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Conserved domains on  [gi|1539065713|ref|WP_125892627|]
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MULTISPECIES: (d)CMP kinase [Providencia]

Protein Classification

(d)CMP kinase( domain architecture ID 10785233)

(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

CATH:  3.40.50.300
Gene Ontology:  GO:0036431|GO:0006220|GO:0005524
PubMed:  10218107

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cmk COG0283
Cytidylate kinase [Nucleotide transport and metabolism];
6-224 3.30e-127

Cytidylate kinase [Nucleotide transport and metabolism];


:

Pssm-ID: 440052 [Multi-domain]  Cd Length: 220  Bit Score: 358.18  E-value: 3.30e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713   6 PVITVDGPSGAGKGTLCQALANEFGWQLLDSGAIYRVLALAALHHHVDIQSEDALVPLAANLDVKFVPENNVLKVILEGE 85
Cdd:COG0283     1 PVIAIDGPAGSGKSTVAKALAKRLGYHYLDTGAMYRAVALAALRNGIDLDDEEALAALARNLDIEFETDPGGQRVFLNGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713  86 DVSNQIRTETVGNTASQTATFPRVREALLRRQRAFRTLPGLIADGRDMGTVVFPDAPVKIFLDASAEERAHRRMKQLQEK 165
Cdd:COG0283    81 DVTDEIRTEEVSNAVSKVAAIPEVREALVALQRAFAKAPGLVADGRDIGTVVFPDAELKIFLTASAEERARRRYKELKEK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1539065713 166 GFDVNFERLLSEIEERDFRDRNRSVAPLIAAKDALVLDSTSMSIEEVIEKAHTYAKKIL 224
Cdd:COG0283   161 GISVSLEELLADIKERDERDSTRAVAPLKPAEDAIVIDTTDLSIEEVVEKILALVRERL 219
 
Name Accession Description Interval E-value
Cmk COG0283
Cytidylate kinase [Nucleotide transport and metabolism];
6-224 3.30e-127

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440052 [Multi-domain]  Cd Length: 220  Bit Score: 358.18  E-value: 3.30e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713   6 PVITVDGPSGAGKGTLCQALANEFGWQLLDSGAIYRVLALAALHHHVDIQSEDALVPLAANLDVKFVPENNVLKVILEGE 85
Cdd:COG0283     1 PVIAIDGPAGSGKSTVAKALAKRLGYHYLDTGAMYRAVALAALRNGIDLDDEEALAALARNLDIEFETDPGGQRVFLNGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713  86 DVSNQIRTETVGNTASQTATFPRVREALLRRQRAFRTLPGLIADGRDMGTVVFPDAPVKIFLDASAEERAHRRMKQLQEK 165
Cdd:COG0283    81 DVTDEIRTEEVSNAVSKVAAIPEVREALVALQRAFAKAPGLVADGRDIGTVVFPDAELKIFLTASAEERARRRYKELKEK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1539065713 166 GFDVNFERLLSEIEERDFRDRNRSVAPLIAAKDALVLDSTSMSIEEVIEKAHTYAKKIL 224
Cdd:COG0283   161 GISVSLEELLADIKERDERDSTRAVAPLKPAEDAIVIDTTDLSIEEVVEKILALVRERL 219
cmk TIGR00017
cytidylate kinase; This family consists of cytidylate kinase, which catalyzes the ...
 4-220 1.39e-108

