KR1_EHV1K
ID KR1_EHV1K Reviewed; 382 AA.
AC P32516;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Serine/threonine-protein kinase;
DE EC=2.7.11.1;
GN Name=US2;
OS Equine herpesvirus 1 (strain Kentucky A) (EHV-1) (Equine abortion virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10329;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1316673; DOI=10.1016/0042-6822(92)90509-n;
RA Colle C.F. III, Flowers C.C., O'Callaghan D.J.;
RT "Open reading frames encoding a protein kinase, homolog of glycoprotein gX
RT of pseudorabies virus, and a novel glycoprotein map within the unique short
RT segment of equine herpesvirus type 1.";
RL Virology 188:545-557(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; M87497; AAA46070.1; -; Genomic_DNA.
DR PIR; A42538; TVBEKA.
DR SMR; P32516; -.
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; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..382
FT /note="Serine/threonine-protein kinase"
FT /id="PRO_0000086178"
FT DOMAIN 93..379
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..75
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 207
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 99..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 382 AA; 42503 MW; DFAE5941A7572588 CRC64;
MENKQCDHLT DWFSTTSDAS ESMDTTPPLP PPTPSVDPSY SGAAADEDLY SDISEGDLEY
SDCDSASESD EDDDDCLIPS KEKAREVAAS FGYTVIKTLT PGSEGRVMVA TKDGQPEPVV
LKIGQKGTTL IEAMMLRNVN HPSVIQMKDT LVSGAITCMV LPHYSSDLYT FLTKESRRIP
IDQALIIEKQ ILEGLRYLHA QRIIHRDVKT ENIFINSVDQ VCIADFGAAQ FPVVEPADLG
LAGTVETNAP EVLARAKYNS KADIWSAGIV LFEMLAYPST LFEDPPSTPE EYVKSCHSQL
LKIISTLKIN PEEFPRDPGS RLVRGYIEYS RLERNAYTRY PCFQRVNLHI DGEFLVHKML
AFNAAMRPSA EELLSYPMFA QL