ID A0A0D9VIT0_9ORYZ Unreviewed; 880 AA.
AC A0A0D9VIT0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=UBX domain-containing protein {ECO:0000259|PROSITE:PS50033};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR02G20860.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR02G20860.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR02G20860.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR02G20860.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484}.
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DR AlphaFoldDB; A0A0D9VIT0; -.
DR STRING; 77586.A0A0D9VIT0; -.
DR EnsemblPlants; LPERR02G20860.1; LPERR02G20860.1; LPERR02G20860.
DR Gramene; LPERR02G20860.1; LPERR02G20860.1; LPERR02G20860.
DR eggNOG; KOG1208; Eukaryota.
DR eggNOG; KOG1364; Eukaryota.
DR HOGENOM; CLU_315774_0_0_1; -.
DR Proteomes; UP000032180; Chromosome 2.
DR CDD; cd02958; UAS; 1.
DR CDD; cd14273; UBA_TAP-C_like; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR006577; UAS.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR PANTHER; PTHR43490; (+)-NEOMENTHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43490:SF127; OS02G0640800 PROTEIN; 1.
DR Pfam; PF00106; adh_short; 2.
DR Pfam; PF13899; Thioredoxin_7; 1.
DR Pfam; PF14555; UBA_4; 1.
DR PRINTS; PR00081; GDHRDH.
DR SMART; SM00594; UAS; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50033; UBX; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000032180};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 498..570
FT /note="UBX"
FT /evidence="ECO:0000259|PROSITE:PS50033"
FT REGION 152..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..186
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..262
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 880 AA; 96230 MW; 5457668DE798BCF6 CRC64;
MVDLPRIKRD LTSLEQESSW PHVKAARYLM IWCFRATAAT SRRGGAGLVA TAAGYTKGTK
QKMDNDGAVT TFMEITSCGS RESAVQLLTA CRWDLETAIN RYFVLGGAAF AARVAAPPPA
PPAAAVDDVA PPAGDGDGVR APIAFRSETL YGDAFGRTKP PKVRPPAPSV WGKPKPPPPP
PSTPAVAPVY IGLDLNLPPN NDDDDDEQPG IRRVVGEEEN KEEDGESKLK EQNEQHEDHD
GYSDGDYGME TADDDDDYDG YDDMIEKTPS PPPASSRPKS LAEMYRLPSE LMHEADFHST
KLHAARLDRW LLLNLQISGD FTSEMHNRDL WANERIAKIV RENFVFSLLE NGDGDHDDEG
SKVPCFYKLH DQLPAVAVID PVTGQMLAKW SGVIDPEAFL VDIEEFIRSK PSARSKPEMF
RRKPMPVPES SAPAVEIAEQ QDSAMADDTA PTQEPDTTAA AVPMDEQSVA QESTSADACG
MQQQTADDEH DDDDQPMEGE KIYRMRVRFP DGSVVTKEFG CKRRVLVLFN YVRSVLHEKM
QPQAFKIKRL VGAAFLELPQ GGVSFEDLGL NCATEHCTME PGSSNTSSGE KRIAVVTGGN
KGIGLEICKQ LAAKGIFVVL TARDEERGAG AAAALRQLGL SDVLFHELDV TEPSSVACLA
DFIKHKFGKL DILVSNAGNL GVTFDFGNSE LDKAIEGKSP NETLKWLMQH TVETTENAEE
CLRINYHGTT AVIQTLFPLL QLSSDGRIFF SGEKLKEELN DADKLSEERL DELAELFIND
FKNGELESRG WPARRDAFVA YKTSKALQHA YTRVLARRHA SSPLRFNCVH PGYVKTDMTL
GTGELTAEEG AAGPVAVALS PPGGATGVFF IRTEPASFVD
//