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: 310.90  E-value: 1.39e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713   4 IAPVITVDGPSGAGKGTLCQALANEFGWQLLDSGAIYRVLALAALHHHVDIQSEDALVPLAANLDVKFVPENNVLKVILE 83
Cdd:TIGR00017   1 MAMIIAIDGPSGAGKSTVAKAVAEKLGYAYLDSGAMYRAIALAALQNRVDLTSEDALAELISHLDIRFIPTNGEVEVFLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713  84 GEDVSNQIRTETVGNTASQTATFPRVREALLRRQRAFRTLPGLIADGRDMGTVVFPDAPVKIFLDASAEERAHRRMKQLQ 163
Cdd:TIGR00017  81 GEDVSEAIRTQEVANAASKVAVFPKVREALLKRQQALAKNDGIIADGRDIGTVVFPNAEVKIFLDASVEERAKRRYKQLQ 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1539065713 164 EKGFDVNFERLLSEIEERDFRDRNRSVAPLIAAKDALVLDSTSMSIEEVIEKAHTYA 220
Cdd:TIGR00017 161 IKGNEVNFEELLAEIKERDDRDSNREVAPLKKADDALYLDTSNLSIDEVVEKILEYA 217
Cytidylate_kin pfam02224
Cytidylate kinase; Cytidylate kinase EC:2.7.4.14 catalyzes the phosphorylation of cytidine 5 ...
 8-222 8.10e-105

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: 301.15  E-value: 8.10e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713   8 ITVDGPSGAGKGTLCQALANEFGWQLLDSGAIYRVLALAALHHHVDIQSEDALVPLAANLDVKFVPEnnvlKVILEGEDV 87
Cdd:pfam02224   1 IAIDGPSGSGKSTVARILARKLGYKYLDTGAMYRALALAALRQKVDLTDEDALAELASEVDISFGHT----EVFLNGEDV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713  88 SNQIRTETVGNTASQTATFPRVREALLRRQRAFRTLPGLIADGRDMGTVVFPDAPVKIFLDASAEERAHRRMKQLQEKGF 167
Cdd:pfam02224  77 SSEIRTDEVAQAASQVAAIPAVRARLNKLQRQLAKNGNIVMEGRDIGTVVFPDAEVKIFLTASPEERAKRRYKQLQAKGL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1539065713 168 DVNFERLLSEIEERDFRDRNRSVAPLIAAKDALVLDSTSMSIEEVIEKAHTYAKK 222
Cdd:pfam02224 157 SVDFEELLAEIKRRDKRDSERAVGPLKPAPDALIIDTSKLTIEEVVEKILELIKQ 211
PRK11860 PRK11860
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
6-215 7.33e-90

bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;


Pssm-ID: 237003 [Multi-domain]  Cd Length: 661  Bit Score: 277.70  E-value: 7.33e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713   6 PVITVDGPSGAGKGTLCQALANEFGWQLLDSGAIYRVLALAALHHHVDIQSEDALVPLAANLDVKFVPEnnvlKVILEGE 85
Cdd:PRK11860  443 PVICIDGPTASGKGTVAARVAEALGYHYLDSGALYRLTALAALRAGVALDDEAAIAALARGLPVRFEGD----RIWLGGE 518

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713  86 DVSNQIRTETVGNTASQTATFPRVREALLRRQRAFRTLPGLIADGRDMGTVVFPDAPVKIFLDASAEERAHRRMKQLQEK 165
Cdd:PRK11860  519 DVTDAIRTEAAGMGASRVSALPAVRAALLALQRSFRRLPGLVADGRDMGTVIFPDAALKVFLTASAEARAERRYKQLISK 598

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1539065713 166 GFDVNFERLLSEIEERDFRDRNRSVAPLIAAKDALVLDSTSMSIEEVIEK 215
Cdd:PRK11860  599 GISANIADLLADLEARDARDTQRSVAPLKPAQDALLLDNSDLTIEQAVAQ 648
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
 7-205 9.73e-68

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: 205.03  E-value: 9.73e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713   7 VITVDGPSGAGKGTLCQALANEFGWQLLDSGaiyrvlalaalhhhvdiqsedalvplaanldvkfvpennvlkvileged 86
Cdd:cd02020     1 IIAIDGPAGSGKSTVAKLLAKKLGLPYLDTG------------------------------------------------- 31

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713  87 vsnQIRTETVGNTASQTATFPRVREALLRRQRAFRTLPGLIADGRDMGTVVFPDAPVKIFLDASAEERAHRRMKQLQEKG 166
Cdd:cd02020    32 ---GIRTEEVGKLASEVAAIPEVRKALDERQRELAKKPGIVLEGRDIGTVVFPDADLKIFLTASPEVRAKRRAKQLQAKG 108

