ID A0A1G2LWR5_9BACT Unreviewed; 499 AA.
AC A0A1G2LWR5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 18.
DE RecName: Full=PKD domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A3A10_01535 {ECO:0000313|EMBL:OHA16003.1};
OS Candidatus Tagabacteria bacterium RIFCSPLOWO2_01_FULL_42_9.
OC Bacteria; Candidatus Tagabacteria.
OX NCBI_TaxID=1802296 {ECO:0000313|EMBL:OHA16003.1, ECO:0000313|Proteomes:UP000178116};
RN [1] {ECO:0000313|EMBL:OHA16003.1, ECO:0000313|Proteomes:UP000178116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OHA16003.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MHRA01000006; OHA16003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2LWR5; -.
DR Proteomes; UP000178116; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00146; PKD; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.60.40.1260; Lamin Tail domain; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001322; Lamin_tail_dom.
DR InterPro; IPR036415; Lamin_tail_dom_sf.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR Pfam; PF00932; LTD; 1.
DR Pfam; PF18911; PKD_4; 1.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF74853; Lamin A/C globular tail domain; 2.
DR SUPFAM; SSF49299; PKD domain; 1.
DR PROSITE; PS51841; LTD; 2.
DR PROSITE; PS50093; PKD; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..499
FT /note="PKD domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009583594"
FT TRANSMEM 474..493
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..134
FT /note="LTD"
FT /evidence="ECO:0000259|PROSITE:PS51841"
FT DOMAIN 237..274
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 278..402
FT /note="LTD"
FT /evidence="ECO:0000259|PROSITE:PS51841"
FT REGION 173..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 499 AA; 53604 MW; 0EDA30CC08A50620 CRC64;
MKKSGFLFLG LILLPSLAFA NVVINEIAWM GSKVDSVDSG QWRYYEWIEL YNSGNDAVDL
TGWILSIVGK KDIYLENTIP ANSFYFIERS GYHAFDNITA DLATSFGAGL SNSGATLALK
DTTNNQVDAV DGNDNWKIGG GDIIGDNTTK ETAQRTSSGW ITATATPKAA NAGFLQSQPP
SQQQPDQSSA GGGSAPYIPP EQLPKIKAYA GEDKTVVVGA SAEFRGKAFG LKNEPLDNAR
YLWNFGDGSS KEGQNIIYFY RYPGEYTVVL NVSSGGYSAS DYALVKAAPN NIFISEVKTG
LETWIELENG FKEEIDISGC QLKSGNQIFI FPQNSRIRAA ANLVIPLSAS GFILYSGKSS
VEFLYPGGFK ADLFNYDGFL SGSESFARDG DKSSIAQVTP GQKNPAKTAV IQKSGKSGVE
KFSTSKSQKT ETMEVELPYI KDSSSENSGS QPGSQGANVI SVGDSGNAKN NAKIYLFAIL
ALILFAGAAV FFIRRQRGV
//
