ID   A0A1V8U4U4_9PEZI        Unreviewed;       399 AA.
AC   A0A1V8U4U4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Agmatinase 2 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=B0A51_14182 {ECO:0000313|EMBL:OQO18739.1};
OS   Rachicladosporium sp. CCFEE 5018.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX   NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO18739.1, ECO:0000313|Proteomes:UP000192386};
RN   [1] {ECO:0000313|Proteomes:UP000192386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00742, ECO:0000256|RuleBase:RU003684}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQO18739.1}.
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DR   EMBL; NAEU01000848; OQO18739.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V8U4U4; -.
DR   STRING; 1974281.A0A1V8U4U4; -.
DR   Proteomes; UP000192386; 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   CDD; cd11592; Agmatinase_PAH; 1.
DR   Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
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; 1.
DR   PIRSF; PIRSF036979; Arginase; 1.
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:UP000192386};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..399
FT                   /note="Agmatinase 2"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012664050"
SQ   SEQUENCE   399 AA;  43378 MW;  8B8D23B26FBBD6C0 CRC64;
     MKLVTTALAL GGLSSLAIAH EAEPTLKSQE PFVGWTKEDL DAKWGTDWGF SGISTFAHLP
     HTRCLQHPGE EYDIAILGAP FDTAVSYRPG ARFGPRAIRA ASSRQSSMRS YNPRAGLNPY
     ADWAKVIDCG DIPITPFDNA LALRQMTEAY TDLAHSKATA ANAKSEVTYR NKPKLLSLGG
     DHSIALPTLR ALNSIYGPVA VVHFDAHLDT WHPAKYPSAW IDPEDPTQQS FFTHGTMFWL
     AHNESLIAKD KSVHAGLRTR LSGIGDNEED TNQGWIRFST DDIDDLGVET LAKQIVEHVG
     TETPVYLSID IDVIDPGLAP GTGTPEPGGW TTRELIRVLR RIDALNVVAA DVVEVSPAFD
     GSGEQTALAG AQVAYEILTS MVKRGKVSEQ ADREPRAEL
//