ID A3LZW6_PICST Unreviewed; 1259 AA.
AC A3LZW6;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 2.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Nuclear protein STH1/NPS1 (Chromatin structure remodeling complex protein STH1) (SNF2 homolog) {ECO:0000313|EMBL:ABN68612.2};
DE EC=3.6.1.3 {ECO:0000313|EMBL:ABN68612.2};
GN Name=STH1 {ECO:0000313|EMBL:ABN68612.2};
GN ORFNames=PICST_85702 {ECO:0000313|EMBL:ABN68612.2};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN68612.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN68612.2, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CP000502; ABN68612.2; -; Genomic_DNA.
DR RefSeq; XP_001386641.2; XM_001386604.1.
DR AlphaFoldDB; A3LZW6; -.
DR STRING; 322104.A3LZW6; -.
DR GeneID; 4841094; -.
DR KEGG; pic:PICST_85702; -.
DR eggNOG; KOG0386; Eukaryota.
DR eggNOG; KOG1827; Eukaryota.
DR HOGENOM; CLU_000315_15_3_1; -.
DR InParanoid; A3LZW6; -.
DR OMA; VNYISHT; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000002258; Chromosome 8.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd17996; DEXHc_SMARCA2_SMARCA4; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 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; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029295; SnAC.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799:SF1012; NUCLEAR PROTEIN STH1_NPS1; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF14619; SnAC; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABN68612.2};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002258};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 312..385
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 492..656
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 803..964
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1175..1245
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1152
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1259 AA; 146312 MW; 556C996FC85D3FCA CRC64;
MNGSTTLANG SKDSYPYQQS SSLQNNTIEP VIEIPTTKEQ LTELLERYYK LLRTGQQLKR
EYDEQPPPFF DATEKERILI EKVLATISDK QQQFLDEEAQ FYEEILQESS TKIESQLDKD
IFEKQIASLQ LLSKDIDLPE TIQSELASSV VDVKEDAVSL DSILKSLSTY SQDFQERAKR
LGIKIPVPST SVDPLQAPLG NYYTEKIITS KIANRLRELE NLPGNLGTFG DDVEIDDLKI
KTLIELKSLR LLPKQKQLKH NIIASEASQA KFTLPDLVNN PLCLQEKRSF NVRPKIEQPN
PHLLATQLEE LKQQEEREFQ RQLHIAKIQQ VLDSSSLYST AKSSRYNYRS NILVKQINNF
HQNTEKEESK KLEKTAKQRL QALKANDEEA YIKLLDQTKD HRITHLLKQT NQFLDTLAQQ
VKAQQAETFI EDVPIEEVNG EEIEEDTVDE LREKIDYYQV AHRIKEEISE QPGILIGGKL
KEYQLKGLQW MVSLYNNKLN GILADEMGLG KTIQSISLVT YLIEKKHEDK FLVIVPLSTI
TNWTLEFEKW APSVRVIVYK GSPQQRRSMQ MDIRMGNFQV MLTTYEYIIR ERPLLAKFHY
SHMIIDEGHR MKNASSKLSI TLKQYYKTKN RLILTGTPLQ NNLPELWALL NFVLPRIFNS
VKSFDEWFNT PFANTGAQEK IELTEEESLL VIRRLHKVLR PFLLRRLKKD VEKDLPDKVE
KVLKCNLSGL QYVLYQQMLK HNAFFVGADA GGAKSGIKGL NNKIMQLRKI CNHPFVFEEV
EAVLNSSKLT NDLIWRTSGK FELLDRVLPK FKASGHRVLM FFQMTQVMDI MEDFLRWRDM
KYLRLDGSTK AEDRQEMLKV FNAPNSDYFC FLLSTRAGGL GLNLQTADTV IIFDTDWNPH
QDLQAQDRAH RIGQKNEVRI LRLITNDSVE EVILERAHQK LDIDGKVIQA GKFDNKSTAE
EQEEFLKRLL EAEANGDENE ENDSLDDDEL NEILARSEDE KVLFAEIDGQ RKKDIESHFK
SRLIERDELP TVFTEDISRH FEKDTKELSR MREKKRVKYD DGLTEEQWLM AMDDDNDTVE
DAIRRKEERM ARRRRKAAKD GDLSEDDEED LEDDEDGSDG RRKRQRRSRT PQTYRDEDIY
GEEDEIADPD EKEADELTVK CTAVIDEIMQ LTAEDGHRTS DIFLKLPSRK LYSDYYQIIK
RPVSINQVIK HLQQEKFDTF EAFIAELRLM CENAKIYNEE SSFVYADAAQ IEEVLDRVS
//
