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Database: UniProt
Entry: A0A162Y825_DIDRA
LinkDB: A0A162Y825_DIDRA
Original site: A0A162Y825_DIDRA 
ID   A0A162Y825_DIDRA        Unreviewed;       503 AA.
AC   A0A162Y825;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   07-JUN-2017, entry version 5.
DE   SubName: Full=Aminopeptidase {ECO:0000313|EMBL:KZM19867.1};
GN   ORFNames=ST47_g8969 {ECO:0000313|EMBL:KZM19867.1};
OS   Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS   rabiei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae;
OC   Didymellaceae; Ascochyta.
OX   NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM19867.1, ECO:0000313|Proteomes:UP000076837};
RN   [1] {ECO:0000313|EMBL:KZM19867.1, ECO:0000313|Proteomes:UP000076837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ArDII {ECO:0000313|EMBL:KZM19867.1,
RC   ECO:0000313|Proteomes:UP000076837};
RX   PubMed=27091329; DOI=10.1038/srep24638;
RA   Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D.,
RA   Verma P.K.;
RT   "Draft genome sequencing and secretome analysis of fungal
RT   phytopathogen Ascochyta rabiei provides insight into the necrotrophic
RT   effector repertoire.";
RL   Sci. Rep. 6:24638-24638(2016).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KZM19867.1}.
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DR   EMBL; JYNV01000290; KZM19867.1; -; Genomic_DNA.
DR   EnsemblFungi; KZM19867; KZM19867; ST47_g8969.
DR   Proteomes; UP000076837; Unassembled WGS sequence.
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   InterPro; IPR001948; Peptidase_M18.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KZM19867.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000076837};
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:UP000076837};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   503 AA;  55326 MW;  A4FB8DF0A19ECCED CRC64;
     MAAKPSLQAA EDFLSFVNAS PTPFHAVRSA KERLEKAGFK QIKERDSWAP TIQPGGKYYL
     TRNGSSIVAF AVGKQWKAGN PIGMIGAHTD SPCLRIKPVS KRQNDGFLQV ACETYGGGLW
     HTWFDRDLSI AGRAMVRTKS GKIEQRLVKV ERPILRIPTL AIHLDRQETF QFNKETQLFP
     IAGLVQAELN RQGKTEESKE DDKKDGPFEP LATPYQRHHS YIVEIIAEEA GADPNDVLDF
     EIVLYDTQKS AIGGLNNELI FSPRLDNLMM SYCSVEGLIK SLSSSTSLDK DSTIRLIALF
     DHEEIGSQTA QGADSNLLPA VIRRLSVLPA SESSTSDKSY DKIEADTATA YEQTLSTSFL
     ISADMAHSVH PNYPAKYEAQ HRPEMNKGTV IKINANARYA TNSPGIVLLQ EAARRAKPAS
     SGLSKEGVPL QLFVVRNDSS CGSTIGPMLS AAMGARTLDL GNPQLSMHSI RETGGAHDVE
     HAVNLFDSFF ENFEELEKNI EVD
//
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