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Conserved domains on  [gi|2217328310|ref|XP_047300443|]
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NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial isoform X1 [Homo sapiens]

Protein Classification

nucleoside/nucleotide kinase family protein; thymidylate kinase( domain architecture ID 10114052)

nucleoside/nucleotide kinase family protein may catalyze the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars| thymidylate kinase with a major facilitator superfamily (MFS) transporter domain may function in the phosphorylation of thymidine monophosphate and the transport across cytoplasmic or internal membranes of various substrates including sugar phosphates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NDUO42 cd02030
NADH:Ubiquinone oxioreductase, 42 kDa (NDUO42) is a family of proteins that are highly similar ...
59-277 2.63e-164

NADH:Ubiquinone oxioreductase, 42 kDa (NDUO42) is a family of proteins that are highly similar to deoxyribonucleoside kinases (dNK). Members of this family have been identified as one of the subunits of NADH:Ubiquinone oxioreductase (complex I), a multi-protein complex located in the inner mitochondrial membrane. The main function of the complex is to transport electrons from NADH to ubiquinone, which is accompanied by the translocation of protons from the mitochondrial matrix to the inter membrane space.


:

Pssm-ID: 238988  Cd Length: 219  Bit Score: 454.89  E-value: 2.63e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328310  59 VITVDGNICTGKGKLAKEIAEKLGFKHFPEAGIHYPDSTTGDGKPLATDYNGNCSLEKFYDDPRSNDGNSYRLQSWLYSS 138
Cdd:cd02030     1 VITVDGNIASGKGKLAKELAEKLGMKYFPEAGIHYLDSTTGDGKPLDPAFNGNCSLEKFYDDPKSNDGNSYRLQSWMYSS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328310 139 RLLQYSDALEHLLTTGQGVVLERSIFSDFVFLEAMYNQGFIRKQCVDHYNEVKSVTICDYLPPHLVIYIDVPVPEVQRRI 218
Cdd:cd02030    81 RLLQYSDALEHLLSTGQGVVLERSPFSDFVFLEAMYKQGYIRKQCVDHYNEVKGNTIPELLPPHLVIYLDVPVPEVQKRI 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217328310 219 QKKGDPHEMKITSAYLQDIENAYKKTFLPEMSEKCEVLQYSAREAQDSKKVVEDIEYLK 277
Cdd:cd02030   161 KKRGDPHEMKVTSAYLQDIENAYKKTFLPEISEHSEVLQYDWTEAGDTEKVVEDIEYLK 219
 
Name Accession Description Interval E-value
NDUO42 cd02030
NADH:Ubiquinone oxioreductase, 42 kDa (NDUO42) is a family of proteins that are highly similar ...
59-277 2.63e-164

NADH:Ubiquinone oxioreductase, 42 kDa (NDUO42) is a family of proteins that are highly similar to deoxyribonucleoside kinases (dNK). Members of this family have been identified as one of the subunits of NADH:Ubiquinone oxioreductase (complex I), a multi-protein complex located in the inner mitochondrial membrane. The main function of the complex is to transport electrons from NADH to ubiquinone, which is accompanied by the translocation of protons from the mitochondrial matrix to the inter membrane space.


Pssm-ID: 238988  Cd Length: 219  Bit Score: 454.89  E-value: 2.63e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328310  59 VITVDGNICTGKGKLAKEIAEKLGFKHFPEAGIHYPDSTTGDGKPLATDYNGNCSLEKFYDDPRSNDGNSYRLQSWLYSS 138
Cdd:cd02030     1 VITVDGNIASGKGKLAKELAEKLGMKYFPEAGIHYLDSTTGDGKPLDPAFNGNCSLEKFYDDPKSNDGNSYRLQSWMYSS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328310 139 RLLQYSDALEHLLTTGQGVVLERSIFSDFVFLEAMYNQGFIRKQCVDHYNEVKSVTICDYLPPHLVIYIDVPVPEVQRRI 218
Cdd:cd02030    81 RLLQYSDALEHLLSTGQGVVLERSPFSDFVFLEAMYKQGYIRKQCVDHYNEVKGNTIPELLPPHLVIYLDVPVPEVQKRI 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217328310 219 QKKGDPHEMKITSAYLQDIENAYKKTFLPEMSEKCEVLQYSAREAQDSKKVVEDIEYLK 277
Cdd:cd02030   161 KKRGDPHEMKVTSAYLQDIENAYKKTFLPEISEHSEVLQYDWTEAGDTEKVVEDIEYLK 219
dNK pfam01712
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2. ...
60-287 6.76e-31

Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2.7.1.74, guanosine EC:2.7.1.113, adenosine EC:2.7.1.76 and thymidine kinase EC:2.7.1.21 (which also phosphorylates deoxyuridine and deoxycytosine.) These enzymes catalyze the production of deoxynucleotide 5'-monophosphate from a deoxynucleoside. Using ATP and yielding ADP in the process.


