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Database: UniProt
Entry: M7AN82_CHEMY
LinkDB: M7AN82_CHEMY
Original site: M7AN82_CHEMY 
ID   M7AN82_CHEMY            Unreviewed;       636 AA.
AC   M7AN82;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Mitogen-activated protein kinase kinase kinase 2 {ECO:0000313|EMBL:EMP26691.1};
DE   Flags: Fragment;
GN   ORFNames=UY3_16229 {ECO:0000313|EMBL:EMP26691.1};
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:EMP26691.1, 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).
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DR   EMBL; KB576444; EMP26691.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7AN82; -.
DR   STRING; 8469.M7AN82; -.
DR   eggNOG; KOG0198; Eukaryota.
DR   Proteomes; UP000031443; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06405; PB1_Mekk2_3; 1.
DR   CDD; cd06652; STKc_MEKK2; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000270; PB1_dom.
DR   InterPro; IPR034879; PB1_MEKK2/3.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   PANTHER; PTHR48016; MAP KINASE KINASE KINASE SSK2-RELATED-RELATED; 1.
DR   PANTHER; PTHR48016:SF50; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 19; 1.
DR   Pfam; PF00564; PB1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00666; PB1; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51745; PB1; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EMP26691.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EMP26691.1}.
FT   DOMAIN          41..120
FT                   /note="PB1"
FT                   /evidence="ECO:0000259|PROSITE:PS51745"
FT   DOMAIN          374..634
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          19..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          309..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..239
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..338
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        355..369
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         403
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EMP26691.1"
FT   NON_TER         636
FT                   /evidence="ECO:0000313|EMBL:EMP26691.1"
SQ   SEQUENCE   636 AA;  71482 MW;  24E27C84D4845CB7 CRC64;
     EQQALNSIMQ DLAVLHKASR PALPVQETGK PKSSSPKKQN DVRVKFEHRG EKRILQFPRP
     VKLEDLASKA KVAFGQPMDL HYSNNELVIP LTTQDDLDKA VELLDRSVHM KSLKILLVIH
     GNSQAPVLSN MEPLPSLEDL DNTVFGVAER KNRLSVIVQE NCSPILPFFF LLKGSNTRDR
     SSPPPGYIPD ELHQVVRNGS FTSINSEGEF IPESMDQMLD PLSLSSPENS GSGSCPSLDS
     PLDGDSYPKS RMPRAQSYPD NHQEFSDYDI PIFEKFGKGG TYPRRYHISY HHQDYNDGRK
     TFPRARRTQG NSFRSPVSFS PTDHSLSTSS GSSTFTPEYE ENRMRRRGSD IDNPTLSVMD
     ISPPSRSPRA PTNWRLGKLL GQGAFGRVYL CYDADTGREL AVKQVQFDPD SPETSKEVNA
     LECEIQLLKN LLHERIVQYY GCLRDPPERT LSIFMEYMPG GSIKDQLKAY GALTENVTRK
     YTRQILEGVY YLHSNMIVHR DIKGANILRD SAGNVKLGDF GASKRLQTIC LSGTGMKSVM
     GTPYWMSPEV ISGEGYGRKA DIWSVGCTVV EMLTEKPPWA EYEAMAAIFK IATQPTNPQL
     PPHVSDHGRD FLKRIFIEAK LRPSADELLR HTFAHY
//
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