ID   KR14_ICHVA              Reviewed;         391 AA.
AC   P15443;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Protein kinase ORF14;
DE            EC=2.7.11.1;
GN   Name=ORF14;
OS   Ictalurid herpesvirus 1 (strain Auburn) (IcHV-1) (Channel catfish
OS   herpesvirus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Alloherpesviridae; Ictalurivirus.
OX   NCBI_TaxID=766178;
OH   NCBI_TaxID=7996; Ictaluridae (bullhead catfishes).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Auburn 1;
RX   PubMed=1727613; DOI=10.1016/0042-6822(92)90056-u;
RA   Davison A.J.;
RT   "Channel catfish virus: a new type of herpesvirus.";
RL   Virology 186:9-14(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 114-391.
RX   PubMed=2349101; DOI=10.1093/nar/18.10.3050;
RA   Lacasa M.;
RT   "A protein kinase-related gene within the channel catfish herpesvirus
RT   genome.";
RL   Nucleic Acids Res. 18:3050-3050(1990).
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=CAA34100.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M75136; AAA88117.1; -; Genomic_DNA.
DR   EMBL; M75136; AAA88195.1; -; Genomic_DNA.
DR   EMBL; X15978; CAA34100.1; ALT_INIT; Genomic_DNA.
DR   PIR; F36787; TVBEI1.
DR   PIR; S14686; S14686.
DR   RefSeq; NP_041105.1; NC_001493.2.
DR   RefSeq; NP_041183.1; NC_001493.2.
DR   GeneID; 1488378; -.
DR   GeneID; 1488413; -.
DR   KEGG; vg:1488378; -.
DR   KEGG; vg:1488413; -.
DR   Proteomes; UP000007643; 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; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
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; 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..391
FT                   /note="Protein kinase ORF14"
FT                   /id="PRO_0000086172"
FT   DOMAIN          109..391
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        235
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         134
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CONFLICT        125..146
FT                   /note="LSATGMAVLKIKTFHGGTQAPD -> CPPREWPCSRSRPFTAAPRPPT (in
FT                   Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        287
FT                   /note="P -> S (in Ref. 2; CAA34100)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        293..328
FT                   /note="GRGRNAGVPGIVFQIGLIALNIMVERMERVFVNHTW -> DRVPDRPDSAQH
FT                   HGGTHGAGIREPHL (in Ref. 2; CAA34100)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        357..358
FT                   /note="LA -> WP (in Ref. 2; CAA34100)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   391 AA;  44003 MW;  7FD4D67ECCB79ECA CRC64;
     MAEKLIPSCR GQWFLPARVL REGFLRARPV AVDGGFKLTI GPLTVATRVW DWVYVHYNEN
     ATDWLRGMNP PFWEEPCDVL DFLPGVACVN EATFLTLKKK YGSYLHLFVP LRHTRGNIFF
     GFSPLSATGM AVLKIKTFHG GTQAPDRPGV PMEVYAWETA HFLDAAPKLI EWEVSGTREN
     RKSAQMVTFS ECGLYGSMEG YFYRERATVD ICATILADLT GKLLALIRKG IYHGDLKSEN
     IIMMSRSGPG KLIDFEHSHG PGETMTSFWY PDRTFFWNPI GTEAYAPPER SRGRGRNAGV
     PGIVFQIGLI ALNIMVERME RVFVNHTWIK GDGYRAHVLK VIKARGTLDL RGGARTLARV
     DELIGLVARC LERDPAMRPS LETLVDEFSK I