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Database: UniProt
Entry: T0HFC1_9SPHN
LinkDB: T0HFC1_9SPHN
Original site: T0HFC1_9SPHN 
ID   T0HFC1_9SPHN            Unreviewed;       422 AA.
AC   T0HFC1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN   ORFNames=L284_12460 {ECO:0000313|EMBL:EQB15071.1};
OS   Novosphingobium lindaniclasticum LE124.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1096930 {ECO:0000313|EMBL:EQB15071.1, ECO:0000313|Proteomes:UP000015527};
RN   [1] {ECO:0000313|EMBL:EQB15071.1, ECO:0000313|Proteomes:UP000015527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LE124 {ECO:0000313|EMBL:EQB15071.1,
RC   ECO:0000313|Proteomes:UP000015527};
RX   PubMed=24029761;
RA   Saxena A., Nayyar N., Sangwan N., Kumari R., Khurana J.P., Lal R.;
RT   "Genome Sequence of Novosphingobium lindaniclasticum LE124T, Isolated from
RT   a Hexachlorocyclohexane Dumpsite.";
RL   Genome Announc. 1:e00715-13(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:EQB15071.1}.
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DR   EMBL; ATHL01000077; EQB15071.1; -; Genomic_DNA.
DR   RefSeq; WP_021234337.1; NZ_ATHL01000077.1.
DR   AlphaFoldDB; T0HFC1; -.
DR   PATRIC; fig|1096930.3.peg.2488; -.
DR   eggNOG; COG0624; Bacteria.
DR   OrthoDB; 9776600at2; -.
DR   Proteomes; UP000015527; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF17; BLL2699 PROTEIN; 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.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015527};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..422
FT                   /note="Peptidase M20 dimerisation domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004563869"
FT   DOMAIN          214..305
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   422 AA;  44988 MW;  BE5A8E7C967CD16E CRC64;
     MIRYFMPGAL MLAALPPIAS AQPVTAEALR RDPAFKAAQA HLARDYDRIV AETIRITEIP
     APPFKEAERA SAVAVMMREA GLRDVHIDEE GNAVGIRPGT GNQSMVAIGA HLDTVFPEGT
     PIKVRREGDR LLAPGISDNS VSVAVLLAFV RALDAGAVKT KQDLLFVANV GEEERGAFRG
     VRYLLQRSPY HSRISAFIGL EPGNTGGITN VGIGVRRYTV TYKGPGGHSM FAFGTVNPAT
     AMAETIVRFD RYRPLDRTTV WNVGLVSGGT SINTIPASVS MSVDMRSTNA ADLDRLDMFF
     RKAVADGTTA ENAARGGAKG TVAAKIETVL PIERPVTHIP DDTMLLRNAV SAIRSGGMEP
     SMRSGSSDSA IPQDMGLPGL TLDSGMEYVA PHSPTEAIVL DRPTNLRVMG NTLATLLLTA
     NQ
//
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