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Conserved domains on  [gi|495141669|ref|WP_007866476|]
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(d)CMP kinase [Cronobacter sakazakii]

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];
6-225 2.99e-130

Cytidylate kinase [Nucleotide transport and metabolism];


:

Pssm-ID: 440052 [Multi-domain]  Cd Length: 220  Bit Score: 365.89  E-value: 2.99e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669   6 PVITIDGPSGAGKGTLCKAMAETLQWHLLDSGAIYRVLALAALHHHVDVASEEALVPLAAHLDVRFVAQQGELEVILEGE 85
Cdd:COG0283    1 PVIAIDGPAGSGKSTVAKALAKRLGYHYLDTGAMYRAVALAALRNGIDLDDEEALAALARNLDIEFETDPGGQRVFLNGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669  86 DVSAEIRTQEVANAASQIAAFPRVREALLRRQRAFREAPGLIADGRDMGTVVFPDAPVKIFLDASSEERAHRRMLQLQEK 165
Cdd:COG0283   81 DVTDEIRTEEVSNAVSKVAAIPEVREALVALQRAFAKAPGLVADGRDIGTVVFPDAELKIFLTASAEERARRRYKELKEK 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669 166 GFSVNFERLLAEIKERDDRDRNRPVAPLVPAHDALVLDSTSLSIEEVIEKALEYAREKLA 225
Cdd:COG0283  161 GISVSLEELLADIKERDERDSTRAVAPLKPAEDAIVIDTTDLSIEEVVEKILALVRERLS 220
 
Name Accession Description Interval E-value
Cmk COG0283
Cytidylate kinase [Nucleotide transport and metabolism];
6-225 2.99e-130

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440052 [Multi-domain]  Cd Length: 220  Bit Score: 365.89  E-value: 2.99e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669   6 PVITIDGPSGAGKGTLCKAMAETLQWHLLDSGAIYRVLALAALHHHVDVASEEALVPLAAHLDVRFVAQQGELEVILEGE 85
Cdd:COG0283    1 PVIAIDGPAGSGKSTVAKALAKRLGYHYLDTGAMYRAVALAALRNGIDLDDEEALAALARNLDIEFETDPGGQRVFLNGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669  86 DVSAEIRTQEVANAASQIAAFPRVREALLRRQRAFREAPGLIADGRDMGTVVFPDAPVKIFLDASSEERAHRRMLQLQEK 165
Cdd:COG0283   81 DVTDEIRTEEVSNAVSKVAAIPEVREALVALQRAFAKAPGLVADGRDIGTVVFPDAELKIFLTASAEERARRRYKELKEK 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669 166 GFSVNFERLLAEIKERDDRDRNRPVAPLVPAHDALVLDSTSLSIEEVIEKALEYAREKLA 225
Cdd:COG0283  161 GISVSLEELLADIKERDERDSTRAVAPLKPAEDAIVIDTTDLSIEEVVEKILALVRERLS 220
cmk TIGR00017
cytidylate kinase; This family consists of cytidylate kinase, which catalyzes the ...
6-220 1.15e-118

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: 336.71  E-value: 1.15e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669    6 PVITIDGPSGAGKGTLCKAMAETLQWHLLDSGAIYRVLALAALHHHVDVASEEALVPLAAHLDVRFVAQQGELEVILEGE 85
Cdd:TIGR00017   3 MIIAIDGPSGAGKSTVAKAVAEKLGYAYLDSGAMYRAIALAALQNRVDLTSEDALAELISHLDIRFIPTNGEVEVFLNGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669   86 DVSAEIRTQEVANAASQIAAFPRVREALLRRQRAFREAPGLIADGRDMGTVVFPDAPVKIFLDASSEERAHRRMLQLQEK 165
Cdd:TIGR00017  83 DVSEAIRTQEVANAASKVAVFPKVREALLKRQQALAKNDGIIADGRDIGTVVFPNAEVKIFLDASVEERAKRRYKQLQIK 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 495141669  166 GFSVNFERLLAEIKERDDRDRNRPVAPLVPAHDALVLDSTSLSIEEVIEKALEYA 220
Cdd:TIGR00017 163 GNEVNFEELLAEIKERDDRDSNREVAPLKKADDALYLDTSNLSIDEVVEKILEYA 217
Cytidylate_kin pfam02224
Cytidylate kinase; Cytidylate kinase EC:2.7.4.14 catalyzes the phosphorylation of cytidine 5 ...
8-222 2.90e-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: 320.02  E-value: 2.90e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669    8 ITIDGPSGAGKGTLCKAMAETLQWHLLDSGAIYRVLALAALHHHVDVASEEALVPLAAHLDVRFVAQqgelEVILEGEDV 87
Cdd:pfam02224   1 IAIDGPSGSGKSTVARILARKLGYKYLDTGAMYRALALAALRQKVDLTDEDALAELASEVDISFGHT----EVFLNGEDV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669   88 SAEIRTQEVANAASQIAAFPRVREALLRRQRAFREAPGLIADGRDMGTVVFPDAPVKIFLDASSEERAHRRMLQLQEKGF 167
Cdd:pfam02224  77 SSEIRTDEVAQAASQVAAIPAVRARLNKLQRQLAKNGNIVMEGRDIGTVVFPDAEVKIFLTASPEERAKRRYKQLQAKGL 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 495141669  168 SVNFERLLAEIKERDDRDRNRPVAPLVPAHDALVLDSTSLSIEEVIEKALEYARE 222
Cdd:pfam02224 157 SVDFEELLAEIKRRDKRDSERAVGPLKPAPDALIIDTSKLTIEEVVEKILELIKQ 211
PRK11860 PRK11860
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
2-223 5.35e-92

bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;


Pssm-ID: 237003 [Multi-domain]  Cd Length: 661  Bit Score: 283.09  E-value: 5.35e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669   2 TASVPVITIDGPSGAGKGTLCKAMAETLQWHLLDSGAIYRVLALAALHHHVDVASEEALVPLAAHLDVRFVAQQgeleVI 81
Cdd:PRK11860 439 ADRVPVICIDGPTASGKGTVAARVAEALGYHYLDSGALYRLTALAALRAGVALDDEAAIAALARGLPVRFEGDR----IW 514
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669  82 LEGEDVSAEIRTQEVANAASQIAAFPRVREALLRRQRAFREAPGLIADGRDMGTVVFPDAPVKIFLDASSEERAHRRMLQ 161
Cdd:PRK11860 515 LGGEDVTDAIRTEAAGMGASRVSALPAVRAALLALQRSFRRLPGLVADGRDMGTVIFPDAALKVFLTASAEARAERRYKQ 594
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495141669 162 LQEKGFSVNFERLLAEIKERDDRDRNRPVAPLVPAHDALVLDSTSLSIEEVIEKALEYAREK 223
Cdd:PRK11860 595 LISKGISANIADLLADLEARDARDTQRSVAPLKPAQDALLLDNSDLTIEQAVAQVLDWWQER 656
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
7-205 1.79e-69

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: 209.27  E-value: 1.79e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669   7 VITIDGPSGAGKGTLCKAMAETLQWHLLDSGaiyrvlalaalhhhvdvaseealvplaahldvrfvaqqgelevileged 86
Cdd:cd02020    1 IIAIDGPAGSGKSTVAKLLAKKLGLPYLDTG------------------------------------------------- 31
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669  87 vsaEIRTQEVANAASQIAAFPRVREALLRRQRAFREAPGLIADGRDMGTVVFPDAPVKIFLDASSEERAHRRMLQLQEKG 166
Cdd:cd02020   32 ---GIRTEEVGKLASEVAAIPEVRKALDERQRELAKKPGIVLEGRDIGTVVFPDADLKIFLTASPEVRAKRRAKQLQAKG 108
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 495141669 167 FSVNFERLLAEIKERDDRDRNRPVAPLVPAHDALVLDST 205
Cdd:cd02020  109 EGVDLEEILAEIIERDERDSTRYVAPLKLAEDAIVIDTS 147
 
Name Accession Description Interval E-value
Cmk COG0283
Cytidylate kinase [Nucleotide transport and metabolism];
6-225 2.99e-130

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440052 [Multi-domain]  Cd Length: 220  Bit Score: 365.89  E-value: 2.99e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669   6 PVITIDGPSGAGKGTLCKAMAETLQWHLLDSGAIYRVLALAALHHHVDVASEEALVPLAAHLDVRFVAQQGELEVILEGE 85
Cdd:COG0283    1 PVIAIDGPAGSGKSTVAKALAKRLGYHYLDTGAMYRAVALAALRNGIDLDDEEALAALARNLDIEFETDPGGQRVFLNGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669  86 DVSAEIRTQEVANAASQIAAFPRVREALLRRQRAFREAPGLIADGRDMGTVVFPDAPVKIFLDASSEERAHRRMLQLQEK 165
Cdd:COG0283   81 DVTDEIRTEEVSNAVSKVAAIPEVREALVALQRAFAKAPGLVADGRDIGTVVFPDAELKIFLTASAEERARRRYKELKEK 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669 166 GFSVNFERLLAEIKERDDRDRNRPVAPLVPAHDALVLDSTSLSIEEVIEKALEYAREKLA 225
Cdd:COG0283  161 GISVSLEELLADIKERDERDSTRAVAPLKPAEDAIVIDTTDLSIEEVVEKILALVRERLS 220
cmk TIGR00017
cytidylate kinase; This family consists of cytidylate kinase, which catalyzes the ...
6-220 1.15e-118

