ID A0A0D9YMT5_9ORYZ Unreviewed; 1016 AA.
AC A0A0D9YMT5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=SUPPRESSOR OF ABI3-5 {ECO:0008006|Google:ProtNLM};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM02G04950.3};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM02G04950.3}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM02G04950.3}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR AlphaFoldDB; A0A0D9YMT5; -.
DR EnsemblPlants; OGLUM02G04950.3; OGLUM02G04950.3; OGLUM02G04950.
DR Gramene; OGLUM02G04950.3; OGLUM02G04950.3; OGLUM02G04950.
DR Proteomes; UP000026961; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd16166; OCRE_SUA_like; 1.
DR CDD; cd12313; RRM1_RRM2_RBM5_like; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 1.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR041591; OCRE.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR035623; SUA-like_OCRE.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR13948:SF3; FI21118P1; 1.
DR PANTHER; PTHR13948; RNA-BINDING PROTEIN; 1.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF17780; OCRE; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS50102; RRM; 2.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT DOMAIN 280..360
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 383..416
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 448..528
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 939..985
FT /note="G-patch"
FT /evidence="ECO:0000259|PROSITE:PS50174"
FT REGION 203..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 975..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..875
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1016 AA; 112918 MW; 0B03264F99F00568 CRC64;
MDHGRYAPQH GWENNSALDG YGVINGPDYR AGGSYNGRRF VDDGFPGDSY GRGAFYQDTH
DRNVYPPAPS VPMLSQPRRF HDDEYSTARD YRRHDTYHCN DGKHHEFESY GGVDILHDNY
AADNYESGSY RDFGFDRNKR IGSRDRAEFH GDFEDRYLSS HQSREDSYER DRDYDRYSYD
SDYEKSRRDG SWRRRDLCES EHERRGLSHE RDRSPYMQHS RSRSRGRDER SRSRSRSRSP
RGKSRGRNQR DGFYDDNSFG RRREYDWDER RHGDLVAPSA TVVVKGLSQK TNEDDLNQIL
AEWGPLRSVR VIKERSSGMS RGFAFIDFPT VEAARRMMEG VGDNGLLIDG RKVFFQYSSK
PTSGMSGPSH GEENFTRYNY GHRTAAAPCD WICTICGCMN FARRTSCFQC NEPRTEDSLP
ADPTSSTPLH PKRGSELGKA LFFYCPTHVL VVRGLDENAD EEMLRYEFAK HAPIKDIRLV
RDKFTHVSRG FAFIHFHSVE EATKALEATN GITLEKNGQV LRVTYAKSTH GPVSGASQSN
SLAAAAIEAA SFSQQYDAIG WAPKEYNPDD KLNSNSEPQS SGSAPQSGFV WDEKSGYYYD
SASGFYYDGN TGLYYDGNAG VWYSYDQQTQ QYVPCSEQNS SKAAGDMANT STKTSESSGK
NVVISAPAAT IKQSEKTSLP EAVQAAASAA LAAEKKEKER AKEIKLASKG SLLANKKKMN
NVLAMWKQRN QEGQAGRAIL DDKEPSNSAD DKLNNLHNST GFAVKAKPKS DVGNAKDMNS
PASYNSLGRT AAPTEMIDSD IKPTPVSNSL GTTIMGVIRG SGRGIVRSDT AFHAPSDAGG
ADSFSNIPTS TWSGKRRFSE APGHSQYRDR AAERRNLYGS SSSLGSDNDG LDPTGEYPRR
GPSEMGSMPF PPGVGERSSG EIGNTENYEV ITADRAIDES NVGNRILRNM GWQEGLGLGK
TGSGIKEPVQ AKSVDVRAGL GSQQRKSSDP SLEAQAGDSY KTIIQKKAMA RFREMS
//
