ID A0A225AKU7_9EURO Unreviewed; 377 AA.
AC A0A225AKU7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Putative agmatinase 2 {ECO:0000313|EMBL:OKL61510.1};
GN ORFNames=UA08_03099 {ECO:0000313|EMBL:OKL61510.1};
OS Talaromyces atroroseus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Trachyspermi.
OX NCBI_TaxID=1441469 {ECO:0000313|EMBL:OKL61510.1, ECO:0000313|Proteomes:UP000214365};
RN [1] {ECO:0000313|EMBL:OKL61510.1, ECO:0000313|Proteomes:UP000214365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 11181 {ECO:0000313|EMBL:OKL61510.1,
RC ECO:0000313|Proteomes:UP000214365};
RA Rasmussen K.B., Rasmussen S., Petersen B., Sicheritz-Ponten T.,
RA Mortensen U.H., Thrane U.;
RT "Talaromyces atroroseus IBT 11181 draft genome.";
RL Submitted (JUN-2015) 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:OKL61510.1}.
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DR EMBL; LFMY01000004; OKL61510.1; -; Genomic_DNA.
DR RefSeq; XP_020121631.1; XM_020265632.1.
DR AlphaFoldDB; A0A225AKU7; -.
DR STRING; 1441469.A0A225AKU7; -.
DR GeneID; 31002854; -.
DR OrthoDB; 161483at2759; -.
DR Proteomes; UP000214365; 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:UP000214365};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..377
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013098668"
SQ SEQUENCE 377 AA; 41370 MW; 4210AC14C62262C9 CRC64;
MRKSLYWAAC ALTLASASLD LGPDYPYIVE DLDKDLPFSQ PVTFAHLEWQ RCLAASHEEP
LDIAILGFPY DTSTSYRPGA RFGPRGIRAG SSREKKGRSY NTVWGVDPYE QGLQIIDCGD
VPITPFDAAH AFKQMEQAYR QILYHQTSEQ NAWKHPRILS LGGDHSIVLP ILRSLKTVYG
PISVIHLDSH LDTWDPYEGY TGIASNQSAI THGTFFWHAS REGCISKGTS VHGGLRTKLF
SPRDYEIDRD VVGFTLIEAH EIDEIGVHGI VEKVRKAVGD TPTYLSIDID VLDPSIAPAT
GTPESGGWTT RELKAFLKGL EGINLVGADV VEVSPPYDSV AETTSVAAAD LLVDILAGMT
KSTTEPSISR PDIKDEL
//
