ID A0A0D3FNB3_9ORYZ Unreviewed; 860 AA.
AC A0A0D3FNB3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=SP-RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Oryza barthii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART03G32110.1};
RN [1] {ECO:0000313|EnsemblPlants:OBART03G32110.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART03G32110.1};
RX DOI=10.1007/s12284-009-9025-z;
RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA Knight J., Niazi F., Egholm M., Wing R.A.;
RT "De novo next generation sequencing of plant genomes.";
RL Rice 2:35-43(2009).
RN [2] {ECO:0000313|EnsemblPlants:OBART03G32110.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
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 AlphaFoldDB; A0A0D3FNB3; -.
DR STRING; 65489.A0A0D3FNB3; -.
DR PaxDb; 65489-OBART03G32110-1; -.
DR EnsemblPlants; OBART03G32110.1; OBART03G32110.1; OBART03G32110.
DR Gramene; OBART03G32110.1; OBART03G32110.1; OBART03G32110.
DR eggNOG; KOG2169; Eukaryota.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000026960; Chromosome 3.
DR GO; GO:0061665; F:SUMO ligase activity; IEA:EnsemblPlants.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
DR CDD; cd15570; PHD_Bye1p_SIZ1_like; 1.
DR CDD; cd16792; SP-RING_Siz-like; 1.
DR Gene3D; 1.10.720.30; SAP domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR031141; SIZ1/2_SP-RING.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10782:SF42; E3 SUMO-PROTEIN LIGASE SIZ2; 1.
DR PANTHER; PTHR10782; ZINC FINGER MIZ DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02037; SAP; 1.
DR Pfam; PF02891; zf-MIZ; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF68906; SAP domain; 1.
DR PROSITE; PS50800; SAP; 1.
DR PROSITE; PS01359; ZF_PHD_1; 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 Reference proteome {ECO:0000313|Proteomes:UP000026960};
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 18..52
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT DOMAIN 404..487
FT /note="SP-RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51044"
FT REGION 88..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 860 AA; 95031 MW; B3367A87A86B4F3D CRC64;
MALDPADDPL LADCKYKLNH FRIKELKDVL HQLGLPKQGR KQELVDKIIA VLSDQQEQDS
RLNGLPNKKM VGKETVAKIV DDTFAKMNGS TNAVPASRNQ TDSGHIVKPK RKSDDSAQLD
VKVRCPCGYS MANDSMIKCE GPQCNTQQHV GCVIISEKPA DSVPPELPPH FYCDMCRITR
ADPFWVTVNH PVLPVSITPC KVASDGSYAV QYFEKTFPLS RANWEMLQKD EYDLQVWCIL
FNDSVPFRMQ WPLHSDIQIN GIPIRVVNRQ PTQQLGVNGR DDGPVLTAYV REGSNKIVLS
RSDSRTFCLG VRIAKRRSVE QLVGYGQNSV DSLSIYNTSW YLGGTWQLLR FRNPVLFIKG
PLNFHSIQVL SLVPKEQDGE NFDNALARVR RCVGGGTEAD NADSDSDIEV VADSVSVNLR
CPMTGSRIKI AGRFKPCVHM GCFDLEAFVE LNQRSRKWQC PICLKNYSLD NIIIDPYFNR
ITALVQSCGD DVSEIDVKPD GSWRVKGGAE LKGLAQWHLP DGTLCMRTDT RSKPNIRIVK
QEIKEEPLSE ETGGRLKLGI RRNNNGQWEI NKRLDSNNVQ NGYIEDENCV VSASNTDDEN
SKNGIYNPEP GQFDQLTSNI YDLDSSPMDA HFPPAPTEQD VIVLSDSDDD NVMVLSPGDV
NFSSAHDNGN AFPPNPPEAS GICGEQPRGA GPDVTSFLDG FDDLELPFWE SSSSQDAAGT
QVTDNQCEMQ NFIVNHQFLH EPILGVNLGG TAASNTLECE HDGALQACQS SDQDGDQNQT
CHDGHSGDLT NLSIISTQDS LTNGKNASQK RTNCEDGTAG LDGSVVRSAN GLRGEMPPLG
QEQDRTVRQK LILTIESDSD
//
