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Conserved domains on  [gi|109101925|ref|XP_001099309|]
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UMP-CMP kinase 2, mitochondrial [Macaca mulatta]

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 ...
256-435 5.46e-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 pfam02223:

Pssm-ID: 450170  Cd Length: 184  Bit Score: 55.39  E-value: 5.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109101925  256 IEGLDATGKTTVTQSVADSLKA----VLLKSPP--SCIGqwRKIFDDEPTIIRRAFYSLGNYIVAS------EIAKESAK 323
Cdd:pfam02223   1 IEGLDGAGKTTQAELLKERLKEqgikVVFTREPggTPIG--EKIRELLLRNEELSPLTEALLFAADriqhleQKIKPALK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109101925  324 SP--VIVDRYWHSTATYAiatEVSGGLQHLppahhpVYQWPEDLLKP-DLILLLTVSPEERLQRLQGRGMektREEAELE 400
Cdd:pfam02223  79 QGktVIVDRYLFSGIAYQ---GAKGGDLDL------VLSLNPDVPGKpDLTFLLDVDPEVALKRLRRRGE---LEKTEFE 146
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 109101925  401 ANSVFRqKVEMSYQRMENPGC--HVVDASPCREKVLQ 435
Cdd:pfam02223 147 QLDFLR-KVRERYLELAKFDEriKIIDASLSIEEVHE 182
 
Name Accession Description Interval E-value
Thymidylate_kin pfam02223
Thymidylate kinase;
256-435 5.46e-09

Thymidylate kinase;


Pssm-ID: 396690  Cd Length: 184  Bit Score: 55.39  E-value: 5.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109101925  256 IEGLDATGKTTVTQSVADSLKA----VLLKSPP--SCIGqwRKIFDDEPTIIRRAFYSLGNYIVAS------EIAKESAK 323
Cdd:pfam02223   1 IEGLDGAGKTTQAELLKERLKEqgikVVFTREPggTPIG--EKIRELLLRNEELSPLTEALLFAADriqhleQKIKPALK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109101925  324 SP--VIVDRYWHSTATYAiatEVSGGLQHLppahhpVYQWPEDLLKP-DLILLLTVSPEERLQRLQGRGMektREEAELE 400
Cdd:pfam02223  79 QGktVIVDRYLFSGIAYQ---GAKGGDLDL------VLSLNPDVPGKpDLTFLLDVDPEVALKRLRRRGE---LEKTEFE 146
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 109101925  401 ANSVFRqKVEMSYQRMENPGC--HVVDASPCREKVLQ 435
Cdd:pfam02223 147 QLDFLR-KVRERYLELAKFDEriKIIDASLSIEEVHE 182
Tmk COG0125
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the ...
248-443 1.82e-08

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: 54.39  E-value: 1.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109101925 248 KGKFqvVAIEGLDATGKTTVTQSVADSLKA-----VLLKsppscigqwrkifddEPT------IIRRAFYSLGNYI---- 312
Cdd:COG0125    2 KGKF--IVFEGIDGSGKSTQIKLLAEYLEArgydvVLTR---------------EPGgtplgeAIRELLLGDNEDMsprt 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109101925 313 ------------VASEIAKESAK-SPVIVDRYWHSTATYAiatevsGGLQHLPPA-----HHPVYQWPE-------Dllk 367
Cdd:COG0125   65 elllfaadraqhVEEVIRPALAAgKIVICDRYVDSSLAYQ------GGGRGLDLEwirqlNRFATGGLKpdltillD--- 135
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109101925 368 pdlillltVSPEERLQRLQGRGMEKTREEAELEAnsvFRQKVEMSYQRM--ENPG-CHVVDASPCREKVLQTVLSLIQN 443
Cdd:COG0125  136 --------VPPEVALARARARGGELDRFESEDLE---FHERVREGYLELaaKEPErIVVIDASQSIEEVHAEIREALAE 203
TMPK cd01672
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
254-442 4.25e-08

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: 53.04  E-value: 4.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109101925 254 VAIEGLDATGKTTVTQSVADSLKA-----VLLKSPPSC-IGQW-RKIF--DDEPTIIRRA---FYSLGNYIVASEIAKES 321
Cdd:cd01672    3 IVFEGIDGAGKTTLIELLAERLEArgyevVLTREPGGTpIGEAiRELLldPEDEKMDPRAellLFAADRAQHVEEVIKPA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109101925 322 --AKSPVIVDRYWHSTATYAiatevsGGLQHLPPAhhpVYQWPEDLLKPDLILLLT----VSPEERLQRLQGRGMEKTRE 395
Cdd:cd01672   83 laRGKIVLSDRFVDSSLAYQ------GAGRGLGEA---LIEALNDLATGGLKPDLTilldIDPEVGLARIEARGRDDRDE 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 109101925 396 EAELEansvFRQKVEMSYQR---MENPGCHVVDASPCREKVLQTVLSLIQ 442
Cdd:cd01672  154 QEGLE----FHERVREGYLElaaQEPERIIVIDASQPLEEVLAEILKAIL 199
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
248-437 5.83e-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: 52.75  E-value: 5.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109101925  248 KGKFqvVAIEGLDATGKTTVTQSVADSLKA----VLLKSPPSCI---GQWRKIF---DDEP-TIIRRAF-------YSLG 309
Cdd:TIGR00041   2 RGMF--IVIEGIDGAGKTTQANLLKKLLQEngydVLFTREPGGTpigEKIRELLlneNDEPlTDKAEALlfaadrhEHLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109101925  310 NYIvasEIAKESAKSpVIVDRYWHSTATYaiatevSGGLQHLPPahHPVYQWPEDLLKPDLILLLTVS--PEERLQRLQG 387
Cdd:TIGR00041  80 DKI---KPALAEGKL-VISDRYVFSSIAY------QGGARGIDE--DLVLELNEDALGDMPDLTIYLDidPEVALERLRK 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 109101925  388 RGMEKTREEAELEansvFRQKVEMSYQRM--ENPGCHVVDASPCREKVLQTV 437
Cdd:TIGR00041 148 RGELDREEFEKLD----FFEKVRQRYLELadKEKSIHVIDATNSVEEVEQDI 195
 
