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Database: UniProt
Entry: B3XVX8_9EUKA
LinkDB: B3XVX8_9EUKA
Original site: B3XVX8_9EUKA 
ID   B3XVX8_9EUKA            Unreviewed;       792 AA.
AC   B3XVX8;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE            EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN   Name=CgPTK-c {ECO:0000313|EMBL:BAG55513.1};
OS   Hartaetosiga gracilis.
OC   Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Hartaetosiga.
OX   NCBI_TaxID=216892 {ECO:0000313|EMBL:BAG55513.1};
RN   [1] {ECO:0000313|EMBL:BAG55513.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18267119; DOI=10.1016/j.febslet.2008.02.002;
RA   Suga H., Sasaki G., Kuma K., Nishiyori H., Hirose N., Su Z.H., Iwabe N.,
RA   Miyata T.;
RT   "Ancient divergence of animal protein tyrosine kinase genes demonstrated by
RT   a gene family tree including choanoflagellate genes.";
RL   FEBS Lett. 582:815-818(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001149};
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DR   EMBL; AB098191; BAG55513.1; -; mRNA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00192; PTKc; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24418:SF468; TYROSINE-PROTEIN KINASE; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAG55513.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   DOMAIN          434..527
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          540..792
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          86..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          244..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          381..405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..100
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..288
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..317
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..395
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         569
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   792 AA;  88149 MW;  3D6E041D6F54934A CRC64;
     MFNIVDVLDR INKDLAFSGI SDLNAFVISE DTHRQIRTFQ SDAKFTTSDL NGNLSVFLQK
     ETTADYGTLN ERPILNTPDV RSMTYFGQTE ENNNDGSDGS NEDNGVREVL MDSGTGTVGD
     RRNTFEDLVM EQRSATLKEH QAKYKAFLEQ YLKKLFREQQ SKMADTLEAL LLGLSNIPKT
     EDLMLQTTIR SRTASDALLM KQVVNKNSSN AQTLPDVGDG SATLKKKGMF NGMLFTKKTS
     KTDVLTPRPK LSRPDLGDEY EEVDDNDASS EISKQEGDGD QQQQHQEDDA DADDTDDADD
     ADDADDADDA DDADDADGDC KDNVKGQNES EVNLGDVESP LMLPIDGVNT SETATDSKTV
     LSKENILDTQ QHTTQDAVTF CHVASSETST TPPPSLPTAE RMPMGQPVVN KQTSMQLTAG
     DGRDGGQSVE DLECYFGPIP RNEVPMILSD PGDFLIRLGS ENSATKYVLS VLEEGGNCRH
     FNIFYCPNGY VKIEKQEFPS ISHLIRHYID NDLSLSKNSG VTIAHGVSRK KMEIWKPKDL
     ESAAKLGKGC FGVVQKMKSK ISDDVFAVKT CSDESVHPWE FLKEALDFAK FKHVNICVHR
     GISLSFPYFI LMDLCGNGAV NSYLHDHKDT SLEIKFKWAL EACEGMEYLT TNNVVHRDLA
     ARNCLLTDDL VLKISDFGLS RLVTDEDQIY LSRKAKIPYK WTAPEALNGE GFTAKSDVWS
     YGVLLWEIYN VNALPFRAIP NNELYDXLKA GSXLPRGDAT QDIYDLVLMP CWTFNRDERP
     SFTDVKALLN SF
//
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