ID H3B914_LATCH Unreviewed; 239 AA.
AC H3B914;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Thymidine kinase {ECO:0000256|RuleBase:RU000544};
DE EC=2.7.1.21 {ECO:0000256|RuleBase:RU000544};
GN Name=TK1 {ECO:0000313|Ensembl:ENSLACP00000018385.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000018385.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000018385.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + thymidine = ADP + dTMP + H(+); Xref=Rhea:RHEA:19129,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17748, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.1.21;
CC Evidence={ECO:0000256|ARBA:ARBA00033702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19130;
CC Evidence={ECO:0000256|ARBA:ARBA00033702};
CC -!- SIMILARITY: Belongs to the thymidine kinase family.
CC {ECO:0000256|ARBA:ARBA00007587, ECO:0000256|RuleBase:RU004165}.
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DR EMBL; AFYH01016955; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01016956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01016957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3B914; -.
DR STRING; 7897.ENSLACP00000018385; -.
DR Ensembl; ENSLACT00000018518.1; ENSLACP00000018385.1; ENSLACG00000016192.1.
DR eggNOG; KOG3125; Eukaryota.
DR GeneTree; ENSGT00390000011309; -.
DR HOGENOM; CLU_064400_3_1_1; -.
DR InParanoid; H3B914; -.
DR OMA; EAYEPRC; -.
DR TreeFam; TF314839; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000016192; Expressed in pelvic fin and 6 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001267; Thymidine_kinase.
DR InterPro; IPR020633; Thymidine_kinase_CS.
DR PANTHER; PTHR11441; THYMIDINE KINASE; 1.
DR PANTHER; PTHR11441:SF0; THYMIDINE KINASE, CYTOSOLIC; 1.
DR Pfam; PF00265; TK; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00603; TK_CELLULAR_TYPE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000544};
KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634,
KW ECO:0000256|RuleBase:RU000544};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000544};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000544};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000544}.
FT REGION 199..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 239 AA; 26884 MW; D333FA3649CC5175 CRC64;
APCATFPAQT PALPSRSQIN IDVIFGPMFS GKSTELLRRV RRFQIARYDC LVIKYSKDTR
YSNTGIATHD RNMMEAVPAS KLKDVYQKAL SCRVIGIDEG QFFPDIVEFC EDMANRGKAV
IVAALDGTFQ RKPFGSILNL VPLAESVVKL NAVCMECFKE ASYTKRLGTE EEVEVIGGAE
KYHAVCRVCH LRKPEMQTED KENWPIARKD ETLPHVQPGR SLDPKVQRTR YAPLLLSQS
//