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: 336.71  E-value: 1.15e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669    6 PVITIDGPSGAGKGTLCKAMAETLQWHLLDSGAIYRVLALAALHHHVDVASEEALVPLAAHLDVRFVAQQGELEVILEGE 85
Cdd:TIGR00017   3 MIIAIDGPSGAGKSTVAKAVAEKLGYAYLDSGAMYRAIALAALQNRVDLTSEDALAELISHLDIRFIPTNGEVEVFLNGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669   86 DVSAEIRTQEVANAASQIAAFPRVREALLRRQRAFREAPGLIADGRDMGTVVFPDAPVKIFLDASSEERAHRRMLQLQEK 165
Cdd:TIGR00017  83 DVSEAIRTQEVANAASKVAVFPKVREALLKRQQALAKNDGIIADGRDIGTVVFPNAEVKIFLDASVEERAKRRYKQLQIK 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 495141669  166 GFSVNFERLLAEIKERDDRDRNRPVAPLVPAHDALVLDSTSLSIEEVIEKALEYA 220
Cdd:TIGR00017 163 GNEVNFEELLAEIKERDDRDSNREVAPLKKADDALYLDTSNLSIDEVVEKILEYA 217
Cytidylate_kin pfam02224
Cytidylate kinase; Cytidylate kinase EC:2.7.4.14 catalyzes the phosphorylation of cytidine 5 ...
8-222 2.90e-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: 320.02  E-value: 2.90e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669    8 ITIDGPSGAGKGTLCKAMAETLQWHLLDSGAIYRVLALAALHHHVDVASEEALVPLAAHLDVRFVAQqgelEVILEGEDV 87
Cdd:pfam02224   1 IAIDGPSGSGKSTVARILARKLGYKYLDTGAMYRALALAALRQKVDLTDEDALAELASEVDISFGHT----EVFLNGEDV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669   88 SAEIRTQEVANAASQIAAFPRVREALLRRQRAFREAPGLIADGRDMGTVVFPDAPVKIFLDASSEERAHRRMLQLQEKGF 167
Cdd:pfam02224  77 SSEIRTDEVAQAASQVAAIPAVRARLNKLQRQLAKNGNIVMEGRDIGTVVFPDAEVKIFLTASPEERAKRRYKQLQAKGL 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 495141669  168 SVNFERLLAEIKERDDRDRNRPVAPLVPAHDALVLDSTSLSIEEVIEKALEYARE 222
Cdd:pfam02224 157 SVDFEELLAEIKRRDKRDSERAVGPLKPAPDALIIDTSKLTIEEVVEKILELIKQ 211
PRK11860 PRK11860
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
2-223 5.35e-92

bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;


Pssm-ID: 237003 [Multi-domain]  Cd Length: 661  Bit Score: 283.09  E-value: 5.35e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669   2 TASVPVITIDGPSGAGKGTLCKAMAETLQWHLLDSGAIYRVLALAALHHHVDVASEEALVPLAAHLDVRFVAQQgeleVI 81
Cdd:PRK11860 439 ADRVPVICIDGPTASGKGTVAARVAEALGYHYLDSGALYRLTALAALRAGVALDDEAAIAALARGLPVRFEGDR----IW 514
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669  82 LEGEDVSAEIRTQEVANAASQIAAFPRVREALLRRQRAFREAPGLIADGRDMGTVVFPDAPVKIFLDASSEERAHRRMLQ 161
Cdd:PRK11860 515 LGGEDVTDAIRTEAAGMGASRVSALPAVRAALLALQRSFRRLPGLVADGRDMGTVIFPDAALKVFLTASAEARAERRYKQ 594
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495141669 162 LQEKGFSVNFERLLAEIKERDDRDRNRPVAPLVPAHDALVLDSTSLSIEEVIEKALEYAREK 223
Cdd:PRK11860 595 LISKGISANIADLLADLEARDARDTQRSVAPLKPAQDALLLDNSDLTIEQAVAQVLDWWQER 656
PRK13477 PRK13477
bifunctional pantoate--beta-alanine ligase/(d)CMP kinase;
6-224 1.09e-72

