ID A0A1Q7I247_9CHLR Unreviewed; 272 AA.
AC A0A1Q7I247;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE RecName: Full=Arginase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AUH85_02450 {ECO:0000313|EMBL:OLC57728.1};
OS Chloroflexi bacterium 13_1_40CM_4_68_4.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1805077 {ECO:0000313|EMBL:OLC57728.1, ECO:0000313|Proteomes:UP000185706};
RN [1] {ECO:0000313|EMBL:OLC57728.1, ECO:0000313|Proteomes:UP000185706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00742}.
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:OLC57728.1}.
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; MNFM01000028; OLC57728.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7I247; -.
DR Proteomes; UP000185706; Unassembled WGS sequence.
DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd09999; Arginase-like_1; 1.
DR Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR43782; ARGINASE; 1.
DR PANTHER; PTHR43782:SF3; ARGINASE; 1.
DR Pfam; PF00491; Arginase; 1.
DR PRINTS; PR00116; ARGINASE.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 3: Inferred from homology;
SQ SEQUENCE 272 AA; 28704 MW; DD153ED28FEF3FBC CRC64;
MPEPWHLIEA GVATATHFAG MTEAPRALAG GIGPLAAPTK YVRIPFVPRE QWVRAARDSC
MALSEAVRGT IAAGSRPLIL GGECSIVAGS VPGLYPRLED LVLVYFDAHG DFNTLATTPS
HFVGGMCLAH VCGKQLGPLL WPGVRALPEE RVCLVGAREL DPGERGNLDR SKVRRFAFGP
ASNSEASSLV AAVRHKRVFL HVDLDVVDPS QMFAVNFPAP GGVSFDALGA LLRSIAGVAT
IVGVEVCGYD PRKDERRALP AKIAAAIAPT LA
//