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Conserved domains on  [gi|1033202815|gb|OAR21286|]
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cytidylate kinase [Mycobacterium leprae 3125609]

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 1033202815   6 VAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMTLAVLRAGIDPADAAAIGESVWKVQMLSDHDRYFLGGEDVSSEI 85
Cdd:pfam02224   1 IAIDGPSGSGKSTVARILARKLGYKYLDTGAMYRALALAALRQKVDLTDEDALAELASEVDISFGHTEVFLNGEDVSSEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033202815  86 RTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEgRGSVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVASGSADD 165
Cdd:pfam02224  81 RTDEVAQAASQVAAIPAVRARLNKLQRQLAK-NGNIVMEGRDIGTVVFPDAEVKIFLTASPEERAKRRYKQLQAKGLSVD 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1033202815 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 1033202815   6 VAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMTLAVLRAGIDPADAAAIGESVWKVQMLSDHDRYFLGGEDVSSEI 85
Cdd:pfam02224   1 IAIDGPSGSGKSTVARILARKLGYKYLDTGAMYRALALAALRQKVDLTDEDALAELASEVDISFGHTEVFLNGEDVSSEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033202815  86 RTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEgRGSVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVASGSADD 165
Cdd:pfam02224  81 RTDEVAQAASQVAAIPAVRARLNKLQRQLAK-NGNIVMEGRDIGTVVFPDAEVKIFLTASPEERAKRRYKQLQAKGLSVD 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1033202815 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 1033202815   4 IVVAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMTLAVLRAGIDPADAAAIGESV----WKVQMLSDHDRYFLGGE 79
Cdd:COG0283     1 PVIAIDGPAGSGKSTVAKALAKRLGYHYLDTGAMYRAVALAALRNGIDLDDEEALAALArnldIEFETDPGGQRVFLNGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033202815  80 DVSSEIRTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEGRGsVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVA 159
Cdd:COG0283    81 DVTDEIRTEEVSNAVSKVAAIPEVREALVALQRAFAKAPG-LVADGRDIGTVVFPDAELKIFLTASAEERARRRYKELKE 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1033202815 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 1033202815   5 VVAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMTLAVLRAGIDPADAAAIGESVWKVQM-----LSDHDRYFLGGE 79
Cdd:PRK13477  286 IIAIDGPAGAGKSTVTRAVAKKLGLLYLDTGAMYRAVTWLVLQEGIDPQDEEALAELLSDLKIelkpsSGSPQRVWINGE 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033202815  80 DVSSEIRTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEgRGSVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVA 159
Cdd:PRK13477  366 DVTEAIRSPEVTSSVSAIAAQPAVRQALVKQQQRIGE-KGGLVAEGRDIGTHVFPDAELKIFLTASVEERARRRALDLQA 444

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1033202815 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 1033202815   5 VVAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMTLAVLRAGIDPADAAAIGESV----WKVQMLSDHDRYFLGGED 80
Cdd:TIGR00017   4 IIAIDGPSGAGKSTVAKAVAEKLGYAYLDSGAMYRAIALAALQNRVDLTSEDALAELIshldIRFIPTNGEVEVFLNGED 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033202815  81 VSSEIRTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEgRGSVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVAS 160
Cdd:TIGR00017  84 VSEAIRTQEVANAASKVAVFPKVREALLKRQQALAK-NDGIIADGRDIGTVVFPNAEVKIFLDASVEERAKRRYKQLQIK 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1033202815 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 1033202815   5 VVAIDGPAGTGKSSVSRGLARELGARYLDTGamyrmmtlavlragidpadaaaigesvwkvqmlsdhdryflggedvssE 84
Cdd:cd02020     1 IIAIDGPAGSGKSTVAKLLAKKLGLPYLDTG------------------------------------------------G 32

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033202815  85 IRTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEGRGsVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVASGSAD 164
Cdd:cd02020    33 IRTEEVGKLASEVAAIPEVRKALDERQRELAKKPG-IVLEGRDIGTVVFPDADLKIFLTASPEVRAKRRAKQLQAKGEGV 111