Pssm-ID: 396326  Cd Length: 201  Bit Score: 114.72  E-value: 6.76e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328310  60 ITVDGNICTGKGKLAKEIAEKLGFKHFPEAgihypdsttgdgkplaTDYNGNCSLEKFYDDPRsndGNSYRLQSWLYSSR 139
Cdd:pfam01712   1 ISIEGNIGAGKSTLTKILSKRLGFKVFEEP----------------VDRWTNPYLDKFYKDPS---RWSFALQTYFLNSR 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328310 140 LLQYSDALEhlltTGQGVVLERSIFSDF-VFLEAMYNQGFIRKQCVDHYNEVKSVTICDYLPPHLVIYIDVPVPEVQRRI 218
Cdd:pfam01712  62 FKQQLEAFF----TGQVVILERSIYSDRyIFAKMLYDKGTMSDEEYKTYKDLYDNMLLEFPKPDLIIYLKTSPETCLERI 137
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217328310 219 QKKGDPHEMKITSAYLQDIENAYKKtflpemsekcevlqySAREAQDSKKVVEDIEYLKFDKGPWLKQD 287
Cdd:pfam01712 138 KKRGRTEEQNISLDYLERLHEKYEA---------------WLKKLNLSPVLVIDGDELDFVFFEEDRED 191
Dck COG1428
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
55-241 9.81e-28

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 106.41  E-value: 9.81e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328310  55 ERSRVITVDGNICTGKGKLAKEIAEKLGFKHFPEAGihypdsttgDGKPLatdyngncsLEKFYDDPRSNdgnSYRLQSW 134
Cdd:COG1428     1 MKPRYIAVEGNIGAGKTTLARLLAEHLGAELLLEPV---------EDNPF---------LEDFYEDPKRW---AFPLQLF 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328310 135 LYSSRLLQysdaLEHLLTTGQGVVLERSIFSDFVFLEAMYNQGFIRKQCVDHYNEVKSVTICDYLPPHLVIYIDVPVPEV 214
Cdd:COG1428    60 FLLSRFKQ----LKDLRQFGGNVVSDRSIYKDAIFAKLLHEMGTLSDREFDLYRQLFDNLTEDLPKPDLVIYLQASVDTL 135
                         170       180
                  ....*....|....*....|....*..
gi 2217328310 215 QRRIQKKGDPHEMKITSAYLQDIENAY 241
Cdd:COG1428   136 LERIKKRGRDYEQNIDLDYLERLNEAY 162
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
135-223 1.86e-03

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: 38.50  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328310 135 LYSSRLLQYSDALEHLLTTGQGVVLERSIFSDFVFleamynQGFIRKQCVDhynEVKsvTICDYLP---PHLVIYIDVPV 211
Cdd:TIGR00041  70 FAADRHEHLEDKIKPALAEGKLVISDRYVFSSIAY------QGGARGIDED---LVL--ELNEDALgdmPDLTIYLDIDP 138
                          90
                  ....*....|..
gi 2217328310 212 PEVQRRIQKKGD 223
Cdd:TIGR00041 139 EVALERLRKRGE 150
PRK11860 PRK11860
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
54-96 7.88e-03

bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;


Pssm-ID: 237003 [Multi-domain]  Cd Length: 661  Bit Score: 37.72  E-value: 7.88e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2217328310  54 TERSRVITVDGNICTGKGKLAKEIAEKLGFkhfpeagiHYPDS 96
Cdd:PRK11860  439 ADRVPVICIDGPTASGKGTVAARVAEALGY--------HYLDS 473
 
Name Accession Description Interval E-value
NDUO42 cd02030
NADH:Ubiquinone oxioreductase, 42 kDa (NDUO42) is a family of proteins that are highly similar ...
59-277 2.63e-164

NADH:Ubiquinone oxioreductase, 42 kDa (NDUO42) is a family of proteins that are highly similar to deoxyribonucleoside kinases (dNK). Members of this family have been identified as one of the subunits of NADH:Ubiquinone oxioreductase (complex I), a multi-protein complex located in the inner mitochondrial membrane. The main function of the complex is to transport electrons from NADH to ubiquinone, which is accompanied by the translocation of protons from the mitochondrial matrix to the inter membrane space.


