ID A0A101UJ85_9ACTN Unreviewed; 519 AA.
AC A0A101UJ85;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:KUO11703.1};
GN ORFNames=AQJ58_11070 {ECO:0000313|EMBL:KUO11703.1};
OS Streptomyces sp. DSM 15324.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1739111 {ECO:0000313|EMBL:KUO11703.1, ECO:0000313|Proteomes:UP000053431};
RN [1] {ECO:0000313|EMBL:KUO11703.1, ECO:0000313|Proteomes:UP000053431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15324 {ECO:0000313|EMBL:KUO11703.1,
RC ECO:0000313|Proteomes:UP000053431};
RA Ruckert C., Winkler A., Kalinowski J., Wink J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces sp. DSM 15324, isolated from soil.";
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:KUO11703.1}.
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DR EMBL; LMXA01000009; KUO11703.1; -; Genomic_DNA.
DR RefSeq; WP_067248190.1; NZ_KQ949025.1.
DR AlphaFoldDB; A0A101UJ85; -.
DR OrthoDB; 4498590at2; -.
DR Proteomes; UP000053431; 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:UP000053431};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..519
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007108061"
FT DOMAIN 413..518
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
FT REGION 24..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 519 AA; 54766 MW; 473E6B0FB21C22DD CRC64;
MARFLRWTAL AAAAALLAAG CAGGSSGGGE DEKRPSADAR PSVGSSRTAR AALPAALTRQ
KVDWGRCRGR ADSAAPGSEW RCATMKVPLD WSKPDGKTIG LALIRARSRG SGGERIGSLL
FNFGGPGGSG VATLPPYGST FSALRERYDL VSWDPRGVGA SEGIRCRDDK DIQAAESLDS
TPDTATEEEA YLSDAAAFGR GCAKAAGDLL AHVSTTDTAR DMDLMRQVLG DTKTHYFGIS
YGTELGGVYA HLFPEHVGRL VLDAVVDPTA DAVGHAENQA RGFQRALDDY LKSTGQDPEQ
GTAKIADLLE RLDGDPLPTS EGRRLNQALA VTGIVLPLYS EQSWPALTSA LESAEQGDGT
ELLALADTYN ERDSSGHYGT ASHAQRVISC SDDKQRPTAE EARKRLPEFE RISPVFGDFL
GWDTAGWCHD WPVAGQYDTP EVSAPGAAPM LLVGNTGDPA TPYEGARRMA DELGEGVGVL
LTWKGEGHVA YGSGSDCVDA TVNAYLLKGT VPQDGKVCS
//