ID A0A0F4PXX3_9GAMM Unreviewed; 499 AA.
AC A0A0F4PXX3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN ORFNames=TW72_06385 {ECO:0000313|EMBL:KJZ00326.1};
OS Pseudoalteromonas ruthenica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=151081 {ECO:0000313|EMBL:KJZ00326.1, ECO:0000313|Proteomes:UP000033664};
RN [1] {ECO:0000313|EMBL:KJZ00326.1, ECO:0000313|Proteomes:UP000033664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S3137 {ECO:0000313|EMBL:KJZ00326.1,
RC ECO:0000313|Proteomes:UP000033664};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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:KJZ00326.1}.
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DR EMBL; JXXZ01000006; KJZ00326.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4PXX3; -.
DR PATRIC; fig|151081.8.peg.2971; -.
DR eggNOG; COG0624; Bacteria.
DR OrthoDB; 9761532at2; -.
DR Proteomes; UP000033664; Unassembled WGS sequence.
DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR Gene3D; 3.30.70.360; -; 2.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR010964; M20A_pepV-rel.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01887; dipeptidaselike; 1.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF33; DIPEPTIDASE SAOUHSC_01868-RELATED; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Dipeptidase {ECO:0000256|ARBA:ARBA00022997};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022997};
KW Reference proteome {ECO:0000313|Proteomes:UP000033664};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..499
FT /note="Peptidase M20 dimerisation domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002474788"
FT DOMAIN 283..395
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 499 AA; 54337 MW; BD08937949667C38 CRC64;
MKSSLFAAAL ALLSHASLSH ATPTYHDALA QYAVDEYQDA QIHTLANMVS FATVNTSAYK
TPDNPEFIGF KHLLKMKAAQ LGLDYQDLGY TVLIGMGEQQ DKVTIVTHGD VQPADATKWA
KSPFVLDSTS EPGKLIARGT EDDKGAIATA LYAMKAIKDQ GIQLDNRIEL MIYLAEESDW
QPLRTFMQSY QQPKYAVTID ASYPVVVAEK GWSLVAPTFS GTYQGSQMYV SELTGGAFVS
QIPEDASVRV HNASAEAIAT LRANAAQLSD VEVQIEELGD NEVLVRVKGT SAHSSEPESG
VNAIAHLGAV FNGLELATNA DGQALLFINE LIGLDLYGKQ FGDIAYSHDF MGPMTVAPTL
IERQNDTLTL SVNLRRPEGK PESQLRTEIN SALNNWQRRH QVELAAVDIE IGTPMLLDDA
PHADALLNIF KHYTGDEQAE FVSIGGGTNA KLFNNAVSFG PSMPGKAYTG HSEHEFMTPE
QLRLNLKMYT AMMVTLGNM
//
