ID   KR73_ICHVA              Reviewed;         962 AA.
AC   Q00094;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Protein kinase ORF73;
DE            EC=2.7.11.1;
GN   Name=ORF73;
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).
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; M75136; AAA88175.1; -; Genomic_DNA.
DR   PIR; H36793; TVBEI4.
DR   RefSeq; NP_041163.1; NC_001493.2.
DR   SMR; Q00094; -.
DR   GeneID; 1488397; -.
DR   KEGG; vg:1488397; -.
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..962
FT                   /note="Protein kinase ORF73"
FT                   /id="PRO_0000086190"
FT   DOMAIN          301..595
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          62..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..152
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        434
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         307..315
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         324
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   962 AA;  106568 MW;  48E813CAF16C6C0E CRC64;
     MADRTPKRSA DGLIHDAKPS KVTKNDRPPV IDFKRILAAK IAEKRGGPPV SAVSLIAAST
     VSTPAPVTYG SVGLPTRQLS DSDDDDEEDN ATAKTHSVPI PVFKPPDQLT APHTVKRKPT
     QPPTPTRPVH QAQATQRRPV VSYDTTGRRA TTQDEITDAF GELDNELRRL AALTPVPGGW
     PESTRGERNQ MVNPVGVKEL PIVVQSITDR AIQIENRLEA QFHGATEMVK TVVPTVSVRG
     GVFTRHVITD TKRQPFLIEA CEFIPSMIQE APIPFRAVAS KPFAAGTKLL TPKAGAPAVD
     LRAAPVLGKG YFGTVYKVGN LACKVQHGRV MPGVSNAISD VVEESLLGSR LQHPNIITFV
     KGFLYHGAVN TEAVCVSLWE LGLMDLLSFT QQSFWQPGKD ACDPLVKRYL ARRFEKHTLL
     GLEHLHERGL MHRDIKSQNI FIFTNRGRLV AKLGDLGCCS KGAFCDAGGT RAYFPPETLA
     INVQCCASDM WAWGVTMWEV HTGRTPFWGG TDISMQKVFR YTGGFDNRAY NQLAVARHAM
     AAADSAVKPV PDLEGLMERG KVSLSPSFTD IMKSVLRLNP NDRATASDLL KSPRYTDESL
     TEGCECTDRK SLEKNAPEMI RLLEHNHLPP QKVIMTTDPH ERDQLAEKER WGQVPMEVTG
     DFRPAPLYMP WLARADMGDD HTAKKLITLT PRDLVSVYPV VATKEYGVKE IRVYRPPEFS
     PTYDIVYLEL KPTIDFEAIQ SLMEGIQAIQ KSIPYVVPVF HYTLGAHGTK RYMIYVTPAK
     RSITELNFDG ETDDGTLLGA VILKQLISLA VAFRDNGINF ITNMYNTHIL YHDPRGVDIG
     PLKLDMVIYM LLHQTNNLNV YKLSSTDRTL RDPGDPVLKT CLAAYTYVKL LMSAPRALER
     LVPKTTISAC KRFDDFFMIP TVKKISIPPD TKIKVPKLFS FIKIEPPQDI SGGTVYASGT
     LS