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


Pssm-ID: 237393 [Multi-domain]  Cd Length: 512  Bit Score: 229.38  E-value: 1.09e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669   6 PVITIDGPSGAGKGTLCKAMAETLQWHLLDSGAIYRVLALAALHHHVDVASEEALVPLAAHLDVRF-VAQQGELEVILEG 84
Cdd:PRK13477 285 PIIAIDGPAGAGKSTVTRAVAKKLGLLYLDTGAMYRAVTWLVLQEGIDPQDEEALAELLSDLKIELkPSSGSPQRVWING 364
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669  85 EDVSAEIRTQEVANAASQIAAFPRVREALLRRQRAFREAPGLIADGRDMGTVVFPDAPVKIFLDASSEERAHRRMLQLQE 164
Cdd:PRK13477 365 EDVTEAIRSPEVTSSVSAIAAQPAVRQALVKQQQRIGEKGGLVAEGRDIGTHVFPDAELKIFLTASVEERARRRALDLQA 444
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495141669 165 KGFSV-NFERLLAEIKERDDRDRNRPVAPLVPAHDALVLDSTSLSIEEVIEKALEYAREKL 224
Cdd:PRK13477 445 QGFPViDLEQLEAQIAERDRLDSTREIAPLRKADDAIELITDGLSIEEVVDKIIDLYRDRI 505
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
7-205 1.79e-69

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: 209.27  E-value: 1.79e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669   7 VITIDGPSGAGKGTLCKAMAETLQWHLLDSGaiyrvlalaalhhhvdvaseealvplaahldvrfvaqqgelevileged 86
Cdd:cd02020    1 IIAIDGPAGSGKSTVAKLLAKKLGLPYLDTG------------------------------------------------- 31
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669  87 vsaEIRTQEVANAASQIAAFPRVREALLRRQRAFREAPGLIADGRDMGTVVFPDAPVKIFLDASSEERAHRRMLQLQEKG 166
Cdd:cd02020   32 ---GIRTEEVGKLASEVAAIPEVRKALDERQRELAKKPGIVLEGRDIGTVVFPDADLKIFLTASPEVRAKRRAKQLQAKG 108
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 495141669 167 FSVNFERLLAEIKERDDRDRNRPVAPLVPAHDALVLDST 205
Cdd:cd02020  109 EGVDLEEILAEIIERDERDSTRYVAPLKLAEDAIVIDTS 147
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
7-218 1.59e-46

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 163.43  E-value: 1.59e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669   7 VITIDGPSGAGKGTLCKAMAETLQWHLLDSGAIYRVLALAALHHHVDVASE--------EALVPLAAHLDVRFVAQQGEL 78
Cdd:PRK09518   3 IVAIDGPAGVGKSSVSRALAQYLGYAYLDTGAMYRACAWWCLKQGIDLDAElvdeqvvtEAVGEFFTGLHFDISVDPDSP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669  79 EVILEGEDVSAEIRTQEVANAASQIAAFPRVREALLRRQRA----------FREAPGLIADGRDMGTVVFPDAPVKIFLD 148
Cdd:PRK09518  83 GVFADGEDISEEIRSPEVSSHVSAVAAIPPVRNVLIAAQRAyiareasadsFSGGLGIVAEGRDITTVVAPDAEVRILLT 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669 149 ASSEERAHRRMLQLQEKgfsvNFERLLAEIKERDDRDrNRPVAPLVPAHDALVLDSTSLSIEEVIEKALE 218
Cdd:PRK09518 163 AREEVRQARRSGQDRSE----TPGVVLEDVAARDEAD-SKVTSFLSAADGVTTLDNSDLDFDETLDLLIG 227
PRK12269 PRK12269
bifunctional cytidylate kinase/ribosomal protein S1; Provisional
7-223 1.77e-29

