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Database: UniProt
Entry: A0A0Q7ZH26_9ACTN
LinkDB: A0A0Q7ZH26_9ACTN
Original site: A0A0Q7ZH26_9ACTN 
ID   A0A0Q7ZH26_9ACTN        Unreviewed;       543 AA.
AC   A0A0Q7ZH26;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=PDZ domain-containing protein {ECO:0000259|PROSITE:PS50106};
GN   ORFNames=ASD66_15555 {ECO:0000313|EMBL:KQZ68690.1};
OS   Nocardioides sp. Root151.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736475 {ECO:0000313|EMBL:KQZ68690.1, ECO:0000313|Proteomes:UP000051274};
RN   [1] {ECO:0000313|EMBL:KQZ68690.1, ECO:0000313|Proteomes:UP000051274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root151 {ECO:0000313|EMBL:KQZ68690.1,
RC   ECO:0000313|Proteomes:UP000051274};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQZ68690.1, ECO:0000313|Proteomes:UP000051274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root151 {ECO:0000313|EMBL:KQZ68690.1,
RC   ECO:0000313|Proteomes:UP000051274};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQZ68690.1}.
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DR   EMBL; LMGG01000005; KQZ68690.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q7ZH26; -.
DR   Proteomes; UP000051274; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000051274}.
FT   DOMAIN          436..524
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          1..180
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        96..113
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..163
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   543 AA;  55592 MW;  EFBDAD94F6FDFC5B CRC64;
     MMSAMSDENA GDDSNPTTAI RPGARKHQQA EPTQPYAAQP YADQPPEPAS PEAEPSVAHA
     INDPGPDHET SPVPPAQAPQ QAAYDGRHAH QPGPYAPPQD QAPPAPQSQF APPQDPGHPG
     QQGQFAPPGQ AAQPYGQGPQ HAQPWEAPPP YPTGYPQPGH QAPLGPPTEH RQTGGSGRGK
     TGIGLLAGAL ILGAAAGFGG GYLHDETSGG GDGKVDAGQI DIAGLNLQDL VSVQNVAEKT
     LPSVVKIEAF GASSGSTGSG IIISDDGLIL TNYHVAFNGI EGDTTVYFDD GSSTTGSFVG
     ADPDMDIALI KADDVSGLTP MKFGAAEDLK VGQAVVAVGS PYGLESTVTA GIISTVNRPV
     NVAGMEASQE AMVYPALQTD AAINPGNSGG ALVNIKGELV GMNSANRTAS SNTGSEGDLG
     SIGIGWAIPV NVIAPIVEEL KNGDEPTHAW LGIIPGNARE SGVAQGATVE DFTSDSPAEE
     AGLKQGDVVV AVDDYPIAQG LGLVTTALQY RPGDKVKLRV LRDGKEQTFE VTLAEKGRLF
     DDL
//
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