ID D8M6S5_BLAHO Unreviewed; 1290 AA.
AC D8M6S5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=GSBLH_T00003363001 {ECO:0000313|EMBL:CBK23493.2};
OS Blastocystis hominis.
OC Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Opalinata; Blastocystidae;
OC Blastocystis.
OX NCBI_TaxID=12968 {ECO:0000313|EMBL:CBK23493.2};
RN [1] {ECO:0000313|EMBL:CBK23493.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Singapore isolate B {ECO:0000313|EMBL:CBK23493.2};
RA Wincker P.;
RT "Sequencing and annotation of the Blastocystis hominis genome.";
RL Submitted (FEB-2010) 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC {ECO:0000256|ARBA:ARBA00008874}.
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; FN668661; CBK23493.2; -; Genomic_DNA.
DR RefSeq; XP_012897541.1; XM_013042087.1.
DR EnsemblProtists; CBK23493; CBK23493; GSBLH_T00003363001.
DR GeneID; 24920466; -.
DR InParanoid; D8M6S5; -.
DR OrthoDB; 248389at2759; -.
DR Proteomes; UP000008312; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd06612; STKc_MST1_2; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR002550; CNNM.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR PANTHER; PTHR48015:SF33; SERINE_THREONINE-PROTEIN KINASE HIPPO; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF01595; CNNM; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51371; CBS; 1.
DR PROSITE; PS51846; CNNM; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Membrane {ECO:0000256|PROSITE-ProRule:PRU01193, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000008312};
KW Transmembrane {ECO:0000256|PROSITE-ProRule:PRU01193,
KW ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|PROSITE-ProRule:PRU01193,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 826..850
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 901..922
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 928..945
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 957..975
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..266
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 822..1017
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 1036..1097
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 314..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1290 AA; 141809 MW; E0A995CFA11223DF CRC64;
MAEQSEVLND PECIFEVKEQ IGKGSYGSVV RATHRQSGRV VAIKIIPIES ETDIFIKETQ
LMKKCNSEFI VKYFGSYVKN VDLWIIMEYC GAGSMSDLMK KGQYVIYEEE IRFIMAQILL
GLAHLHSLNM IHRDIKAGNI LLTDEGVAKL ADFGVSIQLD NSSAKRKTFI GTPFWMAPEV
IKEEEYNSLA DIWSLGITAI ELADGVPPYS TMHPMRAIFL IPNRPAPRLR NEQKWTHEFV
DFVASCLVKD PKKRPSAKEL LKHPFVADLV PKLQNNTADF TIMKDMIKRL REKQSTSKVT
GPNVLRPLQP LQPVQAVQSA QPAQPAQSAH LASPAQPAQP AQPAQPAAPT QSSQPSQPTQ
PSRTKQVLST SSATPSTPSS QTPRAVIQVT QATPTSPKLA PAPLVRPGSP NPNARSSLFK
SANSVVPSSL PDLSPGGQAK PAMHSPPLKP HTLASTSGNA SIVSNASGSQ TPKQWPQSST
PRLSSNPGAE RTSPSIASPR GSLSPPRSMP GMGDNMSATG TMVVLEKSEE SVRSREVPKK
ISLIPVQGTE MDRSVPSVKS AQPQHAVNRS SLPTLLTSSS MGRCKNEAHI FETKHNPNLA
QDSIWTGCLN ERDATKPVLE ILGVYPGVDT IDIWLSLDQE GMVDCVAVET TDPVPDKNAF
RELVKANGNN TYVTIKELKT EHDYHVYCYA ENAYEMSPEQ PISSTLQVTK TFALGNAPVL
LIGDLAPDRE GVVLDVVSTD PGTVYCMVLP LEEEGMCKYR VRNEGKEVPV ASYETKELST
SGLTPATQYA VYCTAESTSN VPMRSDVEKV SRHFTTLEPK ESPLVFTLRI LATVFCVCMS
GIFSGLNLGL MGLDLISLRM VADTNIEEIG GDNVDPKELE DLKRDKRNAQ LIYPIRKKGN
LLLCTLLIGN VMVNSIISIL TADMTTGFIG FLISTCLITA FGEIIPQAYG SRHALEIGAM
SATLVRIIIG ILWIICKPVS MLLDYFLGDE LGAVYNRYQL YTMFELYKEH STFRKDTIST
MQGALVMDTK SILDHMHPLD TVYMIPDTTM LDYSTCLDIF RRGYSRIPVF HDDRQNIVGV
LHVKELIMID PNQCVSVQSI LKLFPSSILV INSNRTVSDS IRDMVNSHTE LAFVSRTIEN
KDIDNTMEIA GIITLEDCIK AVMRLELVDE TSLMEARNAS GSLMSVFNNL TLNSLDSTTL
DILGCFINQA LGNQGYHLPE DVIRNLIREG TISKVTTSDP PLYEVGKPCD FATIIMQGVF
TMVVGEDRMV TEKPIFSVIN LSSLLEDSFM
//