ID Q47UG7_COLP3 Unreviewed; 376 AA.
AC Q47UG7;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=Amidohydrolase family protein {ECO:0000313|EMBL:AAZ26596.1};
GN OrderedLocusNames=CPS_4917 {ECO:0000313|EMBL:AAZ26596.1};
OS Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS psychroerythus).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=167879 {ECO:0000313|EMBL:AAZ26596.1, ECO:0000313|Proteomes:UP000000547};
RN [1] {ECO:0000313|EMBL:AAZ26596.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=34H {ECO:0000313|EMBL:AAZ26596.1};
RX PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT "The psychrophilic lifestyle as revealed by the genome sequence of
RT Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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; CP000083; AAZ26596.1; -; Genomic_DNA.
DR AlphaFoldDB; Q47UG7; -.
DR STRING; 167879.CPS_4917; -.
DR KEGG; cps:CPS_4917; -.
DR HOGENOM; CLU_023257_1_1_6; -.
DR Proteomes; UP000000547; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR CDD; cd05666; M20_Acy1-like; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AAZ26596.1}.
FT DOMAIN 172..265
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 376 AA; 40948 MW; E1876CBBC1B2AA66 CRC64;
MTQWRRHMHR FPECGFDLPL TANFIVEKLE SFGIEVTCNI GQQGIVGVLR CGTGDASIGL
RADMDALHIN EQNSFEHRSC HDGKMHACGH DGHSAMLLGA ASHLAENKGF NGTVHFIFQP
DEEHGKGAQA MIDDGLFERF QINTIYGLHN MPGLAEGQFI VRPGSLMASE SSFEIVIEGV
GGHAAMPHRG IDPIVVGSQI IMALQTIVSR NLNAIEETAV VSATEFITNG TVNVIPSQVI
IKGDCRCFTE DSLVKIEQAM ERIVAGICQA AGAQYQFNFL NTFYPTVNSS TPTEHVIQAA
VAVFGDEHVE RNCLPLTISE DFSSMLRVKP GCYGLLGNGV DSVGGCALHN PEYDFNDNIL
KLGAQYWVQL VSDQLK
//