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Database: UniProt
Entry: A0A0Q6RNW7_9MICO
LinkDB: A0A0Q6RNW7_9MICO
Original site: A0A0Q6RNW7_9MICO 
ID   A0A0Q6RNW7_9MICO        Unreviewed;       477 AA.
AC   A0A0Q6RNW7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=PDZ domain-containing protein {ECO:0000259|PROSITE:PS50106};
GN   ORFNames=ASC54_06320 {ECO:0000313|EMBL:KQV26489.1};
OS   Yonghaparkia sp. Root332.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microcella.
OX   NCBI_TaxID=1736516 {ECO:0000313|EMBL:KQV26489.1, ECO:0000313|Proteomes:UP000051768};
RN   [1] {ECO:0000313|EMBL:KQV26489.1, ECO:0000313|Proteomes:UP000051768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root332 {ECO:0000313|EMBL:KQV26489.1,
RC   ECO:0000313|Proteomes:UP000051768};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQV26489.1, ECO:0000313|Proteomes:UP000051768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root332 {ECO:0000313|EMBL:KQV26489.1,
RC   ECO:0000313|Proteomes:UP000051768};
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:KQV26489.1}.
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DR   EMBL; LMCX01000001; KQV26489.1; -; Genomic_DNA.
DR   RefSeq; WP_055897449.1; NZ_LMCX01000001.1.
DR   AlphaFoldDB; A0A0Q6RNW7; -.
DR   STRING; 1736516.ASC54_06320; -.
DR   OrthoDB; 9758917at2; -.
DR   Proteomes; UP000051768; 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; -; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000051768};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        88..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          378..439
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          272..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..72
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   477 AA;  46597 MW;  E9A0BD396D8EE28C CRC64;
     MTENPTTPEP PAHEPSAGPT PEQHAAPEQH AAPEQHPAPD QHAAPDQQAG PDRHPAPSAP
     VPPAPPAAAA APAPAAAPTA PQRSLAPLIA ALAVGALVGG AAGGGIAAWA LADRGGSMSA
     PTGPASVTVN DPEDATIVTG VVATAMPSVV TIQVAGGGAQ GSGSGVILSD DGYVLTNAHV
     ATLDGAAGDP TIRVTTADGR LWDATLVGAD PIADLAVIRL DGATDLQPIE FADSDELNVG
     DRAIAIGAPL GLAGTVTDGI VSALNRSITV KSSAVPEAPE APEAPGPDSG GPFEFWNFDI
     PGRDSQPSAS STISLAVIQT DAAINPGNSG GALLDQDGRL IGINVAIATA GGGQGSAGSI
     GVGFSIPANF AQRIATEIIE TGSASHGLLG ATVTDASAAA SSDVVGALID QVSPGGPADQ
     AGLRGGDVIT EFNGVPITDQ IDLTAQVRAL AGGESAELTY VRGGRSETLT VTLGELG
//
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