ID A0A091E459_FUKDA Unreviewed; 963 AA.
AC A0A091E459;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
GN ORFNames=H920_01117 {ECO:0000313|EMBL:KFO37508.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO37508.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO37508.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO37508.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) 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}.
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DR EMBL; KN120821; KFO37508.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091E459; -.
DR STRING; 885580.ENSFDAP00000013639; -.
DR eggNOG; KOG0197; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; cd05148; PTKc_Srm_Brk; 1.
DR CDD; cd10358; SH2_PTK6_Brk; 1.
DR CDD; cd11847; SH3_Brk; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR035846; PTK6_SH2.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24418:SF23; TYROSINE-PROTEIN KINASE SRMS; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR Pfam; PF00017; SH2; 2.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 2.
DR SMART; SM00326; SH3; 2.
DR SMART; SM00219; TyrKc; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR SUPFAM; SSF55550; SH2 domain; 2.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 2.
DR PROSITE; PS50001; SH2; 2.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141,
KW ECO:0000256|RuleBase:RU362096}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362096};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192};
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 98..190
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 208..465
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 520..584
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 590..682
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 703..957
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 731
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 963 AA; 108009 MW; 5B22E43ED40E7E09 CRC64;
MGLGVEEGEV AGLRGSLGRG HRPDGTCAAD TGDRAWCPVS WLQGEEGLSV SRGDRLYALK
EEGAYIFARR LSGPPSAGLV PLSYVAEAAW ETPAEQPWYF SGISRTQAQQ LLLSPANAPG
AFLIRPSESS LGGYSLSVRA QAKVCHYRIC TAPGGSLYLQ EGRLFPSLEA LLTYYKANWK
LIQNPLLQPC MPQKSLAQDR WERPRSEFAL RRKLGEGCFG EVWEGLWLGS VPVAVKVIKS
ADMKLADLTK EIEALKSLRH ERLIRLHAVC STGEPVYIVT ELMRKGNLQA YLGSPEGQAL
SLPLLLSFTC QVAEGMSYLE ERHVVHRDLA ARNVLVDDDL TCKVADFGLA RLLKDDIYSP
SSSSKIPVKW TAPEAANHRI FSQKSDVWSF GVLLFEVFSY GQCPYEGMTN HETLQQLSRG
YRLPRPAACP VEVYLLMLEC WKGSPEERPA FAMLREKLGT VHRHLHLAPL MCTPGPGSAD
LGMPSWLRSS CMACMGLAGA HSRPTSQSCC TAMASQGQAY LGPKYVGLWD FEARTDEELS
FRAGDLFHVA RKEDQWWWAT RLDDLGQALT EGYVPHNYLA EKETVESEPW FFGHISRSEA
THRLQAEGSS PGTFLVRVSE KSGADYVLSV RDTQAVRHYR IWQHEGGRLH LNEAVSFPSL
LELVDYHKAQ SLSHGLRLTV PCWKHQAEPL PHWADWERPQ EEFTLCRKLG AGYFGEVFEG
LWKGQVRVAI KVISRDNLLH QHTFQSEIQA MKRLRHKHIL ALYAVASSGD PVYIITELMP
KGNLLQLLRD SEKQALPVSE LVDIASQVAE GMRYLESQNY IHRDLAARNI LVGENNICKV
GDFGLARLIK EDIYLSHDHK IPYKWTAPEA LSRGHYSIKS DVWSFGILLH EILSRGQTPY
PGMSNHEAFL RVDAGYRMPC PPECPPNVYQ LMSSCWSRDP EQRPCFKALC EKLSGFARYE
NLL
//
