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Database: UniProt
Entry: A0A101JN10_9ACTN
LinkDB: A0A101JN10_9ACTN
Original site: A0A101JN10_9ACTN 
ID   A0A101JN10_9ACTN        Unreviewed;       551 AA.
AC   A0A101JN10;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Trypsin {ECO:0000313|EMBL:KUL29523.1};
GN   ORFNames=ADL15_27495 {ECO:0000313|EMBL:KUL29523.1};
OS   Actinoplanes awajinensis subsp. mycoplanecinus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=135947 {ECO:0000313|EMBL:KUL29523.1, ECO:0000313|Proteomes:UP000053244};
RN   [1] {ECO:0000313|EMBL:KUL29523.1, ECO:0000313|Proteomes:UP000053244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-16712 {ECO:0000313|EMBL:KUL29523.1,
RC   ECO:0000313|Proteomes:UP000053244};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S1C family.
CC       {ECO:0000256|ARBA:ARBA00010541}.
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:KUL29523.1}.
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DR   EMBL; LLZH01000278; KUL29523.1; -; Genomic_DNA.
DR   RefSeq; WP_067697231.1; NZ_LLZH01000278.1.
DR   AlphaFoldDB; A0A101JN10; -.
DR   OrthoDB; 9788136at2; -.
DR   Proteomes; UP000053244; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00987; PDZ_serine_protease; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR   PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR   Pfam; PF13180; PDZ_2; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053244};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        193..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          451..538
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          1..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          143..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          363..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..97
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..112
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..408
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   551 AA;  55405 MW;  A5893E3A8105A00B CRC64;
     MNENETNPRP ADAGAEFSST ERVESEQPTA AQPPVASQPA AHQSAAPTSG AHPTPPQYDA
     QPTAHHSPQL LHDAQPTAPS AWAQPAAHQQ SADPQSYQPA APQPPHAPAS PWQQPAPVSA
     IPVTSQPYAA GYSPYAAQQQ PGYAQTGYGQ PAGYQHTGAW QHGATPTPPE GVVPVWAQGP
     GAQPPRSGRG RKILMAGAAA IVIALLSGGV GAATVMAMDD NGSNPTVQTG NSSVTRVVDR
     SSLAQIAAAV QDSVVSITTG SGEGSGVVMS ADGYIVTNNH VVASASGDTV NIIFADGKKA
     TAKIVGTDPR TDLAVVKADG VSGLKAATFG DSSKMEVGDT VLALGSPLGL EGSVTAGIIS
     AKDRTIESSS EEDQQEQQNP LGQSQQQQQQ PSTSTTMTGL LQTDAPINPG NSGGALVNTN
     GEVIGINSAI ATSGSSSGNI GLGFSIPSNK AVDVAKALMA GTKVSHPALG VSVTTAENGG
     ALVSQVTSGS AAAKAGLQQG DVITKVDGKE ISESDDLVAA VQAGSVGQQM NITFTRNGAE
     KSVTVTLAES K
//
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