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Database: UniProt
Entry: G0WFT3_NAUDC
LinkDB: G0WFT3_NAUDC
Original site: G0WFT3_NAUDC 
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
//
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