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}.
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; 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
//