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Database: UniProt
Entry: A0A0D9VIT0_9ORYZ
LinkDB: A0A0D9VIT0_9ORYZ
Original site: A0A0D9VIT0_9ORYZ 
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
//
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