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Database: UniProt
Entry: A0A2P8Q007_9ACTN
LinkDB: A0A2P8Q007_9ACTN
Original site: A0A2P8Q007_9ACTN 
ID   A0A2P8Q007_9ACTN        Unreviewed;       687 AA.
AC   A0A2P8Q007;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Protease {ECO:0000313|EMBL:PSM39582.1};
GN   ORFNames=C6Y14_30955 {ECO:0000313|EMBL:PSM39582.1};
OS   Streptomyces dioscori.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX   NCBI_TaxID=2109333 {ECO:0000313|EMBL:PSM39582.1, ECO:0000313|Proteomes:UP000240429};
RN   [1] {ECO:0000313|EMBL:PSM39582.1, ECO:0000313|Proteomes:UP000240429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A217 {ECO:0000313|EMBL:PSM39582.1,
RC   ECO:0000313|Proteomes:UP000240429};
RA   Zhikuan W.;
RT   "Streptomyces dioscori sp. nov., a novel endophytic actinobacterium
RT   isolated from bulbil of Dioscorea bulbifera L.";
RL   Submitted (MAR-2018) 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:PSM39582.1}.
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DR   EMBL; PYBJ01000024; PSM39582.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P8Q007; -.
DR   OrthoDB; 9758917at2; -.
DR   Proteomes; UP000240429; 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:UniProtKB-KW.
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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:PSM39582.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:PSM39582.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240429};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        324..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          592..672
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
FT   REGION          1..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          607..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..139
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..231
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..258
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   687 AA;  67770 MW;  D91DBC176303CA9D CRC64;
     MDEGKPTKPK WWSRPRTHGP DSAPADPVST GDGASGVHGA DMDGDFELEK PAGTGPGTGP
     GTAATAVGDA GAGAGPTAVG DAGTGAGSTV AQAAGEVGDG VSAPAPGRRT GPLHDPDPYS
     TPPYGGPGPW APAPPVQHPA TTPAHGTTVE AAAPPQDAPP QPQDTPGEAV SGTPTPSAPA
     PRASAPSAPA SHAPASSARA PQTPAPHAPA AHPNSPQTPA PHLPAPRPAV PGAHFPETRF
     SETPFPETPA SGTPVPQTQG VLGPEPPGGR QAPGASPGAG ENGAPAPAPS TPWQNYDPWA
     AAPLQHHGAA AEAPGGRRGR TGRALVLGAA LLALVSGGVG GAVGAYLERT GGIDDVELPQ
     AGVEAEGRAP DSVAGIAASA LPGVVTLHVS GSDAQGTGTG FVLDRRGHIL TNNHVVEPAD
     GSGEITVTFS GGETAKAEVV GHDSGYDLAV VKVAHVSGLK PLSLGNSDNV QVGDPVVAIG
     APFDLENTVT AGIISAKERP ITAGGEEGDG SDISYVDALQ TDAPINPGNS GGPLVDSKAR
     VIGINSAIRS ADSGSDLEGG QSGSIGLGFA IPINQGRRVA EELINTGKAT HPVIGVTLDM
     EYSGDGARVG TKGNDGGSAV TRGGPGARAG IEAGDVITEV DGQRVHSGEE LIVKTRSHRP
     GDRLELTLER DGRERKVTLV LGSADGD
//
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