ID A1BM10_9GAMA Unreviewed; 569 AA.
AC A1BM10;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Thymidine kinase-like protein {ECO:0000313|EMBL:ABB22239.1};
GN ORFNames=OvHV-2gp19 {ECO:0000313|EMBL:ABB22239.1};
OS Ovine gammaherpesvirus 2.
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Gammaherpesvirinae; Macavirus;
OC Macavirus ovinegamma2.
OX NCBI_TaxID=10398 {ECO:0000313|EMBL:ABB22239.1, ECO:0000313|Proteomes:UP000152762};
RN [1] {ECO:0000313|EMBL:ABB22239.1, ECO:0000313|Proteomes:UP000152762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17170434; DOI=10.1099/vir.0.82285-0;
RA Taus N.S., Herndon D.R., Traul D.L., Stewart J.P., Ackermann M., Li H.,
RA Knowles D.P., Lewis G.S., Brayton K.A.;
RT "Comparison of ovine herpesvirus 2 genomes isolated from domestic sheep
RT (Ovis aries) and a clinically affected cow (Bos bovis).";
RL J. Gen. Virol. 88:40-45(2007).
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DR EMBL; DQ198083; ABB22239.1; -; Genomic_DNA.
DR Proteomes; UP000152762; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006230; P:TMP biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_04029; HSV_KITH; 1.
DR InterPro; IPR001889; Herpes_TK.
DR InterPro; IPR013672; Herpes_TK_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10513; DEOXYNUCLEOSIDE KINASE; 1.
DR PANTHER; PTHR10513:SF35; THYMIDINE KINASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF00693; Herpes_TK; 1.
DR Pfam; PF08465; Herpes_TK_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634};
KW Early protein {ECO:0000256|ARBA:ARBA00022518};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABB22239.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000152762};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 522..554
FT /note="Herpesvirus thymidine kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08465"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..76
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 569 AA; 63207 MW; 1F8A579EDF096EF7 CRC64;
MASNSPSPDP YSRPRYGDYD VPKSWEEDNS DYEDIDLWKL AAEGQNESSD DEDEVPPAAH
LPYVPPPNPP NPRRSRAPRV LVPALDVPSL STSSWVLSPG SDLPNPLVSV GAEGGEANSN
SIGSLSSSHS DFTVLHFPEG HPNPISQSAD LYEEPPYANM SSSLNMYTSG RVTGNKLASG
KTPKRSQGEK LSAKAARIKE LSSSLLNALS LSDGAQATRP KTRRRPPPPN TSMIDLLSEP
SYTRACTVFL EGCMAVGKTT LLNYIRRSSP PDEVMTIPEP VQYWTQVYQN VLEEIVRIHK
QWKPGKLSSS AALVACQLKF ATPLKSQCCY VKHCVQEDAG RRAVAPLDRW VVCDRHPLSA
LVVFPLVWLR RGMLSFGDFL DLLAMFEANV GEVIVLISIP TDENMIRLQK RGRACEQHIN
LPYLKEIRGS FHAAYCAWLF LQYFPVEVTM KLCLQQMTME NACAISKKVS LDTAQKMWGN
SLFTTLSDVI GPFTYDPTIL QVCLHFCYQL IKLQFLVIDL SPFQDDLTGA WSEIYMQVMK
NSDIKTRMLN LAAIKALSDE AHNCSVSID
//