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1539065713 167 FDVNFERLLSEIEERDFRDRNRSVAPLIAAKDALVLDST 205
Cdd:cd02020   109 EGVDLEEILAEIIERDERDSTRYVAPLKLAEDAIVIDTS 147
 
Name Accession Description Interval E-value
Cmk COG0283
Cytidylate kinase [Nucleotide transport and metabolism];
6-224 3.30e-127

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440052 [Multi-domain]  Cd Length: 220  Bit Score: 358.18  E-value: 3.30e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713   6 PVITVDGPSGAGKGTLCQALANEFGWQLLDSGAIYRVLALAALHHHVDIQSEDALVPLAANLDVKFVPENNVLKVILEGE 85
Cdd:COG0283     1 PVIAIDGPAGSGKSTVAKALAKRLGYHYLDTGAMYRAVALAALRNGIDLDDEEALAALARNLDIEFETDPGGQRVFLNGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713  86 DVSNQIRTETVGNTASQTATFPRVREALLRRQRAFRTLPGLIADGRDMGTVVFPDAPVKIFLDASAEERAHRRMKQLQEK 165
Cdd:COG0283    81 DVTDEIRTEEVSNAVSKVAAIPEVREALVALQRAFAKAPGLVADGRDIGTVVFPDAELKIFLTASAEERARRRYKELKEK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1539065713 166 GFDVNFERLLSEIEERDFRDRNRSVAPLIAAKDALVLDSTSMSIEEVIEKAHTYAKKIL 224
Cdd:COG0283   161 GISVSLEELLADIKERDERDSTRAVAPLKPAEDAIVIDTTDLSIEEVVEKILALVRERL 219
cmk TIGR00017
cytidylate kinase; This family consists of cytidylate kinase, which catalyzes the ...
 4-220 1.39e-108

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: 310.90  E-value: 1.39e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713   4 IAPVITVDGPSGAGKGTLCQALANEFGWQLLDSGAIYRVLALAALHHHVDIQSEDALVPLAANLDVKFVPENNVLKVILE 83
Cdd:TIGR00017   1 MAMIIAIDGPSGAGKSTVAKAVAEKLGYAYLDSGAMYRAIALAALQNRVDLTSEDALAELISHLDIRFIPTNGEVEVFLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713  84 GEDVSNQIRTETVGNTASQTATFPRVREALLRRQRAFRTLPGLIADGRDMGTVVFPDAPVKIFLDASAEERAHRRMKQLQ 163
Cdd:TIGR00017  81 GEDVSEAIRTQEVANAASKVAVFPKVREALLKRQQALAKNDGIIADGRDIGTVVFPNAEVKIFLDASVEERAKRRYKQLQ 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1539065713 164 EKGFDVNFERLLSEIEERDFRDRNRSVAPLIAAKDALVLDSTSMSIEEVIEKAHTYA 220
Cdd:TIGR00017 161 IKGNEVNFEELLAEIKERDDRDSNREVAPLKKADDALYLDTSNLSIDEVVEKILEYA 217
Cytidylate_kin pfam02224
Cytidylate kinase; Cytidylate kinase EC:2.7.4.14 catalyzes the phosphorylation of cytidine 5 ...
 8-222 8.10e-105

