ID A0A139AAR0_GONPJ Unreviewed; 456 AA.
AC A0A139AAR0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Arginase/deacetylase {ECO:0000313|EMBL:KXS13555.1};
GN ORFNames=M427DRAFT_113360 {ECO:0000313|EMBL:KXS13555.1};
OS Gonapodya prolifera (strain JEL478) (Monoblepharis prolifera).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Monoblepharidomycetes; Monoblepharidales;
OC Gonapodyaceae; Gonapodya.
OX NCBI_TaxID=1344416 {ECO:0000313|EMBL:KXS13555.1, ECO:0000313|Proteomes:UP000070544};
RN [1] {ECO:0000313|EMBL:KXS13555.1, ECO:0000313|Proteomes:UP000070544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL478 {ECO:0000313|EMBL:KXS13555.1,
RC ECO:0000313|Proteomes:UP000070544};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00742, ECO:0000256|RuleBase:RU003684}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ965777; KXS13555.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139AAR0; -.
DR STRING; 1344416.A0A139AAR0; -.
DR OMA; GFLYYEV; -.
DR OrthoDB; 161483at2759; -.
DR Proteomes; UP000070544; 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 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:UP000070544};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..456
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007296073"
FT REGION 250..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 456 AA; 48766 MW; 7D708122933DC837 CRC64;
MQFMLKALAL GAIAALPASG LPVGALTDPT HPTFDTMQRP MFEFAGIPTF AHTPYVTSCF
KSFDKDADAH KLIALGAAAA EKHSDAQKHV GTAKADAKTV IENLLYPKFD IAVVGIPFDT
SVTYRPGARF GPRGIRGASM RLSLNFAHDP LLDVNPLSSW ATIVDCGDVP AAYSDNAVAI
AQMEAYLSEV VARKTADPEA SPDWTKGHPR VVTLGGDHTI VLPILRALHK IHGKSFHVIH
FDSHMDTWEP SSLGGSESGD DAKSGQTESN PYPRVTSSAM LGLNHGTPLW HAAKEGLFEM
DGRNLHVGLR GKLVDMGDYA TDDSVGFKRI HAADIDTLGV KGVIERIVEV VSGGNTDEVP
LVYISLDIDV LDPAFAPATG TPEIGGWSTR ELKSIIRGLQ GRLRVIGADV VEVAPAYDTV
AEQTTLAAAE VAYEFVNLMI TDIKEVAGKK KARGEL
//
