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Database: UniProt
Entry: A0A0L8LSH4_9ACTN
LinkDB: A0A0L8LSH4_9ACTN
Original site: A0A0L8LSH4_9ACTN 
ID   A0A0L8LSH4_9ACTN        Unreviewed;       371 AA.
AC   A0A0L8LSH4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:KOG41103.1};
GN   ORFNames=ADK74_21235 {ECO:0000313|EMBL:KOG41103.1};
OS   Streptomyces decoyicus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=249567 {ECO:0000313|EMBL:KOG41103.1, ECO:0000313|Proteomes:UP000037606};
RN   [1] {ECO:0000313|Proteomes:UP000037606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 2666 {ECO:0000313|Proteomes:UP000037606};
RG   Consortium for Microbial Forensics and Genomics (microFORGE);
RA   Knight B.M., Roberts D.P., Lin D., Hari K., Fletcher J., Melcher U.,
RA   Blagden T., Winegar R.A.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00742, ECO:0000256|RuleBase:RU003684}.
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:KOG41103.1}.
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DR   EMBL; LGUU01000239; KOG41103.1; -; Genomic_DNA.
DR   RefSeq; WP_030075272.1; NZ_LGUU01000239.1.
DR   AlphaFoldDB; A0A0L8LSH4; -.
DR   PATRIC; fig|249567.6.peg.4651; -.
DR   Proteomes; UP000037606; 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   CDD; cd09990; Agmatinase-like; 1.
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:SF26; AGMATINASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11358; ARGINASE/AGMATINASE; 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   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   371 AA;  40330 MW;  79C20364BB9D68A0 CRC64;
     MEGVPPDAWK WELDRTSDPR RDPGPINLQR YAFVPAYAGI ATFFGLPLCL NPDDLRAGHV
     DVAVVGAPVD MSTGHRGAAY GPRAIRADER ILPNTPQMLV NPSTRIKPFE ELTVVDYGDA
     AVDPFSIDNS MEPIRALVRE IAGTGAIPIV LGGDHSILWP DAAAMADVYG AGKVGVIHFD
     AHPDCSHDLF GHLTSHATPI RRLIEDEHVP GRNFIQIGLR SAIAPDDELF DWMREHGLRA
     HFMAEIDRRG FDVVLQQAID EALDGPEHLF VSLDIDVLDP AFAPGTGTPE PPGLTNRELL
     PAIRRICHET PVVGMDIVEV APHLDPGNTT TMNARRAIFE ALTGIAMRRK GLPGPDYLDP
     EVAGPPPGQQ T
//
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