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: 301.15  E-value: 8.10e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713   8 ITVDGPSGAGKGTLCQALANEFGWQLLDSGAIYRVLALAALHHHVDIQSEDALVPLAANLDVKFVPEnnvlKVILEGEDV 87
Cdd:pfam02224   1 IAIDGPSGSGKSTVARILARKLGYKYLDTGAMYRALALAALRQKVDLTDEDALAELASEVDISFGHT----EVFLNGEDV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713  88 SNQIRTETVGNTASQTATFPRVREALLRRQRAFRTLPGLIADGRDMGTVVFPDAPVKIFLDASAEERAHRRMKQLQEKGF 167
Cdd:pfam02224  77 SSEIRTDEVAQAASQVAAIPAVRARLNKLQRQLAKNGNIVMEGRDIGTVVFPDAEVKIFLTASPEERAKRRYKQLQAKGL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1539065713 168 DVNFERLLSEIEERDFRDRNRSVAPLIAAKDALVLDSTSMSIEEVIEKAHTYAKK 222
Cdd:pfam02224 157 SVDFEELLAEIKRRDKRDSERAVGPLKPAPDALIIDTSKLTIEEVVEKILELIKQ 211
PRK11860 PRK11860
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
6-215 7.33e-90

bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;


Pssm-ID: 237003 [Multi-domain]  Cd Length: 661  Bit Score: 277.70  E-value: 7.33e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713   6 PVITVDGPSGAGKGTLCQALANEFGWQLLDSGAIYRVLALAALHHHVDIQSEDALVPLAANLDVKFVPEnnvlKVILEGE 85
Cdd:PRK11860  443 PVICIDGPTASGKGTVAARVAEALGYHYLDSGALYRLTALAALRAGVALDDEAAIAALARGLPVRFEGD----RIWLGGE 518

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713  86 DVSNQIRTETVGNTASQTATFPRVREALLRRQRAFRTLPGLIADGRDMGTVVFPDAPVKIFLDASAEERAHRRMKQLQEK 165
Cdd:PRK11860  519 DVTDAIRTEAAGMGASRVSALPAVRAALLALQRSFRRLPGLVADGRDMGTVIFPDAALKVFLTASAEARAERRYKQLISK 598

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1539065713 166 GFDVNFERLLSEIEERDFRDRNRSVAPLIAAKDALVLDSTSMSIEEVIEK 215
Cdd:PRK11860  599 GISANIADLLADLEARDARDTQRSVAPLKPAQDALLLDNSDLTIEQAVAQ 648
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
 7-205 9.73e-68

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: 205.03  E-value: 9.73e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713   7 VITVDGPSGAGKGTLCQALANEFGWQLLDSGaiyrvlalaalhhhvdiqsedalvplaanldvkfvpennvlkvileged 86
Cdd:cd02020     1 IIAIDGPAGSGKSTVAKLLAKKLGLPYLDTG------------------------------------------------- 31

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713  87 vsnQIRTETVGNTASQTATFPRVREALLRRQRAFRTLPGLIADGRDMGTVVFPDAPVKIFLDASAEERAHRRMKQLQEKG 166
Cdd:cd02020    32 ---GIRTEEVGKLASEVAAIPEVRKALDERQRELAKKPGIVLEGRDIGTVVFPDADLKIFLTASPEVRAKRRAKQLQAKG 108

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1539065713 167 FDVNFERLLSEIEERDFRDRNRSVAPLIAAKDALVLDST 205
Cdd:cd02020   109 EGVDLEEILAEIIERDERDSTRYVAPLKLAEDAIVIDTS 147
PRK13477 PRK13477
bifunctional pantoate--beta-alanine ligase/(d)CMP kinase;
6-215 7.91e-66

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


Pssm-ID: 237393 [Multi-domain]  Cd Length: 512  Bit Score: 211.66  E-value: 7.91e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713   6 PVITVDGPSGAGKGTLCQALANEFGWQLLDSGAIYRVLALAALHHHVDIQSEDALVPLAANLDVKFVP-ENNVLKVILEG 84
Cdd:PRK13477  285 PIIAIDGPAGAGKSTVTRAVAKKLGLLYLDTGAMYRAVTWLVLQEGIDPQDEEALAELLSDLKIELKPsSGSPQRVWING 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713  85 EDVSNQIRTETVGNTASQTATFPRVREALLRRQRAFRTLPGLIADGRDMGTVVFPDAPVKIFLDASAEERAHRRMKQLQE 164
Cdd:PRK13477  365 EDVTEAIRSPEVTSSVSAIAAQPAVRQALVKQQQRIGEKGGLVAEGRDIGTHVFPDAELKIFLTASVEERARRRALDLQA 444

