ID A0A4D9ERX0_9SAUR Unreviewed; 343 AA.
AC A0A4D9ERX0;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=mitogen-activated protein kinase kinase {ECO:0000256|ARBA:ARBA00038999};
DE EC=2.7.12.2 {ECO:0000256|ARBA:ARBA00038999};
GN ORFNames=DR999_PMT03581 {ECO:0000313|EMBL:TFK13156.1};
OS Platysternon megacephalum (big-headed turtle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Platysternidae; Platysternon.
OX NCBI_TaxID=55544 {ECO:0000313|EMBL:TFK13156.1, ECO:0000313|Proteomes:UP000297703};
RN [1] {ECO:0000313|EMBL:TFK13156.1, ECO:0000313|Proteomes:UP000297703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DO16091913 {ECO:0000313|EMBL:TFK13156.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TFK13156.1};
RA Gong S.;
RT "Draft genome of the big-headed turtle Platysternon megacephalum.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TFK13156.1, ECO:0000313|Proteomes:UP000297703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DO16091913 {ECO:0000313|EMBL:TFK13156.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TFK13156.1};
RA Gong S.;
RT "The genome sequence of big-headed turtle.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC Evidence={ECO:0000256|ARBA:ARBA00036883};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.12.2; Evidence={ECO:0000256|ARBA:ARBA00036524};
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=2.7.12.2;
CC Evidence={ECO:0000256|ARBA:ARBA00035978};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase subfamily.
CC {ECO:0000256|ARBA:ARBA00038035}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TFK13156.1}.
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DR EMBL; QXTE01000017; TFK13156.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4D9ERX0; -.
DR STRING; 55544.A0A4D9ERX0; -.
DR Proteomes; UP000297703; 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:0051716; P:cellular response to stimulus; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48013:SF26; DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE 5; 1.
DR PANTHER; PTHR48013; DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE 5-RELATED; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF00069; Pkinase; 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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:TFK13156.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000297703};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304};
KW Transferase {ECO:0000313|EMBL:TFK13156.1}.
FT DOMAIN 1..77
FT /note="PB1"
FT /evidence="ECO:0000259|PROSITE:PS51745"
FT DOMAIN 134..343
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 83..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 343 AA; 38216 MW; ACA475955B9176A0 CRC64;
MKLGAVAKRF FINDVIGQVL PDATTTAFEY EDEDGDRITV RSDEEMKAML SYYYTTVMEQ
QVNGQLIEPL QIYPRACKPP GKRNIHGLKV NTRSGSANNS SSAVSDSLPS NSLKKSSAEL
KKILANGQMN EQDIQYRDVL GHGNGGTVYK AYHVPSGKIL AVKLIPLDIT LELQKQIMSE
LEILYKCDSS YIIGFYGAFF VENRISLCTE FMDGGSLDVY RKIPEHVLGR IAVAVVKGLT
YLWSLKILHR DVKPSNMLVN TRGQVKLCDF GVSTQLVNSI AKTYVGTNAY MAPERISGEQ
YGIHSDVWSL GISFMELALG RFPYPQVRLF ITAACHCDIH SYV
//
