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
//