ID M7AKN2_CHEMY Unreviewed; 1526 AA. AC M7AKN2; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 13-SEP-2023, entry version 52. DE RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903}; DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903}; GN ORFNames=UY3_17936 {ECO:0000313|EMBL:EMP24984.1}; OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira; OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia. OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP24984.1, ECO:0000313|Proteomes:UP000031443}; RN [1] {ECO:0000313|Proteomes:UP000031443} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23624526; DOI=10.1038/ng.2615; RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C., RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y., RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J., RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S., RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.; RT "The draft genomes of soft-shell turtle and green sea turtle yield insights RT into the development and evolution of the turtle-specific body plan."; RL Nat. Genet. 45:701-706(2013). 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KB595547; EMP24984.1; -; Genomic_DNA. DR STRING; 8469.XP_007071282.1; -. DR eggNOG; KOG0197; Eukaryota. DR Proteomes; UP000031443; Unassembled WGS sequence. DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro. DR GO; GO:0016020; C:membrane; IEA:InterPro. 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:0019901; F:protein kinase binding; IEA:InterPro. DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro. DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro. DR Gene3D; 6.10.140.250; -; 1. DR Gene3D; 1.20.58.610; Cdc37, Hsp90 binding domain; 1. DR Gene3D; 3.30.505.10; SH2 domain; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2. DR InterPro; IPR019749; Band_41_domain. DR InterPro; IPR013873; Cdc37_C. DR InterPro; IPR013874; Cdc37_Hsp90-bd. DR InterPro; IPR038189; Cdc37_Hsp90-bd_sf. DR InterPro; IPR013855; Cdc37_N_dom. DR InterPro; IPR035963; FERM_2. DR InterPro; IPR000299; FERM_domain. DR InterPro; IPR041155; FERM_F1. DR InterPro; IPR041046; FERM_F2. DR InterPro; IPR041381; JAK1-3/TYK2_PHL_dom. 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 InterPro; IPR016251; Tyr_kinase_non-rcpt_Jak/Tyk2. DR InterPro; IPR016045; Tyr_kinase_non-rcpt_TYK2_N. DR PANTHER; PTHR45807:SF6; NON-RECEPTOR TYROSINE-PROTEIN KINASE TYK2; 1. DR PANTHER; PTHR45807; TYROSINE-PROTEIN KINASE HOPSCOTCH; 1. DR Pfam; PF08564; CDC37_C; 1. DR Pfam; PF08565; CDC37_M; 1. DR Pfam; PF18379; FERM_F1; 1. DR Pfam; PF18377; FERM_F2; 1. DR Pfam; PF17887; Jak1_Phl; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2. DR PRINTS; PR01823; JANUSKINASE. DR PRINTS; PR00109; TYRKINASE. DR PRINTS; PR01827; YKINASETYK2. DR SMART; SM00295; B41; 1. DR SMART; SM01069; CDC37_C; 1. DR SMART; SM01070; CDC37_M; 1. DR SMART; SM01071; CDC37_N; 1. DR SMART; SM00252; SH2; 1. DR SMART; SM00219; TyrKc; 2. DR SUPFAM; SSF101391; Hsp90 co-chaperone CDC37; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2. DR SUPFAM; SSF47031; Second domain of FERM; 1. DR SUPFAM; SSF55550; SH2 domain; 1. DR PROSITE; PS50057; FERM_3; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141}; KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EMP24984.1}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Receptor {ECO:0000313|EMBL:EMP24984.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000031443}; KW SH2 domain {ECO:0000256|ARBA:ARBA00022999}; KW Transferase {ECO:0000256|ARBA:ARBA00023137}; KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}. FT DOMAIN 345..748 FT /note="FERM" FT /evidence="ECO:0000259|PROSITE:PS50057" FT DOMAIN 911..1193 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 1215..1515 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT COILED 1..71 FT /evidence="ECO:0000256|SAM:Coils" FT BINDING 1248 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 1526 AA; 174567 MW; ED7859772CFA7174 CRC64; MEQFQKEKEE LDKGCRECKR KLAECQKKMK ELEVADAVSG KGELQRLQAE AQQLRKEEKS WEKKIEELRK KEKNMPWNVD TLSKDGFSKS VFNVKPEEDD ESEEQKEKKH KTFVEKYEKQ IKHFGMLRRW DDSQKYLSDN PHLVCEETAN YLVIWCIDLE VEEKHALMEQ VAHQTIVMQF ILELAKSLKV DPRACFRQFF TKIKTADQQY MEGFTDELEA FKERVRGRAK VRIEKAMKEY EEEERQKRLG PGGLDPVEVY ESLPAELQKC FDSKDVQMLQ DAISKMEPAE AKYHMQRCID SGLWVPNAKT AEGAEKGGIG EMSLCQCAVK HSESDVEGCC FSVGGGLKVY LHWNGEEEER CQTYTQGVLS AEEICINIAQ KIGITPLCYS LFALCDVQTR VWLPPNHVFE ISKDTNLNLF FRMRYYFRNW HGMSDKEPAV YRNVPRQSDV PEDKLQGGAL LDKSSFEYLF EQGKYEFIND VVSLKDLQSE QEIHRFKNES LGMAVLHLSH MALKRGVSLE EVAKKTSFKG CIPRSFCRQI QQNNYLTRFR MRNVFRKFVQ RFQRHTVSAG KLTEQDVMYK YLATLENLAP RFGSELFPVL SLETASEGEK VLLYVNGGHT PLEGGCVSSP RDRPATHEVL VTGTDGIQWR TVPVESAESH PHRSYFGRKT RAKELDPKGL CQPVERSEAK WVRFCDFQEI THIVLKDCKV SINRQDNKCL ELVLPSHETA LSLVSLVDGY FRLTADSSHY LCHEVAPPRL VMSVLNGIHG PMQEEFVFAK LKREEQDGLY VIRWSVLNFN RLILSVVKRD HGQGSGTQTT PTYRQFRIQK RGVSFVLEGW EREFSTVREL MDVLKGCTLK SGEESFAVRR CCPPKPGEIS DLIIARKVKD STRQILNLTQ LSFHQIRKNE ITQRAHLGQG TRTNIYEGVL HVCGGAGGDD EAEYFSTEQN NNSREMHVVL KVLDPSHRDI ALAFFETASL MSQVSHIHLA FVHGVCVRGS ENIMVEEYVE HGPLDVLLRK EKGRVTVGWK VTVAKQLASA LSYLEDKNLV HGNVCAKNIL LARKGLEDGL LPFVKLSDPG VSFTVLSREE RVDRIPWIAP ECVQDVSSLS TAADKWSFGT TLLEICFDAD VPLKERTPSE KERFYEKKHR LPEPSCKELA ALISQCLTYA PSERPSFRTI LRDLTQLQPH NLVDVTSVSP DFPVSDPTVF QKRYLKKIRE LGEGHFGKVS LYCYDPTNDG TGEMVAVKSL KSGCSQQLLT SWKREIEILK TLYHENIVKY KGCCSEQGEK IVQLIMEYVP LGSLRDYLPK HNVSLAHILL FAQQICEGMA YLHSLHYIHR DLAARNVLLE NENVVKIGDF GLAKAIPEGH EYYRVCEDGD SPVFWYAMEC LKECKFYYAS DVWSFGVTLY ELLTRCDSSQ SPPVKFIEMI GVTQGQMTVL RLIELLDRGK RLPSPKDCPC EGEHHNCTGA GPGQALDERK YSIYCLMRNC WESKASFRPA FKNLVPILKS FHEKYKAQAP SVFSVC //