ID A0A2P6TLP1_CHLSO Unreviewed; 695 AA.
AC A0A2P6TLP1;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Mitogen-activated protein kinase {ECO:0000256|ARBA:ARBA00012411, ECO:0000256|RuleBase:RU361165};
DE EC=2.7.11.24 {ECO:0000256|ARBA:ARBA00012411, ECO:0000256|RuleBase:RU361165};
GN ORFNames=C2E21_6263 {ECO:0000313|EMBL:PRW45211.1};
OS Chlorella sorokiniana (Freshwater green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=3076 {ECO:0000313|EMBL:PRW45211.1, ECO:0000313|Proteomes:UP000239899};
RN [1] {ECO:0000313|EMBL:PRW45211.1, ECO:0000313|Proteomes:UP000239899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX 1602 {ECO:0000313|Proteomes:UP000239899};
RX PubMed=29178410; DOI=10.1111/tpj.13789;
RA Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA Barney B.M.;
RT "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL Plant J. 93:566-586(2018).
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=2.7.11.24; Evidence={ECO:0000256|RuleBase:RU361165};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU361165};
CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine
CC phosphorylation. {ECO:0000256|RuleBase:RU361165}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily.
CC {ECO:0000256|ARBA:ARBA00008832}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. MAP kinase subfamily. {ECO:0000256|RuleBase:RU361165}.
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:PRW45211.1}.
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DR EMBL; LHPG02000012; PRW45211.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6TLP1; -.
DR STRING; 3076.A0A2P6TLP1; -.
DR OrthoDB; 5474493at2759; -.
DR Proteomes; UP000239899; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1.
DR PANTHER; PTHR24055:SF588; MITOGEN-ACTIVATED PROTEIN KINASE 7; 1.
DR Pfam; PF00646; F-box; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00256; FBOX; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF81383; F-box domain; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS01351; MAPK; 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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361165};
KW Magnesium {ECO:0000256|RuleBase:RU361165};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000239899};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361165};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361165}.
FT DOMAIN 36..322
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 443..490
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT BINDING 66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 695 AA; 77273 MW; F152DB5B9D56D70B CRC64;
MSSGSAQNIP VQKECSVPGK ALYQVWRTNF EIDTKYQPIK AIGKGAYGVV CSAKHADTGE
KVAIKKITNA FENLVDARRT LREMKLLRYL RHENVIAVRD IMRPASQDYN DVYIVYELMD
TDLHQIIRSS QPLSDDHFQY FIYQILRGLK YIHSASVLHR DLKPSNLLLN ATCDLKICDF
GLARTSTENH NFMTEYVVTR WYRAPELLLS CDQYDAGIDV WSVGCILAEL LQRKPLFPGK
DYIDQLKLII RTLGTPTDEE LTFISAPKAR SYVKALTQVE RADLSKLFPD ANPLAVDLLG
RMLQFDPRRR ISVEEALAHP WLAQLHDEAA EPSAPGVFKF DFEEQDLDEP AVRKLVWEEM
AHYDSAAGGA VKAHLPDDLL ARCFAELSLV ERHQTLPLTC RQFNRLVNSP QLLRTVEFDS
TIDYIMSVDD KPGSYLPPML TSSLHLLSLP DDLLARCFAE LSLVERHQAL PLTCRRFSRL
VNSPQLLRTV EFDSIISYDS PDMRKTAPDL AWAQSFACWA VRHAAGTAHR LLLNLGASFR
SPSGEPNAIW SEALGVLAAC GAAGSLQEVQ LYVQFCTASL PAWLPVALRG VRRLDLTIKE
GMLTVDVPLA AMTALTSLRL EVSAGDLGLF LTPAASLPPT LERLHIGGMN WDDDPPEQLP
PQRLAVPGTA WRHDSAQCGR AGLSAAAAAC GGTAA
//
