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Database: UniProt
Entry: A0A0A2KED3_PENIT
LinkDB: A0A0A2KED3_PENIT
Original site: A0A0A2KED3_PENIT 
ID   A0A0A2KED3_PENIT        Unreviewed;       514 AA.
AC   A0A0A2KED3;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   10-MAY-2017, entry version 7.
DE   SubName: Full=Peptidase M18 {ECO:0000313|EMBL:KGO65323.1};
GN   ORFNames=PITC_015910 {ECO:0000313|EMBL:KGO65323.1};
OS   Penicillium italicum (Blue mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO65323.1, ECO:0000313|Proteomes:UP000030104};
RN   [1] {ECO:0000313|EMBL:KGO65323.1, ECO:0000313|Proteomes:UP000030104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI-1 {ECO:0000313|EMBL:KGO65323.1,
RC   ECO:0000313|Proteomes:UP000030104};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L.,
RA   Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium
RT   expansum provide new insights into secondary metabolism and
RT   pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO65323.1}.
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DR   EMBL; JQGA01001510; KGO65323.1; -; Genomic_DNA.
DR   EnsemblFungi; KGO65323; KGO65323; PITC_015910.
DR   PhylomeDB; A0A0A2KED3; -.
DR   Proteomes; UP000030104; Unassembled WGS sequence.
DR   GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:EnsemblFungi.
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   Complete proteome {ECO:0000313|Proteomes:UP000030104};
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:UP000030104};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   514 AA;  56095 MW;  7CD77F2FF89686E3 CRC64;
     MTRKHNTTQG LDMPWASQIS AQLPSAFMPV PAALPVRAQA PIANELFKPE DYSKPYCEFM
     TSNPTIFHAV KSFSKQLEEH GYKQLSERAV WTSELKRGGK FYISRNGSSL IAFNIGSKYE
     SGNGVAIVAG HVDALTAKLK PVSKVPNKAG FQQLGVAPYA GGLGPTWWDR DLGIGGRVLV
     RNPETGKVEN KLVKLDWPIA RIPTLAPHFG APANGPFNQE TQMVPVIGVD NSDLFEHSKI
     ESNDVKFGTF TSTQPEKLVK IISKELGITD YSTIVNWELE LFDTQPAQLG GLEKDMIFAG
     RIDDKLCCYA AQEALIASSD STSPGTVKMV GMFDDEEIGS LLRQGARSNF MSSVIERIAE
     AFAKDSYGPN ILSQTVANSF LVSSDVIHSV NPNFLNVYLE NHAPRLNVGV TVSTDSNGHM
     TTDSVSEGFI RRVAERCGST LQVFQIRNDS RSGGTIGPMT SAQIGMRAID CGIPQLSMHS
     IRATTGSLDP GLGVKLFKGF FDYYEEVDKE FADF
//
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