PTKL_PLABA
ID PTKL_PLABA Reviewed; 1313 AA.
AC A0A509AIU5;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Inactive protein tyrosine kinase pTKL {ECO:0000305};
DE AltName: Full=PbpTKL {ECO:0000303|PubMed:31148576};
DE AltName: Full=Pseudo-tyrosine kinase-like protein {ECO:0000303|PubMed:31148576};
GN Name=pTKL {ECO:0000303|PubMed:31148576};
GN ORFNames=PBANKA_0940100 {ECO:0000312|EMBL:VUC55943.1};
OS Plasmodium berghei (strain Anka).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5823 {ECO:0000312|Proteomes:UP000074855};
RN [1] {ECO:0000312|Proteomes:UP000074855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANKA {ECO:0000312|Proteomes:UP000074855};
RX PubMed=25359557; DOI=10.1186/s12915-014-0086-0;
RA Otto T.D., Bohme U., Jackson A.P., Hunt M., Franke-Fayard B.,
RA Hoeijmakers W.A., Religa A.A., Robertson L., Sanders M., Ogun S.A.,
RA Cunningham D., Erhart A., Billker O., Khan S.M., Stunnenberg H.G.,
RA Langhorne J., Holder A.A., Waters A.P., Newbold C.I., Pain A., Berriman M.,
RA Janse C.J.;
RT "A comprehensive evaluation of rodent malaria parasite genomes and gene
RT expression.";
RL BMC Biol. 12:86-86(2014).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=31148576; DOI=10.1038/s41598-019-44542-3;
RA Gnangnon B., Freville A., Cailliau K., Leroy C., De Witte C., Tulasne D.,
RA Martoriarti A., Jung V., Guerrera I.C., Marion S., Khalife J., Pierrot C.;
RT "Plasmodium pseudo-Tyrosine Kinase-like binds PP1 and SERA5 and is exported
RT to host erythrocytes.";
RL Sci. Rep. 9:8120-8120(2019).
CC -!- SUBCELLULAR LOCATION: Parasitophorous vacuole
CC {ECO:0000269|PubMed:31148576}. Host cell membrane
CC {ECO:0000305|PubMed:31148576}; Peripheral membrane protein
CC {ECO:0000305}. Host cytoplasm, host cytoskeleton
CC {ECO:0000305|PubMed:31148576}. Host cytoplasm
CC {ECO:0000269|PubMed:31148576}. Note=During the trophozoite stages,
CC secreted into the parasitophorous vacuole and into the host erythrocyte
CC cytoplasm (PubMed:31148576). At the schizont stage, localizes to the
CC parasitophorous vacuole but not to the host erythrocyte cytoplasm
CC (PubMed:31148576). {ECO:0000269|PubMed:31148576}.
CC -!- DEVELOPMENTAL STAGE: Expressed during parasite asexual blood stages, in
CC trophozoite and schizont stages. {ECO:0000269|PubMed:31148576}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- DISRUPTION PHENOTYPE: Normal infection and development in host
CC erythrocytes (PubMed:31148576). Normal gametocyte production and male
CC gametocyte activation (PubMed:31148576). {ECO:0000269|PubMed:31148576}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- CAUTION: Although it belongs to the kinase superfamily, contains an
CC asparagine residue at the position of the canonical catalytic aspartic
CC acid and is predicted to lack kinase activity. However, can bind ATP
CC (By similarity). {ECO:0000250|UniProtKB:Q8IIT5,
CC ECO:0000305|PubMed:31148576}.
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DR EMBL; LK023124; VUC55943.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A509AIU5; -.
DR STRING; 5823.A0A509AIU5; -.
DR VEuPathDB; PlasmoDB:PBANKA_0940100; -.
DR OMA; LFSYLHC; -.
