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Conserved domains on  [gi|467155|gb|AAA50919|]
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unknown [Mycobacterium leprae]

Protein Classification

(d)CMP kinase( domain architecture ID 11129747)

(d)CMP kinase catalyzes the phosphorylation of cytidine monophosphate (CMP) or dCMP to produce cytidine diphosphate (CDP) or dCDP, using ATP as the preferred phosphoryl donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cytidylate_kin pfam02224
Cytidylate kinase; Cytidylate kinase EC:2.7.4.14 catalyzes the phosphorylation of cytidine 5 ...
 6-217 1.72e-112

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: 320.41  E-value: 1.72e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155       6 VAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMTLAVLRAGIDPADAAAIGESVWKVQMLSDHDRYFLGGEDVSSEI 85
Cdd:pfam02224   1 IAIDGPSGSGKSTVARILARKLGYKYLDTGAMYRALALAALRQKVDLTDEDALAELASEVDISFGHTEVFLNGEDVSSEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155      86 RTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEgRGSVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVASGSADD 165
Cdd:pfam02224  81 RTDEVAQAASQVAAIPAVRARLNKLQRQLAK-NGNIVMEGRDIGTVVFPDAEVKIFLTASPEERAKRRYKQLQAKGLSVD 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 467155     166 YDRVLAEVRRRDHLDSTRAVSPLYVAQDAMIVDTSKMAEAEVIAHLMDLVKQ 217
Cdd:pfam02224 160 FEELLAEIKRRDKRDSERAVGPLKPAPDALIIDTSKLTIEEVVEKILELIKQ 211
 
Name Accession Description Interval E-value
Cytidylate_kin pfam02224
Cytidylate kinase; Cytidylate kinase EC:2.7.4.14 catalyzes the phosphorylation of cytidine 5 ...
 6-217 1.72e-112

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: 320.41  E-value: 1.72e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155       6 VAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMTLAVLRAGIDPADAAAIGESVWKVQMLSDHDRYFLGGEDVSSEI 85
Cdd:pfam02224   1 IAIDGPSGSGKSTVARILARKLGYKYLDTGAMYRALALAALRQKVDLTDEDALAELASEVDISFGHTEVFLNGEDVSSEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155      86 RTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEgRGSVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVASGSADD 165
Cdd:pfam02224  81 RTDEVAQAASQVAAIPAVRARLNKLQRQLAK-NGNIVMEGRDIGTVVFPDAEVKIFLTASPEERAKRRYKQLQAKGLSVD 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 467155     166 YDRVLAEVRRRDHLDSTRAVSPLYVAQDAMIVDTSKMAEAEVIAHLMDLVKQ 217
Cdd:pfam02224 160 FEELLAEIKRRDKRDSERAVGPLKPAPDALIIDTSKLTIEEVVEKILELIKQ 211
Cmk COG0283
Cytidylate kinase [Nucleotide transport and metabolism];
4-218 2.53e-109

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440052 [Multi-domain]  Cd Length: 220  Bit Score: 312.73  E-value: 2.53e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155     4 IVVAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMTLAVLRAGIDPADAAAIGESV----WKVQMLSDHDRYFLGGE 79
Cdd:COG0283   1 PVIAIDGPAGSGKSTVAKALAKRLGYHYLDTGAMYRAVALAALRNGIDLDDEEALAALArnldIEFETDPGGQRVFLNGE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155    80 DVSSEIRTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEGRGsVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVA 159
Cdd:COG0283  81 DVTDEIRTEEVSNAVSKVAAIPEVREALVALQRAFAKAPG-LVADGRDIGTVVFPDAELKIFLTASAEERARRRYKELKE 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 467155   160 SGSADDYDRVLAEVRRRDHLDSTRAVSPLYVAQDAMIVDTSKMAEAEVIAHLMDLVKQR 218
Cdd:COG0283 160 KGISVSLEELLADIKERDERDSTRAVAPLKPAEDAIVIDTTDLSIEEVVEKILALVRER 218
PRK13477 PRK13477
bifunctional pantoate--beta-alanine ligase/(d)CMP kinase;
5-223 1.27e-75

bifunctional pantoate--beta-alanine ligase/(d)CMP kinase;