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1033202815 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 1033202815   6 VAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMTLAVLRAGIDPADAAAIGESVWKVQMLSDHDRYFLGGEDVSSEI 85
Cdd:pfam02224   1 IAIDGPSGSGKSTVARILARKLGYKYLDTGAMYRALALAALRQKVDLTDEDALAELASEVDISFGHTEVFLNGEDVSSEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033202815  86 RTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEgRGSVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVASGSADD 165
Cdd:pfam02224  81 RTDEVAQAASQVAAIPAVRARLNKLQRQLAK-NGNIVMEGRDIGTVVFPDAEVKIFLTASPEERAKRRYKQLQAKGLSVD 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1033202815 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 1033202815   4 IVVAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMTLAVLRAGIDPADAAAIGESV----WKVQMLSDHDRYFLGGE 79
Cdd:COG0283     1 PVIAIDGPAGSGKSTVAKALAKRLGYHYLDTGAMYRAVALAALRNGIDLDDEEALAALArnldIEFETDPGGQRVFLNGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033202815  80 DVSSEIRTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEGRGsVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVA 159
Cdd:COG0283    81 DVTDEIRTEEVSNAVSKVAAIPEVREALVALQRAFAKAPG-LVADGRDIGTVVFPDAELKIFLTASAEERARRRYKELKE 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1033202815 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 1033202815   5 VVAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMTLAVLRAGIDPADAAAIGESVWKVQM-----LSDHDRYFLGGE 79
Cdd:PRK13477  286 IIAIDGPAGAGKSTVTRAVAKKLGLLYLDTGAMYRAVTWLVLQEGIDPQDEEALAELLSDLKIelkpsSGSPQRVWINGE 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033202815  80 DVSSEIRTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEgRGSVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVA 159
Cdd:PRK13477  366 DVTEAIRSPEVTSSVSAIAAQPAVRQALVKQQQRIGE-KGGLVAEGRDIGTHVFPDAELKIFLTASVEERARRRALDLQA 444

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1033202815 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 1033202815   5 VVAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMTLAVLRAGIDPADAAAIGESV----WKVQMLSDHDRYFLGGED 80
Cdd:TIGR00017   4 IIAIDGPSGAGKSTVAKAVAEKLGYAYLDSGAMYRAIALAALQNRVDLTSEDALAELIshldIRFIPTNGEVEVFLNGED 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033202815  81 VSSEIRTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEgRGSVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVAS 160
Cdd:TIGR00017  84 VSEAIRTQEVANAASKVAVFPKVREALLKRQQALAK-NDGIIADGRDIGTVVFPNAEVKIFLDASVEERAKRRYKQLQIK 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1033202815 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 1033202815   5 VVAIDGPAGTGKSSVSRGLARELGARYLDTGamyrmmtlavlragidpadaaaigesvwkvqmlsdhdryflggedvssE 84
Cdd:cd02020     1 IIAIDGPAGSGKSTVAKLLAKKLGLPYLDTG------------------------------------------------G 32

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033202815  85 IRTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEGRGsVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVASGSAD 164
Cdd:cd02020    33 IRTEEVGKLASEVAAIPEVRKALDERQRELAKKPG-IVLEGRDIGTVVFPDADLKIFLTASPEVRAKRRAKQLQAKGEGV 111

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1033202815 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 1033202815   4 IVVAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMTLAVLRAGIDPAD------------AAAIGESVWKVQMLSDH 71
Cdd:PRK09518    2 IIVAIDGPAGVGKSSVSRALAQYLGYAYLDTGAMYRACAWWCLKQGIDLDAelvdeqvvteavGEFFTGLHFDISVDPDS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033202815  72 DRYFLGGEDVSSEIRTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEGRGS---------VVVEGRDIGTVVLPDAPVKIFL 142
Cdd:PRK09518   82 PGVFADGEDISEEIRSPEVSSHVSAVAAIPPVRNVLIAAQRAYIAREASadsfsgglgIVAEGRDITTVVAPDAEVRILL 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033202815 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 1033202815   5 VVAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMTLAVLRAGIDPADAAAIGESVWKVQMLSDHDRYFLGGEDVSSE 84
Cdd:PRK11860  444 VICIDGPTASGKGTVAARVAEALGYHYLDSGALYRLTALAALRAGVALDDEAAIAALARGLPVRFEGDRIWLGGEDVTDA 523

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033202815  85 IRTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEGRGsVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVASGSAD 164
Cdd:PRK11860  524 IRTEAAGMGASRVSALPAVRAALLALQRSFRRLPG-LVADGRDMGTVIFPDAALKVFLTASAEARAERRYKQLISKGISA 602

