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Database: UniProt/TrEMBL
Entry: M1AV12_SOLTU
LinkDB: M1AV12_SOLTU
Original site: M1AV12_SOLTU 
ID   M1AV12_SOLTU            Unreviewed;       478 AA.
AC   M1AV12;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   07-JUN-2017, entry version 25.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:PGSC0003DMT400030976};
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae;
OC   Solaneae; Solanum.
OX   NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400030976, ECO:0000313|Proteomes:UP000011115};
RN   [1] {ECO:0000313|EnsemblPlants:PGSC0003DMT400030976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DM1-3 516 R44
RC   {ECO:0000313|EnsemblPlants:PGSC0003DMT400030976};
RX   PubMed=21743474; DOI=10.1038/nature10158;
RG   The Potato Genome Sequencing Consortium;
RT   "Genome sequence and analysis of the tuber crop potato.";
RL   Nature 475:189-195(2011).
RN   [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400030976}
RP   IDENTIFICATION.
RC   STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400030976};
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   RefSeq; XP_006363610.1; XM_006363548.2.
DR   ProteinModelPortal; M1AV12; -.
DR   STRING; 4113.PGSC0003DMT400030976; -.
DR   EnsemblPlants; PGSC0003DMT400030976; PGSC0003DMT400030976; PGSC0003DMG400011868.
DR   GeneID; 102589300; -.
DR   Gramene; PGSC0003DMT400030976; PGSC0003DMT400030976; PGSC0003DMG400011868.
DR   KEGG; sot:102589300; -.
DR   eggNOG; KOG1404; Eukaryota.
DR   eggNOG; COG0160; LUCA.
DR   InParanoid; M1AV12; -.
DR   KO; K00827; -.
DR   OMA; YHGVNIA; -.
DR   OrthoDB; EOG09360AH6; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000011115};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011115}.
SQ   SEQUENCE   478 AA;  52216 MW;  D28ADCD7F47246DA CRC64;
     MQRFVTARAK WVGELRGLSQ RCYSQFGLAS QKDDDMIINP RMPHFDYSPP PYNGPSADEI
     LSKRKEFLSP SMFYFYEKNP LHLVHGKMQY LFDSNGRRYL DAFGGIATVS CGHCHPDVVE
     AIVNQTKRLQ HSTILYLNNA ITDFAEALAS KLPGDLKVVF FTNSGTEANE LAIMMARLYT
     GCHDIISLRN AYHGNAAATM STTGQSVWKF NVVQSGVHHA INPDPYRGVF GSDGEKYAKD
     VEDLILFGTS GRVAAFMSEA IQGVGGIVEL APGYLPAAYS AVRKAGGLCI ADEVQSGFAR
     TGSHFWGFEN QGVVPDIVTM AKGIGNGIPL GAVVTTPEIA EVLCHSNYFN TFGGNPVCTS
     AGLAVLRVIE KENLQENAHV VGSYLKERLM AIKNKHEIVG DVRGRGLLLG VELVTDRKLK
     TPAKAETLHI MDKMKEMGVL VGKGGFRGNV FRITPPLCFT KEDADFVADV MDCAMSKI
//
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