ID   UL97_ELHVK              Reviewed;         512 AA.
AC   Q18LD0;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Phosphotransferase UL97 homolog;
DE            EC=2.7.1.-;
OS   Elephantid herpesvirus 1 (isolate Asian elephant/Berlin/Kiba/1998) (EIHV-1)
OS   (Elephant endotheliotropic herpesvirus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Proboscivirus.
OX   NCBI_TaxID=654902;
OH   NCBI_TaxID=9783; Elephas maximus (Indian elephant).
OH   NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH   NCBI_TaxID=99490; Loxodonta cyclotis (African forest elephant).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=17507487; DOI=10.1128/jvi.00255-07;
RA   Ehlers B., Kuchler J., Yasmum N., Dural G., Voigt S., Schmidt-Chanasit J.,
RA   Jakel T., Matuschka F.R., Richter D., Essbauer S., Hughes D.J., Summers C.,
RA   Bennett M., Stewart J.P., Ulrich R.G.;
RT   "Identification of novel rodent herpesviruses, including the first
RT   gammaherpesvirus of Mus musculus.";
RL   J. Virol. 81:8091-8100(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11172087; DOI=10.1099/0022-1317-82-3-475;
RA   Ehlers B., Burkhardt S., Goltz M., Bergmann V., Ochs A., Weiler H.,
RA   Hentschke J.;
RT   "Genetic and ultrastructural characterization of a European isolate of the
RT   fatal endotheliotropic elephant herpesvirus.";
RL   J. Gen. Virol. 82:475-482(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10028};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. {ECO:0000305}.
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DR   EMBL; AF322977; ABG36589.1; -; Genomic_DNA.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
DR   GO; GO:0016032; P:viral process; IEA:InterPro.
DR   InterPro; IPR010615; Herpes_UL97.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   Pfam; PF06734; UL97; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   3: Inferred from homology;
KW   Kinase; Transferase.
FT   CHAIN           1..512
FT                   /note="Phosphotransferase UL97 homolog"
FT                   /id="PRO_0000408175"
FT   ACT_SITE        274
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10028"
SQ   SEQUENCE   512 AA;  58919 MW;  1FE6D34A0B2C39F9 CRC64;
     MLSKIMASKS QSVCSFKKYK NFFMNNVRLL RESILLNTNH DVVTEQKCHK SDQNPKRSRA
     KIQKRYNSEK KHACCVSNLH LTCVEVSLSS SSPSQSDPRT VDNDSSVARK KRVTAYLQQV
     ECDEDFFKDL RLPTKHSETD KWTLVYVPRV FSDCDSYCAR PRKRLLGAGS YGEAYLTDRG
     VTKKVFSNSE ILAEAYMLAN IIQVEGWEIH AAHLRIANSI CFRHNTVSYT FYKTDLYHFN
     AHSVDALENY RYTFRQLCDA ICFLNLRCKL VHADVSASNI LINTDEEYIL HAVLGDYSLC
     SRHDRERAII IMNENNGKSL GVCQSDLQVE GTYQIVYRPL HLMFWCVTMR TLSIWQLCRE
     AREFCVMDLC ALGRVATLFT LHLISHETSV SVRRGLFSVH KKYEKEKTAN GHKVEYGIHV
     ILNSLWIVTC LCPTFYKQSG ISMMTKLIEA FPQHEKCLNT YTKWLGEELP FRGVGIILEN
     KYGQELLDFI SKTSGVDDFR KPLGPIFETL TV