ID C6H8T9_AJECH Unreviewed; 405 AA.
AC C6H8T9;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:EER42722.1};
GN ORFNames=HCDG_02620 {ECO:0000313|EMBL:EER42722.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER42722.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; GG692421; EER42722.1; -; Genomic_DNA.
DR AlphaFoldDB; C6H8T9; -.
DR STRING; 544712.C6H8T9; -.
DR VEuPathDB; FungiDB:HCDG_02620; -.
DR HOGENOM; CLU_021802_3_0_1; -.
DR OMA; RLHKGVM; -.
DR Proteomes; UP000002624; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF8; M20_DIMER DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002624};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..405
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002966068"
FT DOMAIN 246..288
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 405 AA; 42617 MW; F47539DFE54B406F CRC64;
MKLSNLAALL SASTVAPVTA GYVSQDIIRA DTMNVAVAAA ANAQDEDLLE KIISSSPLLS
LHRTICQIES VSNHESAVGE ALIKYLGENG FTTEKQMVPV DEDDDSTDKR FNIWAYPEGS
PKPKIILTSH IDTVPPHIDY NLQAPEGDFD RANITIKGRG TVDAKASVAA MIIAALGHLK
EHPDVPLGLL FVVSEEKGGT GMGNLRLDVE REGASRPTRV TPGSATAPSG EILPVLERIE
KLGDIPVKGG GLPASEKYGR TTLNIGMLKG GAAGNVVPES ASASVAVCLA AGTIEDAQNI
ICKAVADACG GSKNITITFP DSKAYPPVDL DTDVDGFELL TVNYGTDIPK LDIHDEDSDA
KVKRYLYGPG TILVAHGVDE ALTVGDLEKA VEGYARLIDA AVRRG
//
