ID A0A199NV03_9MICC Unreviewed; 304 AA.
AC A0A199NV03;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Arginase {ECO:0000313|EMBL:OAX52428.1};
GN ORFNames=AN277_0203505 {ECO:0000313|EMBL:OAX52428.1};
OS Rothia kristinae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=37923 {ECO:0000313|EMBL:OAX52428.1, ECO:0000313|Proteomes:UP000053171};
RN [1] {ECO:0000313|Proteomes:UP000053171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RuSp02-3 {ECO:0000313|Proteomes:UP000053171};
RA Waterworth S., Matcher G.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAX52428.1, ECO:0000313|Proteomes:UP000053171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RuSp02-3 {ECO:0000313|Proteomes:UP000053171};
RA Waterworth S.C., Walmsley T.A., Matongo T., Davies-Coleman M.T.,
RA Dorrington R.A.;
RT "Identification of putative biosynthetic pathways for the production of
RT bioactive secondary metabolites by the marine actinomycete Kocuria
RT kristinae RUTW2-3.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:OAX52428.1}.
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; LJBJ02000004; OAX52428.1; -; Genomic_DNA.
DR RefSeq; WP_064725085.1; NZ_LJBJ02000004.1.
DR AlphaFoldDB; A0A199NV03; -.
DR Proteomes; UP000053171; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000053171}.
SQ SEQUENCE 304 AA; 32389 MW; 9562A5169514F9B7 CRC64;
MKSADARHET DPQEQTSTLR LIWPQWQGAG QEMVGQLLPE APLDRARRGY ALGARFLEAM
LPEHDGPTEV VPVPQEESGS TGGIESREQI LASLDAAQEI LSRHGDAPRI LTLGGECSVS
VVPFTELARR HGEDLAVVWI DAHPDVDTPE TGYDGYHAMA VSAIVGQGDP EILDRLPAAV
DPARVALAGL HDGEQDALAH LDEWGLSSFS PADLRESTRP LLDWLAGTGA GKVAVHLDVD
VVDSDEAALG LGLVPGGLTR AQVRRIIADL DEAADVVGLS IAEFIPRSVL AMEALVDGLP
LTER
//
