ID R9X974_ASHAC Unreviewed; 897 AA.
AC R9X974;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=AaceriAAR121Wp {ECO:0000313|EMBL:AGO10113.1};
GN ORFNames=AACERI_AaceriAAR121W {ECO:0000313|EMBL:AGO10113.1};
OS Ashbya aceri (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=566037 {ECO:0000313|EMBL:AGO10113.1, ECO:0000313|Proteomes:UP000016920};
RN [1] {ECO:0000313|Proteomes:UP000016920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- SIMILARITY: Belongs to the PIAS family.
CC {ECO:0000256|ARBA:ARBA00005383}.
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DR EMBL; CP006020; AGO10113.1; -; Genomic_DNA.
DR AlphaFoldDB; R9X974; -.
DR HOGENOM; CLU_014307_0_0_1; -.
DR OrthoDB; 20246at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000016920; Chromosome I.
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; 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; 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 16..50
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT DOMAIN 127..274
FT /note="PINIT"
FT /evidence="ECO:0000259|PROSITE:PS51466"
FT DOMAIN 306..391
FT /note="SP-RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51044"
FT REGION 103..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..832
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 897 AA; 97734 MW; 6161F7501E87A9B4 CRC64;
MSTPIKYDIQ QTCHEMSLLR VPELKAVCRS IGLPLSGRKA DLQARIKEYV ENSLRPNHVD
PFRPKAIMAL IQKSKVGDVL PTYESILQAL RTGAFTHPVA TGHAPPSSLF SPGSVDGVPR
EEVGDHQTPR AAGRKGSPSS VFFPSPFYNL KRMVSGSPKM AAKSPGRGTC NMKFKLSETE
SKLILDSKDT KLLLFCGPVS QGNRVHIQFP HPNEIKLNDN MIKDNVRGLK NKIGTAKPAD
LTPFVKHNAE NYLQLVYAFT KEDFLVYIYI VTMNTPETIL EGVLARPKIV KPATLAYIKK
ILSEDEDDDL MTTSTIMTLQ CPISYSRMKY PVKSVRCDHL QCFDAMSFIL SQMQIPTWQC
PVCQKQIEIK DLAVCDYVDD IIKSSGENVE QVVINSDGSW VAKEEETENR PGKSSDSEQP
AQTNIKDEDI DQVILDEEMS TKKAVNEPIV ISLDSDDEDD DVSLAEELAK LKNHPQPHAN
GNTSPPKQSR TPDSLLNGKI SRASSVPLAT EQATSFGANE RPLTSSSGNS TLNQTFSSEV
SARITSVPSQ SADSLSNGSG MLSNQPVITT PNHSLQDSAR STVGRLPRDM PATNLHRVLT
EYSQNGHFSA QHDAALSNLS PKTRVETRPS TSSSSSTGPQ QRASIPNILG STPLSNQNRT
PDHRLARNTS IHENPRLELN GDQSLLFSGN TGQTAANSMG IPSSENSRRN NSHDQSQYIL
HSNAFHSNGT PSEPSHNSSP GITTAPANVD STNTRSTIRG PSADVPHESI EQLKLAPRVS
GESSVRSLSP HHSTDPVLPV STVSANVRPP ILPPLPPIQR PLISPSPPID DAPSGYYPAR
QDHSKTYPSG NARHKKPPVS PFIPRKYSSV VPKKRLLSTS DGTTKGDTNS ACTNHGD
//
