ID A0A117PAR0_9ACTN Unreviewed; 555 AA.
AC A0A117PAR0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Protease {ECO:0000313|EMBL:KUM76252.1};
GN ORFNames=AQI70_14940 {ECO:0000313|EMBL:KUM76252.1};
OS Streptomyces curacoi.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=146536 {ECO:0000313|EMBL:KUM76252.1, ECO:0000313|Proteomes:UP000054024};
RN [1] {ECO:0000313|EMBL:KUM76252.1, ECO:0000313|Proteomes:UP000054024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40107 {ECO:0000313|EMBL:KUM76252.1,
RC ECO:0000313|Proteomes:UP000054024};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces curacoi DSM 40107, type strain for
RT the species Streptomyces curacoi.";
RL Submitted (OCT-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:KUM76252.1}.
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DR EMBL; LMWJ01000009; KUM76252.1; -; Genomic_DNA.
DR RefSeq; WP_062149069.1; NZ_KQ947987.1.
DR AlphaFoldDB; A0A117PAR0; -.
DR STRING; 146536.AQI70_14940; -.
DR OrthoDB; 4498590at2; -.
DR Proteomes; UP000054024; Unassembled WGS sequence.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:KUM76252.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054024};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..555
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038620243"
FT DOMAIN 416..515
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
FT REGION 513..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 555 AA; 60347 MW; D69CEFD3B2C60FEB CRC64;
MRAPALYSAV GVLLLTALSA APAGSTGAAP GTAELHGTAV AAARARAAGI DFGKCPKEQD
MPAALQCGKV SVPLDYAHPN GKQIELTVSR VRATHKDPHN SKRRVPRKGA LVYNPGGPGA
SGMYFPLIGV MPAWKRLAAA YDLVGYAPRG VERSAPLSCQ EPKQVFKGPL LAPTHPSESH
KKERIARAKA YARGCAQRAG SALRHYNSLN NARDLDVLRA ALGEEKLTFM GASYGTYFGA
LYATLFPSHV RRMVFDSAVN PDPAMVWYRN NLAQSAAFEG RWADFREWVA EHHKVYGLGD
TAEEVLRSYE KVRARLAAEP AGGKVGQEQL QETFLQAGYY DDYWPSRARA LSAYLKGDSK
PLVELAAPAT EAAAEEENSD AVYTAVECND APWPTDWDVW DRDNTRLARV APFETWDNVW
MNLPCAYWQA PRQEPLDVRT GPGEVPPLLI LAAERDAATP YDGALEMHRR LSGSVLVTER
DAGTHGIAYG PNACVNGYVD AYLLEGRLPA RRAACEGHPE PKPERPDDRT DKKRGAHPGT
APGDRPRTAA ARLPH
//
