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Database: UniProt
Entry: A0A1H9DJN2_9PSEU
LinkDB: A0A1H9DJN2_9PSEU
Original site: A0A1H9DJN2_9PSEU 
ID   A0A1H9DJN2_9PSEU        Unreviewed;       506 AA.
AC   A0A1H9DJN2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Serine protease, S1-C subfamily, contains C-terminal PDZ domain {ECO:0000313|EMBL:SEQ13527.1};
GN   ORFNames=SAMN05216188_102177 {ECO:0000313|EMBL:SEQ13527.1};
OS   Lentzea xinjiangensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Lentzea.
OX   NCBI_TaxID=402600 {ECO:0000313|EMBL:SEQ13527.1, ECO:0000313|Proteomes:UP000199352};
RN   [1] {ECO:0000313|Proteomes:UP000199352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3525 {ECO:0000313|Proteomes:UP000199352};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOFR01000002; SEQ13527.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9DJN2; -.
DR   STRING; 402600.SAMN05216188_102177; -.
DR   OrthoDB; 9758917at2; -.
DR   Proteomes; UP000199352; 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; 2.40.10.120; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
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   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:SEQ13527.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:SEQ13527.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        161..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          382..494
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          83..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..145
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   506 AA;  51812 MW;  59FBA14C0D439914 CRC64;
     MSQQSPNGQT STPVSGVDDG AHRRLRPRPL VQPPVDPAHA SAFGRPEGVA GAFAARDVPV
     TEVQSAPPPP ESLATAFGRQ GSQELLQRPP QPVSDPDPDI DPVFWGDQPA GDPWRDPASG
     AVIGPPAVGE DGPGEPEPKP QPGPQLSVPE LLFGRRVQPS ALALLMVAAL LVGAAGGLVG
     WLIGRSGNPL TDSTVTLAEV EQGKERPAGS ISDIAKRVTP SVVSIEFKGT NVAGVGSGVV
     IDGGGYVLTN DHVIAPAAQD SSAKLSAVFT DGTRAQARVV GRDPKTDLAV IKVEVTNPTV
     LQFGNSDELE VGDSVIAIGS PLQLSNTVTE GIVSALHRPV TAAGENGGPQ VTYDAIQTDA
     AINPGNSGGA LVDSRGALIG INSSIRTETG GSVGLGFAIS GNQARKISQE LIRNGQVKHA
     DMNVNVKSVS AETSEGAQVQ NVPAGGAAAA AGIQEGDVIT KVGDRMVRNA AELVVAVREH
     EIGETVQVVL ARQGRELKLD VTLKSD
//
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