Pssm-ID: 237393 [Multi-domain]  Cd Length: 512  Bit Score: 236.70  E-value: 1.27e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155      5 VVAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMTLAVLRAGIDPADAAAIGESVWKVQM-----LSDHDRYFLGGE 79
Cdd:PRK13477 286 IIAIDGPAGAGKSTVTRAVAKKLGLLYLDTGAMYRAVTWLVLQEGIDPQDEEALAELLSDLKIelkpsSGSPQRVWINGE 365

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155     80 DVSSEIRTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEgRGSVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVA 159
Cdd:PRK13477 366 DVTEAIRSPEVTSSVSAIAAQPAVRQALVKQQQRIGE-KGGLVAEGRDIGTHVFPDAELKIFLTASVEERARRRALDLQA 444

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 467155    160 SGSAD-DYDRVLAEVRRRDHLDSTRAVSPLYVAQDAMIVDTSKMAEAEVIAHLMDLVKQR-SGAVW 223
Cdd:PRK13477 445 QGFPViDLEQLEAQIAERDRLDSTREIAPLRKADDAIELITDGLSIEEVVDKIIDLYRDRiPEEVW 510
cmk TIGR00017
cytidylate kinase; This family consists of cytidylate kinase, which catalyzes the ...
 5-208 5.61e-70

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: 213.06  E-value: 5.61e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155       5 VVAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMTLAVLRAGIDPADAAAIGESV----WKVQMLSDHDRYFLGGED 80
Cdd:TIGR00017   4 IIAIDGPSGAGKSTVAKAVAEKLGYAYLDSGAMYRAIALAALQNRVDLTSEDALAELIshldIRFIPTNGEVEVFLNGED 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155      81 VSSEIRTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEgRGSVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVAS 160
Cdd:TIGR00017  84 VSEAIRTQEVANAASKVAVFPKVREALLKRQQALAK-NDGIIADGRDIGTVVFPNAEVKIFLDASVEERAKRRYKQLQIK 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 467155     161 GSADDYDRVLAEVRRRDHLDSTRAVSPLYVAQDAMIVDTSKMAEAEVI 208
Cdd:TIGR00017 163 GNEVNFEELLAEIKERDDRDSNREVAPLKKADDALYLDTSNLSIDEVV 210
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
 5-200 2.56e-64

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: 196.17  E-value: 2.56e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155     5 VVAIDGPAGTGKSSVSRGLARELGARYLDTGamyrmmtlavlragidpadaaaigesvwkvqmlsdhdryflggedvssE 84
Cdd:cd02020   1 IIAIDGPAGSGKSTVAKLLAKKLGLPYLDTG------------------------------------------------G 32

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155    85 IRTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEGRGsVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVASGSAD 164
Cdd:cd02020  33 IRTEEVGKLASEVAAIPEVRKALDERQRELAKKPG-IVLEGRDIGTVVFPDADLKIFLTASPEVRAKRRAKQLQAKGEGV 111

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 467155   165 DYDRVLAEVRRRDHLDSTRAVSPLYVAQDAMIVDTS 200
Cdd:cd02020 112 DLEEILAEIIERDERDSTRYVAPLKLAEDAIVIDTS 147
 
Name Accession Description Interval E-value
Cytidylate_kin pfam02224
Cytidylate kinase; Cytidylate kinase EC:2.7.4.14 catalyzes the phosphorylation of cytidine 5 ...
 6-217 1.72e-112

