ID A0A1Y2VQL4_9PEZI Unreviewed; 398 AA.
AC A0A1Y2VQL4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Agmatinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=M426DRAFT_68816 {ECO:0000313|EMBL:OTA98916.1};
OS Hypoxylon sp. CI-4A.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTA98916.1, ECO:0000313|Proteomes:UP000242955};
RN [1] {ECO:0000313|EMBL:OTA98916.1, ECO:0000313|Proteomes:UP000242955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CI-4A {ECO:0000313|EMBL:OTA98916.1,
RC ECO:0000313|Proteomes:UP000242955};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00742, ECO:0000256|RuleBase:RU003684}.
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DR EMBL; KZ111640; OTA98916.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2VQL4; -.
DR STRING; 1001833.A0A1Y2VQL4; -.
DR InParanoid; A0A1Y2VQL4; -.
DR OrthoDB; 161483at2759; -.
DR Proteomes; UP000242955; 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:UP000242955};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..398
FT /note="Agmatinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012824797"
SQ SEQUENCE 398 AA; 43430 MW; 23115FA5D685D5C2 CRC64;
MRPTNLFFLA LSYGSVIIRA CSGGLGHNHE VREWSQEELD ELEKKWGQEW GFVGISTFAH
LEYHKCLTTP SELFDIAIIG APFDTAVSYR PGARFGPRAI RAASARQTSF RGFNARAGIN
PYANWARILD CGDIPITPVD NGVAVQQMTA AFKELGSRSP VSPLLAKPKL ITLGGDHSLS
LPALRATHEL HGPVRVLHFD AHLDTWHPAK YPSYWWSEQS RFTHGSMFWL AGDEGLLSNA
SAAPNVHAGL RTRLSGIEDY EEDTAQNWMR ISADEIDDLG TKGVVDAIMS TLGTEDPVYL
SVDIDVLDPA FAPGTGTPEP GGWTTRELIR IIRGLEDLNL VGADIVEVAP AYQGTGEETA
LAAAQVVFEI ITSMVKKGMG EMGKTDEVAS EELLVEEL
//
