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Conserved domains on  [gi|157819837|ref|NP_001101487|]
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UMP-CMP kinase 2, mitochondrial [Rattus norvegicus]

Protein Classification

nucleoside/nucleotide kinase family protein( domain architecture ID 106737)

nucleoside/nucleotide kinase family protein may catalyze the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NK super family cl17190
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
225-413 2.01e-09

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


The actual alignment was detected with superfamily member cd01672:

Pssm-ID: 450170  Cd Length: 200  Bit Score: 56.89  E-value: 2.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819837 225 IAIEGLDATGKTTLTQSVSESLQA-----VLLQSP--PPCISQWRKLF--DDEPTIIRRA---FYSLGNYLVASEI--AK 290
Cdd:cd01672    3 IVFEGIDGAGKTTLIELLAERLEArgyevVLTREPggTPIGEAIRELLldPEDEKMDPRAellLFAADRAQHVEEVikPA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819837 291 QSAKFPVIVDRYWHSTATYAiatevsGGLQYLPPAhhpVYQWPRDLLKPDLVLLLT----VNSEERVRRLQGRGQEKTKE 366
Cdd:cd01672   83 LARGKIVLSDRFVDSSLAYQ------GAGRGLGEA---LIEALNDLATGGLKPDLTilldIDPEVGLARIEARGRDDRDE 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 157819837 367 EAELEvnsvFRQKVEATYQR---MENPSCRLVDASPSRETVLQTVLQLIQ 413
Cdd:cd01672  154 QEGLE----FHERVREGYLElaaQEPERIIVIDASQPLEEVLAEILKAIL 199
 
Name Accession Description Interval E-value
TMPK cd01672
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
225-413 2.01e-09

Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the phosphorylation of thymidine monophosphate (TMP) to thymidine diphosphate (TDP) utilizing ATP as its preferred phophoryl donor. TMPK represents the rate-limiting step in either de novo or salvage biosynthesis of thymidine triphosphate (TTP).


Pssm-ID: 238835  Cd Length: 200  Bit Score: 56.89  E-value: 2.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819837 225 IAIEGLDATGKTTLTQSVSESLQA-----VLLQSP--PPCISQWRKLF--DDEPTIIRRA---FYSLGNYLVASEI--AK 290
Cdd:cd01672    3 IVFEGIDGAGKTTLIELLAERLEArgyevVLTREPggTPIGEAIRELLldPEDEKMDPRAellLFAADRAQHVEEVikPA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819837 291 QSAKFPVIVDRYWHSTATYAiatevsGGLQYLPPAhhpVYQWPRDLLKPDLVLLLT----VNSEERVRRLQGRGQEKTKE 366
Cdd:cd01672   83 LARGKIVLSDRFVDSSLAYQ------GAGRGLGEA---LIEALNDLATGGLKPDLTilldIDPEVGLARIEARGRDDRDE 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 157819837 367 EAELEvnsvFRQKVEATYQR---MENPSCRLVDASPSRETVLQTVLQLIQ 413
Cdd:cd01672  154 QEGLE----FHERVREGYLElaaQEPERIIVIDASQPLEEVLAEILKAIL 199
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
219-408 8.95e-08

dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage pathways of DTTP synthesis. Catalytic activity: ATP + thymidine 5'-phosphate = ADP + thymidine 5'-diphosphate. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 161676  Cd Length: 195  Bit Score: 51.98  E-value: 8.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819837  219 KGKFqvIAIEGLDATGKTTLTQSVSESLQAVLLQspppcisqwrKLFDDEPT------IIRRAFYSLGN---------YL 283
Cdd:TIGR00041   2 RGMF--IVIEGIDGAGKTTQANLLKKLLQENGYD----------VLFTREPGgtpigeKIRELLLNENDepltdkaeaLL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819837  284 VAS----------EIAKQSaKFPVIVDRYWHSTATYaiatevSGGLQYLPPahHPVYQWPRDLLKPD--LVLLLTVNSEE 351
Cdd:TIGR00041  70 FAAdrhehledkiKPALAE-GKLVISDRYVFSSIAY------QGGARGIDE--DLVLELNEDALGDMpdLTIYLDIDPEV 140
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 157819837  352 RVRRLQGRGQEKTKEEAELEvnsvFRQKVEATYQRM--ENPSCRLVDASPSRETVLQTV 408
Cdd:TIGR00041 141 ALERLRKRGELDREEFEKLD----FFEKVRQRYLELadKEKSIHVIDATNSVEEVEQDI 195
Thymidylate_kin pfam02223
Thymidylate kinase;
227-406 2.28e-07

