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Database: UniProt
Entry: A0A1S3V7N3_VIGRR
LinkDB: A0A1S3V7N3_VIGRR
Original site: A0A1S3V7N3_VIGRR 
ID   A0A1S3V7N3_VIGRR        Unreviewed;       523 AA.
AC   A0A1S3V7N3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   12-SEP-2018, entry version 9.
DE   SubName: Full=probable aspartyl aminopeptidase {ECO:0000313|RefSeq:XP_014514300.1};
GN   Name=LOC106772421 {ECO:0000313|RefSeq:XP_014514300.1};
OS   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
OC   50 kb inversion clade; NPAAA clade; indigoferoid/millettioid clade;
OC   Phaseoleae; Vigna.
OX   NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014514300.1};
RN   [1] {ECO:0000313|Proteomes:UP000087766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. VC1973A {ECO:0000313|Proteomes:UP000087766};
RX   PubMed=25384727; DOI=10.1038/ncomms6443;
RA   Kang Y.J., Kim S.K., Kim M.Y., Lestari P., Kim K.H., Ha B.K.,
RA   Jun T.H., Hwang W.J., Lee T., Lee J., Shim S., Yoon M.Y., Jang Y.E.,
RA   Han K.S., Taeprayoon P., Yoon N., Somta P., Tanya P., Kim K.S.,
RA   Gwag J.G., Moon J.K., Lee Y.H., Park B.S., Bombarely A., Doyle J.J.,
RA   Jackson S.A., Schafleitner R., Srinives P., Varshney R.K., Lee S.H.;
RT   "Genome sequence of mungbean and insights into evolution within Vigna
RT   species.";
RL   Nat. Commun. 5:5443-5443(2014).
RN   [2] {ECO:0000313|RefSeq:XP_014514300.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_014514300.1};
RG   RefSeq;
RL   Submitted (JUN-2017) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   RefSeq; XP_014514300.1; XM_014658814.1.
DR   GeneID; 106772421; -.
DR   KEGG; vra:106772421; -.
DR   KO; K01267; -.
DR   Proteomes; UP000087766; Genome assembly.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 2.30.250.10; -; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|RefSeq:XP_014514300.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000087766};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087766};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   523 AA;  57913 MW;  CCCAB47BECFE4034 CRC64;
     MTSITGPQIL LHSRSPSLKL KLKPSSAFLL FPNPPFSAKC TRRRAFCSIN SNSKPQASTS
     IVPDLLHYLN HSWTQFHATA EAKRQLLAAG FHMLNENQDW DLKPGGRYFF TRNMSCLVAF
     AVGEKYNVGD AFHVIAAHTD SPCLKLKPKT ASCKCNYSMV NVQTYGAGLW YTWFDRDLSV
     AGRVILRNGH NSFVHKLVKV DRPILRIPTL AIHLDRTVNQ DGFKPNLETH LLPLLSIKPE
     DTSLESKEKN SALSSKSYHH SLLMQVLSDE LNCDVDDIVN IELNVCDTQP SCLGGGNSEF
     IFSGRLDNLA SSYCALRALI DSCESPGNLA SEHAIRMVAL FDNEEVGSGS IQGAGAPTMF
     QAMRRIVGDL ANNYVGEGSF ERTIRQSFLV SADMAHGVHP NFMDKHEELH RPELQKGLVI
     KHNANQRYAT SGITSFLFKE VGKIHNLPTQ DFAVRNDMGC GSTIGPILAS GVGIRTVDCG
     IAQLSMHSIR EMCGKEDIDI AYKHFKAFYQ SFSSVDKMLT VDN
//
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