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Database: UniProt
Entry: G0WCL6_NAUDC
LinkDB: G0WCL6_NAUDC
Original site: G0WCL6_NAUDC 
ID   G0WCL6_NAUDC            Unreviewed;      1084 AA.
AC   G0WCL6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   03-MAY-2023, entry version 68.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CCD25527.1};
GN   Name=NDAI0F02090 {ECO:0000313|EMBL:CCD25527.1};
GN   OrderedLocusNames=NDAI_0F02090 {ECO:0000313|EMBL:CCD25527.1};
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:CCD25527.1, ECO:0000313|Proteomes:UP000000689};
RN   [1] {ECO:0000313|EMBL:CCD25527.1, 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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC       {ECO:0000256|ARBA:ARBA00009687}.
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DR   EMBL; HE580272; CCD25527.1; -; Genomic_DNA.
DR   RefSeq; XP_003670770.1; XM_003670722.1.
DR   AlphaFoldDB; G0WCL6; -.
DR   STRING; 1071378.G0WCL6; -.
DR   GeneID; 11496865; -.
DR   KEGG; ndi:NDAI_0F02090; -.
DR   eggNOG; KOG0385; Eukaryota.
DR   HOGENOM; CLU_000315_0_2_1; -.
DR   OMA; EFQFRES; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000000689; Chromosome 6.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProt.
DR   CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR   CDD; cd00167; SANT; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR   Gene3D; 1.20.5.1190; iswi atpase; 1.
DR   Gene3D; 1.10.1040.30; ISWI, HAND domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR044754; Isw1/2_DEXHc.
DR   InterPro; IPR015194; ISWI_HAND-dom.
DR   InterPro; IPR036306; ISWI_HAND-dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   InterPro; IPR015195; SLIDE.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   PANTHER; PTHR45623:SF49; ISW-1; 1.
DR   Pfam; PF09110; HAND; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF09111; SLIDE; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51293; SANT; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000689}.
FT   DOMAIN          153..318
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          451..602
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          838..891
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          84..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1026..1052
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          896..923
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..122
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1084 AA;  126165 MW;  97678AC50619C028 CRC64;
     MEDETSYQDR LTPFKEEGDP IPKWGPKQYL LPNANGKHFD VEGTTKRFKH LLSLSGLFRH
     FIESKASKDP KFKKVLESLD DDAFKGKSSD GDRRRRKTER EEDAELLKEE EQAEEESDLE
     NGTEGVEFQF RESPGFINGQ LRTYQIQGLN WLISLHHYKL AGILADEMGL GKTLQTISFL
     GYLRYVEKIP GPFIVIAPKS TLNNWLREIN KWTPEVDAFI LQGDKDERNQ LVKERLLPCK
     FDVVIASYEI VIKEKSSFRK FDWQYIIIDE AHRIKNEESL LSQVLREFTS SNRLLITGTP
     LQNNLHELWA LLNFLLPDIF ADSQDFDEWF SSETTEDDQD KIVKQLHTVL QPFLLRRLKN
     DVETSLLPKK ELNLYVGMSS MQKKWYKQIL EKDIDAVNGS NVNKESKTRL LNIVMQLRKC
     CNHPYLFDGA EPGPPYTTDE HLIYNSAKLK VLDKLLKKMK EEGSRVLIFS QMSRVLDILE
     DYCYFRGYKY CRIDGSTDHE DRIQAIDDYN APDSEKFIFL LTTRAGGLGI NLTSANIVVL
     YDSDWNPQAD LQAMDRAHRI GQKKQVRVFR LVTNNSVEEK ILERATQKLR LDQLVIQQNR
     TSLKKKKETK KESKDALLSM IQHGAADVFQ SGTSVSTSTA VSSRNTPQPD PDAADDIDLD
     SILALSENKT QSLNAKYESL GLDDLQKFNQ DSAYEWNGQD FKKKVQKNII DPTWIHPAKR
     ERKENYSVDG YYKDVLQTGG RSSTPSHTRM PKLHYFSSHQ LQPVQLKVLY EKERLWNAKK
     ARYIPTMDDF KSVFGNEDSL SETEDVKEQK LNMLRLSVEN AQPLTEEEER LKAEWEVQGF
     TNWNKIEFRK FVNASGKYGR NSIQAIAMDL EQTKTVEEVR EYAKAFWANL EMLEDYEKYL
     KIIETEEEKV NKLKYQQEAL RRKLAQYQNP MFELEFLHPP KYFSKEQDVF LLLMLFKYGL
     DRSDVYDLMK DEIRDCPLFE IDFGFKSKTS TELARRTQVL LQCLEREFNQ PIALTNEVKL
     RMEEEDERGK RMREEYEQEN DTSNIEEDRS IKKATSDLNG VVGLIDEKVD AVDVQEDVET
     PTVT
//
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