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Database: UniProt
Entry: A0A074L0G0_9BACT
LinkDB: A0A074L0G0_9BACT
Original site: A0A074L0G0_9BACT 
ID   A0A074L0G0_9BACT        Unreviewed;       485 AA.
AC   A0A074L0G0;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN   ORFNames=EL17_02765 {ECO:0000313|EMBL:KEO74614.1};
OS   Anditalea andensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Anditalea.
OX   NCBI_TaxID=1048983 {ECO:0000313|EMBL:KEO74614.1, ECO:0000313|Proteomes:UP000027821};
RN   [1] {ECO:0000313|EMBL:KEO74614.1, ECO:0000313|Proteomes:UP000027821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LY1 {ECO:0000313|EMBL:KEO74614.1,
RC   ECO:0000313|Proteomes:UP000027821};
RA   Yang L., Wei S., Tay Q.X.M.;
RT   "Characterization and application of a salt tolerant electro-active
RT   bacterium.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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:KEO74614.1}.
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DR   EMBL; JMIH01000014; KEO74614.1; -; Genomic_DNA.
DR   RefSeq; WP_035070546.1; NZ_JMIH01000014.1.
DR   AlphaFoldDB; A0A074L0G0; -.
DR   STRING; 1048983.EL17_02765; -.
DR   eggNOG; COG0624; Bacteria.
DR   OrthoDB; 9792335at2; -.
DR   Proteomes; UP000027821; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.150.900; -; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR047177; Pept_M20A.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR45962; N-FATTY-ACYL-AMINO ACID SYNTHASE/HYDROLASE PM20D1; 1.
DR   PANTHER; PTHR45962:SF1; N-FATTY-ACYL-AMINO ACID SYNTHASE/HYDROLASE PM20D1; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF036696; ACY-1; 2.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027821};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          234..378
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   485 AA;  53709 MW;  87114E640EC47220 CRC64;
     MKNLLIISLI LVGALVGYII FTTFTFSSKQ IQPDPAEKIL IPNSAIENFS RALSIPTISH
     EDPANFDPSA FYEFARFLKE AYPLSSSQLE ITYINEFSII YKWEGSDNSL PPIILMGHID
     VVPVEDPTQW TEPPFSGNIR DGKIWGRGAI DDKISVIGNM EAVEILLQEE YKPNRTVYLC
     FGHDEEIGGE KGASAIVDHL KNRGVNAAFV LDEGFAITQG MVPGITKDVA LIGTAEKGFV
     TLELSVSIEG GHSSMPAHET SIDVMAKAVT KLKDNPFPYL ISQPVQDFMA YAGPEMNSFT
     SRMAFANPSI FRPLIISTLS KEPSGNALIR TTTSPTIFRA GIKDNIIPIQ AKATVNFRTL
     PGTTMQDVKD RVLTLIDDDR IVIKEGTFNS EAPGSSQVET FGYETLHQSI KEIFPQVIVA
     PNLVLGATDS RHYYPISDQI YRFVPFYLNK DNISTFHGTD EHLAISDLEN AIRFYRQLIL
     NATSK
//
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