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Database: UniProt
Entry: A0A099FBP0_9RHOB
LinkDB: A0A099FBP0_9RHOB
Original site: A0A099FBP0_9RHOB 
ID   A0A099FBP0_9RHOB        Unreviewed;       388 AA.
AC   A0A099FBP0;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:KGJ07653.1};
GN   ORFNames=IC63_07775 {ECO:0000313|EMBL:KGJ07653.1};
OS   Paracoccus sphaerophysae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=690417 {ECO:0000313|EMBL:KGJ07653.1, ECO:0000313|Proteomes:UP000029917};
RN   [1] {ECO:0000313|EMBL:KGJ07653.1, ECO:0000313|Proteomes:UP000029917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAMBI 3106 {ECO:0000313|EMBL:KGJ07653.1,
RC   ECO:0000313|Proteomes:UP000029917};
RA   McGinnis J.M., Wolfgang W.J.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KGJ07653.1, ECO:0000313|Proteomes:UP000029917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAMBI 3106 {ECO:0000313|EMBL:KGJ07653.1,
RC   ECO:0000313|Proteomes:UP000029917};
RA   Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT   "Paracoccus sanguinis sp. nov., isolated from clinical specimens of New
RT   York State patients.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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:KGJ07653.1}.
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DR   EMBL; JRKS01000018; KGJ07653.1; -; Genomic_DNA.
DR   RefSeq; WP_036718629.1; NZ_JRKS01000018.1.
DR   AlphaFoldDB; A0A099FBP0; -.
DR   STRING; 690417.IC63_07775; -.
DR   OrthoDB; 9777385at2; -.
DR   Proteomes; UP000029917; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:KGJ07653.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029917}.
FT   DOMAIN          188..272
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   388 AA;  41548 MW;  49CDE3FAB2DB9A9F CRC64;
     MPVKNRFAEM LPEITAWRRE FHENPELLYE VHRTAGRVAE LLREFGVDEV TEGIGRTGVV
     GVIRGKTDTR GRVIGLRADM DALPINEITG LDYASKTPGV MHACGHDGHT AMLLGAAKYL
     AETRNFDGTA VVIFQPAEEG GAGGLAMVED GLVDRWGIQE FYGMHNMPGI PVGSFAIREG
     GIMAAADQFD IVVTGKGGHA AKPHECIDST LIAAQIIVAL QSIVSRNVDP LKNAVVSTCV
     VQTDSTAYNV IPQVVRLKGT ARSLDPGVRA QLESGISRVS QGIAAAFGAQ VEVTYHRGYP
     VTVNHPEETG HAISVARDLS ADVNTDVAPM MGGEDFSYML EQKPGAYIFV GNGDTAMVHH
     PAYNFDDDAI PFGSSWYAGM VEARMPAA
//
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