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Database: UniProt
Entry: A0A0C1R316_9CYAN
LinkDB: A0A0C1R316_9CYAN
Original site: A0A0C1R316_9CYAN 
ID   A0A0C1R316_9CYAN        Unreviewed;       344 AA.
AC   A0A0C1R316;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:KAF3884111.1, ECO:0000313|EMBL:KIE11959.1};
GN   ORFNames=DA73_0209980 {ECO:0000313|EMBL:KIE11959.1}, DA73_0400000305
GN   {ECO:0000313|EMBL:KAF3884111.1};
OS   Tolypothrix bouteillei VB521301.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC   Tolypothrix.
OX   NCBI_TaxID=1479485 {ECO:0000313|EMBL:KIE11959.1};
RN   [1] {ECO:0000313|EMBL:KIE11959.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VB521301 {ECO:0000313|EMBL:KIE11959.1};
RX   PubMed=25700407;
RA   Chandrababunaidu M.M., Singh D., Sen D., Bhan S., Das S., Gupta A.,
RA   Adhikary S.P., Tripathy S.;
RT   "Draft Genome Sequence of Tolypothrix boutellei Strain VB521301.";
RL   Genome Announc. 3:e00001-15(2015).
RN   [2] {ECO:0000313|EMBL:KAF3884111.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VB521301 {ECO:0000313|EMBL:KAF3884111.1};
RA   Sarangi A.N., Mukherjee M., Ghosh S., Singh D., Das A., Kant S., Prusty A.,
RA   Tripathy S.;
RT   "Improved Assembly of Tolypothrix boutellei genome.";
RL   Submitted (NOV-2019) 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:KIE11959.1}.
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DR   EMBL; JHEG04000001; KAF3884111.1; -; Genomic_DNA.
DR   EMBL; JHEG02000037; KIE11959.1; -; Genomic_DNA.
DR   RefSeq; WP_038077646.1; NZ_JHEG04000001.1.
DR   AlphaFoldDB; A0A0C1R316; -.
DR   STRING; 1479485.DA73_0209980; -.
DR   OrthoDB; 9788689at2; -.
DR   Proteomes; UP000029738; 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:UniProtKB-KW.
DR   CDD; cd11593; Agmatinase-like_2; 1.
DR   Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR   InterPro; IPR006035; Ureohydrolase.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR11358:SF44; AGMATINASE 1; 1.
DR   PANTHER; PTHR11358; ARGINASE/AGMATINASE; 1.
DR   Pfam; PF00491; Arginase; 1.
DR   PIRSF; PIRSF036979; Arginase; 2.
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:UP000029738}.
SQ   SEQUENCE   344 AA;  38335 MW;  E5BB4CD5DAE64402 CRC64;
     MQLQDYNPSG VGQINGNLLG LPFDYESAKL IVFGVPWEVT VSYGAGTANG PQRVLDASTQ
     LDLFDIDNPD GWKQGIFMVE IPQDILEKNA YYRDRAAEII QRLEQGKPLT ATPDLTPVLT
     EINQACQQVN QWLFEKTKEA IDNGKRVAAI GGDHSVPLGY YQALATAYPN FGILHIDAHA
     DLRDAYEGFE FSHASIMFNA MKIPQISKLV QVALRDISHD EVQTIDRSNG RIVAYYDPII
     KQKLYSGTTW IEMCREIISH LPEQVYISFD VDGLDPKLCS STGTPVPGGL ELEQAFFLFR
     ELVHSGRKII GFDLCEVGDA EWDGNVGARI VYKLSNLMDL SQKS
//
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