MKK5_LEIME
ID MKK5_LEIME Reviewed; 525 AA.
AC Q0PKV7;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Mitogen-activated protein kinase kinase 5 {ECO:0000303|PubMed:20178803};
DE EC=2.7.12.2 {ECO:0000269|PubMed:20178803};
DE AltName: Full=LmxMKK5 {ECO:0000303|PubMed:20178803};
GN Name=MKK5 {ECO:0000303|PubMed:20178803};
OS Leishmania mexicana.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5665 {ECO:0000312|EMBL:ABG91277.1};
RN [1] {ECO:0000312|EMBL:ABG91277.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP COFACTOR.
RC STRAIN=MNYC/BZ/62/M379 {ECO:0000312|EMBL:ABG91277.1};
RX PubMed=20178803; DOI=10.1016/j.ijpara.2010.02.004;
RA von Freyend S.J., Rosenqvist H., Fink A., Melzer I.M., Clos J.,
RA Jensen O.N., Wiese M.;
RT "LmxMPK4, an essential mitogen-activated protein kinase of Leishmania
RT mexicana is phosphorylated and activated by the STE7-like protein kinase
RT LmxMKK5.";
RL Int. J. Parasitol. 40:969-978(2010).
CC -!- FUNCTION: Protein kinase which phosphorylates and activates MPK4 in
CC vitro. {ECO:0000269|PubMed:20178803}.
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:0000269|PubMed:20178803};
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:0000305|PubMed:20178803};
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:0000269|PubMed:20178803};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:20178803};
CC Note=Mn(2+) was used in the in vitro kinase assay but Mg(2+) is likely
CC to be the in vivo cofactor. {ECO:0000305|PubMed:20178803};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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DR EMBL; DQ812908; ABG91277.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0PKV7; -.
DR SMR; Q0PKV7; -.
DR VEuPathDB; TriTrypDB:LmxM.36.0860; -.
DR OMA; YGAFAHE; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004708; F:MAP kinase kinase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:UniProtKB.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000165; P:MAPK cascade; IDA:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..525
FT /note="Mitogen-activated protein kinase kinase 5"
FT /id="PRO_0000449292"
FT DOMAIN 59..317
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 358..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 65..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 525 AA; 55857 MW; D2F53A6397C3D67E CRC64;
MSRLKINLDA IERDGASATE GFCADGVRIG SLLVSSEGVR DNQGNLCVLS LSDLEVVPET
EGGFLGKGSS GSVRRAVHRG SNKVVALKEI KVTGQTHINE IRRELETLHA GDFATPYLVS
FYGAFAHEGS VFIAMEAMDG SLHELYKPVP PPVLACITRL MLKGLTYLHR NRHLIHRDLK
PSNVLYNSRT GDIKISDFGV SSNLECTKAD AHSFVGTVTY MSPERLRGEH YSYGADIWSL
GLVVAELAVG VCPYAGLRGG SSEARFWALL QHLNGDGTAL ELPPEMDSDL ADFISACVVK
SPDRRPTCTE LLRHPFIVRY TGAAPEAEAK PFSTTTPTVL APGGLSSLLN RASPAAGSAL
PLASEGGTPK ATSPSPAPVS PLTLSCPLER HDGETDADIA DRTVVARWIH AVMKRAVLHK
ARGHGREELH QEPLAAVSAS VATDSGEGGG AAGVSAASLD NGQAAQHREF RAERNLDGHS
GDGGSAPVEE DCTAGVRSLT CDDLRWTSTG EPSVNLDDEL NRLLF
