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Conserved domains on  [gi|117606366|ref|NP_065582|]
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UMP-CMP kinase 2, mitochondrial precursor [Mus musculus]

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 ...
255-444 1.90e-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: 57.28  E-value: 1.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606366 255 IAIEGLDATGKTTLTQSVSESLKA-----VLLQSP--PPCISQWRKIF--DDEPTIIRRA---FYSLGNYLVASEIAKES 322
Cdd:cd01672    3 IVFEGIDGAGKTTLIELLAERLEArgyevVLTREPggTPIGEAIRELLldPEDEKMDPRAellLFAADRAQHVEEVIKPA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606366 323 --TNFPVIVDRYWHSTATY-------------AIATEVSGGLQ-----YLppahhpvyqwpgdllkpdlvlllTVNSEER 382
Cdd:cd01672   83 laRGKIVLSDRFVDSSLAYqgagrglgealieALNDLATGGLKpdltiLL-----------------------DIDPEVG 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 117606366 383 VRRLQGRGQEKTKEEAELEannvFRQKVEMTYQR---MENPSCHLVDASPSRETVLQKVLELIQS 444
Cdd:cd01672  140 LARIEARGRDDRDEQEGLE----FHERVREGYLElaaQEPERIIVIDASQPLEEVLAEILKAILE 200
 
Name Accession Description Interval E-value
TMPK cd01672
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
255-444 1.90e-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: 57.28  E-value: 1.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606366 255 IAIEGLDATGKTTLTQSVSESLKA-----VLLQSP--PPCISQWRKIF--DDEPTIIRRA---FYSLGNYLVASEIAKES 322
Cdd:cd01672    3 IVFEGIDGAGKTTLIELLAERLEArgyevVLTREPggTPIGEAIRELLldPEDEKMDPRAellLFAADRAQHVEEVIKPA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606366 323 --TNFPVIVDRYWHSTATY-------------AIATEVSGGLQ-----YLppahhpvyqwpgdllkpdlvlllTVNSEER 382
Cdd:cd01672   83 laRGKIVLSDRFVDSSLAYqgagrglgealieALNDLATGGLKpdltiLL-----------------------DIDPEVG 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 117606366 383 VRRLQGRGQEKTKEEAELEannvFRQKVEMTYQR---MENPSCHLVDASPSRETVLQKVLELIQS 444
Cdd:cd01672  140 LARIEARGRDDRDEQEGLE----FHERVREGYLElaaQEPERIIVIDASQPLEEVLAEILKAILE 200
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
249-438 3.68e-07

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: 50.44  E-value: 3.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606366  249 KGKFqvIAIEGLDATGKTTLTQSVSESLKAVLLQspppcisqwrKIFDDEPT------IIRRAFYSLGN---------YL 313
Cdd:TIGR00041   2 RGMF--IVIEGIDGAGKTTQANLLKKLLQENGYD----------VLFTREPGgtpigeKIRELLLNENDepltdkaeaLL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606366  314 VAS----------EIAKEStNFPVIVDRYWHSTATYaiatevSGGLQYLPPahHPVYQ----WPGDLLKPDLVLLltVNS 379
Cdd:TIGR00041  70 FAAdrhehledkiKPALAE-GKLVISDRYVFSSIAY------QGGARGIDE--DLVLElnedALGDMPDLTIYLD--IDP 138
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 117606366  380 EERVRRLQGRGQEKTKEEAELEannvFRQKVEMTYQRM--ENPSCHLVDASPSRETVLQKV 438
Cdd:TIGR00041 139 EVALERLRKRGELDREEFEKLD----FFEKVRQRYLELadKEKSIHVIDATNSVEEVEQDI 195
Tmk COG0125
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the ...
249-444 5.40e-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: 50.16  E-value: 5.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606366 249 KGKFqvIAIEGLDATGKTTLTQSVSESLKA----VLLqspppcisqWRkifddEPT------IIRRAFYSLGN------- 311
Cdd:COG0125    2 KGKF--IVFEGIDGSGKSTQIKLLAEYLEArgydVVL---------TR-----EPGgtplgeAIRELLLGDNEdmsprte 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606366 312 ---------YLVASEIAKE-STNFPVIVDRYWHSTATY-------------AIATEVSGGLQ-----YL--PPahhpvyq 361
Cdd:COG0125   66 lllfaadraQHVEEVIRPAlAAGKIVICDRYVDSSLAYqgggrgldlewirQLNRFATGGLKpdltiLLdvPP------- 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606366 362 wpgdllkpdlvllltvnsEERVRRLQGRGQEKTKEEAELEAnnvFRQKVEMTYQRM--ENPS-CHLVDASPSRETVLQKV 438
Cdd:COG0125  139 ------------------EVALARARARGGELDRFESEDLE---FHERVREGYLELaaKEPErIVVIDASQSIEEVHAEI 197

                 ....*.
gi 117606366 439 LELIQS 444
Cdd:COG0125  198 REALAE 203
Thymidylate_kin pfam02223
Thymidylate kinase;
257-438 2.41e-06

Thymidylate kinase;


