GenomeNet

Database: UniProt
Entry: A0A2A2HEJ7_9EURY
LinkDB: A0A2A2HEJ7_9EURY
Original site: A0A2A2HEJ7_9EURY 
ID   A0A2A2HEJ7_9EURY        Unreviewed;       295 AA.
AC   A0A2A2HEJ7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:PWL07709.1};
DE            EC=3.5.3.11 {ECO:0000313|EMBL:PWL07709.1};
GN   Name=speB {ECO:0000313|EMBL:PWL07709.1};
GN   ORFNames=ASJ82_06795 {ECO:0000313|EMBL:PAV07891.1}, MSCUN_14620
GN   {ECO:0000313|EMBL:PWL07709.1};
OS   Methanosphaera cuniculi.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=1077256 {ECO:0000313|EMBL:PAV07891.1, ECO:0000313|Proteomes:UP000217528};
RN   [1] {ECO:0000313|EMBL:PWL07709.1, ECO:0000313|Proteomes:UP000246004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4103 {ECO:0000313|EMBL:PWL07709.1,
RC   ECO:0000313|Proteomes:UP000246004};
RA   Poehlein A., Seedorf H., Daniel R.;
RT   "Genome sequence of Methanosphaera cuniculi DSM 4103.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PAV07891.1, ECO:0000313|Proteomes:UP000217528}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1R-7 {ECO:0000313|EMBL:PAV07891.1,
RC   ECO:0000313|Proteomes:UP000217528};
RX   PubMed=28826405; DOI=10.1186/s12864-017-4036-4;
RA   Gilmore S.P., Henske J.K., Sexton J.A., Solomon K.V., Seppala S., Yoo J.I.,
RA   Huyett L.M., Pressman A., Cogan J.Z., Kivenson V., Peng X., Tan Y.,
RA   Valentine D.L., O'Malley M.A.;
RT   "Genomic analysis of methanogenic archaea reveals a shift towards energy
RT   conservation.";
RL   BMC Genomics 18:639-639(2017).
CC   -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC       {ECO:0000256|ARBA:ARBA00009227}.
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:PAV07891.1}.
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; LMVN01000006; PAV07891.1; -; Genomic_DNA.
DR   EMBL; LWMS01000045; PWL07709.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2HEJ7; -.
DR   OrthoDB; 7186at2157; -.
DR   Proteomes; UP000217528; Unassembled WGS sequence.
DR   Proteomes; UP000246004; Unassembled WGS sequence.
DR   GO; GO:0008783; F:agmatinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR   CDD; cd11593; Agmatinase-like_2; 1.
DR   Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR   InterPro; IPR005925; Agmatinase-rel.
DR   InterPro; IPR006035; Ureohydrolase.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR   NCBIfam; TIGR01230; agmatinase; 1.
DR   PANTHER; PTHR11358:SF43; AGMATINASE; 1.
DR   PANTHER; PTHR11358; ARGINASE/AGMATINASE; 1.
DR   Pfam; PF00491; Arginase; 1.
DR   PIRSF; PIRSF036979; Arginase; 1.
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
SQ   SEQUENCE   295 AA;  33326 MW;  54D5961B50F6A4C8 CRC64;
     MFFYADNMMN FAFAESLDDD DYIPGGYGLF GVPFDSTTSY MAGSRYGPKA IREASYNFES
     YNMRFNKDVS AVCYDIGDVQ VNNGNYMATN MMIKDTVKSL LEMDLKPIAM GGEHTITNGV
     LGGIYEYDED LYHDMSIIHF DAHFDMRDEY MGEKFSHAAV LRRLHELKPK DITQLGIRSA
     EYDEFEYVKS HDNINYFTSY DIKDNIQNVL NYLEDLENPL YISVDIDVLD PAYAPSVGTP
     ASCGITPFEL EDMMAIICKK DVIGLDVVEV SSNTIGDPTS VNAAKVIYDF LTHKS
//
DBGET integrated database retrieval system