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1539065713 165 KGFDV-NFERLLSEIEERDFRDRNRSVAPLIAAKDALVLDSTSMSIEEVIEK 215
Cdd:PRK13477  445 QGFPViDLEQLEAQIAERDRLDSTREIAPLRKADDAIELITDGLSIEEVVDK 496
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 7-215 1.25e-43

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 155.34  E-value: 1.25e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713   7 VITVDGPSGAGKGTLCQALANEFGWQLLDSGAIYRVLALAALHHHVDIQSE--------DALVPLAANLDVKFVPENNVL 78
Cdd:PRK09518    3 IVAIDGPAGVGKSSVSRALAQYLGYAYLDTGAMYRACAWWCLKQGIDLDAElvdeqvvtEAVGEFFTGLHFDISVDPDSP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713  79 KVILEGEDVSNQIRTETVGNTASQTATFPRVREALLRRQRA----------FRTLPGLIADGRDMGTVVFPDAPVKIFLD 148
Cdd:PRK09518   83 GVFADGEDISEEIRSPEVSSHVSAVAAIPPVRNVLIAAQRAyiareasadsFSGGLGIVAEGRDITTVVAPDAEVRILLT 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1539065713 149 ASAEERAHRRMKQLQEKGFDVnferLLSEIEERDFRDrNRSVAPLIAAKDALVLDSTSMSIEEVIEK 215
Cdd:PRK09518  163 AREEVRQARRSGQDRSETPGV----VLEDVAARDEAD-SKVTSFLSAADGVTTLDNSDLDFDETLDL 224
PRK12269 PRK12269
bifunctional cytidylate kinase/ribosomal protein S1; Provisional
 7-215 4.39e-30

bifunctional cytidylate kinase/ribosomal protein S1; Provisional


Pssm-ID: 105491 [Multi-domain]  Cd Length: 863  Bit Score: 117.12  E-value: 4.39e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713   7 VITVDGPSGAGKGTLCQALANEFGWQLLDSGAIYRVLALAALHHHVDIQSED-------------ALVPLAANLDVKFVP 73
Cdd:PRK12269   36 IIALDGPAGSGKSSVCRLLASRLGAQCLNTGSFYRAFTLAALRRVSELAVQAcspspdpdaavgcAAVPHATNLDTSYAP 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713  74 ENNVLKVIL------------------------EGEDVSNQIRTETVGNTASQTATFPRVREALLRRQRAFRTLPGLIAD 129
Cdd:PRK12269  116 LTAQKKVALfdeaywvsfartvalsyragvmyvGEENVESLLRSDEVESAVSYFAAMPAIRAIMTGKIRSAVCGARVVCE 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713 130 GRDMGTVVFPDAPVKIFLDASAEERAHRRMKQLQEKgfdVNFERLLSEIEERDFRDRNRSVAPLIAAKDALVLDSTSMSI 209
Cdd:PRK12269  196 GRDLTTVVFVDADLKCYLDASIEARVARRWAQGTSR---LSKQELEQRMRARDAHDRARTVGGLRCAPDALYVDTSCLTI 272


                  ....*.
gi 1539065713 210 EEVIEK 215
Cdd:PRK12269  273 EEVCER 278
CmkB COG1102
Cytidylate kinase [Nucleotide transport and metabolism];
7-224 1.28e-12

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440719 [Multi-domain]  Cd Length: 188  Bit Score: 64.08  E-value: 1.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713   7 VITVDGPSGAGKGTLCQALANEFGWQLLDsGAIyrvLALAALHHHVDIQSEDALVPLAANLDVKFVPENNvlkvileged 86
Cdd:COG1102     2 VITISREPGSGGTTIAKRLAEKLGLPLYD-GEI---LREAAKERGLSEEEFEKLDEKAPSLLYRDTAEED---------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713  87 vsnqirtetvgntasqtatfpRVREALLRRQRAFRTLPGLIADGRdMGTVVFPDAP--VKIFLDASAEERAHRRMKQLqe 164
Cdd:COG1102    68 ---------------------EIDRALDKVIRELARKGNCVIVGR-LADWILRDRPnvLKVFLTAPLEVRVKRIAERE-- 123

