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Database: UniProt
Entry: A0A2S6GUS5_9PSEU
LinkDB: A0A2S6GUS5_9PSEU
Original site: A0A2S6GUS5_9PSEU 
ID   A0A2S6GUS5_9PSEU        Unreviewed;       260 AA.
AC   A0A2S6GUS5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Trypsin {ECO:0000313|EMBL:PPK68992.1};
GN   ORFNames=CLV40_104239 {ECO:0000313|EMBL:PPK68992.1};
OS   Actinokineospora auranticolor.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinokineospora.
OX   NCBI_TaxID=155976 {ECO:0000313|EMBL:PPK68992.1, ECO:0000313|Proteomes:UP000239203};
RN   [1] {ECO:0000313|EMBL:PPK68992.1, ECO:0000313|Proteomes:UP000239203}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YU 961-1 {ECO:0000313|EMBL:PPK68992.1,
RC   ECO:0000313|Proteomes:UP000239203};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000256|ARBA:ARBA00007664}.
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:PPK68992.1}.
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DR   EMBL; PTIX01000004; PPK68992.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S6GUS5; -.
DR   OrthoDB; 1496095at2; -.
DR   Proteomes; UP000239203; Unassembled WGS sequence.
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; 2.
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; IPR018114; TRYPSIN_HIS.
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; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000239203};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..260
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018252877"
FT   DOMAIN          31..255
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
SQ   SEQUENCE   260 AA;  27311 MW;  207E94DC3EBCCBA2 CRC64;
     MSRSRRFLIP LLGLVLALAG IPATADVPAR VVGGTRAPQG AYPWMARLSM GCGGSLIAPE
     VVLTAGHCVD GTGPDATIQA TFGVVDLQSP KATVVKSVYV YRPEQYTTVS RGYDWALIKL
     ATRVKAPVLP LKRATVTAGP FRVLGWGADK EGGDQQRYLL HAEVPYVDDA TCAPLYTRYG
     YPFLPSGMLC AGIVNVGGVD TCQGDSGGPM VIGEADGTPK QVGIVSWGVG CARPRFPGIY
     TEIATYAPAI QAAVALLTDR
//
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