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Database: UniProt
Entry: A0A086THT8_ACRC1
LinkDB: A0A086THT8_ACRC1
Original site: A0A086THT8_ACRC1 
ID   A0A086THT8_ACRC1        Unreviewed;       500 AA.
AC   A0A086THT8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   28-FEB-2018, entry version 16.
DE   SubName: Full=Aspartyl aminopeptidase-like protein {ECO:0000313|EMBL:KFH48920.1};
GN   ORFNames=ACRE_000490 {ECO:0000313|EMBL:KFH48920.1};
OS   Acremonium chrysogenum (strain ATCC 11550 / CBS 779.69 / DSM 880 / JCM
OS   23072 / IMI 49137).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales;
OC   Hypocreales incertae sedis; Acremonium.
OX   NCBI_TaxID=857340 {ECO:0000313|EMBL:KFH48920.1, ECO:0000313|Proteomes:UP000029964};
RN   [1] {ECO:0000313|Proteomes:UP000029964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11550 / CBS 779.69 / DSM 880 / JCM 23072 / IMI 49137
RC   {ECO:0000313|Proteomes:UP000029964};
RX   PubMed=25291769; DOI=10.1128/genomeA.00948-14;
RA   Terfehr D., Dahlmann T.A., Specht T., Zadra I., Kuernsteiner H.,
RA   Kueck U.;
RT   "Genome sequence and annotation of Acremonium chrysogenum, producer of
RT   the beta-lactam antibiotic cephalosporin C.";
RL   Genome Announc. 2:E0094814-E0094814(2014).
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:KFH48920.1}.
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DR   EMBL; JPKY01000001; KFH48920.1; -; Genomic_DNA.
DR   EnsemblFungi; KFH48920; KFH48920; ACRE_000490.
DR   Proteomes; UP000029964; 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   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|EMBL:KFH48920.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029964};
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:UP000029964};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   500 AA;  54170 MW;  14E3F76FEC0924C1 CRC64;
     MAPNQTALDF VDFVNASPTP YHAVHSAVQR FEKAGFKPIR ERDSWASTLR PGGKYYLTRN
     GSSIVAFTIG RKWRPGNAVA IVGAHTDSPC LRVKPVSKKS GAGFLQIGVE TYGGGIWHSW
     FDRDLSLAGR VLVREGDNFV QKLVKIEKPL LRIPTLAIHL HRSSVFDPNK ETELFPIAGL
     AAAELNKGAG GKSDQAEKDE DTKEGAAEGE EEFSPLSQMS ERHHPKVLDV IASELNTDVG
     AIVDFELVLY DTQKSCIGGI NDEFIFSPRL DNLGMTYCSV EGLIASVKAD DALDNDGTIR
     LTVCFDHEEI GSTSAQGANS NLLPSVIRRL SVLPGNRDAS SDGSFEPVGH EGDEATAYEQ
     TLSRSFLVSA DMAHSVHPNY TGKYESSHQP AMNKGTVIKV NANQRYATNS PGIVLLQECA
     RSAGVPLQLF VVRNDSPCGS TIGPGLAASL GMRTIDLGNP QLSMHSIRET GGTEDVAHAI
     KLFEHFFEHY GALEPRILVD
//
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