ID F2UHN1_SALR5 Unreviewed; 1188 AA.
AC F2UHN1;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=TK protein kinase {ECO:0000313|EMBL:EGD76630.1};
GN ORFNames=PTSG_07743 {ECO:0000313|EMBL:EGD76630.1};
OS Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN [1] {ECO:0000313|Proteomes:UP000007799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Salpingoeca rosetta.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001171};
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DR EMBL; GL832974; EGD76630.1; -; Genomic_DNA.
DR RefSeq; XP_004991544.1; XM_004991487.1.
DR AlphaFoldDB; F2UHN1; -.
DR STRING; 946362.F2UHN1; -.
DR EnsemblProtists; EGD76630; EGD76630; PTSG_07743.
DR GeneID; 16072103; -.
DR KEGG; sre:PTSG_07743; -.
DR eggNOG; KOG4258; Eukaryota.
DR InParanoid; F2UHN1; -.
DR Proteomes; UP000007799; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00112; LDLa; 1.
DR CDD; cd00192; PTKc; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR032675; LRR_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; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24416:SF600; PDGF-AND VEGF-RECEPTOR RELATED, ISOFORM J; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Kinase {ECO:0000313|EMBL:EGD76630.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000007799};
KW Transferase {ECO:0000313|EMBL:EGD76630.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 48..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 764..786
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 840..1111
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 872
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1188 AA; 126284 MW; 0020DFBE1AF4CBA9 CRC64;
MTAMTTHTTS LQQHHRQQQK QQHQKQQQQR RRQRRCTRWQ WQRPIVNVGR VLLSLVVVPV
ILLDLHSLVI SPSSPSTPSL LCSAACPESV PGFAPMTCPD TTVGAACALS CPANPNVDAQ
YVCASLSNGD AWVVQGSTCM QNAICALCTC SESNTRVSCD PAVVTPNQLA GISPTVTHVT
IATQDTLGTN GTSFQLPAHL LYALPQLLEL RLENQEHFSF DNDAAAVAQA LARNGQVAPG
LQVLAVTGAA TGSATALDDL LRRVVPGGST CPAPAAAGLT VDLRGNGAWL QQQPLPWRRL
QRATHVILDN NALVSLEVAA ADITDCCLRS VSALHNAITT LDLAELGDCE QLAQLHLRNN
SLTHLHAGAL NQEPLLTFLD IRDNNIALVD TFAFDLSFSR YSQYWSSIAQ ALHMSGNPSV
CTLQLEDGER LVMCACANGY TGVPSCLDLQ PIACPDGNGT VMAQQLCDGV QDCADGWDEQ
QCTAHLVAYE DSPCSSFHRS EPCEITCRGQ LFLTTASGHV TIESHPNACD NCAVGLGSIA
DDAVSSGISS WTSLSFEVDG GFVRVRSIVP ARDGDEGPVF VLQCNELYRV VGGSWLGLNA
SVSATASLST ATSSQPSSSS APITPTPLAT LCPDMTSTFR ASHCSLVPAS TCTPDCINSR
IAPFPITCTA TGAWSADPCA DVGDDCGGAA SLTRLSPSCS NLPSPNSKGA AYCNVTCTDE
EDAVALCTGD SWSFFCRDDP DVELSCTGDS LPASSSSSLA TGSIIGIVIG VLVLTLVAAV
IVTVMYRRRQ AATAAALGLL DRHQSRVMHE LERCNVVISQ LGGGSKDWRH RIQHIDRSSV
SLQEELGRGA FGVVRKGIWT NKKGVQTSVA VKMMAGSGAS LEEQASFLVE AHIMAVLSHP
CLVQVLGVVT GDSAPPLIVV ELMRNGNLRD FLRARATINP CPLTWGQLLD VCISIADGMA
FLASNNIVHR DLACRNVLVG ESIATVKISD YGMARYLMQA DYYRMTSDTA LPMAWMAPES
VKDNKWSIAS DVWSCGVTFW EVVSLGETPF SGLSLPQIPH AQSAVHRYLP APPTLPHSIY
DVMKSCWTID PDTRPTCNHV LARLTAIRET LGAAATAAAV PLPTNPSTSP SPSPSSSFSA
VGHGGRLTFV QNRSYDHNSG CKPLQAWAHD DAADGGDDDD DSDSETRL
//
