ID G0WFT3_NAUDC Unreviewed; 1434 AA.
AC G0WFT3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=NDAI0I00750 {ECO:0000313|EMBL:CCD26644.1};
GN OrderedLocusNames=NDAI_0I00750 {ECO:0000313|EMBL:CCD26644.1};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD26644.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD26644.1, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446}.
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DR EMBL; HE580275; CCD26644.1; -; Genomic_DNA.
DR RefSeq; XP_003671887.1; XM_003671839.1.
DR STRING; 1071378.G0WFT3; -.
DR GeneID; 11493498; -.
DR KEGG; ndi:NDAI_0I00750; -.
DR eggNOG; KOG0351; Eukaryota.
DR HOGENOM; CLU_001103_22_1_1; -.
DR OMA; LCHKNCD; -.
DR OrthoDB; 5474026at2759; -.
DR Proteomes; UP000000689; Chromosome 9.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd17920; DEXHc_RecQ; 1.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR Gene3D; 1.10.150.80; HRDC domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR022758; Helicase_Sgs1.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR018982; RQC_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF105; BLOOM SYNDROME PROTEIN; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF11408; Helicase_Sgs1; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR Pfam; PF09382; RQC; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00341; HRDC; 1.
DR SMART; SM00956; RQC; 1.
DR SUPFAM; SSF47819; HRDC-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50967; HRDC; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000689}.
FT DOMAIN 677..854
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 861..1025
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1269..1351
FT /note="HRDC"
FT /evidence="ECO:0000259|PROSITE:PS50967"
FT REGION 102..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1403..1434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..394
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1403..1417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1420..1434
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1434 AA; 163180 MW; 733EDEE0F8E1F131 CRC64;
MIVKPSHNLR REHKWLKETN VLQHDKDLVL QIINNNVFPN KRRKQSIPIP QNSTTSNMVE
SVNEDQREEL FLFNANKPLM SPIQEIGLNN NDSTSVRNNQ IINDGTGRIP KGSSSSHIIN
NSNNNNNNHS HFASSPVMPK NAIKPAISQI YLDQTSTPPP PPQPRMSSTS LHDKDTLINL
QKCLIDTLKD QSQTYEEKIS IIESTSLSED NKKYKLSQLI NPKLAKYNIT VSDLETKISN
LLTLLSPATV PPTTQILPNA TTGSNNNFTH SVSTNEKNQQ IITTSETYNL IDALDDDDDD
DDVDPVPINE IEQPRNKEST SITTTAATRS MRTRKAKINY RIPEKDDPFD YKIGKINDSI
NNSNTTHTSF NQFEEEEEDD DDDDDDEEDP EEDGYSSYMN TREEERIEND LLNQSDLDFV
INDEDDAPLL TDDAPFTQAQ SLIQHNENDD ADDDSNESEE FHDAADDLNN IQIILSSPQK
QPIVEPIELL DDDEDDDSFV ATALTPQSNI PRTITTIPHT VPHSDLEDLS SDLDDPSPFD
NDHSDDSGLS DSDLEFFDEE RENRTQLNSI KELDNDLKII TERNLNANEK NNWVPIVIKR
ENSTTTTMPT HTMNLSDNED LENDFSLLED INSPVKNHQQ QQKNNGVTNF PWSNEVKLKL
RQIFKLPGFR PNQEEAVSAT LSGKDVFILM PTGGGKSLCY QLPAVIKSGK TKGTTIVISP
LISLMQDQVQ HLLDKNIKAS MFSSRGTVEE KRQVFNLFIC GLLDVVYISP EMISASEQCK
RAIKRLHSDG KLARVVVDEA HCVSNWGHDF RPDYKELKYF KREYPDVPMM ALTATASEQV
RMDIIHNLEL KDPVFLKQSF NRTNLYYEVR KKNKNTIFEI ADMIKSKFRN QTGIIYCHSK
NSCEQTSNQM QRAGIKSAYY HAGMEPDDRL KIQKAWQADE IQVICATVAF GMGIDKPDVR
FVFHFTVPRT LEGYYQETGR AGRDGKYSYC ITYFCFRDVR TMQTMIQKDE NLDRENKEKH
LNKLQQVMAY CDNATDCRRK LVLSYFNEDF DSKLCHKNCD NCKNSSHAMT EERDITDIAK
QIVTMVEKIQ NDKVTLINCQ DIFKGSRSSK IVQSGYSNLQ QHGQGRKMSK SDIERIFFHL
ITIRLLQEYS VMNKGGFATT YVKVGPSVSK LRDGSLKVTM QFTSSTPATR SASSSSNSPY
SNSNNNYVRR SHTTPLPHTD NDRANSKVMP TFISAKDHLS SYAYTENQSE YSKPISFKDS
TESRSTQELS ALTSAYVKLR EVSLNLGNRM NPPIAHFLSD TSLKKLATNL PITEGQFVAI
PTIGEKQRKK FKYFKSTLLM LRKQRNIAMQ STNINNNLKS QGSSLPEVDT SFGRKSRYFS
IDPEAEKENQ AIINQLRDSQ LQTSVGTRSS YEVGGNNKRR FNKNHKNYYK KKRP
//