ID L9VXK1_9EURY Unreviewed; 1115 AA.
AC L9VXK1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ELY41904.1};
GN ORFNames=C496_08916 {ECO:0000313|EMBL:ELY41904.1};
OS Natronorubrum tibetense GA33.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronorubrum.
OX NCBI_TaxID=1114856 {ECO:0000313|EMBL:ELY41904.1, ECO:0000313|Proteomes:UP000011599};
RN [1] {ECO:0000313|EMBL:ELY41904.1, ECO:0000313|Proteomes:UP000011599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GA33 {ECO:0000313|EMBL:ELY41904.1,
RC ECO:0000313|Proteomes:UP000011599};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:ELY41904.1}.
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DR EMBL; AOHW01000026; ELY41904.1; -; Genomic_DNA.
DR RefSeq; WP_006089602.1; NZ_KB913017.1.
DR AlphaFoldDB; L9VXK1; -.
DR STRING; 1114856.GCA_000383975_02206; -.
DR PATRIC; fig|1114856.3.peg.1861; -.
DR eggNOG; arCOG02492; Archaea.
DR eggNOG; arCOG07560; Archaea.
DR OrthoDB; 145878at2157; -.
DR Proteomes; UP000011599; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR011635; CARDB.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR026453; PGF_pre_PGF.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR NCBIfam; TIGR04213; PGF_pre_PGF; 1.
DR PANTHER; PTHR34512; CELL SURFACE PROTEIN; 1.
DR PANTHER; PTHR34512:SF30; OUTER MEMBRANE PROTEIN ASSEMBLY FACTOR BAMB; 1.
DR Pfam; PF13620; CarboxypepD_reg; 1.
DR Pfam; PF07705; CARDB; 2.
DR Pfam; PF01011; PQQ; 1.
DR Pfam; PF13360; PQQ_2; 2.
DR SMART; SM00564; PQQ; 8.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 3.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ELY41904.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ELY41904.1};
KW Transferase {ECO:0000313|EMBL:ELY41904.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 432..516
FT /note="CARDB"
FT /evidence="ECO:0000259|Pfam:PF07705"
FT DOMAIN 981..1060
FT /note="CARDB"
FT /evidence="ECO:0000259|Pfam:PF07705"
FT REGION 605..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..631
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1115 AA; 119473 MW; B09E782C7956929B CRC64;
MRSNPSDTGP PTWTRTLAVA VVGLGAVFLV ASLAVVSGGT ATGESPAVDG GHDAVALETV
GADAFASYRL YSTTEPDEPP VKWAFDAGGT VNSAPTIVDG TVYVGSGGGD GHLYAIDVAT
GDEVWAFETG GGISSSPFVD SGTVYIGSSD DHLYAVDAES GTEEWSFEVD HTVNSPFLYD
GTVYVSSWDE NIYAVDAETG EKEWVFETGD TVRSSPTVVN GTVYVGSQDG HLYALDATSG
NEEWAFETDD EVRSSPTVYN ETVYAGSWDG HMYALDAQSG AYVWSHSVGD NHISPSPTVA
NDTLYFGSHN NNVYALNAST GEYVWSRATF DNVLSSPTVA DDTVYIGSSD ARLYALDAHT
GAKHWTFETD DEFGIQTTGP TVVDGTVYFG SRDDHVYALE TGSEGSSVDS RVLLGTLGHH
DVAISDDPET QPDISIVDLS LSETNVDEGD QVTITAQIEN TGDATGEYTA ELEIEGDVEA
TETVSVDANS TREVTFTHTF DDAGEFDVRV DGVAAGTVEV TVEDGTLRVP VTGVRNEPIP
GALVWVVPAG DSIDGEPSIA DGDGIYETDK QPGMYDVEVA ADGYETERVE DIEIVPDEWT
NVDVELEPES TSSPSPSPSP SPSPSPDPAP EEPETTVLFE QINESVAATV TNAVANESVS
LPVADEIEDN DTVLRQLNVT PRSDADFDVT IERSDDRPAD VDELPNAAAE LRYFEINASL
EREAIENATF EFVVTTDELE ERGLEPEDVT LYHYVDGEWV DRETTAQFPG DHWTEAETAE
DLFPDDMWEE AGVDDPDALF PEETIEAAET AEELFPGDMW EEADSPEDLF PGDHWEEAGV
DDPEVLFPGD MWEEAETAED LFPGDHWAET ETAEDLFPGD HWEEAETAED LFPGDHWAKA
GVDDPDALFP EETIEEAETA EELFPGDTWE EAETAEDLFP GDTWEEAGVD DPEALFPGGT
WEVTYSAEVP HFSAFALAGD QPDLDVVEMS VSPSDLSVGE TVTVETTVRN DGGAAGETDL
ALEIDGAVVE TKSVSVDPGT ERVVTFTQTF EESGEFAVHV DDLEVGTVTV EADSVGETPE
EPSDDDTTDG TPGFGALVTA VVLLAVAALS TRTRS
//
