ID   M7AKN2_CHEMY            Unreviewed;      1526 AA.
AC   M7AKN2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   08-MAY-2019, entry version 37.
DE   SubName: Full=Non-receptor tyrosine-protein kinase TYK2 {ECO:0000313|EMBL:EMP24984.1};
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; Testudines; Cryptodira; Durocryptodira; Americhelydia;
OC   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.,
RA   Li C., White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y.,
RA   Zheng Y., Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M.,
RA   Li Q., Wang J., Zhang H., Yu L., Shigenobu S., Wang J., Liu J.,
RA   Flicek P., Searle S., Wang J., Kuratani S., Yin Y., Aken B., Zhang G.,
RA   Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield
RT   insights into the development and evolution of the turtle-specific
RT   body plan.";
RL   Nat. Genet. 45:701-706(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-
CC         tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136,
CC         Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
CC         EC=2.7.10.2; Evidence={ECO:0000256|SAAS:SAAS01115681};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. {ECO:0000256|SAAS:SAAS00941529}.
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DR   EMBL; KB595547; EMP24984.1; -; Genomic_DNA.
DR   STRING; 8469.XP_007071282.1; -.
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-KW.
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   Gene3D; 1.20.58.610; -; 1.
DR   Gene3D; 3.30.505.10; -; 1.
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_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   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; Pkinase_Tyr; 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; SSF47031; SSF47031; 1.
DR   SUPFAM; SSF55550; SSF55550; 1.
DR   SUPFAM; SSF56112; SSF56112; 2.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|SAAS:SAAS00990534};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000031443};
KW   Kinase {ECO:0000256|SAAS:SAAS00987901, ECO:0000313|EMBL:EMP24984.1};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00987259};
KW   Receptor {ECO:0000313|EMBL:EMP24984.1};
KW   Transferase {ECO:0000256|SAAS:SAAS00989498};
KW   Tyrosine-protein kinase {ECO:0000256|SAAS:SAAS00897698}.
FT   DOMAIN      345    748       FERM. {ECO:0000259|PROSITE:PS50057}.
FT   DOMAIN      911   1193       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
FT   DOMAIN     1215   1515       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
FT   COILED        1     35       {ECO:0000256|SAM:Coils}.
FT   COILED       37     71       {ECO:0000256|SAM:Coils}.
FT   COILED      226    246       {ECO:0000256|SAM:Coils}.
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
//