ID A0A1J4NPL3_9ACTN Unreviewed; 519 AA.
AC A0A1J4NPL3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:OIJ63110.1};
GN ORFNames=WN71_036040 {ECO:0000313|EMBL:OIJ63110.1};
OS Streptomyces mangrovisoli.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1428628 {ECO:0000313|EMBL:OIJ63110.1, ECO:0000313|Proteomes:UP000034196};
RN [1] {ECO:0000313|EMBL:OIJ63110.1, ECO:0000313|Proteomes:UP000034196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC149T {ECO:0000313|Proteomes:UP000034196};
RA Lee L.-H., Ser H.-L.;
RT "Genome sequence of Streptomyces mangrovisoli MUSC 149.";
RL Submitted (OCT-2016) 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:OIJ63110.1}.
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DR EMBL; LAVA02000116; OIJ63110.1; -; Genomic_DNA.
DR RefSeq; WP_046591212.1; NZ_LAVA02000116.1.
DR AlphaFoldDB; A0A1J4NPL3; -.
DR STRING; 1428628.WN71_036040; -.
DR OrthoDB; 4498590at2; -.
DR Proteomes; UP000034196; 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:UP000034196};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..519
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039496871"
FT DOMAIN 412..517
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
FT REGION 23..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 519 AA; 54585 MW; 20D473F652636F9F CRC64;
MQRFVRWTAA VAAAVLLAGC SGGSSGGGGD DKAKGTSTGP SASAASTGAS ALPASLTSQK
LDWGRCRATR GSAAPSSDWQ CATMRAPLDW SKPDGSTIGI ALIREKADGS PGKRIGSLLF
NFGGPGGSGI STMPSYAAIV PQLRERYDLV SWDPRGVGAS EGVRCRSDKD IQTAESIDVT
PDTPAEEKAY FADATSFGKG CERAAGSLMA HVSTTDTARD MDLMRQVLGD KQMHYFGISY
GTELGGVYAH LFPKNVGRLI LDAVVDPSAD AVGHAENQAR GFQRALNDYL KSTGQDPEQG
SQKIVDLLKR IDAKPLPASS GRKLTQTLAL TGIVLPLYSR TSWPTLTSAL DSAEHGDGSE
LLALADDYNE RDASGHYATT THSQRVISCL DDKQRPTPEQ TKKLLPTFEK ISPVFGDFLG
WDTAGWCHDW PVAGEYDTPE VSAPGAAPIL LVGNTGDPAT PYEGARKMAD ELGKGVGVEL
TWKGEGHGAY GNGSDCVDST VDAYLLKGTV PKDGKVCSS
//
