ID A0A267EMM0_9PLAT Unreviewed; 915 AA.
AC A0A267EMM0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
GN ORFNames=BOX15_Mlig007730g1 {ECO:0000313|EMBL:PAA62748.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA62748.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA62748.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA62748.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA62748.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) 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=2.7.10.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001149,
CC ECO:0000256|RuleBase:RU362096};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000256|RuleBase:RU362096}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAA62748.1}.
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DR EMBL; NIVC01001904; PAA62748.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267EMM0; -.
DR STRING; 282301.A0A267EMM0; -.
DR Proteomes; UP000215902; Unassembled WGS sequence.
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; cd10361; SH2_Fps_family; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR035849; Fes/Fps/Fer_SH2.
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:SF418; TYROSINE-PROTEIN KINASE FER; 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; SSF103657; BAR/IMD domain-like; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141,
KW ECO:0000256|RuleBase:RU362096}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362096};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141,
KW ECO:0000256|RuleBase:RU362096};
KW Reference proteome {ECO:0000313|Proteomes:UP000215902};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362096};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW ECO:0000256|RuleBase:RU362096}.
FT DOMAIN 561..649
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 661..905
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 481..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 109..136
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 491..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 688
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 915 AA; 102435 MW; 392B573CFAF3484F CRC64;
MGTYFLPHPA TMSAFHEDEL AVYGCLFKFM QARARIESDY ANALRAAHAE FAGKPLPTKI
MVGTPVYKLW QAVLSNTQAL SGQLSSQLTQ LNTNLHQLAL LCQERKMLKK RYLTEKAQLD
AEARRLADEA AKTEHQYMKQ LDKVVYDREK FELLASRRRR SSTASGGSST RSSKMENYRM
QYLKSSVKLH NCHNKLVLCI DEANSHSDLA ENSQTPALCE YVENTACDCA QRCVAVMEEA
GAHLAHSNEA FAGLQSQLMR ALRDIRVVSD YQRLGEEAAV AVARLGNNSR QGGQLGRQPQ
LQRLASRSQQ QLQQVGRPML AFNAQLLREY SGRLKPGQLS YDSFTREHLL EHLQALNDRR
SVVEPQLADR RAYLAELSRD SNFASSEQNS ARARELIQLR YECSSLECRL SKIDRQIGLI
SGLVNQYPNG SEVPMGLSLD CGPGSGQGLR HMSSTEILNH PASADRGFGF DRLQRFGSSI
GKRLRRHRRS TSMVSLSQSR TRSNSVTQSS RSVFQQSTAD IPSSSGVSGG GMNSQSSPEP
QAHSSHIADV HATKDIVEQA WYHGLLPRDM ANQLLTEDGD FLVRSGDDKY VLVVMHRQQC
RHFVISGTED GMYKIDADKY RNVPAMVYHL LDKGLPVTQA SQARLFRPVA RLPWQLANQD
VSVIERIGKG EFGQVYRGTY QGRAVAVKTC GSDPTRFVAE GRLLLTLQHQ NIVQVYGIAL
LRQPVLLVME YLSHGSLLAY LRANRSVLES NDLLYMSLDA ACGLAYLETK QFIHRDIAAR
NCLVNDTKVV KIADFGMCRT EGVYQVSGGL KQIPIKWTSP ESLNSGTYTL KSDCWSFGIL
LWEIFSFGES PYSGLTNKET RARVEAGYRL PQPPDCPDWV YRLMASCWDI DPEQRPPMST
VYSTLLSKIN RTSTV
//