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1539065713 165 kgfDVNFERLLSEIEERDFRDRNRSVAplIAAKDA-------LVLDSTSMSIEEVIEKAHTYAKKIL 224
Cdd:COG1102   124 ---GISEEEAEKEIKKRDKSRAKYYKY--YYGIDWgdpsnydLVINTSRLGIEEAVDLILAAIEARE 185
PRK04182 PRK04182
cytidylate kinase; Provisional
 7-225 4.70e-08

cytidylate kinase; Provisional


Pssm-ID: 235244 [Multi-domain]  Cd Length: 180  Bit Score: 50.96  E-value: 4.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713   7 VITVDGPSGAGKGTLCQALANEFGWQLLDSGAIYRVLA------LAALHhhvdiqsedalvplaanldvKFVPENnvlkv 80
Cdd:PRK04182    2 IITISGPPGSGKTTVARLLAEKLGLKHVSAGEIFRELAkergmsLEEFN--------------------KYAEED----- 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713  81 ilegedvsnqirtetvgntasqtatfPRVREALLRRQRAF-RTLPGLIADGRDMGTVVFPDAPVKIFLDASAEERAHRRM 159
Cdd:PRK04182   57 --------------------------PEIDKEIDRRQLEIaEKEDNVVLEGRLAGWMAKDYADLKIWLKAPLEVRAERIA 110

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1539065713 160 KqlQEKGfdvNFERLLSEIEERDFRDRNR------------SVApliaakDaLVLDSTSMSIEEVIEKAHTYAKKILQ 225
Cdd:PRK04182  111 E--REGI---SVEEALEETIEREESEAKRykeyygididdlSIY------D-LVINTSRWDPEGVFDIILTAIDKLLK 176
Dck COG1428
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
6-34 1.47e-05

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 44.39  E-value: 1.47e-05
                          10        20
                  ....*....|....*....|....*....
gi 1539065713   6 PVITVDGPSGAGKGTLCQALANEFGWQLL 34
Cdd:COG1428     4 RYIAVEGNIGAGKTTLARLLAEHLGAELL 32
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 7-190 6.93e-05

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: 42.52  E-value: 6.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713   7 VITVDGPSGAGKGTLCQALANEFGWQL-----LDSgaIYRVLALAALHHHVDIqseDALVPLAANLDVkfvpENNVLKVI 81
Cdd:COG0572     9 IIGIAGPSGSGKTTFARRLAEQLGADKvvvisLDD--YYKDREHLPLDERGKP---NFDHPEAFDLDL----LNEHLEPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713  82 LEGEDVSNQIRTETVGNTASQTATFPRVR----EALLrrqrAFRtlPGLIADGRDmgtvvfpdapVKIFLDASAEERAHR 157
Cdd:COG0572    80 KAGESVELPVYDFATGTRSGETVKVEPADviivEGIH----ALN--DELLRDLLD----------LKIYVDADTDVRLIR 143

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1539065713 158 RMKqlqekgfdvnferllseieeRDFRDRNRSV 190
Cdd:COG0572   144 RIV--------------------RDGEERGRTA 156
AAA_17 pfam13207
AAA domain;
12-160 8.91e-05