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1033202815 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 1033202815   1 MTDIVVAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMTLAVLR---------AGIDPADAAAIG------------ 59
Cdd:PRK12269   32 MGTVIIALDGPAGSGKSSVCRLLASRLGAQCLNTGSFYRAFTLAALRrvselavqaCSPSPDPDAAVGcaavphatnldt 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033202815  60 ---------------ESVW-----KVQMLSDHDRYFLGGEDVSSEIRTEEVTQAVSAVSAIPAVRVRLVDLQRQMAEGrG 119
Cdd:PRK12269  112 syapltaqkkvalfdEAYWvsfarTVALSYRAGVMYVGEENVESLLRSDEVESAVSYFAAMPAIRAIMTGKIRSAVCG-A 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033202815 120 SVVVEGRDIGTVVLPDAPVKIFLTASPETRARRRNDQNVASGSADDYDRvlaEVRRRDHLDSTRAVSPLYVAQDAMIVDT 199
Cdd:PRK12269  191 RVVCEGRDLTTVVFVDADLKCYLDASIEARVARRWAQGTSRLSKQELEQ---RMRARDAHDRARTVGGLRCAPDALYVDT 267

                         250       260
                  ....*....|....*....|....
gi 1033202815 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 1033202815   4 IVVAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMtlavlragidpadAAAIGESVWKvqmlsdhdryFLGGEDVSS 83
Cdd:TIGR02173   1 MIITISGPPGSGKTTVAKILAEKLSLKLISAGDIFREL-------------AAKMGLDLIE----------FLNYAEENP 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033202815  84 EIRteevtqavsavsaipavrvRLVD-LQRQMAEGRGSVVVEGRDIGTVVLPDAPVKIFLTASPETRARRrndqnVASGS 162
Cdd:TIGR02173  58 EID-------------------KKIDrRIHEIALKEKNVVLESRLAGWIVREYADVKIWLKAPLEVRARR-----IAKRE 113

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1033202815 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 1033202815   5 VVAIDGPAGTGKSSVSRGLARELGARYLDTGAMYRMMtlAVLRaGIDPADAAAIGESvwkvqmlsDH--DRYflggedvs 82
Cdd:PRK04182    2 IITISGPPGSGKTTVARLLAEKLGLKHVSAGEIFREL--AKER-GMSLEEFNKYAEE--------DPeiDKE-------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033202815  83 seirteevtqavsavsaipavrvrlVD-LQRQMAEGRGSVVVEGRDIGTVVLPDAPVKIFLTASPETRARRrndqnVASG 161
Cdd:PRK04182   63 -------------------------IDrRQLEIAEKEDNVVLEGRLAGWMAKDYADLKIWLKAPLEVRAER-----IAER 112

                         170       180
                  ....*....|....*....|..
gi 1033202815 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 1033202815   5 VVAIDGPAGTGKSSVSRGLARELGARYLDTgamyRMMTLAVLRAGIDPADAAAIGESVWKVQMLSDHDRYFLGGEDVSSE 84
Cdd:pfam13189   1 VITISRQYGSGGTTIAKKLAEKLGYPFYDR----EILDEIAKELGISEEEFELFDEKSRLSSFLYSLAGGRVRGDALSDD 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033202815  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 1033202815  10 GPAGTGKSSVSRGLARELGARYLDTGAmyrmmtLAVLRAGIDPADAAAI-GESvwkvqmlsdhdrYFlggedvsseiRTE 88
Cdd:COG0703     5 GMMGAGKSTVGRLLAKRLGLPFVDTDA------EIEERAGMSIPEIFAEeGEA------------GF----------REL 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033202815  89 EvTQAVSAVSAIPavrvRLVdlqrqMAEGRGSVVVEG-----RDIGTVVlpdapvkiFLTASPETRARR-RNDQN---VA 159
Cdd:COG0703    57 E-REVLAELLEEE----NAV-----IATGGGAVLSPEnrellKEHGTVV--------YLDASPETLLERlRRDDNrplLQ 118

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1033202815 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 1033202815   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 1033202815   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 1033202815   5 VVAIDGPAGTGKSSVSRGLARELGARYLDtgamyrmmtlavlragidpadaaaigesvwkvqmlSDHDRYFLGGEDVSSE 84
Cdd:COG0645     1 LILVCGLPGSGKSTLARALAERLGAVRLR-----------------------------------SDVVRKRLFGAGLAPL 45

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033202815  85 IRTEEVTQavsavsaipAVRVRLVDLQRQMAEGRGSVVVEG-----------RDIGTVVlpDAPVK-IFLTASPETRARR 152
Cdd:COG0645    46 ERSPEATA---------RTYARLLALARELLAAGRSVILDAtflrraqreafRALAEEA--GAPFVlIWLDAPEEVLRER 114

                         170       180
                  ....*....|....*....|....
gi 1033202815 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 1033202815  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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