ID A0A0N1D285_9MICO Unreviewed; 586 AA.
AC A0A0N1D285;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=PDZ domain-containing protein {ECO:0000259|PROSITE:PS50106};
GN ORFNames=AEQ27_02870 {ECO:0000313|EMBL:KPG87237.1};
OS Frigoribacterium sp. RIT-PI-h.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frigoribacterium.
OX NCBI_TaxID=1690245 {ECO:0000313|EMBL:KPG87237.1, ECO:0000313|Proteomes:UP000037934};
RN [1] {ECO:0000313|Proteomes:UP000037934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIT-PI-h {ECO:0000313|Proteomes:UP000037934};
RA Tran P.N., Lee Y.P., Gan H.M., Savka M.A.;
RT "Whole genome sequencing of endophytes isolated from poison ivy
RT (Toxicodendron radicans).";
RL Submitted (JUL-2015) 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:KPG87237.1}.
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DR EMBL; LHOZ01000038; KPG87237.1; -; Genomic_DNA.
DR RefSeq; WP_054145308.1; NZ_LHOZ01000038.1.
DR AlphaFoldDB; A0A0N1D285; -.
DR PATRIC; fig|1690245.3.peg.274; -.
DR Proteomes; UP000037934; 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; 2.40.10.10; 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.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000037934};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 199..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 486..572
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 586 AA; 59178 MW; 3179FEFCAB1B4A95 CRC64;
MTDTPRHDDT DDGAPRTPEG TADGSQGVPG DDRSAHDGAQ PTTPYPADQG VTYGAPPLPG
STPQAGSFES GADESRHDRA HDRTQPHPGS YQQPPSYQQF GSYQQPGSQQ QPASYQQAGS
HQEPGSHQQP GAYPQPGSYQ QPGSYQQNDP YQQPGSYQQG DPYRQPSDPS AFAYDTTNSY
AAAGWQAPSQ KPKKSRRGVG SVAAALLVGV LVGGAAGGGV AAVLSRDSGA GVSATGESRD
LTVNDYDDAT VVTAVAAKAT KSVVTINVTA GESGGTGSGV ILSDDGYIVT NTHVVTLDGA
SASGTVTVTL SDGSILPAEV VGLDPTVDLA VLKVDATGLT PIEFADSSKL NVGDTAVAIG
APLGLSNTVT DGIVSTLNRS ITVQSSAAPT DGSDEGQQND NNGQGPFSFN NGDGSPQNQA
SSVISLPVIQ TDASINPGNS GGALLNSQGE LIGLNVAIAS SGESSGSIGV GFSVPSNLVQ
RVAKEIMANG KASHGLLGAS VNDATSDAAA TRVGALIVQL SPGGAAQNAG LRQGDVVTEF
NGVPISDRTD LTAQVRFLAG GATADLTYVR DGTTDTTKVT LDTLTS
//
