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Database: UniProt
Entry: A0A163LCT1_DIDRA
LinkDB: A0A163LCT1_DIDRA
Original site: A0A163LCT1_DIDRA 
ID   A0A163LCT1_DIDRA        Unreviewed;       443 AA.
AC   A0A163LCT1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   25-OCT-2017, entry version 6.
DE   SubName: Full=Aminopeptidase {ECO:0000313|EMBL:KZM27677.1};
GN   Name=apeB {ECO:0000313|EMBL:KZM27677.1};
GN   ORFNames=ST47_g1185 {ECO:0000313|EMBL:KZM27677.1};
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:KZM27677.1, ECO:0000313|Proteomes:UP000076837};
RN   [1] {ECO:0000313|EMBL:KZM27677.1, ECO:0000313|Proteomes:UP000076837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ArDII {ECO:0000313|EMBL:KZM27677.1,
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:KZM27677.1}.
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DR   EMBL; JYNV01000060; KZM27677.1; -; Genomic_DNA.
DR   EnsemblFungi; KZM27677; KZM27677; ST47_g1185.
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   HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR   InterPro; IPR022984; M18_aminopeptidase_2.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KZM27677.1};
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   443 AA;  46751 MW;  E192C3C33188759A CRC64;
     MMRGMTSQTS RAARAGAASL TGADADGLCS FVDSSPSPFH VCATVATELT AGGFVEVHET
     QSWPAEPGRY FLVRGGSLIA WSTEGVGNAT PFRIVGGHTD SPNLRVKQHP DLTSAGWQMV
     GLEPYGGAWL NSWLDRDLGI SGRLSVRVGN TVEQKLVRID DPILRVPQLA IHLSEDCKGV
     TLDPQRHVNG IWGVGSKPKS FIGFVAERAG VAASSVLGWE LMTHDLAPSA VVGVDKELVS
     APRLDNQGTC YAGTQALLAA VESPGQQVPV LALFDHEEVG SMSDRGAFSD LLNTVLERIV
     LGRGGGREEF LQAMAGSVCA SGDMAHATHP NYPDRHEPAH RIEINGGPVL KVNQNLRYAT
     DAAGAGEFAL ACDQAGVPMQ RYVHRADLPC GSTIGPITAS RTGLSTVDVG APQLAMHSAR
     ELMGAADVRM YADALGAFLT PRS
//
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