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Database: UniProt
Entry: A0A095C1R8_CRYGR
LinkDB: A0A095C1R8_CRYGR
Original site: A0A095C1R8_CRYGR 
ID   A0A095C1R8_CRYGR        Unreviewed;       502 AA.
AC   A0A095C1R8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   25-OCT-2017, entry version 17.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:KGB74900.1};
GN   ORFNames=CNBG_0738 {ECO:0000313|EMBL:KGB74900.1};
OS   Cryptococcus gattii serotype B (strain R265) (Filobasidiella gattii)
OS   (Cryptococcus bacillisporus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Tremellomycetes; Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus gattii species complex.
OX   NCBI_TaxID=294750 {ECO:0000313|EMBL:KGB74900.1, ECO:0000313|Proteomes:UP000029445};
RN   [1] {ECO:0000313|EMBL:KGB74900.1, ECO:0000313|Proteomes:UP000029445}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R265 {ECO:0000313|EMBL:KGB74900.1,
RC   ECO:0000313|Proteomes:UP000029445};
RX   PubMed=21304167; DOI=10.1128/mBio.00342-10;
RA   D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA   Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T.,
RA   Sawkins J., McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q.,
RA   Bartlett K., Li W., Wang X., Heitman J., Stajich J.E., Fraser J.A.,
RA   Meyer W., Carter D., Schein J., Krzywinski M., Kwon-Chung K.J.,
RA   Varma A., Wang J., Brunham R., Fyfe M., Ouellette B.F., Siddiqui A.,
RA   Marra M., Jones S., Holt R., Birren B.W., Galagan J.E., Cuomo C.A.;
RT   "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT   immunocompetent hosts.";
RL   MBio 2:E342-E342(2011).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; KQ410558; KGB74900.1; -; Genomic_DNA.
DR   EnsemblFungi; KGB74900; KGB74900; CNBG_0738.
DR   OMA; CFDHEEI; -.
DR   Proteomes; UP000029445; 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:KGB74900.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029445};
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:UP000029445};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   502 AA;  55734 MW;  9CB3F0B9E255FA0F CRC64;
     MKASISPPPK DAVNFCDFVT HAPTPFHAVA HLTTRLFTSG FVPISERSSS ASLEPGGKYY
     YTRNQSSLVA FTLPAKPLSE TAISFAVGHL DSPCLKVRPV SKKTKSNYLQ VGVELYGGGI
     WHSWFDRDLS LAGRVIVANR EALHSDDPKF VSKLVKIDRP ILRIPTLAIH LDRTANDSFT
     FNKETEFQPI LGLVEDALNA TDAALGMKRS HSGTPHRPLA KDDSHETEKS DDLFDVANME
     DKHHPKLLAV LAEELGCDIA DIQDFELSLF DTQPSTVGGL SNEFVYSPRI DNLMTSFCTI
     EALCEAVKTS NAEEESNIRC VILFDNEEVG SVSHHGAESN LLPAFVERIV QLKDYKDVGY
     YTMLANSFLI SADMGHAIHP NYESRYETNL APKINGGIVI KTNANQRYTS NAQTTFLLRR
     VAKKAGVPVQ EFEIRNDSSC GSTVGPHLST HVRTVDIGLA QLSMHSIRET AGSHDVRHYI
     DFFKVFFHGF GEIDRELRVD WH
//
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