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Database: UniProt
Entry: D8M6S5_BLAHO
LinkDB: D8M6S5_BLAHO
Original site: D8M6S5_BLAHO 
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}.
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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
//
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