ID Q4Q5D6_LEIMA Unreviewed; 3207 AA.
AC Q4Q5D6;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 128.
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=LMJF_32_1460 {ECO:0000313|EMBL:CAJ08666.1};
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664 {ECO:0000313|EMBL:CAJ08666.1, ECO:0000313|Proteomes:UP000000542};
RN [1] {ECO:0000313|EMBL:CAJ08666.1, ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX PubMed=16020728; DOI=10.1126/science.1112680;
RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M.,
RA De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S.,
RA Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K.,
RA Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA Barrell B., Myler P.J.;
RT "The genome of the kinetoplastid parasite, Leishmania major.";
RL Science 309:436-442(2005).
RN [2] {ECO:0000313|EMBL:CAJ08666.1, ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC {ECO:0000256|ARBA:ARBA00010769}.
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DR EMBL; FR796428; CAJ08666.1; -; Genomic_DNA.
DR RefSeq; XP_001685462.1; XM_001685410.1.
DR STRING; 5664.Q4Q5D6; -.
DR EnsemblProtists; CAJ08666; CAJ08666; LMJF_32_1460.
DR GeneID; 5656259; -.
DR KEGG; lma:LMJF_32_1460; -.
DR VEuPathDB; TriTrypDB:LmjF.32.1460; -.
DR VEuPathDB; TriTrypDB:LMJFC_320022900; -.
DR VEuPathDB; TriTrypDB:LMJLV39_320020600; -.
DR VEuPathDB; TriTrypDB:LMJSD75_320020600; -.
DR eggNOG; KOG0890; Eukaryota.
DR HOGENOM; CLU_225445_0_0_1; -.
DR InParanoid; Q4Q5D6; -.
DR OMA; MEFAREC; -.
DR Proteomes; UP000000542; Chromosome 32.
DR GO; GO:0005730; C:nucleolus; ISO:GeneDB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; ISO:GeneDB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR CDD; cd00892; PIKKc_ATR; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF72; SERINE-PROTEIN KINASE ATM; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CAJ08666.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000542};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAJ08666.1}.
FT DOMAIN 2866..3176
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 3175..3207
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 887..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1417..1450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1778..1801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3207 AA; 351233 MW; EBA77C3D27BAC0EC CRC64;
MEAVTDDEGL VPAAVRQRTE KGVLSSCNTS RHDSAGIRDE LAGIGEQIKA LQLQLSSNLA
PETKVSEVVT QTLWDLLWRL RTFLFLASPS AAHQWKIGGA LFDVYYRRHY GRDAAHVAIA
LRLYLVLLRF TVVCPAAALH GCLTLFGVLA VLNDPRLRSW KDTSERLLDG FLFVSRAQHR
SENDVFAQLM NIVFELLSEV TAHFNGSAAE TESALFLQLS VEPSAALLSQ TEASLPSFAS
PNSASDAEGR ARRLQEMFST CTCVETLYEA RCIQACLLRL VVRLSEERLL LSLSPDRVGL
LCDVACHIVS SAIPGAEGGV VNRVQHDAAW HTLRYFAVVD RRLLPHLQGP LILSVLAAQW
SRRGAQTCSS IFNITVAEKA LFDWCRHLST AELDSLVVAA YHRGGAGPGG QDVMTECLVQ
MWEVGVQWCA ELYTSPSTAV DGIVANTASS TPSSLSAMFT LQQWVCLCER VFRSTVVQRS
AFAGLTQMGE PKLLAAYDHQ LQLLVSELPL SSLTASLLCT QLPSFAVESE LAFLPSRILS