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 41.07  E-value: 8.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713  12 GPSGAGKGTLCQALANEFGWQLLDSGAIYRvlalaalhhhvDIQSEDALVPLAANLDvkfvpennvlKVILEGEDVSNQI 91
Cdd:pfam13207   2 GVPGSGKTTQLKKLAEKLGFPHISAGDLLR-----------EEAKERGLVEDRDEMR----------KLPLEPQKELQKL 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1539065713  92 RTETVGNTASQTA----TFPRVREallrrQRAFrtLPGLIadgRDMGTVVFPDApvKIFLDASAEERAHRRMK 160
Cdd:pfam13207  61 AAERIAEEAGEGGvivdGHPRIKT-----PAGY--LPGLP---VEVLRELKPDA--IILLEADPEEILERRLK 121
dNK cd01673
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to ...
 7-34 1.60e-04

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: 41.06  E-value: 1.60e-04
                          10        20
                  ....*....|....*....|....*...
gi 1539065713   7 VITVDGPSGAGKGTLCQALANEFGWQLL 34
Cdd:cd01673     1 VIVVEGNIGAGKSTLAKELAEHLGYEVV 28
PRK06547 PRK06547
hypothetical protein; Provisional
 5-33 1.87e-04

hypothetical protein; Provisional


Pssm-ID: 235825  Cd Length: 172  Bit Score: 40.88  E-value: 1.87e-04
                          10        20
                  ....*....|....*....|....*....
gi 1539065713   5 APVITVDGPSGAGKGTLCQALANEFGWQL 33
Cdd:PRK06547   15 MITVLIDGRSGSGKTTLAGALAARTGFQL 43
ADK pfam00406
Adenylate kinase;
12-41 6.17e-04

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 39.21  E-value: 6.17e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1539065713  12 GPSGAGKGTLCQALANEFGWQLLDSGAIYR 41
Cdd:pfam00406   3 GPPGAGKGTQAEKIVQKYGLPHLSTGDLLR 32
PLN02200 PLN02200
adenylate kinase family protein
 5-127 1.44e-03

adenylate kinase family protein


Pssm-ID: 215125 [Multi-domain]  Cd Length: 234  Bit Score: 38.72  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539065713   5 APVIT-VDGPSGAGKGTLCQALANEFGWQLLDSGAIYRvlalaalhHHVDIQSEDALVPLAANLDVKFVPENNVLKVIle 83
Cdd:PLN02200   42 TPFITfVLGGPGSGKGTQCEKIVETFGFKHLSAGDLLR--------REIASNSEHGAMILNTIKEGKIVPSEVTVKLI-- 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1539065713  84 gedvsnQIRTETVGNTASQTATFPRVREALLRRQRAFRTLPGLI 127
Cdd:PLN02200  112 ------QKEMESSDNNKFLIDGFPRTEENRIAFERIIGAEPNVV 149
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 12-41 1.91e-03

Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or related kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440329 [Multi-domain]  Cd Length: 212  Bit Score: 38.18  E-value: 1.91e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1539065713  12 GPSGAGKGTLCQALANEFGWQLLDSGAIYR 41
Cdd:COG0563     7 GPPGAGKGTQAKRLAEKYGIPHISTGDMLR 36
UMP_CMP_kin_fam TIGR01359
UMP-CMP kinase family; This subfamily of the adenylate kinase superfamily contains examples of ...
 7-41 2.38e-03

UMP-CMP kinase family; This subfamily of the adenylate kinase superfamily contains examples of UMP-CMP kinase, as well as others proteins with unknown specificity, some currently designated adenylate kinase. All known members are eukaryotic.


Pssm-ID: 273576 [Multi-domain]  Cd Length: 185  Bit Score: 37.74  E-value: 2.38e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1539065713   7 VITVDGPSGAGKGTLCQALANEFGWQLLDSGAIYR 41
Cdd:TIGR01359   1 VVFVLGGPGSGKGTQCAKIVENFGFTHLSAGDLLR 35
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 7-40 4.18e-03

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.


Pssm-ID: 238977 [Multi-domain]  Cd Length: 69  Bit Score: 35.00  E-value: 4.18e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1539065713   7 VITVDGPSGAGKGTLCQALANEFG---WQLLDSGAIY 40
Cdd:cd02019     1 IIAITGGSGSGKSTVAKKLAEQLGgrsVVVLDEIVIL 37
 
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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