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: 320.41  E-value: 1.72e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155       6 VAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMTLAVLRAGIDPADAAAIGESVWKVQMLSDHDRYFLGGEDVSSEI 85
Cdd:pfam02224   1 IAIDGPSGSGKSTVARILARKLGYKYLDTGAMYRALALAALRQKVDLTDEDALAELASEVDISFGHTEVFLNGEDVSSEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155      86 RTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEgRGSVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVASGSADD 165
Cdd:pfam02224  81 RTDEVAQAASQVAAIPAVRARLNKLQRQLAK-NGNIVMEGRDIGTVVFPDAEVKIFLTASPEERAKRRYKQLQAKGLSVD 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 467155     166 YDRVLAEVRRRDHLDSTRAVSPLYVAQDAMIVDTSKMAEAEVIAHLMDLVKQ 217
Cdd:pfam02224 160 FEELLAEIKRRDKRDSERAVGPLKPAPDALIIDTSKLTIEEVVEKILELIKQ 211
Cmk COG0283
Cytidylate kinase [Nucleotide transport and metabolism];
4-218 2.53e-109

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440052 [Multi-domain]  Cd Length: 220  Bit Score: 312.73  E-value: 2.53e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155     4 IVVAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMTLAVLRAGIDPADAAAIGESV----WKVQMLSDHDRYFLGGE 79
Cdd:COG0283   1 PVIAIDGPAGSGKSTVAKALAKRLGYHYLDTGAMYRAVALAALRNGIDLDDEEALAALArnldIEFETDPGGQRVFLNGE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155    80 DVSSEIRTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEGRGsVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVA 159
Cdd:COG0283  81 DVTDEIRTEEVSNAVSKVAAIPEVREALVALQRAFAKAPG-LVADGRDIGTVVFPDAELKIFLTASAEERARRRYKELKE 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 467155   160 SGSADDYDRVLAEVRRRDHLDSTRAVSPLYVAQDAMIVDTSKMAEAEVIAHLMDLVKQR 218
Cdd:COG0283 160 KGISVSLEELLADIKERDERDSTRAVAPLKPAEDAIVIDTTDLSIEEVVEKILALVRER 218
PRK13477 PRK13477
bifunctional pantoate--beta-alanine ligase/(d)CMP kinase;
5-223 1.27e-75

bifunctional pantoate--beta-alanine ligase/(d)CMP kinase;


Pssm-ID: 237393 [Multi-domain]  Cd Length: 512  Bit Score: 236.70  E-value: 1.27e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155      5 VVAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMTLAVLRAGIDPADAAAIGESVWKVQM-----LSDHDRYFLGGE 79
Cdd:PRK13477 286 IIAIDGPAGAGKSTVTRAVAKKLGLLYLDTGAMYRAVTWLVLQEGIDPQDEEALAELLSDLKIelkpsSGSPQRVWINGE 365

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155     80 DVSSEIRTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEgRGSVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVA 159
Cdd:PRK13477 366 DVTEAIRSPEVTSSVSAIAAQPAVRQALVKQQQRIGE-KGGLVAEGRDIGTHVFPDAELKIFLTASVEERARRRALDLQA 444

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 467155    160 SGSAD-DYDRVLAEVRRRDHLDSTRAVSPLYVAQDAMIVDTSKMAEAEVIAHLMDLVKQR-SGAVW 223
Cdd:PRK13477 445 QGFPViDLEQLEAQIAERDRLDSTREIAPLRKADDAIELITDGLSIEEVVDKIIDLYRDRiPEEVW 510
cmk TIGR00017
cytidylate kinase; This family consists of cytidylate kinase, which catalyzes the ...
 5-208 5.61e-70

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: 213.06  E-value: 5.61e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155       5 VVAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMTLAVLRAGIDPADAAAIGESV----WKVQMLSDHDRYFLGGED 80
Cdd:TIGR00017   4 IIAIDGPSGAGKSTVAKAVAEKLGYAYLDSGAMYRAIALAALQNRVDLTSEDALAELIshldIRFIPTNGEVEVFLNGED 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155      81 VSSEIRTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEgRGSVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVAS 160
Cdd:TIGR00017  84 VSEAIRTQEVANAASKVAVFPKVREALLKRQQALAK-NDGIIADGRDIGTVVFPNAEVKIFLDASVEERAKRRYKQLQIK 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 467155     161 GSADDYDRVLAEVRRRDHLDSTRAVSPLYVAQDAMIVDTSKMAEAEVI 208
Cdd:TIGR00017 163 GNEVNFEELLAEIKERDDRDSNREVAPLKKADDALYLDTSNLSIDEVV 210
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
 5-200 2.56e-64

