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Database: UniProt
Entry: A0A0J8RYF8_COCIT
LinkDB: A0A0J8RYF8_COCIT
Original site: A0A0J8RYF8_COCIT 
ID   A0A0J8RYF8_COCIT        Unreviewed;       529 AA.
AC   A0A0J8RYF8;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   12-APR-2017, entry version 8.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:KMU89812.1};
GN   ORFNames=CIHG_07845 {ECO:0000313|EMBL:KMU89812.1};
OS   Coccidioides immitis H538.4.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Coccidioides.
OX   NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU89812.1, ECO:0000313|Proteomes:UP000054563};
RN   [1] {ECO:0000313|Proteomes:UP000054563}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H538.4 {ECO:0000313|Proteomes:UP000054563};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; DS017015; KMU89812.1; -; Genomic_DNA.
DR   EnsemblFungi; KMU89812; KMU89812; CIHG_07845.
DR   Proteomes; UP000054563; 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   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KMU89812.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000054563};
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:UP000054563};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   529 AA;  57942 MW;  AF4485C52BA4C131 CRC64;
     MRLNILESSL ARTSQLSQTA IRTATNQPYR AHSTMTDFKE KALDFCSFVN ASPTPFHAVA
     SARTRLVDAG FKEIKEKDAW SSVCKPGGKY YLTRNGSTII AFAVGRKWKP GNSIAMLGAH
     TDSPCLRVKP VSKKRAEGFI QIGVETYGGG LWHTWFDRDL GIAGRVMARN NDGSISARLL
     RIDRPILRIP TLAIHFERQE TFSFNKETQL FPIAGLVEAE LSRVGGDHAS TEPSKSEDKT
     DDAPTAPLKV ITERHHPYLI ELMASELALK PDDIVDFEIL LYDTQKACLG GLLDEFIFSA
     RLDNLNMSYC ATMGFIESLS NSSALDNETS IRLVALFDHE EIGSKTAQGA DSNALPAILR
     RLAVLPSSGK EDTSTAYEQS LSTSFLLSAD MSHSVNPNYA FKYEPDHKPE MNKGPVIKIN
     ANARYATNSP GIVLVQEAAR LAKSGSDTAN TVGVPLQLFV VRNDSLCGST IGPMLSAALG
     TRTVDLGNAQ LSMHSIRETG GTRDVGYAVR LFKSFFENFS QLSQRIFVD
//
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