Pssm-ID: 396690  Cd Length: 184  Bit Score: 47.68  E-value: 2.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606366  257 IEGLDATGKTTLTQSVSESLKAVLLQ---SPPPCISQWRKIFDD--------EPTIIRRAFYSLGNYLVASEIAKE-STN 324
Cdd:pfam02223   1 IEGLDGAGKTTQAELLKERLKEQGIKvvfTREPGGTPIGEKIRElllrneelSPLTEALLFAADRIQHLEQKIKPAlKQG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606366  325 FPVIVDRYWHSTATYAIATEVSGGLqylppahhpVYQWPGDLLKP-DLVLLLTVNSEERVRRLQGRGQEKTKEEAELEAN 403
Cdd:pfam02223  81 KTVIVDRYLFSGIAYQGAKGGDLDL---------VLSLNPDVPGKpDLTFLLDVDPEVALKRLRRRGELEKTEFEQLDFL 151
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 117606366  404 NVFRQKvemtYQRM--ENPSCHLVDASPSRETVLQKV 438
Cdd:pfam02223 152 RKVRER----YLELakFDERIKIIDASLSIEEVHEEI 184
 
Name Accession Description Interval E-value
TMPK cd01672
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
255-444 1.90e-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: 57.28  E-value: 1.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606366 255 IAIEGLDATGKTTLTQSVSESLKA-----VLLQSP--PPCISQWRKIF--DDEPTIIRRA---FYSLGNYLVASEIAKES 322
Cdd:cd01672    3 IVFEGIDGAGKTTLIELLAERLEArgyevVLTREPggTPIGEAIRELLldPEDEKMDPRAellLFAADRAQHVEEVIKPA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606366 323 --TNFPVIVDRYWHSTATY-------------AIATEVSGGLQ-----YLppahhpvyqwpgdllkpdlvlllTVNSEER 382
Cdd:cd01672   83 laRGKIVLSDRFVDSSLAYqgagrglgealieALNDLATGGLKpdltiLL-----------------------DIDPEVG 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 117606366 383 VRRLQGRGQEKTKEEAELEannvFRQKVEMTYQR---MENPSCHLVDASPSRETVLQKVLELIQS 444
Cdd:cd01672  140 LARIEARGRDDRDEQEGLE----FHERVREGYLElaaQEPERIIVIDASQPLEEVLAEILKAILE 200
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
249-438 3.68e-07

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: 50.44  E-value: 3.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606366  249 KGKFqvIAIEGLDATGKTTLTQSVSESLKAVLLQspppcisqwrKIFDDEPT------IIRRAFYSLGN---------YL 313
Cdd:TIGR00041   2 RGMF--IVIEGIDGAGKTTQANLLKKLLQENGYD----------VLFTREPGgtpigeKIRELLLNENDepltdkaeaLL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606366  314 VAS----------EIAKEStNFPVIVDRYWHSTATYaiatevSGGLQYLPPahHPVYQ----WPGDLLKPDLVLLltVNS 379
Cdd:TIGR00041  70 FAAdrhehledkiKPALAE-GKLVISDRYVFSSIAY------QGGARGIDE--DLVLElnedALGDMPDLTIYLD--IDP 138
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 117606366  380 EERVRRLQGRGQEKTKEEAELEannvFRQKVEMTYQRM--ENPSCHLVDASPSRETVLQKV 438
Cdd:TIGR00041 139 EVALERLRKRGELDREEFEKLD----FFEKVRQRYLELadKEKSIHVIDATNSVEEVEQDI 195
Tmk COG0125
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the ...
249-444 5.40e-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: 50.16  E-value: 5.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606366 249 KGKFqvIAIEGLDATGKTTLTQSVSESLKA----VLLqspppcisqWRkifddEPT------IIRRAFYSLGN------- 311
Cdd:COG0125    2 KGKF--IVFEGIDGSGKSTQIKLLAEYLEArgydVVL---------TR-----EPGgtplgeAIRELLLGDNEdmsprte 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606366 312 ---------YLVASEIAKE-STNFPVIVDRYWHSTATY-------------AIATEVSGGLQ-----YL--PPahhpvyq 361
Cdd:COG0125   66 lllfaadraQHVEEVIRPAlAAGKIVICDRYVDSSLAYqgggrgldlewirQLNRFATGGLKpdltiLLdvPP------- 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606366 362 wpgdllkpdlvllltvnsEERVRRLQGRGQEKTKEEAELEAnnvFRQKVEMTYQRM--ENPS-CHLVDASPSRETVLQKV 438
Cdd:COG0125  139 ------------------EVALARARARGGELDRFESEDLE---FHERVREGYLELaaKEPErIVVIDASQSIEEVHAEI 197

                 ....*.
gi 117606366 439 LELIQS 444
Cdd:COG0125  198 REALAE 203
Thymidylate_kin pfam02223
Thymidylate kinase;
257-438 2.41e-06

Thymidylate kinase;


Pssm-ID: 396690  Cd Length: 184  Bit Score: 47.68  E-value: 2.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606366  257 IEGLDATGKTTLTQSVSESLKAVLLQ---SPPPCISQWRKIFDD--------EPTIIRRAFYSLGNYLVASEIAKE-STN 324
Cdd:pfam02223   1 IEGLDGAGKTTQAELLKERLKEQGIKvvfTREPGGTPIGEKIRElllrneelSPLTEALLFAADRIQHLEQKIKPAlKQG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606366  325 FPVIVDRYWHSTATYAIATEVSGGLqylppahhpVYQWPGDLLKP-DLVLLLTVNSEERVRRLQGRGQEKTKEEAELEAN 403
Cdd:pfam02223  81 KTVIVDRYLFSGIAYQGAKGGDLDL---------VLSLNPDVPGKpDLTFLLDVDPEVALKRLRRRGELEKTEFEQLDFL 151
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 117606366  404 NVFRQKvemtYQRM--ENPSCHLVDASPSRETVLQKV 438
Cdd:pfam02223 152 RKVRER----YLELakFDERIKIIDASLSIEEVHEEI 184
 
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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