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: 196.17  E-value: 2.56e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155     5 VVAIDGPAGTGKSSVSRGLARELGARYLDTGamyrmmtlavlragidpadaaaigesvwkvqmlsdhdryflggedvssE 84
Cdd:cd02020   1 IIAIDGPAGSGKSTVAKLLAKKLGLPYLDTG------------------------------------------------G 32

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155    85 IRTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEGRGsVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVASGSAD 164
Cdd:cd02020  33 IRTEEVGKLASEVAAIPEVRKALDERQRELAKKPG-IVLEGRDIGTVVFPDADLKIFLTASPEVRAKRRAKQLQAKGEGV 111

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 467155   165 DYDRVLAEVRRRDHLDSTRAVSPLYVAQDAMIVDTS 200
Cdd:cd02020 112 DLEEILAEIIERDERDSTRYVAPLKLAEDAIVIDTS 147
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 4-217 1.03e-61

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 204.64  E-value: 1.03e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155      4 IVVAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMTLAVLRAGIDPAD------------AAAIGESVWKVQMLSDH 71
Cdd:PRK09518   2 IIVAIDGPAGVGKSSVSRALAQYLGYAYLDTGAMYRACAWWCLKQGIDLDAelvdeqvvteavGEFFTGLHFDISVDPDS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155     72 DRYFLGGEDVSSEIRTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEGRGS---------VVVEGRDIGTVVLPDAPVKIFL 142
Cdd:PRK09518  82 PGVFADGEDISEEIRSPEVSSHVSAVAAIPPVRNVLIAAQRAYIAREASadsfsgglgIVAEGRDITTVVAPDAEVRILL 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 467155    143 TASPETRARRRNDQNvasgSADDYDRVLAEVRRRDHLDStRAVSPLYVAQDAMIVDTSKMAEAEVIAHLMDLVKQ 217
Cdd:PRK09518 162 TAREEVRQARRSGQD----RSETPGVVLEDVAARDEADS-KVTSFLSAADGVTTLDNSDLDFDETLDLLIGLVED 231
PRK11860 PRK11860
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
5-218 7.35e-60

bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;


Pssm-ID: 237003 [Multi-domain]  Cd Length: 661  Bit Score: 198.73  E-value: 7.35e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155      5 VVAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMTLAVLRAGIDPADAAAIGESVWKVQMLSDHDRYFLGGEDVSSE 84
Cdd:PRK11860 444 VICIDGPTASGKGTVAARVAEALGYHYLDSGALYRLTALAALRAGVALDDEAAIAALARGLPVRFEGDRIWLGGEDVTDA 523

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155     85 IRTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEGRGsVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVASGSAD 164
Cdd:PRK11860 524 IRTEAAGMGASRVSALPAVRAALLALQRSFRRLPG-LVADGRDMGTVIFPDAALKVFLTASAEARAERRYKQLISKGISA 602

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 467155    165 DYDRVLAEVRRRDHLDSTRAVSPLYVAQDAMIVDTSKMAEAEVIAHLMDLVKQR 218
Cdd:PRK11860 603 NIADLLADLEARDARDTQRSVAPLKPAQDALLLDNSDLTIEQAVAQVLDWWQER 656
PRK12269 PRK12269
bifunctional cytidylate kinase/ribosomal protein S1; Provisional
 1-223 3.29e-31

