ID M7B6U9_CHEMY Unreviewed; 1574 AA.
AC M7B6U9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=UY3_18951 {ECO:0000313|EMBL:EMP24007.1};
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:EMP24007.1, 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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. RAF subfamily. {ECO:0000256|ARBA:ARBA00010507}.
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DR EMBL; KB604211; EMP24007.1; -; Genomic_DNA.
DR STRING; 8469.M7B6U9; -.
DR eggNOG; ENOG502QV3E; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR032770; DUF4537.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR003116; RBD_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR14343:SF4; DUF4537 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR14343; VWFA DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF15057; DUF4537; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR Pfam; PF02196; RBD; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00455; RBD; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50898; RBD; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EMP24007.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EMP24007.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 150..222
FT /note="RBD"
FT /evidence="ECO:0000259|PROSITE:PS50898"
FT DOMAIN 229..275
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 492..769
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 52..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1445..1468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1490..1530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..338
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1379..1420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1447..1468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 518
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1574 AA; 176899 MW; 175D26EF3293F2EF CRC64;
MIKLTQEHIE ALLDKFGGEH NPPSIYLEAY EEYTSKLDAL QQREQQLLES MGNGTDFSVS
SSASTDTVTS SSSSSLSVAP SSLSVYQNPT DMSRNNPKSP QKPIVRVFLP NKQRTVAPPL
QFLANGSCVV SARGGGSVQR PPGPLLSPRD VSVTSRSSAE PGQVPARCGV TVRDSLKKAL
MMRGLIPECC AVYRIQDGEK KPIGWDTDIS WLTGEELHVE VLENVPLTTH NFVRKTFFTL
AFCDFCRKLL FQGFRCQTCG YKFHQRCSTE VPLMCVNYDQ LDLLFVSKFF EHHPISQEEA
SLGETTQASG SYSSVPPSDS IGPPILPSPS PSKSIPIPQP FRPADEDHRN QFGQRDRSSS
APNVHINTIE PVNIDDLIRD QGLRGEGAPL NQLMRCLRKY QSRTPSPLLH SVPSEIVFDF
EPGPVFRGST TGLSATPPAS LPGSLTSVKA LQKSPGPQRE RKSSSSSEDR NRMKTLGRRD
SSDDWEIPDG QITVGQRIGS GSFGTVYKGK WHGDVAVKML NVTAPTPQQL QAFKNEVGVL
RKTRHVNILL FMGYSTKPQL AIVTQWCEGS SLYHHLHIIE TKFEMIKLID IARQTAQGME
VSLWQAARRF VYLSVHRCAR LQLPAALVRR SQPMGAVGSS AGRATASHNS HWPGMANHGH
WELRAGVPAD AQAPEVIRMQ DKNPYSFQSD VYAFGIVLYE LMTGQLPYSN INNRDQIIFM
VGRGYLSPDL SKVRSNCPKA MKRLMAECLK KKRDERPLFP QILASIELLA RSLPKIHRSA
SEPSLNRAGF QTEDFSLYTC ASPKTPIQAG GYAGCLRALA MSVLSHPCCA TLPLVGDLQD
RNVTFVVNML EGMSSKQDFL KEHLIKTLFL MANSPTESTF NIISFASKVI KWCNSLVKCS
LSNIIEATAW IRALQCGNGA DAVSALAMAF EDPTCQVVYL VTDALSESAS EEICSLLAET
GEERPVHTVY LVEKPGDYES STQKEMEKVA RQSGGSFQVI TPHPPGASEE VNPGCTSSIH
CCNAISKYPS CSLLMSHPKA YFPVCVCANS PTIPLTTLTK EDLMDWFLES PHLLRGAQVL
ARRETDGYYY LGHIAQEVKG SRERFLIEFE RSRLLKGKVQ FRMQETPLYD IIHYEDARRQ
PLAPGDRVLA PWEAKGERYG PGTVLKAAES CEAQLASGNS RVLVNFWNGQ TKKVSSDLAV
RIPLPLSERI ILELQMPLVA RQMLVDSSSD YPYTVTPGYR ASGHCRQDLV CWQGSTQVQS
CPNCSSGCSS LCHCCLRAWL PIRPTVNRAQ PENVLIPGTS LTKEELSRKI EEQLSKGRVP
ISERVSREED KKEKKKRLKK ENAPKDLGSC VKMGNKVTEP KKKSVTKGAT QESLRKMNFN
TARIEHRRQQ AEQRQQKREQ QQEAEGLKRQ LMRDSRRQRS LQRTLQSLEK QLEYNNMVCQ
HMAKLQTARA ERSRKESSLQ EEEKRKESQR LQFLKAQRLQ REELQVEYNQ RNYDQDKKRQ
DLLRSRMQSR QETLEREIQE PDTQQRKRED AKWRAFQNQD HFQQKLEKEC QKHHHLQQYL
REQNLLMLRA SLLS
//
