRERAQIRAKEKLDKFD 101
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672059437  600 VLIVSPEALVGCgakgpanlppAAQLPPVAFACI--DEVHCL----SQWShnfrpcylRVCKVLREHMgvRcfLGLTAT 672
Cdd:cd17919   102 VVLTTYETLRRD----------KASLRKFRWDLVvvDEAHRLknpkSQLS--------KALKALRAKR--R--LLLTGT 158
HELICc smart00490
helicase superfamily c-terminal domain;
572-604 7.14e-03

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 36.81  E-value: 7.14e-03
                            10        20        30
                    ....*....|....*....|....*....|...
gi 672059437    572 LKAACLHSGMTKKQRESVLKKVRAAQVHVLIVS 604
Cdd:smart00490   12 IKVARLHGGLSQEEREEILDKFNNGKIKVLVAT 44
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
774-845 8.05e-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: 8.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672059437  774 HAGMCSQERKRVQQAFMQGHLRMVVATVAFGMGLDRPD--VRAVLH---LGLppsfESYVQAIGRAGRDGKPAHCHL 845
Cdd:cd18811    68 HGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatVMVIEDaerFGL----SQLHQLRGRVGRGDHQSYCLL 140
zf-CCHC pfam00098
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ...
393-410 9.77e-03

Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.


Pssm-ID: 395050 [Multi-domain]  Cd Length: 18  Bit Score: 34.81  E-value: 9.77e-03
                           10
                   ....*....|....*...
gi 672059437   393 DTCFRCGQFGHWASQCSQ 410
Cdd:pfam00098    1 GKCYNCGEPGHIARDCPK 18
 
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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