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
//