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Database: UniProt
Entry: E9DGH9_COCPS
LinkDB: E9DGH9_COCPS
Original site: E9DGH9_COCPS 
ID   E9DGH9_COCPS            Unreviewed;       529 AA.
AC   E9DGH9;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   25-OCT-2017, entry version 24.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:EFW14340.1};
GN   ORFNames=CPSG_08928 {ECO:0000313|EMBL:EFW14340.1};
OS   Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Coccidioides.
OX   NCBI_TaxID=443226 {ECO:0000313|Proteomes:UP000002497};
RN   [1] {ECO:0000313|Proteomes:UP000002497}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 757 / Silveira {ECO:0000313|Proteomes:UP000002497};
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Neafsey D., Orbach M., Henn M.R., Cole G.T., Galgiani J.,
RA   Gardner M.J., Kirkland T.N., Taylor J.W., Young S.K., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Howarth C., Jen D., Larson L.,
RA   Mehta T., Neiman D., Park D., Pearson M., Richards J., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA   White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Coccidioides posadasii strain Silveira.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; GL636506; EFW14340.1; -; Genomic_DNA.
DR   MEROPS; M18.002; -.
DR   EnsemblFungi; EFW14340; EFW14340; CPSG_08928.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000002497; 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   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 2.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EFW14340.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002497};
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:UP000002497};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   529 AA;  57912 MW;  8803697EF02DACE9 CRC64;
     MRLNILESSL ARTSQLSQTA IRTATNQPYR AHSTMTDFKE KALDFCSFVN ASPTPFHAVA
     SARTRLVDAG FKEIKEKDAW SSICKPGGKY YLTRNGSTII AFAVGRKWKP GNSIAMLGAH
     TDSPCLRVKP VSKKRAEGFI QIGVETYGGG LWHTWFDRDL GIAGRVMARN NDGSISARLL
     RIDRPILRIP TLAIHFERQE TFSFNKETQL FPIAGLVEAE LSRVGGDHAS TEPSKSEDKT
     DDAPTAPLKV ITERHHPYLI ELMASELALK PDDIVDFEIL LYDTQKACLG GLLDEFIFSA
     RLDNLNMSYC ATMGFIESLS KSSALDNETS IRLVALFDHE EIGSKTAQGA DSNALPAILR
     RLAVLPSSGK EDTSTAYEQS LSTSFLLSAD MSHSVNPNYA FKYEPDHKPE MNKGPVIKIN
     ANARYATNSP GIVLVQEAAR LAKSGGDTAN TVGVPLQLFV VRNDSLCGST IGPMLSAALG
     TRTVDLGNAQ LSMHSIRETG GTKDVGYAVR LFKSFFENFS QLSQRIFVD
//
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