DR Proteomes; UP000074855; Chromosome 9.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:UniProtKB.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044163; C:host cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0020003; C:symbiont-containing vacuole; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003409; MORN.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF02493; MORN; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Glycoprotein; Host cell membrane; Host cytoplasm;
KW Host cytoskeleton; Host membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..1313
FT /note="Inactive protein tyrosine kinase pTKL"
FT /id="PRO_0000450199"
FT REPEAT 20..42
FT /note="MORN 1"
FT /evidence="ECO:0000255"
FT REPEAT 45..63
FT /note="MORN 2"
FT /evidence="ECO:0000255"
FT DOMAIN 300..365
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 962..1294
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 569..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1052..1055
FT /note="RVxF motif"
FT /evidence="ECO:0000250|UniProtKB:Q8IIT5"
FT COMPBIAS 580..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 782
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 592
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 598
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 661
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 678
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 729
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 735
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 790
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 868
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 940
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 983
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1000
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1313 AA; 154563 MW; 5E2B5A619E532BBD CRC64;
MGNINSIQTK NYIKFEKYYY AGDLNVDNLP HGRGLMLYEN GNSFFGHFIN GKKHGKGIYI
DKNLTKYISK WKYDHISNKV KVKQFDSDIV YLFYYKNGLI DHCKVYEYIS NKKKKKKKKN
DGILEDSEIQ NRSINFEKDN IMIIQNCQEK SIVNKKEEII DIPNNKYNEN DDTDKVDNFS
KKINLEQSQN NMLKYKKKKT FDEMNSLNDS IFCSSCESTS KSIGSDYISH FEKKEKQINK
QEDELKKSKE NYMNHSEYSN SSTNFENNKI KDISDESIML RLKNIINNNT DLKIENYELW
NKEQVAQWLS LCNVPMKWAL SVYKNNINGQ RLNNLNLYFI RNKLGILSYG QAIKFLQLIK
NLRVTAYNTR FSNTLNLEEY EIYLKKKMKK KKMRENKDGE YTATTSSQAE DFQKNNQKII
MNQIKSMIDQ KNDDDKSFSD KIKNGFFKGN TNIRNLQNLV INSIWNKSKD EFKIPIDENN
VPMNIEKGKE LNTNDQITGK KKKKLKNKYI NHIQKNISML KKLNNASNES QSSNESVTQI
LSTSSESSFA NIHSGLSSKM LFHDKLEPEP IKPNKEKEEN NPNLSPIINS KNETNLLNDS
NPTKLQDELP KSPCSIDSES SSEKSSETSS ETSSFCSEHS EFANFHNNNK IVKYSNNIYI
NSSLAFSYIY SFIIPPENLT FLYQIRNYYV RDVENDLNPN NELDFCDSFN FYKNCEIIKN
RIINPGIRNC SYASNHSKFQ QNKNRKYFNY SDCKNERKKT KPQKMKSRVF RGRYMGKDVA
IKVLVGNIKN FTKFHKVLYK LYILRHTNIA LIMGVSISYP FVFIIYEYIK NLCLFSYLHC
VKYKHIYVSK LLKYYQKKFI NQNFQQQNNT MSSDRKYISN DDNEKINFDS RNILRNKLLE
IKCKNNAKNK ITEKNNLKDE QIYSSSTSIK SLDTSSSNMN NTKLKNINFN KNRYINKIHS
MFRNKNNILC GNYYYLFRKK KNNISISHEH KNSDRTIFTN ESQNLLKNKI SQKKINKKLN
FKAKIKINRP YAFPPLQEDF NFYLEKKKKK KKILFSYLKT HSYFKSKKCD SRKNKLSDHQ
IMKIIMDITL ACSYLEKQKV RWINLKPTNI LLDGSLNAKI SDFGIKEIEQ CLDINIDYSY
IVFPNNVIKF NNKHFKNKIK KIKIVNKGSE DMLHVFSSKN HIYKYNTREI NVSSNTHNSS
VFFWTSPEIL KGKQSPSLYS DVYAYGIILW ELMTNSVPFN YRFKSHLLAS VGYAKESLPF
QNIPPFIKNL IKSCINRNKY KRPTFDRILI EISMIYEQIN PKEEDALMSF MDG