Pssm-ID: 238988  Cd Length: 219  Bit Score: 454.89  E-value: 2.63e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328310  59 VITVDGNICTGKGKLAKEIAEKLGFKHFPEAGIHYPDSTTGDGKPLATDYNGNCSLEKFYDDPRSNDGNSYRLQSWLYSS 138
Cdd:cd02030     1 VITVDGNIASGKGKLAKELAEKLGMKYFPEAGIHYLDSTTGDGKPLDPAFNGNCSLEKFYDDPKSNDGNSYRLQSWMYSS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328310 139 RLLQYSDALEHLLTTGQGVVLERSIFSDFVFLEAMYNQGFIRKQCVDHYNEVKSVTICDYLPPHLVIYIDVPVPEVQRRI 218
Cdd:cd02030    81 RLLQYSDALEHLLSTGQGVVLERSPFSDFVFLEAMYKQGYIRKQCVDHYNEVKGNTIPELLPPHLVIYLDVPVPEVQKRI 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217328310 219 QKKGDPHEMKITSAYLQDIENAYKKTFLPEMSEKCEVLQYSAREAQDSKKVVEDIEYLK 277
Cdd:cd02030   161 KKRGDPHEMKVTSAYLQDIENAYKKTFLPEISEHSEVLQYDWTEAGDTEKVVEDIEYLK 219
dNK cd01673
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to ...
59-277 1.09e-84

Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to yield corresponding monophosphates (dNMPs). This family consists of various deoxynucleoside kinases including deoxyribo- cytidine (EC 2.7.1.74), guanosine (EC 2.7.1.113), adenosine (EC 2.7.1.76), and thymidine (EC 2.7.1.21) kinases. They are key enzymes in the salvage of deoxyribonucleosides originating from extra- or intracellular breakdown of DNA.


Pssm-ID: 238836  Cd Length: 193  Bit Score: 252.53  E-value: 1.09e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328310  59 VITVDGNICTGKGKLAKEIAEKLGFKHFPEagihypdsttgdgkPLATDYNGNCSLEKFYDDPRsndGNSYRLQSWLYSS 138
Cdd:cd01673     1 VIVVEGNIGAGKSTLAKELAEHLGYEVVPE--------------PVEPDVEGNPFLEKFYEDPK---RWAFPFQLYFLLS 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328310 139 RLLQYSDALEHLlTTGQGVVLERSIFSDFVFLEAMYNQGFIRKQCVDHYNEVKSVTICDYLPPHLVIYIDVPVPEVQRRI 218
Cdd:cd01673    64 RLKQYKDALEHL-STGQGVILERSIFSDRVFAEANLKEGGIMKTEYDLYNELFDNLIPELLPPDLVIYLDASPETCLKRI 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217328310 219 QKKGDPHEMKITSAYLQDIENAYKKTFLPEMSEKCEVLQYSAREAqdskkvveDIEYLK 277
Cdd:cd01673   143 KKRGRPEEQGIPLDYLEDLHEAYEKWFLPQMYEKAPVLIIDANEA--------DIEYNK 193
dNK pfam01712
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2. ...
60-287 6.76e-31

Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2.7.1.74, guanosine EC:2.7.1.113, adenosine EC:2.7.1.76 and thymidine kinase EC:2.7.1.21 (which also phosphorylates deoxyuridine and deoxycytosine.) These enzymes catalyze the production of deoxynucleotide 5'-monophosphate from a deoxynucleoside. Using ATP and yielding ADP in the process.


Pssm-ID: 396326  Cd Length: 201  Bit Score: 114.72  E-value: 6.76e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328310  60 ITVDGNICTGKGKLAKEIAEKLGFKHFPEAgihypdsttgdgkplaTDYNGNCSLEKFYDDPRsndGNSYRLQSWLYSSR 139
Cdd:pfam01712   1 ISIEGNIGAGKSTLTKILSKRLGFKVFEEP----------------VDRWTNPYLDKFYKDPS---RWSFALQTYFLNSR 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328310 140 LLQYSDALEhlltTGQGVVLERSIFSDF-VFLEAMYNQGFIRKQCVDHYNEVKSVTICDYLPPHLVIYIDVPVPEVQRRI 218
Cdd:pfam01712  62 FKQQLEAFF----TGQVVILERSIYSDRyIFAKMLYDKGTMSDEEYKTYKDLYDNMLLEFPKPDLIIYLKTSPETCLERI 137
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217328310 219 QKKGDPHEMKITSAYLQDIENAYKKtflpemsekcevlqySAREAQDSKKVVEDIEYLKFDKGPWLKQD 287
Cdd:pfam01712 138 KKRGRTEEQNISLDYLERLHEKYEA---------------WLKKLNLSPVLVIDGDELDFVFFEEDRED 191
Dck COG1428
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
55-241 9.81e-28