bifunctional cytidylate kinase/ribosomal protein S1; Provisional


Pssm-ID: 105491 [Multi-domain]  Cd Length: 863  Bit Score: 120.20  E-value: 3.29e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155      1 MTDIVVAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMTLAVLR---------AGIDPADAAAIG------------ 59
Cdd:PRK12269  32 MGTVIIALDGPAGSGKSSVCRLLASRLGAQCLNTGSFYRAFTLAALRrvselavqaCSPSPDPDAAVGcaavphatnldt 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155     60 ---------------ESVW-----KVQMLSDHDRYFLGGEDVSSEIRTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEGrG 119
Cdd:PRK12269 112 syapltaqkkvalfdEAYWvsfarTVALSYRAGVMYVGEENVESLLRSDEVESAVSYFAAMPAIRAIMTGKIRSAVCG-A 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155    120 SVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVASGSADDYDRvlaEVRRRDHLDSTRAVSPLYVAQDAMIVDT 199
Cdd:PRK12269 191 RVVCEGRDLTTVVFVDADLKCYLDASIEARVARRWAQGTSRLSKQELEQ---RMRARDAHDRARTVGGLRCAPDALYVDT 267

                        250       260
                 ....*....|....*....|....
gi 467155    200 SKMAEAEVIAHLMDLVKQRsgAVW 223
Cdd:PRK12269 268 SCLTIEEVCERIAREAHRR--ALW 289
cyt_kin_arch TIGR02173
cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. ...
 4-207 1.06e-14

cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. Members of this family are found in the archaea and in spirochaetes, and differ considerably from the common bacterial form of cytidylate kinase described by TIGR00017.


Pssm-ID: 274012 [Multi-domain]  Cd Length: 171  Bit Score: 68.99  E-value: 1.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155       4 IVVAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMtlavlragidpadAAAIGESVWKvqmlsdhdryFLGGEDVSS 83
Cdd:TIGR02173   1 MIITISGPPGSGKTTVAKILAEKLSLKLISAGDIFREL-------------AAKMGLDLIE----------FLNYAEENP 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155      84 EIRteevtqavsavsaipavrvRLVD-LQRQMAEGRGSVVVEGRDIGTVVLPDAPVKIFLTASPETRARRrndqnVASGS 162
Cdd:TIGR02173  58 EID-------------------KKIDrRIHEIALKEKNVVLESRLAGWIVREYADVKIWLKAPLEVRARR-----IAKRE 113

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 467155     163 ADDYDRVLAEVRRRDHLDSTRAVSplYVAQDA-------MIVDTSKMAEAEV 207
Cdd:TIGR02173 114 GKSLTVARSETIEREESEKRRYLK--FYGIDIddlsiydLVINTSNWDPNNV 163
PRK04182 PRK04182
cytidylate kinase; Provisional
 5-183 3.41e-13

cytidylate kinase; Provisional


Pssm-ID: 235244 [Multi-domain]  Cd Length: 180  Bit Score: 65.21  E-value: 3.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155      5 VVAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMtlAVLRaGIDPADAAAIGESvwkvqmlsDH--DRYflggedvs 82
Cdd:PRK04182   2 IITISGPPGSGKTTVARLLAEKLGLKHVSAGEIFREL--AKER-GMSLEEFNKYAEE--------DPeiDKE-------- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155     83 seirteevtqavsavsaipavrvrlVD-LQRQMAEGRGSVVVEGRDIGTVVLPDAPVKIFLTASPETRARRrndqnVASG 161
Cdd:PRK04182  63 -------------------------IDrRQLEIAEKEDNVVLEGRLAGWMAKDYADLKIWLKAPLEVRAER-----IAER 112

                        170       180
                 ....*....|....*....|..
gi 467155    162 SADDYDRVLAEVRRRDHLDSTR 183
Cdd:PRK04182 113 EGISVEEALEETIEREESEAKR 134
Cytidylate_kin2 pfam13189
Cytidylate kinase-like family; This family includes enzymes related to cytidylate kinase.
 5-152 1.55e-07

Cytidylate kinase-like family; This family includes enzymes related to cytidylate kinase.


