ID YR517_MIMIV Reviewed; 450 AA.
AC Q5UQ78; Q5UQ77;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Putative serine/threonine-protein kinase R517/R518;
DE EC=2.7.11.1;
GN OrderedLocusNames=MIMI_R517, MIMI_R518;
OS Acanthamoeba polyphaga mimivirus (APMV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Imitervirales; Mimiviridae; Megamimivirinae; Mimivirus;
OC Mimivirus bradfordmassiliense.
OX NCBI_TaxID=212035;
OH NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rowbotham-Bradford;
RX PubMed=15486256; DOI=10.1126/science.1101485;
RA Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA La Scola B., Susan M., Claverie J.-M.;
RT "The 1.2-megabase genome sequence of Mimivirus.";
RL Science 306:1344-1350(2004).
RN [2]
RP SEQUENCE REVISION.
RA Audic S.;
RL Submitted (SEP-2007) to UniProtKB.
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=2.7.11.1;
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=2.7.11.1;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV50781.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAV50782.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY653733; AAV50781.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY653733; AAV50782.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; YP_003987031.1; NC_014649.1.
DR SMR; Q5UQ78; -.
DR GeneID; 9925150; -.
DR KEGG; vg:9925150; -.
DR OrthoDB; 8955at10239; -.
DR Proteomes; UP000001134; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR045269; Atg1-like.
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 PANTHER; PTHR24348:SF22; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..450
FT /note="Putative serine/threonine-protein kinase R517/R518"
FT /id="PRO_0000253439"
FT DOMAIN 9..290
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 140
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 15..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 450 AA; 51879 MW; 1AE60AD2F2144583 CRC64;
MEIINSRYKM TDTVLGKGGF SEVFLGTDMY TDNKVAIKKI NITGKNSSDI KFLNKLDFEI
RTMQILNHPN IVAYYDVMKT ENYWYIVMEY CNFGTLNDVI KFNKNKGISS LDLEKNTHYY
LNQLRDALNY IINMGYIHRD IKPMNILLTK SISENNENNE NTNYDRSNSL ILKLADFGLT
KKCSENEEDI MNTICGSPLY MAPELFFNQH YNSQSDIWSF GIIMYQLLFH DHPINATNYS
QLKNGLKNQK INFPKNNMFS NYCFDLLSKT LAKDPKNRLN WSELFHHYWF IHWSEQHCPK
NKSDDSNNKK IPDKSQFNEI LSSTKSPLIS LRQFGQLGQS NLSKFKNNGA INCSIDFPKY
TNNFPSAVNQ SIKIGLSGSS SPINIPVRNN SSKKINYDDI ELISNGNIFP ETLYGSISPV
DSIINKETRN KTNNPSSLNL SEFVLSDYEI
//
