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Database: UniProt
Entry: A0A0Q5JRD4_9MICO
LinkDB: A0A0Q5JRD4_9MICO
Original site: A0A0Q5JRD4_9MICO 
ID   A0A0Q5JRD4_9MICO        Unreviewed;       605 AA.
AC   A0A0Q5JRD4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Amidase domain-containing protein {ECO:0000259|Pfam:PF01425};
GN   ORFNames=ASF76_00400 {ECO:0000313|EMBL:KQR25802.1};
OS   Microbacterium sp. Leaf151.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1736276 {ECO:0000313|EMBL:KQR25802.1, ECO:0000313|Proteomes:UP000051582};
RN   [1] {ECO:0000313|EMBL:KQR25802.1, ECO:0000313|Proteomes:UP000051582}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf151 {ECO:0000313|EMBL:KQR25802.1,
RC   ECO:0000313|Proteomes:UP000051582};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQR25802.1, ECO:0000313|Proteomes:UP000051582}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf151 {ECO:0000313|EMBL:KQR25802.1,
RC   ECO:0000313|Proteomes:UP000051582};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQR25802.1}.
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DR   EMBL; LMOR01000001; KQR25802.1; -; Genomic_DNA.
DR   RefSeq; WP_055951368.1; NZ_LMOR01000001.1.
DR   AlphaFoldDB; A0A0Q5JRD4; -.
DR   STRING; 1736276.ASF76_00400; -.
DR   OrthoDB; 182039at2; -.
DR   Proteomes; UP000051582; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR   Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR   InterPro; IPR020556; Amidase_CS.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   InterPro; IPR002105; Dockerin_1_rpt.
DR   InterPro; IPR036439; Dockerin_dom_sf.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR42678; AMIDASE; 1.
DR   PANTHER; PTHR42678:SF34; AMIDASE C869.01-RELATED; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   Pfam; PF00404; Dockerin_1; 1.
DR   SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR   SUPFAM; SSF63446; Type I dockerin domain; 1.
DR   PROSITE; PS00571; AMIDASES; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..605
FT                   /note="Amidase domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006254010"
FT   DOMAIN          134..424
FT                   /note="Amidase"
FT                   /evidence="ECO:0000259|Pfam:PF01425"
SQ   SEQUENCE   605 AA;  61814 MW;  F2293B0764EA4543 CRC64;
     MTPLSRRALA VAAALGVVAA GSLVVPAAAV AAPAPAAAPF LAPYYTELDL TGDEQVTEAD
     LDVLAARIGL ASDDAGWSDA AAADLDDDGA ITASDLALLS QRVIYDDGPF QLVEADTVAM
     QAAMNAGVIT SVSLTQQYLD RIAAYDKVVR QDGGRPLNSL ITTSTVALQA AAEADAVRAE
     KGMTSMLLGI PVALKDNYNT VDMPTTAGCG CWNANQTTTD ATMVEGLRAD GAVIVAKASM
     DEFAINLSSQ WSALQPAGTA LTVSSPYDTT KTSGGSSGGT GAAIAANLAG LGFGTDTGGS
     IRIPSTYNQL VGVRPTVGLA SRAGIVPLAL SQDTGGPMAR SVLDATVALD AVVGQDAGDP
     ITARQEGKVP ETYTSYLDAD SLAGTKIGYI ASMLGTDPIT QRLFTEARAS LEARGAAVVE
     VAEPEGFAAI VGEGSGSGPE FNHDLNDYIA AYLNPAVTTR SLLEISQSPN IVPGRAESPY
     GARAAITEET YQAWAGPEGT HTLQLARGKE IMTALMEDQN LDAVIYPSGN PYSTIGTNMR
     LSPNTGLPAV TVPMGQGVAG EASTGGVNLE FLGRDFAEGP LLGLAYSFEQ ATHARTSPAA
     YGPLG
//
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