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Database: UniProt/TrEMBL
Entry: A0A0M4DMA0_9ACTN
LinkDB: A0A0M4DMA0_9ACTN
Original site: A0A0M4DMA0_9ACTN 
ID   A0A0M4DMA0_9ACTN        Unreviewed;       276 AA.
AC   A0A0M4DMA0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Serine protease {ECO:0000313|EMBL:ALC27088.1};
GN   ORFNames=ABE83_08325 {ECO:0000313|EMBL:ALC27088.1};
OS   Streptomyces sp. CFMR 7.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1649184 {ECO:0000313|EMBL:ALC27088.1, ECO:0000313|Proteomes:UP000061366};
RN   [1] {ECO:0000313|EMBL:ALC27088.1, ECO:0000313|Proteomes:UP000061366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFMR-7 {ECO:0000313|EMBL:ALC27088.1,
RC   ECO:0000313|Proteomes:UP000061366};
RA   Sudesh K.;
RT   "Complete genome sequence of Streptomyces sp strain CFMR 7, a natural
RT   rubber degrading Actinomycetes isolated from Penang, Malaysia.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000256|ARBA:ARBA00007664}.
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DR   EMBL; CP011522; ALC27088.1; -; Genomic_DNA.
DR   RefSeq; WP_053559071.1; NZ_VEHK01000011.1.
DR   AlphaFoldDB; A0A0M4DMA0; -.
DR   KEGG; scz:ABE83_08325; -.
DR   PATRIC; fig|1649184.3.peg.1788; -.
DR   Proteomes; UP000061366; Chromosome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR   PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000313|EMBL:ALC27088.1};
KW   Protease {ECO:0000313|EMBL:ALC27088.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..276
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005792402"
FT   DOMAIN          36..276
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
SQ   SEQUENCE   276 AA;  28043 MW;  5751963D1D0721D6 CRC64;
     MPRPVVRALT GVLALTAAAV VTPLAAPLPA AADSVVVGGQ PAPVADSPWA VALSSRDRFG
     GARSGQFCGG VVVAPTKVLT VAHCLGEEAL GGPVSRVRDL RVIAGRERLS ETTGQEIPVR
     GVWVNPAYDP DTNAGDLAVL TLSRALPRSS VIPMARTGDE AYRAGTGAAV YGWGDTTGAG
     TYASVLRSAR VQVLPDAECA RAYPGGREGT YNASGMLCAG DPRGGRDACQ GDSGGPLVAR
     GRLIGLVSWG SGCGRPGSPG VYTRVSAALK WAEGRI
//
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