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Database: UniProt
Entry: Q1YLD4_AURMS
LinkDB: Q1YLD4_AURMS
Original site: Q1YLD4_AURMS 
ID   Q1YLD4_AURMS            Unreviewed;       388 AA.
AC   Q1YLD4;
DT   02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Peptidase, M20 family, amidohydrolase family protein {ECO:0000313|EMBL:EAS51797.1};
GN   ORFNames=SI859A1_02613 {ECO:0000313|EMBL:EAS51797.1};
OS   Aurantimonas manganoxydans (strain ATCC BAA-1229 / DSM 21871 / SI85-9A1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Aurantimonadaceae; Aurantimonas.
OX   NCBI_TaxID=287752 {ECO:0000313|EMBL:EAS51797.1, ECO:0000313|Proteomes:UP000000321};
RN   [1] {ECO:0000313|EMBL:EAS51797.1, ECO:0000313|Proteomes:UP000000321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SI85-9A1 {ECO:0000313|EMBL:EAS51797.1,
RC   ECO:0000313|Proteomes:UP000000321};
RX   PubMed=18344346; DOI=10.1128/AEM.01656-07;
RA   Dick G.J., Podell S., Johnson H.A., Rivera-Espinoza Y., Bernier-Latmani R.,
RA   McCarthy J.K., Torpey J.W., Clement B.G., Gaasterland T., Tebo B.M.;
RT   "Genomic insights into Mn(II) oxidation by the marine alphaproteobacterium
RT   Aurantimonas sp. strain SI85-9A1.";
RL   Appl. Environ. Microbiol. 74:2646-2658(2008).
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:EAS51797.1}.
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DR   EMBL; AAPJ01000001; EAS51797.1; -; Genomic_DNA.
DR   RefSeq; WP_009210435.1; NZ_CH672387.1.
DR   AlphaFoldDB; Q1YLD4; -.
DR   HOGENOM; CLU_023257_1_0_5; -.
DR   OrthoDB; 9777385at2; -.
DR   BioCyc; AURANTIMONAS:SI859A1_02613-MONOMER; -.
DR   Proteomes; UP000000321; Unassembled WGS sequence.
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:SF170; CLAN MH, FAMILY M20, PEPTIDASE T-LIKE METALLOPEPTIDASE; 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:EAS51797.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000321}.
FT   DOMAIN          189..286
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   388 AA;  40646 MW;  5CA6361BAB2A497E CRC64;
     MEKVAERLLS AADLGVLRDL RHALHREPEV SGEEAETARR VAAFLGETGP DRLVTSLGGH
     GVAAVYDSGE PGPTLMVRAE LDALPIEQKS DRAWRSTRPG TSHLCGHDGH MATLAGVALA
     LGRERPGQGR AVLLFQPAEE DGSGAAAVLA DPAFDAIAPD IAIALHNMPG IARGRAALIE
     GPANCASRSL QIALSGTTAH ASSPDQGRSP MTALCELMPG LTALGCGGDL DADFSLVTIT
     HASMGEREAG IAPGTAELWA TLRTLTDARM GDLVARAEAL VRDAAERSGL GVAIRYDDVF
     AHCVNDGEAT AILRRALDEE GVPHDTSLLP TRASEDFGRF GAKARSAMFL LGSGEDHSGL
     HTPQYDFPDE LIGLGARIFL RAIRKVLG
//
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