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 106.41  E-value: 9.81e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328310  55 ERSRVITVDGNICTGKGKLAKEIAEKLGFKHFPEAGihypdsttgDGKPLatdyngncsLEKFYDDPRSNdgnSYRLQSW 134
Cdd:COG1428     1 MKPRYIAVEGNIGAGKTTLARLLAEHLGAELLLEPV---------EDNPF---------LEDFYEDPKRW---AFPLQLF 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328310 135 LYSSRLLQysdaLEHLLTTGQGVVLERSIFSDFVFLEAMYNQGFIRKQCVDHYNEVKSVTICDYLPPHLVIYIDVPVPEV 214
Cdd:COG1428    60 FLLSRFKQ----LKDLRQFGGNVVSDRSIYKDAIFAKLLHEMGTLSDREFDLYRQLFDNLTEDLPKPDLVIYLQASVDTL 135
                         170       180
                  ....*....|....*....|....*..
gi 2217328310 215 QRRIQKKGDPHEMKITSAYLQDIENAY 241
Cdd:COG1428   136 LERIKKRGRDYEQNIDLDYLERLNEAY 162
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
59-95 1.22e-04

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 41.32  E-value: 1.22e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2217328310  59 VITVDGNICTGKGKLAKEIAEKLGFKHFPEAGIHYPD 95
Cdd:cd02020     1 IIAIDGPAGSGKSTVAKLLAKKLGLPYLDTGGIRTEE 37
TMPK cd01672
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
154-245 1.01e-03

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: 39.56  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328310 154 GQGVVLERSIFSDFVFleamynQGFIRKQCVDHYNEVKSVTICDyLPPHLVIYIDVPVPEVQRRIQKKG--DPHEMKiTS 231
Cdd:cd01672    86 GKIVLSDRFVDSSLAY------QGAGRGLGEALIEALNDLATGG-LKPDLTILLDIDPEVGLARIEARGrdDRDEQE-GL 157
                          90
                  ....*....|....
gi 2217328310 232 AYLQDIENAYKKTF 245
Cdd:cd01672   158 EFHERVREGYLELA 171
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
135-223 1.86e-03

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: 38.50  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328310 135 LYSSRLLQYSDALEHLLTTGQGVVLERSIFSDFVFleamynQGFIRKQCVDhynEVKsvTICDYLP---PHLVIYIDVPV 211
Cdd:TIGR00041  70 FAADRHEHLEDKIKPALAEGKLVISDRYVFSSIAY------QGGARGIDED---LVL--ELNEDALgdmPDLTIYLDIDP 138
                          90
                  ....*....|..
gi 2217328310 212 PEVQRRIQKKGD 223
Cdd:TIGR00041 139 EVALERLRKRGE 150
cmk TIGR00017
cytidylate kinase; This family consists of cytidylate kinase, which catalyzes the ...
59-86 3.58e-03

cytidylate kinase; This family consists of cytidylate kinase, which catalyzes the phosphorylation of cytidine 5-monophosphate (dCMP) to cytidine 5 -diphosphate (dCDP) in the presence of ATP or GTP. UMP and dCMP can also act as acceptors. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 129128 [Multi-domain]  Cd Length: 217  Bit Score: 37.79  E-value: 3.58e-03
                          10        20
                  ....*....|....*....|....*...
gi 2217328310  59 VITVDGNICTGKGKLAKEIAEKLGFKHF 86
Cdd:TIGR00017   4 IIAIDGPSGAGKSTVAKAVAEKLGYAYL 31
Cytidylate_kin pfam02224
Cytidylate kinase; Cytidylate kinase EC:2.7.4.14 catalyzes the phosphorylation of cytidine 5 ...
60-93 7.24e-03

Cytidylate kinase; Cytidylate kinase EC:2.7.4.14 catalyzes the phosphorylation of cytidine 5'-monophosphate (dCMP) to cytidine 5'-diphosphate (dCDP) in the presence of ATP or GTP.


Pssm-ID: 280401 [Multi-domain]  Cd Length: 211  Bit Score: 36.90  E-value: 7.24e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2217328310  60 ITVDGNICTGKGKLAKEIAEKLGFKHFpEAGIHY 93
Cdd:pfam02224   1 IAIDGPSGSGKSTVARILARKLGYKYL-DTGAMY 33
PRK11860 PRK11860
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
54-96 7.88e-03

bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;


Pssm-ID: 237003 [Multi-domain]  Cd Length: 661  Bit Score: 37.72  E-value: 7.88e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2217328310  54 TERSRVITVDGNICTGKGKLAKEIAEKLGFkhfpeagiHYPDS 96
Cdd:PRK11860  439 ADRVPVICIDGPTASGKGTVAARVAEALGY--------HYLDS 473
 
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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