ID A0A1V0DEX1_9BACT Unreviewed; 935 AA.
AC A0A1V0DEX1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=AWN76_010720 {ECO:0000313|EMBL:ARA93584.1};
OS Rhodothermaceae bacterium RA.
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rhodothermaceae.
OX NCBI_TaxID=1779382 {ECO:0000313|EMBL:ARA93584.1, ECO:0000313|Proteomes:UP000055617};
RN [1] {ECO:0000313|EMBL:ARA93584.1, ECO:0000313|Proteomes:UP000055617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA {ECO:0000313|EMBL:ARA93584.1,
RC ECO:0000313|Proteomes:UP000055617};
RA Liew K.J.;
RT "Complete genome of the potential lignocellulosic biomass degrader
RT Rhodothermaceae bacterium RA isolated from the saline hot spring in
RT Malaysia.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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; CP020382; ARA93584.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V0DEX1; -.
DR STRING; 1779382.AWN76_010720; -.
DR KEGG; rbar:AWN76_010720; -.
DR OrthoDB; 9813021at2; -.
DR Proteomes; UP000055617; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002151; Kinesin_light.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR45641:SF1; NEPHROCYSTIN-3; 1.
DR PANTHER; PTHR45641; TETRATRICOPEPTIDE REPEAT PROTEIN (AFU_ORTHOLOGUE AFUA_6G03870); 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13374; TPR_10; 1.
DR Pfam; PF13424; TPR_12; 4.
DR PRINTS; PR00381; KINESINLIGHT.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00028; TPR; 9.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 4.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50005; TPR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000055617};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 92..409
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 629..662
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 321..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 935 AA; 101356 MW; FD172155E6E4D5ED CRC64;
MTPERWQRIE ALYAEALEQP RAAQADYVVA RAGADTTLRD EVLSLIDAHY ADADFLAQPV
EAGRLAAWLD ALPEVPGLLP GAPRPGDDIG GYRLLRVLGR GGMGTVYLAE RRTEAFTQRV
ALKLLRRGLD TGDLLARFFA EQRILARLSH PHIARLIDGG VTADGLPYFA LEYVDGCPIT
DYADRHGLGV EARLRLFDQV CEAVQCAHQH LVVHRDLKPS NLLVTTDPGS EPGRATVKLL
DFGIAKLLQP GPADAPVLTA TGVRVMTPAY AAPEQVRGGP ITTATDVYAL GVILYELLTG
QRPYDLDGAS GATIERIVCE TSPPRPSTQV SRRTDAPPAG PARAGLDPER LRRRLKGDLD
TIILKALRKD PAERYGTVDQ LREDLRRHLA GLPVRARPLT WRYRTHRFVR RHRAPVVAAV
LIAALLAGFS ILTARQAARI ETQAAVVAEE RDKAEEVARF LVSLFRSADP GEARGEDVTA
RTLLERGRAR VEEELAGQPA VQATMLGVMG EVYEALGDYA EAEALARQAL LREQAVHGPR
HAATATALNR LGWIRHLRGD EAGADSTLRA ALALRQAVLG PDHLDVARTM NDLAVVAQAR
GDYAATDTLL RAALALRQAR LGPEHMAVAT TLNNLAALRW RLGDYDGAAR YFEQALTVFR
TTLGEMHPRI AITLNNLAVT YQVQGDLDRA EARYREALAM RRRLFGDAHP EVARSLNTLG
HLLTRRGDYA AADSLLTEAL ALRRALLGPR HPDLASTLVT LAGLREAQGR YAEAERLHRE
ALAMREALLG HGHAEVAESL GGLARLERRR GRPADAARLY REALAVERQA LGPQHPRVAE
TLRQLGLVEQ DLGHLDAAVA HLREALALAR TALGAEHATV AGLHVDLAAA LIAQGAAAEA
VGLLRHAAEV GDAETAARAR ALMARIAPPP PPADD
//
