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Database: UniProt
Entry: A0A086TBF3_ACRC1
LinkDB: A0A086TBF3_ACRC1
Original site: A0A086TBF3_ACRC1 
ID   A0A086TBF3_ACRC1        Unreviewed;       564 AA.
AC   A0A086TBF3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   25-OCT-2017, entry version 12.
DE   SubName: Full=Vacuolar aminopeptidase-like protein {ECO:0000313|EMBL:KFH46685.1};
GN   ORFNames=ACRE_025170 {ECO:0000313|EMBL:KFH46685.1};
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:KFH46685.1, 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:KFH46685.1}.
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DR   EMBL; JPKY01000017; KFH46685.1; -; Genomic_DNA.
DR   EnsemblFungi; KFH46685; KFH46685; ACRE_025170.
DR   Proteomes; UP000029964; 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   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:KFH46685.1};
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   564 AA;  60699 MW;  D925E3C32169ACC1 CRC64;
     MTRRSPGMLS SQASLLSLRQ YASAAASASL TQPSTATTTI RAAVPDKPSG PSRNFILADM
     DGRNPRDNNI CAACVSKLAP SEVAQTCWLV TEDERCRLCG IAECKPEAFI KPFTDFMEEN
     PTIFHTVEYF KKKLEHVGFT ELPSRDSWTH TLQPGGKYYV TRNGSSLIAF TIGKAYKPGN
     GVGMIAGHID ALTAKLKPVS KKPNKAGYVQ LGVAPYAGGL NATWWDRDLS IGGRVVVRDG
     ETGKTSTRLV KLGWPIAKIP TLAPHFGVGM MGSNNKETQA VPIVGLEGAD DAEQTLGDDG
     SFARTQPPRL VKLIAKELGI TSYNSIVNWE LELFDSQPAQ TLGLDKEFIT AGRIDDKLCS
     WSALMALLAS PDREDDGYIK LVALFDNEEI GSLLRQGARG NFLPITIERI VEALNPSAFG
     PGLLGQTYAR SFLTSADVTH AGNPNFLANY LDEHVPQLNV GVVISADSNG HMTTDAVSTA
     IMHRAAELSG SRTQVFQIRN DSRSGGTVGP MLSSAMGVRA ADVGIPQLSM HSVRATTGAL
     DPGLGVKFFK GFLDHWEKID GEWA
//
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