Thymidylate kinase;


Pssm-ID: 396690  Cd Length: 184  Bit Score: 50.76  E-value: 2.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819837  227 IEGLDATGKTTLTQSVSESLQAVLLQ---SPPPCISQWRKLFDD--------EPTIIRRAFYSLGNYLVASEIAKQSAK- 294
Cdd:pfam02223   1 IEGLDGAGKTTQAELLKERLKEQGIKvvfTREPGGTPIGEKIRElllrneelSPLTEALLFAADRIQHLEQKIKPALKQg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819837  295 FPVIVDRYWHSTATYAIATEVSGGLqylppahhpVYQWPRDLLKP-DLVLLLTVNSEERVRRLQGRGQEKTKEEAELEvn 373
Cdd:pfam02223  81 KTVIVDRYLFSGIAYQGAKGGDLDL---------VLSLNPDVPGKpDLTFLLDVDPEVALKRLRRRGELEKTEFEQLD-- 149
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 157819837  374 svFRQKVEATYQRMENPSCRL--VDASPSRETVLQ 406
Cdd:pfam02223 150 --FLRKVRERYLELAKFDERIkiIDASLSIEEVHE 182
Tmk COG0125
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the ...
219-414 2.96e-07

Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the Pathway/BioSystem: Thymidylate biosynthesis


Pssm-ID: 439895 [Multi-domain]  Cd Length: 206  Bit Score: 50.54  E-value: 2.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819837 219 KGKFqvIAIEGLDATGKTTLTQSVSESLQA----VLLqspppcisqWRklfddEPT------IIRRAFYSLGN------- 281
Cdd:COG0125    2 KGKF--IVFEGIDGSGKSTQIKLLAEYLEArgydVVL---------TR-----EPGgtplgeAIRELLLGDNEdmsprte 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819837 282 ---------YLVASEIAKQSAK-FPVIVDRYWHSTATY-AIATEVsgGLQYLPPAHHPVYQWPR-------Dllkpdlvl 343
Cdd:COG0125   66 lllfaadraQHVEEVIRPALAAgKIVICDRYVDSSLAYqGGGRGL--DLEWIRQLNRFATGGLKpdltillD-------- 135
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157819837 344 lltVNSEERVRRLQGRGQEKTKEEAE-LEvnsvFRQKVEATYQRM--ENPS-CRLVDASPSRETVLQTVLQLIQR 414
Cdd:COG0125  136 ---VPPEVALARARARGGELDRFESEdLE----FHERVREGYLELaaKEPErIVVIDASQSIEEVHAEIREALAE 203
 
Name Accession Description Interval E-value
TMPK cd01672
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
225-413 2.01e-09

Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the phosphorylation of thymidine monophosphate (TMP) to thymidine diphosphate (TDP) utilizing ATP as its preferred phophoryl donor. TMPK represents the rate-limiting step in either de novo or salvage biosynthesis of thymidine triphosphate (TTP).


Pssm-ID: 238835  Cd Length: 200  Bit Score: 56.89  E-value: 2.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819837 225 IAIEGLDATGKTTLTQSVSESLQA-----VLLQSP--PPCISQWRKLF--DDEPTIIRRA---FYSLGNYLVASEI--AK 290
Cdd:cd01672    3 IVFEGIDGAGKTTLIELLAERLEArgyevVLTREPggTPIGEAIRELLldPEDEKMDPRAellLFAADRAQHVEEVikPA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819837 291 QSAKFPVIVDRYWHSTATYAiatevsGGLQYLPPAhhpVYQWPRDLLKPDLVLLLT----VNSEERVRRLQGRGQEKTKE 366
Cdd:cd01672   83 LARGKIVLSDRFVDSSLAYQ------GAGRGLGEA---LIEALNDLATGGLKPDLTilldIDPEVGLARIEARGRDDRDE 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 157819837 367 EAELEvnsvFRQKVEATYQR---MENPSCRLVDASPSRETVLQTVLQLIQ 413
Cdd:cd01672  154 QEGLE----FHERVREGYLElaaQEPERIIVIDASQPLEEVLAEILKAIL 199
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
219-408 8.95e-08

dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage pathways of DTTP synthesis. Catalytic activity: ATP + thymidine 5'-phosphate = ADP + thymidine 5'-diphosphate. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 161676  Cd Length: 195  Bit Score: 51.98  E-value: 8.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819837  219 KGKFqvIAIEGLDATGKTTLTQSVSESLQAVLLQspppcisqwrKLFDDEPT------IIRRAFYSLGN---------YL 283
Cdd:TIGR00041   2 RGMF--IVIEGIDGAGKTTQANLLKKLLQENGYD----------VLFTREPGgtpigeKIRELLLNENDepltdkaeaLL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819837  284 VAS----------EIAKQSaKFPVIVDRYWHSTATYaiatevSGGLQYLPPahHPVYQWPRDLLKPD--LVLLLTVNSEE 351
Cdd:TIGR00041  70 FAAdrhehledkiKPALAE-GKLVISDRYVFSSIAY------QGGARGIDE--DLVLELNEDALGDMpdLTIYLDIDPEV 140
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 157819837  352 RVRRLQGRGQEKTKEEAELEvnsvFRQKVEATYQRM--ENPSCRLVDASPSRETVLQTV 408
Cdd:TIGR00041 141 ALERLRKRGELDREEFEKLD----FFEKVRQRYLELadKEKSIHVIDATNSVEEVEQDI 195
Thymidylate_kin pfam02223
Thymidylate kinase;
227-406 2.28e-07

Thymidylate kinase;


Pssm-ID: 396690  Cd Length: 184  Bit Score: 50.76  E-value: 2.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819837  227 IEGLDATGKTTLTQSVSESLQAVLLQ---SPPPCISQWRKLFDD--------EPTIIRRAFYSLGNYLVASEIAKQSAK- 294
Cdd:pfam02223   1 IEGLDGAGKTTQAELLKERLKEQGIKvvfTREPGGTPIGEKIRElllrneelSPLTEALLFAADRIQHLEQKIKPALKQg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819837  295 FPVIVDRYWHSTATYAIATEVSGGLqylppahhpVYQWPRDLLKP-DLVLLLTVNSEERVRRLQGRGQEKTKEEAELEvn 373
Cdd:pfam02223  81 KTVIVDRYLFSGIAYQGAKGGDLDL---------VLSLNPDVPGKpDLTFLLDVDPEVALKRLRRRGELEKTEFEQLD-- 149
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 157819837  374 svFRQKVEATYQRMENPSCRL--VDASPSRETVLQ 406
Cdd:pfam02223 150 --FLRKVRERYLELAKFDERIkiIDASLSIEEVHE 182
Tmk COG0125
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the ...
219-414 2.96e-07

Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the Pathway/BioSystem: Thymidylate biosynthesis


Pssm-ID: 439895 [Multi-domain]  Cd Length: 206  Bit Score: 50.54  E-value: 2.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819837 219 KGKFqvIAIEGLDATGKTTLTQSVSESLQA----VLLqspppcisqWRklfddEPT------IIRRAFYSLGN------- 281
Cdd:COG0125    2 KGKF--IVFEGIDGSGKSTQIKLLAEYLEArgydVVL---------TR-----EPGgtplgeAIRELLLGDNEdmsprte 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819837 282 ---------YLVASEIAKQSAK-FPVIVDRYWHSTATY-AIATEVsgGLQYLPPAHHPVYQWPR-------Dllkpdlvl 343
Cdd:COG0125   66 lllfaadraQHVEEVIRPALAAgKIVICDRYVDSSLAYqGGGRGL--DLEWIRQLNRFATGGLKpdltillD-------- 135
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157819837 344 lltVNSEERVRRLQGRGQEKTKEEAE-LEvnsvFRQKVEATYQRM--ENPS-CRLVDASPSRETVLQTVLQLIQR 414
Cdd:COG0125  136 ---VPPEVALARARARGGELDRFESEdLE----FHERVREGYLELaaKEPErIVVIDASQSIEEVHAEIREALAE 203
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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