FFNGQALTAC IAEVVDRAKN CIDVSAYRLL EANALAVQSR LKVSSWMVQC DAAAFQSALA
ETLQVMQHHE APSHSLLVQA IIVLVHAFPV DSENGEVRKS DTVARVIEAL DNSISSRHDG
SYAALEVAAP LWHMLDRETA TTLFRAGSGL GWTRRLLALP PHTATSAKTA ELFLCRAAGL
AEALQHALAE TMVREGASTS RSTSHAPAPK VLPGAAAARG QMPARLQRAY ESIASHFPVV
VQLLQTLSTL ITTLQRDVQW WRCMRNGKGG TYADANGAIV ALGTLFSHAT GILVLLLDAK
YRFAAIAGSE AGKGRNSALA GAAPICEQGS TTKQPLAQAA TVVDVDDDDN ADGVSEEKEE
AKQPYRHRKT TARGATLSSK AGKASAKAGV GGALQASNVS QQSIAKTKQL EKIVQLNRSK
LLPALLAFTR HLVYEARGRG ASPDADEVQN EDGRSSQRAA GGMQSHASAL ECVVLSLAYT
SLALSPPFSL TDENALFSLA SVGAYNVTDS ILYCALRELV LWSPELAWRE REAGNSAIPT
LLLVQLSGTE RLLSTVLTAR RDGNTTYIAE CGAQILQLLW YGRRFFQRSG DARATAVDKP
EREQRLSLTD ASAAVQEDCM AASERVTQEG HAWLCLCFDL YAVYHSVRPA HNDTALAVMG
LCLETARGVM ALFSWSATDL LRFRERPFVF SSFFKAIVDK EDRDMKVILT SSLDVLGRYV
ISAGVGQAGG GTVAATATMS TVVPGDSVTR AKLKHLMDQE KIADWRAAAG ALAYALYECG
SKPVAKQMLS LAEAASYAKR SIKDVPAMVR STIHFVAFHI VSLEADAQML AHDRRCHSGR
DRRRFLGGAV ALHAPLAVVG GSAHSLFLCD RSEGGDGAEA ADVEDASASP PQRTTTGELH
PAEGDGDDAS ASKEVLDGIA FSVFERALVQ LVTLGEAAET AAGVENSLRK PVVRAVAAEE
LRKNMFAVLD AVYKAIRIEP AVAYRSEGAG AADEEEASAA PPGSLRTRRR WLLGLASFIR
FMGPQTTPIA LMLPTLLGHC ARFPSLLPSV CIVWRELICA CTDEYLAESA AAIVLSLVSL
EQHAALESES KGLLLCTLRH LYTRTEAAEF WDSYQVVLGT FSELVRATLH SRHSGCGEAA
ERSEESRRDS AHVLLLGFAS VMRSGSLQSS TVFVRALYQY LCAADEATRR QLSHAAADHP
EVLQTLLRCT EADSDSALYA MRCISILGAV AAPNAAVSTG APRATKTADD ERRSSLTPSS
ASALDGWNRM TWTQSFYLDA ETVLNWRKFS FTLLRDYFPR VFASTADPVL HNCIAFAVQE
LIRASTRQER LQHKGVELRR EDVVHLDELD RYIWWMRLTP HVKQLLGGFT TTRYSLTVNW
QTRLRTPEYM PSLGHRRWLF AFFNHLVMSC KGWFAEMVQP LRNVAKKNAS LVLYLLPYLV
VHILESGKVE DVQYIEHEVK AVLEAAAGGP NVAVLSLRSQ SIYEASPETV SQEEPREHAH
TVLSLLEDVE QLRWTLLRNR GRVACVFEPQ EQTESLCIRL AEMYGDFLRG ISWPLRCRAA
LRIGSHIRAL RSVESQRRIP GLASVIAAVP LQRIFAALND RESSRSIHRA SPGLSLEDTA
FSFENNGDWL SALGSSELVL QHRPHSGQHQ LTALHCMNEL GELYMTSRYA ASLLASASVS
DGDVRGFEAT EYLSGAALKG RSTFSQMVSE APGEAAAVSD FAQLRHHVQA YANEAAWRLG
QWDMLLPSGA ATAPVSSRMP TVGSDGGRSV SLAMPAAYLQ RALSGNGSLA FVRCVTDNER
AKVVPVVRTP CQEDLTAQGY TVTLLLHALG DVDAVSELCA RAFITNGSGH RCGGDGSDAS
QSSAPTMKLA APLLPSSVKE EIASLLSQRE SYVEDTIAAR EPLLALHRLI YRELDMPQKV
AETWLKQSEL LRNGGLGEAA LTAARQAAFE CREHVTATSY YVLVANLLHD TQSPTPAMEF
ARECVADVRI PATTRAQLQI LLTNWLIETG SERPEHIFAE YEKARELDRK SELVHHQMAL
FYDHLHTLAS NASEGAAAQL TAAATSPTSS STANVSAAVM YNAALQHQKE MVDSIQRCAT
RAIVHFGEAL LRGVEKASVS LPRMLTLWLD SAVFLGGLLG TTVGKLDGTT SAVLGEMNNR
IREFVLSTVQ PVIPPAVVMT ALPQLLSRLG HPVTAVRNVL TDIVLHLMDH FPQQCLWLVL
PMALSKEGPK EVVETQIIKP FADNPRNERV LRHAKILCDT LLTICNCSAS LFPKEKGLTQ
LSPVQKITPM LAAAKFIVPV LSNLTPDIRA SSSEDVFPTA PCFDHFDDRV VVMRSLQKPK
RIWVHTNDGR EMSFLCKAKD EPRKDIRMME VAALMNSFFL SDPEAKRKRF SLRRYSITAL
SDDCAVIEWL NDTTPLAKVA MECYALDRSG VHISSVKKWM TLVDEKKMSK MELFTKYILP
EAPPVMHQWL DRTFASNQSW YEARTLFTQS TALWSIAGHI VGLGDRHAEN LMIDMERGEL
MHVDFACMFD KGEKLEVPEQ VRFRLTQNLT DVMGVLGAHG PFQATCEVAL RCEMKNKSAV
MSIIETLLHE PLIEWRRQSS RSHSSNGPKQ LMERVARRLD GFLDLYSVPA KRDTLSLNVE
SQVAKLIHHS SDLNNLSQMY IWWMAWI
//