Pssm-ID: 433023 [Multi-domain]  Cd Length: 176  Bit Score: 49.55  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155       5 VVAIDGPAGTGKSSVSRGLARELGARYLDTgamyRMMTLAVLRAGIDPADAAAIGESVWKVQMLSDHDRYFLGGEDVSSE 84
Cdd:pfam13189   1 VITISRQYGSGGTTIAKKLAEKLGYPFYDR----EILDEIAKELGISEEEFELFDEKSRLSSFLYSLAGGRVRGDALSDD 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155      85 irteevtqavsavsaipAVRVRLVDLQRQMAEGRGSVVVeGRDiGTVVLPDAP--VKIFLTASPETRARR 152
Cdd:pfam13189  77 -----------------RLFDAQSKVIRELAAEDNCVIV-GRG-ADYILKDIPnvLRVFLTAPLEDRVKR 127
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
 10-217 3.72e-04

Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440467 [Multi-domain]  Cd Length: 165  Bit Score: 39.73  E-value: 3.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155    10 GPAGTGKSSVSRGLARELGARYLDTGAmyrmmtLAVLRAGIDPADAAAI-GESvwkvqmlsdhdrYFlggedvsseiRTE 88
Cdd:COG0703   5 GMMGAGKSTVGRLLAKRLGLPFVDTDA------EIEERAGMSIPEIFAEeGEA------------GF----------REL 56

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155    89 EvTQAVSAVSAIPavrvRLVdlqrqMAEGRGSVVVEG-----RDIGTVVlpdapvkiFLTASPETRARR-RNDQN---VA 159
Cdd:COG0703  57 E-REVLAELLEEE----NAV-----IATGGGAVLSPEnrellKEHGTVV--------YLDASPETLLERlRRDDNrplLQ 118

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 467155   160 SGSADDYDRVLAEVRRrdhldstravsPLYvAQDA-MIVDTSKMAEAEVIAHLMDLVKQ 217
Cdd:COG0703 119 GEDPRERLEELLAERE-----------PLY-REVAdITVDTDGRSPEEVVDEILEALEE 165
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 4-30 5.10e-04

Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440337 [Multi-domain]  Cd Length: 206  Bit Score: 39.82  E-value: 5.10e-04
                        10        20
                ....*....|....*....|....*..
gi 467155     4 IVVAIDGPAGTGKSSVSRGLARELGAR 30
Cdd:COG0572   8 RIIGIAGPSGSGKTTFARRLAEQLGAD 34
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 4-55 1.12e-03

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 38.00  E-value: 1.12e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 467155     4 IVVAidGPAGTGKSSVSRGLARELGARYLDTGAMYRMMTLAVLRAGIDPADA 55
Cdd:cd02021   2 IVVM--GVSGSGKSTVGKALAERLGAPFIDGDDLHPPANIAKMAAGIPLNDE 51
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
5-172 1.42e-03

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 37.97  E-value: 1.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155     5 VVAIDGPAGTGKSSVSRGLARELGARYLDtgamyrmmtlavlragidpadaaaigesvwkvqmlSDHDRYFLGGEDVSSE 84
Cdd:COG0645   1 LILVCGLPGSGKSTLARALAERLGAVRLR-----------------------------------SDVVRKRLFGAGLAPL 45

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 467155    85 IRTEEVTQavsavsaipAVRVRLVDLQRQMAEGRGSVVVEG-----------RDIGTVVlpDAPVK-IFLTASPETRARR 152
Cdd:COG0645  46 ERSPEATA---------RTYARLLALARELLAAGRSVILDAtflrraqreafRALAEEA--GAPFVlIWLDAPEEVLRER 114

                       170       180
                ....*....|....*....|....
gi 467155   153 ---RNDQNVAS-GSADDYDRVLAE 172
Cdd:COG0645 115 leaRNAEGGDSdATWEVLERQLAF 138
aroK PRK00131
shikimate kinase; Reviewed
 10-34 8.21e-03

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 35.94  E-value: 8.21e-03
                         10        20
                 ....*....|....*....|....*
gi 467155     10 GPAGTGKSSVSRGLARELGARYLDT 34
Cdd:PRK00131  11 GFMGAGKSTIGRLLAKRLGYDFIDT 35
 
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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