ID H0GEL7_SACCK Unreviewed; 904 AA.
AC H0GEL7;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Siz1p {ECO:0000313|EMBL:EHN07701.1};
GN ORFNames=VIN7_1101 {ECO:0000313|EMBL:EHN07701.1};
OS Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
OS (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1095631 {ECO:0000313|EMBL:EHN07701.1, ECO:0000313|Proteomes:UP000009009};
RN [1] {ECO:0000313|EMBL:EHN07701.1, ECO:0000313|Proteomes:UP000009009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VIN7 {ECO:0000313|EMBL:EHN07701.1,
RC ECO:0000313|Proteomes:UP000009009};
RX PubMed=22136070; DOI=10.1111/j.1567-1364.2011.00773.x;
RA Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA Pretorius I.S., Egholm M., Chambers P.J.;
RT "The genome sequence of the wine yeast VIN7 reveals an allotriploid hybrid
RT genome with Saccharomyces cerevisiae and Saccharomyces kudriavzevii
RT origins.";
RL FEMS Yeast Res. 12:88-96(2012).
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- SIMILARITY: Belongs to the PIAS family.
CC {ECO:0000256|ARBA:ARBA00005383}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHN07701.1}.
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DR EMBL; AGVY01000015; EHN07701.1; -; Genomic_DNA.
DR HOGENOM; CLU_014307_0_0_1; -.
DR PhylomeDB; H0GEL7; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000009009; Unassembled WGS sequence.
DR GO; GO:0019789; F:SUMO transferase activity; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
DR CDD; cd16793; SP-RING_ScSiz-like; 1.
DR Gene3D; 2.60.120.780; PINIT domain; 1.
DR Gene3D; 1.10.720.30; SAP domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR023321; PINIT.
DR InterPro; IPR038654; PINIT_sf.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR031141; SIZ1/2_SP-RING.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10782:SF97; SUPPRESSOR OF VARIEGATION 2-10, ISOFORM I; 1.
DR PANTHER; PTHR10782; ZINC FINGER MIZ DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF14324; PINIT; 1.
DR Pfam; PF02037; SAP; 1.
DR Pfam; PF02891; zf-MIZ; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF68906; SAP domain; 1.
DR PROSITE; PS51466; PINIT; 1.
DR PROSITE; PS50800; SAP; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00452}.
FT DOMAIN 34..68
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT DOMAIN 162..314
FT /note="PINIT"
FT /evidence="ECO:0000259|PROSITE:PS51466"
FT DOMAIN 344..431
FT /note="SP-RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51044"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 904 AA; 100794 MW; AA99F960D943497B CRC64;
MINLEDYWED ETPGPDREPT NELRNEVEET ITLMELLKVS ELKDICRSVS FPVSGRKAVL
QDLIRNFLQN ALVVGKSDPY RVQAVKFLIE RIRKNEPLPV YKDLWNALRK GTPLSAITVR
SMEGPPTVQQ QSPSVIRQSP TQRRKTSTTS STSRAPPPTN PDASSSSSSF AVPTIHFKES
PFYKIQRLIP ELVMNVEVTG GRGMCSAKFK LSKADYNLLS NPXSKHRLYL FSGMINPLGS
RGNEPIQFPF PNELRCNNVQ IKDNIRGFKS KPGTAKPADL TPHLKPYTQQ NNVELIYAFT
TKEYKLFGYI VEMITPEQLL EKVLEHPKII KQATLLYLKK TLREDEEMGL TTTSTIMSLQ
CPISYTRMKY PSKSINCKHL QCFDALWFLH SQLQIPTWQC PVCQIDIALE NLAISEFVDD
ILQNCQKNVE QVELTSDGKW TAILEDDDDS DSDSNDGSRS PEKGTSVSDH HCSSSHPSEP
IIINLDSDDD EPNGNNPHVT NNHDDSNRHS NDNNNNSIKN NDSHNKNNNN NNNNNNNNND
NNNSIENNDS NSNNKHDHGS RSNTPSHNHT KNLMNDNDDD DDDRLMAEIT SNHLKSTNTD
ILTEKGSSAP SRTLDPKSYN IVASETTTPV TNRVIPEYLG NSSSYIGKQL PNILGKTPLN
VTAVDNSSHL ISPDVSVSSP TPRNTASNAS SSALSTPPLI RMSSLDPRGS TVPDKTIRPP
INSNSYTASI SDSFVQPQES SVFPPREQNM DMSFPSTVNS RFNDPRLNTT RFPDSTLRGA
TILSNNGLDQ RNNSLPTTEA ITRNDVGRQN STPVLPTLPQ NVPIRTNSNK SGLPLINNEN
SVPNPPNTAT IPLQKSRLIV NPFIPRRPYS NVLPQKRQLS NTSSTSPIMG TWKTQDYGKK
YNSG
//
