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Database: UniProt
Entry: A0A418KUL8_9ACTN
LinkDB: A0A418KUL8_9ACTN
Original site: A0A418KUL8_9ACTN 
ID   A0A418KUL8_9ACTN        Unreviewed;       391 AA.
AC   A0A418KUL8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=PDZ domain-containing protein {ECO:0000313|EMBL:RIQ32183.1};
DE   Flags: Fragment;
GN   ORFNames=DY240_05670 {ECO:0000313|EMBL:RIQ32183.1};
OS   Jiangella rhizosphaerae.
OC   Bacteria; Actinomycetota; Actinomycetes; Jiangellales; Jiangellaceae;
OC   Jiangella.
OX   NCBI_TaxID=2293569 {ECO:0000313|EMBL:RIQ32183.1, ECO:0000313|Proteomes:UP000284057};
RN   [1] {ECO:0000313|EMBL:RIQ32183.1, ECO:0000313|Proteomes:UP000284057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEAU-YY265 {ECO:0000313|EMBL:RIQ32183.1,
RC   ECO:0000313|Proteomes:UP000284057};
RA   Han C.;
RT   "Isolation, diversity and antifungal activity of actinobacteria from
RT   wheat.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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:RIQ32183.1}.
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DR   EMBL; QUAL01000046; RIQ32183.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A418KUL8; -.
DR   OrthoDB; 3870557at2; -.
DR   Proteomes; UP000284057; 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; 2.40.10.120; -; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          325..377
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:RIQ32183.1"
SQ   SEQUENCE   391 AA;  38607 MW;  2F9AFF4EBAD18158 CRC64;
     DGTTRFLATG PDGTPSDTGA AGAAAVSDGA AHRRPPKRRR GLATLGILVL ALAAGGAGGV
     VAEAIDDDGE GGGGTVTVIG ADPAGLVERP PESIAGVAAS VLPSVVSVSV ADAGGSGFVI
     SEDGYVITNN HVIASAGDDG IELAFTDGRR LEAELVGTSP SYDIAVLRVD ADDLQPVVFG
     DSDSVAVGDP VVAIGSPLGL DATVTSGIVS ALERPVTAGG EDDQSYINAL QTDAAINPGN
     SGGPLVDSSG RVIGVNSAIA SLGMGQQAGS IGLGFAIPIE QVQRTAQQLI ADGEAVYPVM
     GVLLDNGFVG VGARVAEDGD NGPGVTPGGP ADEVGIESGD VVVAINGEDV RTPAELIVRL
     RAHEPGEDIT VVVDRDGEEL EFTLTLGSAV G
//
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