ID Q63XD9_BURPS Unreviewed; 1359 AA.
AC Q63XD9;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 24-JAN-2024, entry version 120.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN OrderedLocusNames=BPSL0597 {ECO:0000313|EMBL:CAH34590.1};
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH34590.1, ECO:0000313|Proteomes:UP000000605};
RN [1] {ECO:0000313|EMBL:CAH34590.1, ECO:0000313|Proteomes:UP000000605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243 {ECO:0000313|EMBL:CAH34590.1,
RC ECO:0000313|Proteomes:UP000000605};
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M., Atkins T.,
RA Crossman L.C., Pitt T., Churcher C., Mungall K., Bentley S.D., Sebaihia M.,
RA Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F.,
RA Challis G.L., Cherevach I., Chillingworth T., Cronin A., Crosset B.,
RA Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H.,
RA Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S.,
RA Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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};
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DR EMBL; BX571965; CAH34590.1; -; Genomic_DNA.
DR RefSeq; WP_011204838.1; NZ_CP009538.1.
DR RefSeq; YP_107226.1; NC_006350.1.
DR STRING; 272560.BPSL0597; -.
DR KEGG; bps:BPSL0597; -.
DR PATRIC; fig|272560.51.peg.1034; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG3899; Bacteria.
DR OMA; GYPRAHE; -.
DR Proteomes; UP000000605; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR023889; TOMM_kin_cyc.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR NCBIfam; TIGR03903; TOMM_kin_cyc; 1.
DR PANTHER; PTHR16305; TESTICULAR SOLUBLE ADENYLYL CYCLASE; 1.
DR PANTHER; PTHR16305:SF35; TRANSCRIPTIONAL ACTIVATOR DOMAIN; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000000605}.
FT DOMAIN 38..307
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1330..1359
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1359 AA; 145131 MW; 4D7036EE41312757 CRC64;
MSASVLAERA RAGNRRAPRA LAPPLPGDGD ELQGEHRYRL GAVLGEGGAG RVHEAIRLDT
SARVAIKLLR EDAPRGARER ARLRARFRRE TALCARLSHP HIVALLDSGE TPDGLLFAVF
EHVAGRTLRA LLAADGALAA ETTGALMAQV LDGLAHAHAN GVVHRDLKPQ NVMVTTRDGE
PCAKILDFGI GALLPDAHAA DELTLTATTE VLGSPQYCAP EQLRGEPPTA KSDFYAWGLI
VIECLTGHPV MQGASLADVL YQHLSPVDVA LPPAIAAHPL GDVLRDALNK DPRQRAESAQ
ALANRFRAIH FPALVGGLRY GARHGRRAQA EPGVAAREPG GTIALDAPVG RRQVTALCCR
VSVVSTLARP ADAAADDEAL DAFHAHWLTR CSDIAVRYGG HVAGALGDTL LFYFGYPEGI
DRPAQRACRA ALEMTRHAGQ PAGAPRSSDG DARACAPAWR IDIAGAIHVG TAFATARGAS
GGVLASAALG LQRIAQPGGI LLSDEAARAL ERHVDAAPTA LTFAAPGAAP QPVRELLGER
YERGPFESLE LGDATPIVGR DREQAALARA WRDAVRAAAG GRRARRRATL VVGEPGIGKS
RLVHALRELV RAQRGACAAC VCLPEQTNHA LFPILRFVRA HWQLDVGDPH ALDRMLEAFD
GDRASARATL AAWLGLPGGA DTLRWSGARQ QQALFDVLCQ LLGSLGGGGP VLLIVDDVQW
CDSATDDFLD ALAHHPACAA VCVVLTSRPE RLERWRRGAE RLMLRRLSAA ATRNLIVSLM
PGAGTQRAAL DFLVKRTGGV PLYVEETVRA LAEGGVAPGA GARLPDLAQA GRCPLPGSLR
ETLELALERA DDALDTVQLA ATIGLEVDAR LLAEASPHAG AELDERLRRL IEGRVLYAQH
RIGGATYVFR HALLREAAYE SMPAATRREY HRRVAQALLA CVAQGDPAAR SASIADHFAR
AHAFAAAVPH GIEAARRALA RALHDDAIRY AGAVRGWLLH CDYPGQHEDA VSVDLTLAHA
QMARDGWGDP RVREHTDRVL SRVGELSDAK AAAGALWTIA VYHHVAGDRD AVRRIGGQLS
ALARASARAD LGVAADTLHG MALWIDGHYT LALDAFDAAL AAYDPRRDGD HRHVFGLDTR
AWAQSARACV LWGIDDDVAR TLALARDAVQ LATCTDHLPT IGLTMMYLAR MQQCVGDREG
ARATADAVLR LSRCHGLNAV ERYAAVVRAW CDGDRDAARA NVDALRASGC MLGLTYYASV
AADIDAERGD ARAALATLDE CLALAESMDE RHYVAELLLK KARCVRDAHG RRAADDAQAL
CARAAAVARR SGMARIERKA QAELRELQRE LRSTTGEER
//