Name Accession Description Interval E-value
Thymidylate_kin pfam02223
Thymidylate kinase;
256-435 5.46e-09

Thymidylate kinase;


Pssm-ID: 396690  Cd Length: 184  Bit Score: 55.39  E-value: 5.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109101925  256 IEGLDATGKTTVTQSVADSLKA----VLLKSPP--SCIGqwRKIFDDEPTIIRRAFYSLGNYIVAS------EIAKESAK 323
Cdd:pfam02223   1 IEGLDGAGKTTQAELLKERLKEqgikVVFTREPggTPIG--EKIRELLLRNEELSPLTEALLFAADriqhleQKIKPALK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109101925  324 SP--VIVDRYWHSTATYAiatEVSGGLQHLppahhpVYQWPEDLLKP-DLILLLTVSPEERLQRLQGRGMektREEAELE 400
Cdd:pfam02223  79 QGktVIVDRYLFSGIAYQ---GAKGGDLDL------VLSLNPDVPGKpDLTFLLDVDPEVALKRLRRRGE---LEKTEFE 146
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 109101925  401 ANSVFRqKVEMSYQRMENPGC--HVVDASPCREKVLQ 435
Cdd:pfam02223 147 QLDFLR-KVRERYLELAKFDEriKIIDASLSIEEVHE 182
Tmk COG0125
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the ...
248-443 1.82e-08

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: 54.39  E-value: 1.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109101925 248 KGKFqvVAIEGLDATGKTTVTQSVADSLKA-----VLLKsppscigqwrkifddEPT------IIRRAFYSLGNYI---- 312
Cdd:COG0125    2 KGKF--IVFEGIDGSGKSTQIKLLAEYLEArgydvVLTR---------------EPGgtplgeAIRELLLGDNEDMsprt 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109101925 313 ------------VASEIAKESAK-SPVIVDRYWHSTATYAiatevsGGLQHLPPA-----HHPVYQWPE-------Dllk 367
Cdd:COG0125   65 elllfaadraqhVEEVIRPALAAgKIVICDRYVDSSLAYQ------GGGRGLDLEwirqlNRFATGGLKpdltillD--- 135
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109101925 368 pdlillltVSPEERLQRLQGRGMEKTREEAELEAnsvFRQKVEMSYQRM--ENPG-CHVVDASPCREKVLQTVLSLIQN 443
Cdd:COG0125  136 --------VPPEVALARARARGGELDRFESEDLE---FHERVREGYLELaaKEPErIVVIDASQSIEEVHAEIREALAE 203
TMPK cd01672
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
254-442 4.25e-08

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: 53.04  E-value: 4.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109101925 254 VAIEGLDATGKTTVTQSVADSLKA-----VLLKSPPSC-IGQW-RKIF--DDEPTIIRRA---FYSLGNYIVASEIAKES 321
Cdd:cd01672    3 IVFEGIDGAGKTTLIELLAERLEArgyevVLTREPGGTpIGEAiRELLldPEDEKMDPRAellLFAADRAQHVEEVIKPA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109101925 322 --AKSPVIVDRYWHSTATYAiatevsGGLQHLPPAhhpVYQWPEDLLKPDLILLLT----VSPEERLQRLQGRGMEKTRE 395
Cdd:cd01672   83 laRGKIVLSDRFVDSSLAYQ------GAGRGLGEA---LIEALNDLATGGLKPDLTilldIDPEVGLARIEARGRDDRDE 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 109101925 396 EAELEansvFRQKVEMSYQR---MENPGCHVVDASPCREKVLQTVLSLIQ 442
Cdd:cd01672  154 QEGLE----FHERVREGYLElaaQEPERIIVIDASQPLEEVLAEILKAIL 199
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
248-437 5.83e-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: 52.75  E-value: 5.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109101925  248 KGKFqvVAIEGLDATGKTTVTQSVADSLKA----VLLKSPPSCI---GQWRKIF---DDEP-TIIRRAF-------YSLG 309
Cdd:TIGR00041   2 RGMF--IVIEGIDGAGKTTQANLLKKLLQEngydVLFTREPGGTpigEKIRELLlneNDEPlTDKAEALlfaadrhEHLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109101925  310 NYIvasEIAKESAKSpVIVDRYWHSTATYaiatevSGGLQHLPPahHPVYQWPEDLLKPDLILLLTVS--PEERLQRLQG 387
Cdd:TIGR00041  80 DKI---KPALAEGKL-VISDRYVFSSIAY------QGGARGIDE--DLVLELNEDALGDMPDLTIYLDidPEVALERLRK 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 109101925  388 RGMEKTREEAELEansvFRQKVEMSYQRM--ENPGCHVVDASPCREKVLQTV 437
Cdd:TIGR00041 148 RGELDREEFEKLD----FFEKVRQRYLELadKEKSIHVIDATNSVEEVEQDI 195
 
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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