ID G4U7P8_NEUT9 Unreviewed; 386 AA.
AC G4U7P8;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 03-MAY-2023, entry version 48.
DE SubName: Full=Arginase/deacetylase {ECO:0000313|EMBL:EGZ78338.1};
GN ORFNames=NEUTE2DRAFT_54717 {ECO:0000313|EMBL:EGZ78338.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ78338.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ78338.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00742, ECO:0000256|RuleBase:RU003684}.
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DR EMBL; GL890999; EGZ78338.1; -; Genomic_DNA.
DR AlphaFoldDB; G4U7P8; -.
DR STRING; 510952.G4U7P8; -.
DR eggNOG; KOG2964; Eukaryota.
DR HOGENOM; CLU_039478_1_0_1; -.
DR Proteomes; UP000008513; 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 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; ARGINASE/AGMATINASE; 1.
DR PANTHER; PTHR11358:SF28; HYPOTHETICAL ARGINASE FAMILY PROTEIN (EUROFUNG); 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:UP000008513};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..386
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003469379"
SQ SEQUENCE 386 AA; 41713 MW; 1F6635703C4EB3F1 CRC64;
MRSFVFFSLG IGGVVAHGIP HSFSSSSSSF WVSSNNRGHL TSLDDPTEDD IDIVTGSQFH
GLKTFASLPY PSCLTRNTLS CRLSPDDQEP AMGRQELESE VNALEDSITT RVTAPRFQLT
RCNGWLLADE DALHEWATIV DCGDATLTWL DNTVAFKHLD KAHRVISGRP TANDTVATVP
RILTLGGDHS TTLSALRSTF QRWGQVSVIH FDSHIDTWSP DVLGGISDYA GLNHGTFLHI
AHEEGLIRNT SIHAGTRGPI IMHSDRDNDK RCGFAVITAR DIDKHGSDWI ISTIKARVGN
SRVYISVDID VLDPAFAPGT GTAEPGGWST RELLTIIDGL RGLSVVGADV VEVSPVYDNT
GETTVLAAAQ VGLSLISLMV ARPVSD
//
