ID   019R_FRG3G              Reviewed;         851 AA.
AC   Q6GZV6;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Putative serine/threonine-protein kinase 019R;
DE            EC=2.7.11.1;
GN   ORFNames=FV3-019R;
OS   Frog virus 3 (isolate Goorha) (FV-3).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Pimascovirales; Iridoviridae; Alphairidovirinae; Ranavirus.
OX   NCBI_TaxID=654924;
OH   NCBI_TaxID=30343; Dryophytes versicolor (chameleon treefrog).
OH   NCBI_TaxID=8404; Lithobates pipiens (Northern leopard frog) (Rana pipiens).
OH   NCBI_TaxID=45438; Lithobates sylvaticus (Wood frog) (Rana sylvatica).
OH   NCBI_TaxID=8316; Notophthalmus viridescens (Eastern newt) (Triturus viridescens).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15165820; DOI=10.1016/j.virol.2004.02.019;
RA   Tan W.G., Barkman T.J., Gregory Chinchar V., Essani K.;
RT   "Comparative genomic analyses of frog virus 3, type species of the genus
RT   Ranavirus (family Iridoviridae).";
RL   Virology 323:70-84(2004).
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}.
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DR   EMBL; AY548484; AAT09678.1; -; Genomic_DNA.
DR   RefSeq; YP_031597.1; NC_005946.1.
DR   PRIDE; Q6GZV6; -.
DR   GeneID; 2947739; -.
DR   KEGG; vg:2947739; -.
DR   Proteomes; UP000008770; 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:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR014901; 2-cysteine_adaptor.
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; PF08793; 2C_adapt; 5.
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   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..851
FT                   /note="Putative serine/threonine-protein kinase 019R"
FT                   /id="PRO_0000410576"
FT   DOMAIN          456..851
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          61..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          190..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          340..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..212
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..380
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        608
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         462..470
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         485
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   851 AA;  92929 MW;  5FB497EDDDD37D89 CRC64;
     MATNYCDEFE RNPTRNPRTG RTIKRGGPVF RALERECSDG AARVFPAAAV RGAAAARAAS
     PRVAAASPCP EFARDPTRNP RTGRPIKRGG PVFRALEREC ADYGGASPRR VSPARAFPNR
     RVSPARRQSP AEAAEASPCP EFARDPTRNP RTGRTIKRGG PTYRALEAEC ADYGRLSPIR
     SPWSDWSSTG LSPFRSHMRK SPARRSPARR SPARRSLARY TEHLTSDSET EVDYDARNVI
     RSQVGPGGVC ERFAADPTRN PVTGSPLSRN DPLYTDLMEI CKGYPDTPLT KSLTGEGTDD
     DTCEAFCRDP TRNPVTGQKM RRNGIEYQMF AEECDCSGIS RPSGVSRTSG TSGSSGSSAS
     SRPPNSFEAP GASSRPPNSF EASGAARVPG TPSVSRGEPR WMSSISTRHN YDESNPMSVA
     FRLRHVKDIR KFLRTVRPGR SGFCATDKGG WLGSAAVSDN VIGQGSWGSV HMVKFRDFPE
     EFVVKEAVLM SVSEKHRYKP TVVWDEWAAG SVPDEVVVNN MVTEIAATGM TPFVPLTAGA
     GACDSCNPQL LEKAAKVTKC YLQAMEAADF SLDRVLPTMS PDQAASALAQ ILLGLQSLQT
     TLGIMHNDIK AHNILVKRVP PGGYWKVTDS FNGQVFYIPN EGYLCMLADY GVVRLVKPAV
     GMDTLYGTRN ARFVPRDVGR WGKGAGTEYV VTPIRSKISV VVRGGRFVGV EPNKAVRYWK
     NTDTSKVGDV ITTNNVFYMG YDIEPDMQVQ LDDTNSFPVW ESRGDVADCV RTFVGGKRAS
     QPGFHRLFYK KTGSAWEKAA ETVAKQNPLF SGFTLDGSGL KYIRAATACA YIFPGMAVPR
     PGEREIESFT M