ID R2S6L5_9ENTE Unreviewed; 287 AA.
AC R2S6L5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Arginase {ECO:0008006|Google:ProtNLM};
GN ORFNames=UAU_03704 {ECO:0000313|EMBL:EOH91165.1};
OS Enterococcus pallens ATCC BAA-351.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1158607 {ECO:0000313|EMBL:EOH91165.1, ECO:0000313|Proteomes:UP000013782};
RN [1] {ECO:0000313|EMBL:EOH91165.1, ECO:0000313|Proteomes:UP000013782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-351 {ECO:0000313|EMBL:EOH91165.1,
RC ECO:0000313|Proteomes:UP000013782};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus pallens BAA-351.";
RL Submitted (FEB-2013) 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:EOH91165.1}.
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DR EMBL; AJAQ01000035; EOH91165.1; -; Genomic_DNA.
DR RefSeq; WP_010758674.1; NZ_KB946310.1.
DR AlphaFoldDB; R2S6L5; -.
DR STRING; 160454.RV10_GL002035; -.
DR PATRIC; fig|1158607.3.peg.3703; -.
DR eggNOG; COG0010; Bacteria.
DR HOGENOM; CLU_085654_1_0_9; -.
DR OrthoDB; 9789727at2; -.
DR Proteomes; UP000013782; 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 SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000013782}.
SQ SEQUENCE 287 AA; 32076 MW; 115029516EA4EECD CRC64;
MKNKTIRLLL PQWQGGNNSD YYFGAELLAH IVPQSKESAL IRVPVNTDLA QELSIEHGVE
GEGQLLAQLE ATTKILEEES PDKIIVLGGD CSISQAPFDY LNGKYDGKLG VLWLDAHPDV
ATIEDSTRDH EMVLGNLLGH GAPQFSDKVK NIIKPDNVFF AGLIYDELRS KDQDVNRLNL
RYAVPDQLKK DSQPILDWLK ENQIEHIAVH FDLDVLSPQD FRSIYPAEPY LEEFGAAIGE
LTLKEVTRIL TDISKQADIV GLSIAEHLPW DAMNLRAALA QLPLFND
//
