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Database: UniProt
Entry: A6R3T9_AJECN
LinkDB: A6R3T9_AJECN
Original site: A6R3T9_AJECN 
ID   A6R3T9_AJECN            Unreviewed;       479 AA.
AC   A6R3T9;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   25-OCT-2017, entry version 55.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDN07787.1};
GN   ORFNames=HCAG_04297 {ECO:0000313|EMBL:EDN07787.1};
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=339724 {ECO:0000313|EMBL:EDN07787.1, ECO:0000313|Proteomes:UP000009297};
RN   [1] {ECO:0000313|Proteomes:UP000009297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J.,
RA   Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E.,
RA   Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M.,
RA   Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N., Orbach M.J.,
RA   Kirkland T.N., Cole G.T., Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens
RT   Coccidioides and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CH476658; EDN07787.1; -; Genomic_DNA.
DR   RefSeq; XP_001540457.1; XM_001540407.1.
DR   ProteinModelPortal; A6R3T9; -.
DR   STRING; 339724.XP_001540457.1; -.
DR   MEROPS; M18.002; -.
DR   EnsemblFungi; EDN07787; EDN07787; HCAG_04297.
DR   GeneID; 5446942; -.
DR   KEGG; aje:HCAG_04297; -.
DR   EuPathDB; FungiDB:HCAG_04297; -.
DR   eggNOG; KOG2596; Eukaryota.
DR   eggNOG; COG1362; LUCA.
DR   KO; K01267; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000009297; 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   Complete proteome {ECO:0000313|Proteomes:UP000009297};
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:UP000009297};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   479 AA;  51923 MW;  1AABD0B6C2DA1D98 CRC64;
     MLLLQFVNER DSWTSVCKPG GKYYVTRNGS TVIAFAIGHK WKPGNSISMV GAHTDSPCLR
     IKPVSKKTGD GFVQIGVETY GGGLWHTWFD RDLSIAGRAM VRNSNGSIEA KLVHIDRPIL
     RIPTLAIHLD RQETFSFNKE TQLFPIAGMV AAELARKSGD RDSNTGLEIR AKDNGSGGNT
     QFNAPFSPLR DATDRHHPYL VELIASELSA QPQDIVDFEM LLYDSQKACL GGLLNEFIFS
     ARLDNLNMTF CATMGLINSL ANPEALDNES CIRLISLFDH EEIGSRTAQG ADSNALPTVL
     RRLCLVPGSS SSSSSADLST AYEQSLSSSF LLSADMAHSV NPNYAFKYET DHKPEMNKGP
     VIKINANARY ATNSPGIVLL QECAKLAHSA GNSAGADGAS LQGIPLQLFV VRNDSSCGST
     IGPMLSAALG VRTLDLGNPQ LSMHSIRETG GTYDVGYATK LFESFFQNYS RLAETILVN
//
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