ID A3GFG8_PICST Unreviewed; 1643 AA.
AC A3GFG8;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 2.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAZ63754.2};
GN Name=SIZ1 {ECO:0000313|EMBL:EAZ63754.2};
GN ORFNames=PICST_28241 {ECO:0000313|EMBL:EAZ63754.2};
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:EAZ63754.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:EAZ63754.2, 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 -!- 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:EAZ63754.2}.
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DR EMBL; AAVQ01000001; EAZ63754.2; -; Genomic_DNA.
DR RefSeq; XP_001387777.2; XM_001387740.1.
DR STRING; 322104.A3GFG8; -.
DR GeneID; 4851017; -.
DR KEGG; pic:PICST_28241; -.
DR eggNOG; KOG2169; Eukaryota.
DR HOGENOM; CLU_242741_0_0_1; -.
DR InParanoid; A3GFG8; -.
DR OMA; NIFITSH; -.
DR OrthoDB; 20246at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000002258; Chromosome 1.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.120.780; PINIT 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; 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; SSF101447; Formin homology 2 domain (FH2 domain); 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002258};
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 20..54
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT DOMAIN 149..300
FT /note="PINIT"
FT /evidence="ECO:0000259|PROSITE:PS51466"
FT DOMAIN 329..414
FT /note="SP-RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51044"
FT REGION 112..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1381..1482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1608..1643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1187..1221
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1280..1311
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 423..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..606
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..884
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1425..1442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1608..1623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1643 AA; 179312 MW; 51A91496A4A8D4BD CRC64;
MSSDIARLTP TEFSDTIARL NQMKVAEIKD ILRSLDFKLT GRRHEVIARI EDYFKHGIEL
QDPVRLLAVR VLILMRGEGR QLPIYKDLYR KISKGEFVPG QMNNFATMMS SSGRNVTRQN
GNVNATNQNS NSSRSHSNHS GSDSNHNQYG VNESSPYRRH ALYFADNPFY KLRRLIHGSP
QPCFPQSGRG TCDIAFSLSD SESSLLASDS TIKAYVLCGV QANSSPASTD VAVHFPQPCE
LHVNGSQVQH FRGIKNKIGT SKPADITNHL RARPALNKIQ FVYTRTTETF LLYVYIVQTV
SIQEILQGIL NRPMIHKNST RDRIRAQNDD DDIVVSDISV TLRDPVSYTR MKYPVQSVYC
DHTQCFDALI FLQSQAQIPT WSCPYCQRNV KVDDLAISEY FTDILNTVSA DVEQVLIHSD
GSWSLEGSAT PAPRSNTPAR SPSSSPRVVT KIEEDANSSI PPDVEIVSLD SESESESEIP
LSNIPRRHHP QAISRDSSTS PIQRDDSPQI SETTRPLALV NPPEATVQPQ HVSMDVNDIS
GVGNSVPPVR TVPTASDVSV ASGIAIGSIV TPASTSASQV PTAIAPSPPP PPPPPPPPPP
PPPSSHLQET SASNYIATQL PLPSVLSQSQ STSSESPLVP PPLQPPREHP QSNIHKSHSH
SNTPSASNHL VKLDSHPFKD KNVSATAFSS TIPSTTDDSH MEIDSDTPIS SIHAPTQSSS
HLSSQIPLHS TTNPTTQPLT EEPPHLSSTT PVKRPTGARS KPTPNIFITS HSRLNNRPIY
RPKPATGKRP LQEANIRVDN NLRILTARNP AISARSENAS SPSISASKKT RTENSSSEMS
SERTTVEVSA SSSSEKSSSE SSLEKSHPPP PPPPPPPPPP PVSDNSTNNS NQSEHTSSTE
NSQTQDQPAI ENHSQNNNSA VEHSHAVGMT ISNERSSENQ KSVEELPVNT IPSGRPSTTI
DSQVRSAHVT SESFKSQHIS LAKSINVVAT AANVTSSTSS TAQKASETNG TGKELTLAGD
TFIGDSQKEV TAKKNANTSA VILSLPSPIN SSTSHADGVE DKNGIHSAVI GRSAESTLRP
TENLPMASSP SNNGTGIRAD IVQHSKTTSP LSALEVNNDN STITPDLCID KIRPGVTSHS
EAPSADKLRH SVARMIEIEQ QLQGVRNVRN QQCADSREHI ISYNDYLQES ANAILQLKDL
MTQLEQQSRI QTHQLVALQD EQLQEKGNLE MKIAASLLNS PEKESRVSYP DIFRKALEDQ
EKNRSQRKRH EFDVQRQALV ERHRLQLKTL QERQQQEKDI LSEQVRRLVV EVDSRKSLSV
GNVFSHVLDL PEFQQLKAHI KSMTPFAASP SLSTNYGSVS SESGMRSISY ANLAPSQKGN
SLIAPNSNHG YSISLSPDIR RGHEQQQLSH SQIQQQISQL QPESRHARLS EEQLKQSMKR
HDPSFGRSVV STRYEQPLHS SQAATVSQSQ TPTPTPSLQR YASMPTVQYS KSVFDRVADR
TSSASESPAL KKQRITGLLG IELNQDAISS NVTVTDPVSP INGKIGHMTI NSPVSTRHLS
IGSRNFTAIE SPREPGNRRV SDGSVPPQIH AGVARNVPEG FITEVFRQKN TESNKSTSAP
TAANVDHKAG MEVISLLSDS EEE
//
