ID A0A2D5ZDQ3_9BACT Unreviewed; 609 AA.
AC A0A2D5ZDQ3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=PDZ domain-containing protein {ECO:0000259|PROSITE:PS50106};
DE Flags: Fragment;
GN ORFNames=CMJ18_23830 {ECO:0000313|EMBL:MAE67304.1};
OS Phycisphaeraceae bacterium.
OC Bacteria; Planctomycetota; Phycisphaerae; Phycisphaerales;
OC Phycisphaeraceae.
OX NCBI_TaxID=2026777 {ECO:0000313|EMBL:MAE67304.1, ECO:0000313|Proteomes:UP000222953};
RN [1] {ECO:0000313|Proteomes:UP000222953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Graham E.D., Heidelberg J.F.;
RT "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT Global Oceans.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family.
CC {ECO:0000256|ARBA:ARBA00007931}.
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:MAE67304.1}.
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DR EMBL; NYZC01000372; MAE67304.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2D5ZDQ3; -.
DR Proteomes; UP000222953; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00989; PDZ_metalloprotease; 1.
DR Gene3D; 2.30.42.10; -; 4.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR42837:SF2; MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR42837; REGULATOR OF SIGMA-E PROTEASE RSEP; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 3.
DR SUPFAM; SSF50156; PDZ domain-like; 3.
DR PROSITE; PS50106; PDZ; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 67..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 535..568
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 580..602
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 96..171
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 272..329
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:MAE67304.1"
SQ SEQUENCE 609 AA; 65195 MW; 29595698A05E69C0 CRC64;
RAEAPGDEDS AYDGERTDRA AAALGLGETE YRLNWMPLGG YVKMLGQDDM NPAAQVDDER
SFNCKPIWAR AVVVSAGVVM NLIFGVLFFI VCFLDGVEFP SAIAGDIDPS GPAALTYAMG
HDKDPAYRGL RAGDHIVQID GKPVTDFMQV AVSTALARRG SVLDVAVERE GHDGPLHYKL
TPTPNPATRL LSLGIEAPRT PEIELVPTSG DFAFLHEQGV KPHMLVTAVD GKPVERYAQY
HRAVAAARGR PTPVTFEDME TNETVTVQLS SRAALVRDAN GPEHLIGLVP AVRISSVAEG
SPAEAAGIRV GDHLAQVADE RWPSIEMVTR LVRGADGAMM QLSVWRDGEE VTLDATAPGS
DGMLGIGLEY DAAVIGRTID GTTAAALDLI GGSRVTSIDG APVETWSDMQ RALQTIADGA
DGPVVVNLEI AEAIAGNPTR QKQVTIDADA QAELQTARWY PSLGSQVFAM NRQEISAATP
MAAAALGIRK THQFMLQTYV TLVRLFQGTV KLEHLRGPVG IVHEGTRIAK QGWSYLLFFL
GVISVNLVVI NFLPIPITDG GLMVFLIIEK LKGSPVSPKV QTAAFFVGLA LIGSVFLITL
YYDTGRLLP
//