ID A0A0Q4H6G0_9MICO Unreviewed; 440 AA.
AC A0A0Q4H6G0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Proline iminopeptidase {ECO:0000313|EMBL:KQM81517.1};
GN ORFNames=ASE68_17360 {ECO:0000313|EMBL:KQM81517.1};
OS Agromyces sp. Leaf222.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agromyces.
OX NCBI_TaxID=1735688 {ECO:0000313|EMBL:KQM81517.1, ECO:0000313|Proteomes:UP000050813};
RN [1] {ECO:0000313|EMBL:KQM81517.1, ECO:0000313|Proteomes:UP000050813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf222 {ECO:0000313|EMBL:KQM81517.1,
RC ECO:0000313|Proteomes:UP000050813};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM81517.1, ECO:0000313|Proteomes:UP000050813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf222 {ECO:0000313|EMBL:KQM81517.1,
RC ECO:0000313|Proteomes:UP000050813};
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 -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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:KQM81517.1}.
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DR EMBL; LMKQ01000002; KQM81517.1; -; Genomic_DNA.
DR RefSeq; WP_055862498.1; NZ_LMKQ01000002.1.
DR AlphaFoldDB; A0A0Q4H6G0; -.
DR STRING; 1735688.ASE68_17360; -.
DR OrthoDB; 9796770at2; -.
DR Proteomes; UP000050813; Unassembled WGS sequence.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR002410; Peptidase_S33.
DR PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR43248:SF2; PROLYL AMINOPEPTIDASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 51..201
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
SQ SEQUENCE 440 AA; 48507 MW; 4C5BAF2764CB446D CRC64;
MIAAEYTIPG MHVRDHVVEV PLDWFDDTDT RTITVFAREL VDPVKRRDEL PVLVYLQGGP
GGKGPRPTGP DGWVGEALKA HRVVLLDQRG TGRSSRVDGS VIASIGDPAA QADHLAHFRA
DSIVADAEHL RTTVFGGRRW STLGQSYGGF LTLSYLSHAP EGLAACYVTG GLASVHPDAA
EVYRRTYPRV EAKNREFRAR YPHHVDTLAR IADRLADGDV RLPDGDVLTV RRFQSLGIDF
GMKPGYERMH FLVDEAFDAA SDELTGTFLA QVEARSSYRD NPLFAVMQES IYASDATGAT
NWAAQAERDR LPQFAESARP LLMTGEMMYP WMFREISALQ PFEAAVELMA ARTEWSALYD
LDRLAANEVP LAAAVYFDDM YVDAGLQLAT AEHVGNARAW VTNEYEHDGI GAERVVPRLF
ELVDELGGPR RDRAGEGAAA
//