ID A0A1Q4VEX3_9ACTN Unreviewed; 521 AA.
AC A0A1Q4VEX3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:OKH96374.1};
GN ORFNames=AB852_07200 {ECO:0000313|EMBL:OKH96374.1};
OS Streptomyces uncialis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1048205 {ECO:0000313|EMBL:OKH96374.1, ECO:0000313|Proteomes:UP000186455};
RN [1] {ECO:0000313|EMBL:OKH96374.1, ECO:0000313|Proteomes:UP000186455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCA2648 {ECO:0000313|EMBL:OKH96374.1,
RC ECO:0000313|Proteomes:UP000186455};
RA Yan X., Huang T., Ge H., Shen B.;
RT "Cloning and characterization of the uncialamcin biosynthetic gene
RT cluster.";
RL Submitted (JUN-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:OKH96374.1}.
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DR EMBL; LFBV01000001; OKH96374.1; -; Genomic_DNA.
DR RefSeq; WP_073784687.1; NZ_LFBV01000001.1.
DR AlphaFoldDB; A0A1Q4VEX3; -.
DR STRING; 1048205.AB852_07200; -.
DR Proteomes; UP000186455; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013595; Pept_S33_TAP-like_C.
DR PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000186455};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..521
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012795546"
FT DOMAIN 416..520
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
FT REGION 23..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 521 AA; 55366 MW; 4D1F4A8F19D45093 CRC64;
MPKPLPVRAA ALAATAVLLS ASTAGCGGDD TKDRKDPKAD DLTAQRLTWK DCPAPAQSEG
GGPAPSPLPD GELWECATLK APLDWGDPDG DTIGIALIRA RTSGTDGERI GSLIFNFGGP
GGSGVTTLPA FAGEYEKLRT RYDLVSFDPR GVGRSAGVKC EDDEQLDEYF QQDATPDDTA
EQRKLVDNTR AFNAACEDNS ARVLPRVRTT DAARDLDLMR QVLGDDELHY FGISYGTELG
GVYAHLFPKN VGRAVFDAVV DPTQDPEQGA LGQARGFQLA LDNYAKDCTS QVEDCPVGDT
AQDVKDRIAK LLADLEKKPL PGVFPRDLTQ TAATGGIAQS LYSKDFWEYL TEGLQQAYDG
DGKILMTLSD SMNGRNQDGR YSNIQAANVA INCADDKPRY TPDDVVSRLP RFRAASPLFG
DYLAWSMVSC TDWAVAGAAD HPDVSAPGAA PILVVGNTGD PATPYEGTRK MVDALGPGVG
VELTYKGQGH GAYDSGDPCV REAVDGYLLD GKVPSSGTVC P
//
