ID R4VVY5_9EURY Unreviewed; 1058 AA.
AC R4VVY5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=PKD domain-containing protein {ECO:0000313|EMBL:AGN00426.1};
GN ORFNames=L593_02375 {ECO:0000313|EMBL:AGN00426.1};
OS Salinarchaeum sp. Harcht-Bsk1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Natronoarchaeaceae; Salinarchaeum.
OX NCBI_TaxID=1333523 {ECO:0000313|EMBL:AGN00426.1, ECO:0000313|Proteomes:UP000014072};
RN [1] {ECO:0000313|EMBL:AGN00426.1, ECO:0000313|Proteomes:UP000014072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Harcht-Bsk1 {ECO:0000313|EMBL:AGN00426.1};
RX PubMed=23868130;
RA Dominova I.N., Sorokin D.Y., Kublanov I.V., Patrushev M.V.,
RA Toshchakov S.V.;
RT "Complete Genome Sequence of Salinarchaeum sp. Strain HArcht-Bsk1T,
RT Isolated from Hypersaline Lake Baskunchak, Russia.";
RL Genome Announc. 1:E00505-13(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP005962; AGN00426.1; -; Genomic_DNA.
DR RefSeq; WP_020445320.1; NC_021313.1.
DR AlphaFoldDB; R4VVY5; -.
DR STRING; 1333523.L593_02375; -.
DR GeneID; 16181459; -.
DR KEGG; sali:L593_02375; -.
DR PATRIC; fig|1333523.5.peg.482; -.
DR eggNOG; arCOG02546; Archaea.
DR eggNOG; arCOG03509; Archaea.
DR HOGENOM; CLU_289620_0_0_2; -.
DR OrthoDB; 8638at2157; -.
DR Proteomes; UP000014072; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd12215; ChiC_BD; 1.
DR CDD; cd00146; PKD; 5.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 2.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR46730:SF1; PLAT DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46730; POLYCYSTIN-1; 1.
DR Pfam; PF02839; CBM_5_12; 1.
DR Pfam; PF18911; PKD_4; 5.
DR SMART; SM00495; ChtBD3; 2.
DR SMART; SM00089; PKD; 5.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 2.
DR SUPFAM; SSF49503; Cupredoxins; 1.
DR SUPFAM; SSF49299; PKD domain; 5.
DR PROSITE; PS50268; CADHERIN_2; 1.
DR PROSITE; PS50093; PKD; 5.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000014072};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 93..179
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 156..279
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 183..269
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 329..417
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 521..602
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 609..690
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT REGION 92..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1058 AA; 110486 MW; FC7AE5C1E520E00D CRC64;
MERTRRGILR SVSVLSALAV GASATASAAD CSSAPAWDET VLYSSGDQVQ HPDGDGIDVL
WKAELDSRNA EPSRSSSYWN YVGDCSGDTN TAPTASFTTD VSTPEPGQDV SFDASGSGDS
DGSIASYSWD FGDGSSATGQ TATHSYSSTG DYDVILTVTD DDGASDTSTK TVSVTDGSTN
QSPNASFTVT PADPGTGETV TVDAADSSDS DGTIASYEWD FGDGTTASGQ TASHSYSSTG
DYSISLTVTD DDGATDSNTT TVTVSDSGSG GQCEGVPAWD SAATYTGGDQ VTHDGALWTA
EWWTQGTEPA ESENVWTLEG DCSGGNETPT ASFTTDVSTP EPGQQVGFDA SGSSDSDGSI
ASYSWDFGDG SSATGQTATH SYSSSGDYTV TLTVTDDAGA TDSASTIVSV SEQATQITID
SSVDGWVGVT PSEIDGQTNP AIDLVSGEPY AFTWNNVDGV PHNLTIRNAA GDALLQTETV
GEAGQSRTLE FTPTEEMVEY ICSIHPQAMV GDLAIDGNQP PTATLSVDPT NPSPGQSVSF
DASGSTDSDG TISSYEWTFG DGATGTGQSA SHTYSDAGEY TVQVTVTDDG GAAAIASSTI
TVGDPNQGPT ASFTTSPSSP DPGQSVSFDA SGSSDSDGTI SSYEWDFGDG TTATGETATH
TYADGGSYEV TLTVTDDAGA TDSTTSTLGI GGDVSASTTL SEFYSAYDED FNHEYTEGGV
SGLLKNELNP DASEFGADVD AISNNAGDGS MELGSLGDRG LELVKRFDAD GVPRETTGRL
MAWLTGLPTQ TEPVPFNDGE GRDGGLTADA GPVSATNDPS VLVQDTWPRG EQFDDVYLQP
QRVDWSSSVS DSQYTNTDNP IIDAVKDKVH PVTGETLGSG FTSNAPLEAT AELHDDGWIF
DMSMIFKNTT DVPVLIDGAI MWWVGPEKGA AGLDQFSYDN RERKNYSVGH PQRDVIEVSL
PNAKKPGPFE GTDAPLSAYG IRVAHHDNPY QYRTLYPNQK FAMTYHNVTG PGQYDWPLQD
LVDVMLDTCH VEFREEMSSI DTNTELVDAI DARNRYGN
//
