PTKL_PLAF7
ID PTKL_PLAF7 Reviewed; 1501 AA.
AC Q8IIT5;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Inactive protein tyrosine kinase pTKL {ECO:0000305};
DE AltName: Full=PfpTKL {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=PF3D7_1106800 {ECO:0000312|EMBL:CZT98734.1};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329 {ECO:0000312|Proteomes:UP000001450};
RN [1] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2] {ECO:0000305}
RP LACK OF CATALYTIC ACTIVITY, INTERACTION WITH SERA5 AND PP1C, AND DOMAIN.
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 -!- SUBUNIT: Interacts (via RVxF motif 1 and/or 2) with phosphatase PP1C
CC (PubMed:31148576). May interact (via SAM domain) with SERA5 (via C-
CC terminus) (PubMed:31148576). {ECO:0000269|PubMed:31148576}.
CC -!- SUBCELLULAR LOCATION: Parasitophorous vacuole
CC {ECO:0000250|UniProtKB:A0A509AIU5}. Host cell membrane
CC {ECO:0000250|UniProtKB:A0A509AIU5}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:A0A509AIU5}. Host cytoplasm, host cytoskeleton
CC {ECO:0000250|UniProtKB:A0A509AIU5}. Host cytoplasm
CC {ECO:0000250|UniProtKB:A0A509AIU5}. Note=During the trophozoite stages,
CC secreted into the parasitophorous vacuole and into the host erythrocyte
CC cytoplasm. At the schizont stage, localizes to the parasitophorous
CC vacuole but not to the host erythrocyte cytoplasm.
CC {ECO:0000250|UniProtKB:A0A509AIU5}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive (By similarity). There is a second N-terminal lobe-like kinase
CC domain at residues 830-1095 that contains functional ATP binding sites
CC (PubMed:31148576). {ECO:0000255|PROSITE-ProRule:PRU00159,
CC 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 does not have kinase activity (PubMed:31148576). However, can
CC bind ATP (PubMed:31148576). {ECO:0000269|PubMed:31148576}.
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DR EMBL; LN999945; CZT98734.1; -; Genomic_DNA.
DR RefSeq; XP_001347755.2; XM_001347719.2.
DR AlphaFoldDB; Q8IIT5; -.
DR STRING; 5833.PF11_0079; -.
DR PRIDE; Q8IIT5; -.
DR EnsemblProtists; CZT98734; CZT98734; PF3D7_1106800.
DR GeneID; 810631; -.
DR KEGG; pfa:PF3D7_1106800; -.
DR VEuPathDB; PlasmoDB:PF3D7_1106800; -.
DR HOGENOM; CLU_248690_0_0_1; -.
DR InParanoid; Q8IIT5; -.
DR OMA; LFSYLHC; -.
DR PhylomeDB; Q8IIT5; -.
DR Proteomes; UP000001450; Chromosome 11.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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; PF07714; PK_Tyr_Ser-Thr; 3.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00454; SAM; 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 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Glycoprotein; Host cell membrane; Host cytoplasm;
KW Host cytoskeleton; Host membrane; Membrane; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1501
FT /note="Inactive protein tyrosine kinase pTKL"
FT /id="PRO_0000450198"
FT DOMAIN 301..366
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 1088..1483
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 204..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 399..433
FT /evidence="ECO:0000255"
FT MOTIF 483..486
FT /note="RVxF motif 1"
FT /evidence="ECO:0000305|PubMed:31148576"
FT MOTIF 1238..1241
FT /note="RVxF motif 2"
FT /evidence="ECO:0000305|PubMed:31148576"
FT COMPBIAS 204..221
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..425
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 836..844
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 864
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 712
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 737
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 811
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 819
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1024
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1031
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1074
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1501 AA; 176120 MW; E517CBE251A2999F CRC64;
MGNTLDSNKP KNFVTYADYK YIGKLNNKNE HHGIGIILYN SGESFYGSFI NGKKEGKGIY
IDKNLTRYIN TWVDNKVFGK VKVVPYNSNR VYYFYYKNYM IEKCIYFDNN INNKESHHKN
NIYNNYDNNS YNNNSCDDEE KRKYPIGVTK FKEDLSNYIH STHIMKKNNK LFNKNDNEYN
IFSSSLSYSS DSENINLLDI LKKKKNKKNK KNKKKKNKKT KNTQILSCTQ HKMYEHNMNE
SNFTKKDNVN CEHTDKMNIS LHEKNDKKNE KKNEKKNKKK KLFKYFSNNI ENLIIENYQT
WSLREVIQWL MLCNVPVKWL ISFYKNNITG DKLKYININT IRNELGIIAY GHAIKILQLI
KNLQVMAYNK KFNNLIQIEE YKNYIRQKEN TNKNIKKGKN IKKEKKKKKE KNIKKEKKKK
KKETKKFNNM DKKYIDLAIH KNVKNIQNDT FYNKHENIYN CKNQTNFIYQ NDSEIKKIMN
KKKVSFEYDN NEEKKKKNII KFIKNNKSLQ NSNGEYYLIN HLSKGICSDS IFYKSSQSKS
SSQLSSPLSS PLSSPSPSSS PSSSPSSSPS SSPSSSPSPS SSPSPSSSPS SSPSSSPSSP
PSPLSYKDNF PISSSCSSLE RLPSYEKKLL SSSQSNIEHI KNLPLDVLSN NNSSANIKIK
KSKSKYNNDK KEQKKLPLIL NKSSSEFSPS HSYTSKSYHY NIKPSLQSSS NNSSDSSYSI
SSTCSSSSSY VSSLYSNRSN DILNFYRNKI IKYCNNIYMN TKLAYSYMNG FIIPHEDLIF
IHPIENYYMD NTNEKNNINN PYTKEKIMNH NFSFNTKNNT SFIDINTNIF SSNKQQNINN
FGKYKKMKSR MFKGKYMGKE VAIKILVGKI KNFKKLHQIL YNLYNLRHSN LVLIMGVSIH
YPFVFIIYEY MKNKCLFSYL HCIKYKHVYI STFLQRYKTL LHITQQEKIK KTNNINNNNN
INHNNINNNN INHNNINHNN INNNNINNNN INYNKDYNNK KKKEDEQHNI EHQDTFIDLP
EKSNISSDDN NSTDISQIQK ENFHFLNKKI EENKNIIYDD HTSTLSDHSI HNINKSYDNV
YKNKMNIFHY QHNVLCGAYD NNDNNINDND IYCNNIYDNN INDNHIYCNN INDNHIYCNN
INDNHIYCNN IYDHHKNTSL NSKEQNTDHN IEQINECNKY ASETKYNIKK SNLKNNIISH
KNFQKCNQIQ MNQPYTFPPY QKELSSYLKN EKIKRKRKVL FSYLKTHIHF NSQQINDQHN
RLSVQKIMKI ITDVTLACTY LEKEKMSPIN LKPTNILLDE SLNAKISDFG ISKIENCLDM
NIDYSYKISS NSVIKINKKE YEQKKAKKIK IVNKNNNDLL YLYDHNNNVY KYNTQYIDVT
YNNSYPSIFY WTPPEILRGK KNKKFYSDIY AFGIILWEML SNDIPYNYPF ASHIMAVVGY
ANEELSFNNI PVSIQSLIKA CVNRNKYKRP TFEHILKTIS TLYQKANTKV EDALISFMDG
T
