ID G8YTC6_PICSO Unreviewed; 827 AA.
AC G8YTC6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Piso0_000200 protein {ECO:0000313|EMBL:CCE73177.1};
GN Name=Piso0_000200 {ECO:0000313|EMBL:CCE73177.1};
GN ORFNames=GNLVRS01_PISO0B04269g {ECO:0000313|EMBL:CCE73177.1};
OS Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS 10061 / NRRL Y-12695) (Hybrid yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE73177.1, ECO:0000313|Proteomes:UP000005222};
RN [1] {ECO:0000313|Proteomes:UP000005222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(2012).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; FO082058; CCE73177.1; -; Genomic_DNA.
DR AlphaFoldDB; G8YTC6; -.
DR STRING; 559304.G8YTC6; -.
DR eggNOG; KOG1002; Eukaryota.
DR HOGENOM; CLU_000315_2_1_1; -.
DR InParanoid; G8YTC6; -.
DR OMA; LLRYPFC; -.
DR Proteomes; UP000005222; Chromosome B.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd16567; RING-HC_RAD16-like; 1.
DR CDD; cd18793; SF2_C_SNF; 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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF12; DNA REPAIR PROTEIN RAD16; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000005222};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 228..403
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 571..615
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 660..817
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..108
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..166
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 827 AA; 95039 MW; CD68E9F07A4BBA1D CRC64;
MCPVGIEHTE SSSDENLEDL GAGGFIVGDE HFAGNRRRTR RNNSDKTSYK EISSDEDDAV
VASSSNGANK RGRKSNNRPN NKKRIKNSSG DDDDDYHESA DERNAEDDIE ESIQQGHLGT
SVDDAINVSE DEEDDVPLVN RKPPAKKRRR ANEGTKRTRT KKKKEPKVKV PYFTRVTDRL
YENHPELKDV FPYLASVERI KCERAIQPGG MTIKLLPFQL EGLNWLQRQE DGEYGGGVLA
DEMGMGKTIQ TIALFMNDRG NSPNLVVGPT VALMQWKNEI EAHTEPGMLK VLLYHGANRS
TDVDEIRKYD VVLTSYSVLE SVYRKEYYGF KRKGGLVKEK SPLHSIPFYR VILDEAHNIK
DRTSGTAKAA NKLNCKKRWC LTGTPLQNRI GEMYSLIRFL KLDPFYKYFC TKCDCSSDEW
RFSDWRHCDI CDHTPMLHTN FFNHFMLKNI QKYGIEGDGF TSFQNIRLLL NNVMLRRTKL
ERADDLGLPP RVVEIRKDRF NEEEKDLYTS LYSDSKRKFN AYVAEGVVLN NYANIFTLIT
RMRQLADHPD LVLKRVGTNQ ISEEVEGIII CQLCDDEAEE PIESKCHHRF CRMCISEYVE
SFSGNEKNLE CPVCHIGLSI DLQQPALEVD EELFTKASIV NRIKMGAHGG EWRSSTKIEA
LVEELYRLRS DRKTIKSIVF SQFTSMLDLV EWRLKRAGFE TVKLQGSMSP QQRDKTIKHF
MENTQVEVFL VSLKAGGVAL NLCEASQVFI LDPWWNPSVE WQSMDRVHRI GQRRPIRITR
FCIEDSIESK IIELQDKKAN MINATINHDD SAVNRLTPED LQFLFMN
//
