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Database: UniProt
Entry: A0A135LMF6_PENPA
LinkDB: A0A135LMF6_PENPA
Original site: A0A135LMF6_PENPA 
ID   A0A135LMF6_PENPA        Unreviewed;       517 AA.
AC   A0A135LMF6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   22-NOV-2017, entry version 8.
DE   SubName: Full=Peptidase M18, domain 2 {ECO:0000313|EMBL:KXG50129.1};
GN   ORFNames=PGRI_060960 {ECO:0000313|EMBL:KXG50129.1};
OS   Penicillium patulum (Penicillium griseofulvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG50129.1, ECO:0000313|Proteomes:UP000070168};
RN   [1] {ECO:0000313|EMBL:KXG50129.1, ECO:0000313|Proteomes:UP000070168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG3 {ECO:0000313|EMBL:KXG50129.1,
RC   ECO:0000313|Proteomes:UP000070168};
RX   PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA   Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA   Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT   "Genome sequencing and secondary metabolism of the postharvest
RT   pathogen Penicillium griseofulvum.";
RL   BMC Genomics 17:19-19(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:KXG50129.1}.
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DR   EMBL; LHQR01000048; KXG50129.1; -; Genomic_DNA.
DR   EnsemblFungi; KXG50129; KXG50129; PGRI_060960.
DR   Proteomes; UP000070168; 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   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
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   Complete proteome {ECO:0000313|Proteomes:UP000070168};
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:UP000070168};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   517 AA;  56428 MW;  EC04F176858DC3AC CRC64;
     MTRKYNSIQD LDMPWASKIS AQLPNPLMPV PAALPVRAQQ SIADESVRSF RPEDYSKPYC
     EFMTSNPTIF HAVKSFSEQL EEHGYKYLSE RAIWTSELKQ GGKFYTTRNG SSLIAFHVGS
     KYESGNGIAI VAGHVDALTA KLKPVSKLPN KAGFQQLGVA PYAGGLGTTW WDRDLGIGGR
     VLVRDPETGK VETKLVKLDW PIARVPTLAP HFGSPANGPF NPETQMVPVI GIDNSDLFEH
     SKAESSNIKF GTFTSTQPEK LVKIIAQELG ITDHSTIVNW ELELFDTQPA QLGGLEKDMI
     FAGRIDDKLC CYAAQEALIA SSDDKSTGTV KMVGMFDDEE IGSLLRQGAR SNFMSSVIER
     IAEAFAEGNY GPSLLSQTVA NSFLVSSDVI HAVNPNFLNV YLENHAPRLN VGVAVSADSN
     GHMTTDSVSE GIMRRVAERC GSTLQVFQIR NDSRSGGTIG PMTSAQIGMR AIDCGIPQLS
     MHSIRATTGS LDPGLGVKLF KGFFDHYEEV DKEFSDF
//
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