ID   F0U8I1_AJEC8            Unreviewed;       433 AA.
AC   F0U8I1;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Agmatine ureohydrolase {ECO:0000313|EMBL:EGC41731.1};
GN   ORFNames=HCEG_01093 {ECO:0000313|EMBL:EGC41731.1};
OS   Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS   capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN   [1] {ECO:0000313|Proteomes:UP000008142}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA   Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA   Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA   McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Ajellomyces capsulatus strain H88.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00742, ECO:0000256|RuleBase:RU003684}.
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DR   EMBL; DS990636; EGC41731.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0U8I1; -.
DR   STRING; 544711.F0U8I1; -.
DR   VEuPathDB; FungiDB:I7I53_07285; -.
DR   HOGENOM; CLU_039478_1_1_1; -.
DR   OMA; YELTTIM; -.
DR   Proteomes; UP000008142; Unassembled WGS sequence.
DR   GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.800.10; Ureohydrolase domain; 2.
DR   InterPro; IPR006035; Ureohydrolase.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR   PANTHER; PTHR11358:SF26; AGMATINASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11358; ARGINASE/AGMATINASE; 1.
DR   Pfam; PF00491; Arginase; 2.
DR   PRINTS; PR00116; ARGINASE.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR   PROSITE; PS01053; ARGINASE_1; 1.
DR   PROSITE; PS51409; ARGINASE_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003684};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008142}.
SQ   SEQUENCE   433 AA;  47640 MW;  D1B4D3F02F90DC0D CRC64;
     MAMLCVRGFK CFSALDGKSS NRRWCLPLPP ASNPEAWRHC KFFQVAVRHS LQGKHRITIF
     AAQERGKMLL RSWASILGGF LLYYVNPIYT HDGHDYSNHE KSSIDRREEL LEKWDQEHVK
     CLLEPDEHYD IAILGAPFDT SVSFRPGARF GPRAIPAASA RQLPANSYNT RAAINPYLNW
     ARILDCGDIP IMPFDNGVAE RQMYEAFLEL GTREAPNAIP GISHGKPKIV TLGGDHSITL
     PALRALHKIY GKPITVFFHT ASREGLISNT SSAHAGLCTR LTGLDDGDYS NPGPEQGFLR
     IHADEIDDVG PNGIINTIIS RIGLSPEDPV YLSLDIDVLD PGIAPGTGTP EPGGWTTREL
     IRILRGIEKL NFVGADIVEV SPSYDTGGET TALAAAQVAF EIITSMVKLG VKEEVGGWYG
     KKEEAGKKKR DEL
//