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Database: UniProt
Entry: A1C4U0_ASPCL
LinkDB: A1C4U0_ASPCL
Original site: A1C4U0_ASPCL 
ID   A1C4U0_ASPCL            Unreviewed;       504 AA.
AC   A1C4U0;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   22-NOV-2017, entry version 58.
DE   SubName: Full=Vacuolar aspartyl aminopeptidase Lap4, putative {ECO:0000313|EMBL:EAW14708.1};
GN   ORFNames=ACLA_001190 {ECO:0000313|EMBL:EAW14708.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 /
OS   NCTC 3887 / NRRL 1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW14708.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW14708.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P.,
RA   Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A.,
RA   Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A.,
RA   Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R.,
RA   Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M.,
RA   Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R.,
RA   Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R.,
RA   Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; DS027004; EAW14708.1; -; Genomic_DNA.
DR   RefSeq; XP_001276134.1; XM_001276133.1.
DR   ProteinModelPortal; A1C4U0; -.
DR   STRING; 5057.CADACLAP00000300; -.
DR   MEROPS; M18.001; -.
DR   EnsemblFungi; CADACLAT00000304; CADACLAP00000300; CADACLAG00000304.
DR   GeneID; 4708613; -.
DR   KEGG; act:ACLA_001190; -.
DR   EuPathDB; FungiDB:ACLA_001190; -.
DR   HOGENOM; HOG000253244; -.
DR   KO; K01268; -.
DR   OMA; SIVNWEL; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000006701; 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   ECO:0000313|EMBL:EAW14708.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006701};
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:UP000006701};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   504 AA;  54917 MW;  FE7FEF3003670426 CRC64;
     MAYRLSGQFP EPTPSYPSST ASRPAEQSKP AAFSPEDYAQ PYCNFMTAYP TIFHAVDGFT
     KELESKGYKH LPEREAWTSK LQRGGKYYVT RNGSAFIAFS IGKEYESGNG LAIVAGHIDA
     LTAKLKPVSK LPNKAGFVQL GVAPYAGALN ETWWDRDLSI GGRVLVKDRD SGKVESKLVK
     LDWPIARIPT LAPHFGAPSQ GPFNKETQMV PIVGIDNSDL FQHQVSASAS SDNGIKPGSF
     AATQPERLVK IIAKELGITD YDTILNWELE LYDSQPARLG GLEKDLIFAG RVDDKLCCYA
     AQQALLASPD STSPASIKMV GMFDDEEIGS LLRQGARSNF MSSVIERITE AFASSNYGPN
     LLSQTVANSF FVSSDVIHAV NPNFLNVYLE NHAPRLNVGV AVSADSNGHM TTDSVSYGFI
     KRVADRCDAK LQVFQIRNDS RSGGTIGPMT SARIGMRAID VGIPQLSMHS IRATTGSLDP
     GLGVKLFKGF FDYFEEVDKE FADF
//
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