ID S7Q4G1_GLOTA Unreviewed; 383 AA.
AC S7Q4G1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 03-MAY-2023, entry version 39.
DE SubName: Full=Arginase/deacetylase {ECO:0000313|EMBL:EPQ54906.1};
GN ORFNames=GLOTRDRAFT_139359 {ECO:0000313|EMBL:EPQ54906.1};
OS Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ54906.1, ECO:0000313|Proteomes:UP000030669};
RN [1] {ECO:0000313|EMBL:EPQ54906.1, ECO:0000313|Proteomes:UP000030669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ54906.1,
RC ECO:0000313|Proteomes:UP000030669};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00742, ECO:0000256|RuleBase:RU003684}.
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DR EMBL; KB469303; EPQ54906.1; -; Genomic_DNA.
DR RefSeq; XP_007867127.1; XM_007868936.1.
DR AlphaFoldDB; S7Q4G1; -.
DR STRING; 670483.S7Q4G1; -.
DR GeneID; 19304228; -.
DR KEGG; gtr:GLOTRDRAFT_139359; -.
DR eggNOG; KOG2964; Eukaryota.
DR HOGENOM; CLU_039478_1_1_1; -.
DR OMA; GQRAIHN; -.
DR OrthoDB; 161483at2759; -.
DR Proteomes; UP000030669; 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:SF30; AGMATINASE 1-RELATED; 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:UP000030669};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..383
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004543846"
SQ SEQUENCE 383 AA; 41860 MW; 1AE6AF1061E904DD CRC64;
MLSLGLLVLA ASLVHASQAP YHLSAPTDFE RLFSSDLLSR DKWSQESWNG LVSFARAQPL
RCFGSDADVK YDVAVLGAPF DTATSFRPGA RFGPNGIRQG ARRLGVDRIN VPHKIRASDY
LNIADCGDVP MTFVDNKVAL RQLELANKEL LSREAARSYN ETSLAKDGKY HPRVLTLGGD
HTITLPLLRG VAEVYGPVSV IHFDSHLDTW KPNFMSGPWL PGEEIPVTHG SYFYYAYKEG
LLAPNNSNIH VGIRGALGSW DDYKNDWEVG FHISHAEDIE EVGYQGIVDK IREVVGDNPV
YITLDIDVID PGMAPATGTP EIGGFTTREI KKILKGLVGL KIVGADIVEV APGYDSQDEI
TQIAAANIGW DMLALMAKTP TVA
//
