ID D6ZGH0_MOBCV Unreviewed; 409 AA.
AC D6ZGH0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:ADI67728.1};
GN OrderedLocusNames=HMPREF0573_11409 {ECO:0000313|EMBL:ADI67728.1};
OS Mobiluncus curtisii (strain ATCC 43063 / DSM 2711 / V125) (Falcivibrio
OS vaginalis).
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Mobiluncus.
OX NCBI_TaxID=548479 {ECO:0000313|EMBL:ADI67728.1, ECO:0000313|Proteomes:UP000006742};
RN [1] {ECO:0000313|Proteomes:UP000006742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43063 / DSM 2711 / V125
RC {ECO:0000313|Proteomes:UP000006742};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R., Gibbs R.;
RT "Complete sequence of Mobiluncus curtisii ATCC 43063.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001992; ADI67728.1; -; Genomic_DNA.
DR RefSeq; WP_013189371.1; NC_014246.1.
DR AlphaFoldDB; D6ZGH0; -.
DR STRING; 548479.HMPREF0573_11409; -.
DR GeneID; 55565520; -.
DR KEGG; mcu:HMPREF0573_11409; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_6_0_11; -.
DR Proteomes; UP000006742; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:0000313|EMBL:ADI67728.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006742}.
FT DOMAIN 196..292
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 409 AA; 43899 MW; B2D5074AC2787AE1 CRC64;
MSNLDIHAAV TELGSWQDET YQWLHQHPEL SMSETETCNF IEKQLQDFGY QTEIIGGGVV
GILRNGTGKT TLFRADMDGL PVREETGLPY ASTITRRDRD GNEVPVMHAC GHDVHITAGL
GAARVLAAHR DSWSGTHIAL FQPGEETAEG AKSMVAAGLV DKIPRPDVAF GQHVLTGPMP
TGAVGTHVGA ILSTGASLKI TLHGKGSHGS MPHMGIDPVV LASTIVMRLQ TIVSREIDPF
QMAVVTVGSV QAGTKSNIIP ERATLLVNIR AYDVAVREHL LTAIKRIVNA ECVAAGSPKP
AEFELYDSYP LTANDPQVTK KVTEAFLAHF GAERVGDCGE VPASEDFSTI PDAFGIPYCY
WGLGGFRDDD PKFPNHNPKF APVMQPTLAT GIEAVLAAVM AWLGKSEQE
//
