| General information | | DisProt: | DP00419 | | Name: | Thymidine kinase | | Synonym(s): | KITH_HHV11
EC 2.7.1.21
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | P03176 | | UniGene: | | | SwissProt: | KITH_HHV11 | | TrEMBL: | | | NCBI (GI): | 2851625 | | Source organism: | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) | | Sequence length: | 376 | | Percent disordered: | 16% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MASYPCHQHA SAFDQAARSR GHNNRRTALR PRRQQEATEV RPEQKMPTLL RVYIDGPHGM - 60
GKTTTTQLLV ALGSRDDIVY VPEPMTYWRV LGASETIANI YTTQHRLDQG EISAGDAAVV - 120
MTSAQITMGM PYAVTDAVLA PHIGGEAGSS HAPPPALTLI FDRHPIAALL CYPAARYLMG - 180
SMTPQAVLAF VALIPPTLPG TNIVLGALPE DRHIDRLAKR QRPGERLDLA MLAAIRRVYG - 240
LLANTVRYLQ CGGSWREDWG QLSGTAVPPQ GAEPQSNAGP RPHIGDTLFT LFRAPELLAP - 300
NGDLYNVFAW ALDVLAKRLR SMHVFILDYD QSPAGCRDAL LQLTSGMVQT HVTTPGSIPT - 360
ICDLARTFAR EMGEAN
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| Functional narrative |
In latent infection, may allow the virus to be reactivated and to grow in cells lacking a high concentration of phosphorylated nucleic acid precursors, such as nerve cells that do not replicate their genome.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | | | Location: | 34 - 49 | | Length: | 16 | | Region sequence: |
QQEATEVRPEQKMPTL | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (277 K; pH: 5.5; DTT 1 mM; KH2PO4 (40-50mM); NaN3 0.02 %; PEG 8000 (15-20%); thymidine 50 uM)
| References:
- Wild K, Bohner T, Aubry A, Folkers G, Schulz GE. "The three-dimensional structure of thymidine kinase from herpes simplex virus type 1." FEBS Lett. 1995; 368(2): 289-92. PubMed: 7628623
| Comments:
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| Region 2 | | Type: | Disordered | | Name: | | | Location: | 146 - 151 | | Length: | 6 | | Region sequence: |
EAGSSH | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (277 K; pH: 5.5; DTT 1 mM; KH2PO4 (40-50mM); NaN3 0.02 %; PEG 8000 (15-20%); thymidine 50 uM)
| References:
- Wild K, Bohner T, Aubry A, Folkers G, Schulz GE. "The three-dimensional structure of thymidine kinase from herpes simplex virus type 1." FEBS Lett. 1995; 368(2): 289-92. PubMed: 7628623
| Comments:
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| Region 3 | | Type: | Disordered | | Name: | | | Location: | 251 - 287 | | Length: | 37 | | Region sequence: |
CGGSWREDWGQLSGTAVPPQGAEPQSNAGPRPHIGDT | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (277 K; pH: 5.5; DTT 1 mM; KH2PO4 (40-50mM); NaN3 0.02 %; PEG 8000 (15-20%); thymidine 50 uM)
| References:
- Wild K, Bohner T, Aubry A, Folkers G, Schulz GE. "The three-dimensional structure of thymidine kinase from herpes simplex virus type 1." FEBS Lett. 1995; 368(2): 289-92. PubMed: 7628623
| Comments:
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| Region 4 | | Type: | Disordered | | Name: | | | Location: | 34 - 45 | | Length: | 12 | | Region sequence: |
QQEATEVRPEQK | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (298 K; ATP 1.25 mM; dT 0.05 mM; DTT 2 mM; EDTA 1 mM)
| References:
- Wild K, Bohner T, Folkers G, Schulz GE. "The structures of thymidine kinase from herpes simplex virus type 1 in complex with substrates and a substrate analogue." Protein Sci. 1997; 6(10): 2097-106. PubMed: 9336833
| Comments:
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| Region 5 | | Type: | Disordered | | Name: | | | Location: | 150 - 152 | | Length: | 3 | | Region sequence: |
SHA | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (298 K; ATP 1.25 mM; dT 0.05 mM; DTT 2 mM; EDTA 1 mM)
| References:
- Wild K, Bohner T, Folkers G, Schulz GE. "The structures of thymidine kinase from herpes simplex virus type 1 in complex with substrates and a substrate analogue." Protein Sci. 1997; 6(10): 2097-106. PubMed: 9336833
| Comments:
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| Region 6 | | Type: | Disordered | | Name: | | | Location: | 265 - 279 | | Length: | 15 | | Region sequence: |
TAVPPQGAEPQSNAG | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (298 K; ATP 1.25 mM; dT 0.05 mM; DTT 2 mM; EDTA 1 mM)
| References:
- Wild K, Bohner T, Folkers G, Schulz GE. "The structures of thymidine kinase from herpes simplex virus type 1 in complex with substrates and a substrate analogue." Protein Sci. 1997; 6(10): 2097-106. PubMed: 9336833
| Comments:
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| Comments |
The sequence from the Wild paper matches the UniProt sequence with 99% identity. The sequence presented in the paper appears to be a natural variant with changes in the sequence at residues 6 (C to G) and 23 (N to S).
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