bifunctional cytidylate kinase/ribosomal protein S1; Provisional


Pssm-ID: 105491 [Multi-domain]  Cd Length: 863  Bit Score: 115.58  E-value: 1.77e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669   7 VITIDGPSGAGKGTLCKAMAETLQWHLLDSGAIYRVLALAALHHHVDVASEE-------------ALVPLAAHLDVRFVA 73
Cdd:PRK12269  36 IIALDGPAGSGKSSVCRLLASRLGAQCLNTGSFYRAFTLAALRRVSELAVQAcspspdpdaavgcAAVPHATNLDTSYAP 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669  74 QQGELEVIL------------------------EGEDVSAEIRTQEVANAASQIAAFPRVREALLRRQRAFREAPGLIAD 129
Cdd:PRK12269 116 LTAQKKVALfdeaywvsfartvalsyragvmyvGEENVESLLRSDEVESAVSYFAAMPAIRAIMTGKIRSAVCGARVVCE 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669 130 GRDMGTVVFPDAPVKIFLDASSEERAHRRMLQLQEKgfsVNFERLLAEIKERDDRDRNRPVAPLVPAHDALVLDSTSLSI 209
Cdd:PRK12269 196 GRDLTTVVFVDADLKCYLDASIEARVARRWAQGTSR---LSKQELEQRMRARDAHDRARTVGGLRCAPDALYVDTSCLTI 272
                        250
                 ....*....|....
gi 495141669 210 EEVIEKALEYAREK 223
Cdd:PRK12269 273 EEVCERIAREAHRR 286
CmkB COG1102
Cytidylate kinase [Nucleotide transport and metabolism];
7-225 2.97e-12

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440719 [Multi-domain]  Cd Length: 188  Bit Score: 62.92  E-value: 2.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669   7 VITIDGPSGAGKGTLCKAMAETLQWHLLDsGAIyrvLALAALHHHVDVASEEALVPLAAHLDVRFVAQQGELevileged 86
Cdd:COG1102    2 VITISREPGSGGTTIAKRLAEKLGLPLYD-GEI---LREAAKERGLSEEEFEKLDEKAPSLLYRDTAEEDEI-------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669  87 vsaeirtqevanaasqiaafprvREALLRRQRAFREAPGLIADGRdMGTVVFPDAP--VKIFLDASSEERAHRRMlqlqe 164
Cdd:COG1102   70 -----------------------DRALDKVIRELARKGNCVIVGR-LADWILRDRPnvLKVFLTAPLEVRVKRIA----- 120
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495141669 165 KGFSVNFERLLAEIKERDDRDRNR--------PvaplvpaHDA----LVLDSTSLSIEEVIEKALEYAREKLA 225
Cdd:COG1102  121 EREGISEEEAEKEIKKRDKSRAKYykyyygidW-------GDPsnydLVINTSRLGIEEAVDLILAAIEAREK 186
PRK04182 PRK04182
cytidylate kinase; Provisional
7-224 1.21e-08

cytidylate kinase; Provisional


Pssm-ID: 235244 [Multi-domain]  Cd Length: 180  Bit Score: 52.89  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669   7 VITIDGPSGAGKGTLCKAMAETLQWHLLDSGAIYRVLAlaalhhhvdvasEEALVPLAahldvrfvaqqgELEVILEgED 86
Cdd:PRK04182   2 IITISGPPGSGKTTVARLLAEKLGLKHVSAGEIFRELA------------KERGMSLE------------EFNKYAE-ED 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669  87 vsaeirtqevanaasqiaafPRVREALLRRQRAF-REAPGLIADGRDMGTVVFPDAPVKIFLDASSEERAHRrmLQLQEK 165
Cdd:PRK04182  57 --------------------PEIDKEIDRRQLEIaEKEDNVVLEGRLAGWMAKDYADLKIWLKAPLEVRAER--IAEREG 114
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495141669 166 GfsvNFERLLAEIKERDDRDRNR-------PVAPLVPAHdaLVLDSTSLSIEEVIEKALEYAREKL 224
Cdd:PRK04182 115 I---SVEEALEETIEREESEAKRykeyygiDIDDLSIYD--LVINTSRWDPEGVFDIILTAIDKLL 175
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
7-40 1.91e-04

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: 38.47  E-value: 1.91e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 495141669   7 VITIDGPSGAGKGTLCKAMAETL---QWHLLDSGAIY 40
Cdd:cd02019    1 IIAITGGSGSGKSTVAKKLAEQLggrSVVVLDEIVIL 37
dNK cd01673
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to ...
7-34 1.10e-03

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: 38.75  E-value: 1.10e-03
                         10        20
                 ....*....|....*....|....*...
gi 495141669   7 VITIDGPSGAGKGTLCKAMAETLQWHLL 34
Cdd:cd01673    1 VIVVEGNIGAGKSTLAKELAEHLGYEVV 28
Cytidylate_kin2 pfam13189
Cytidylate kinase-like family; This family includes enzymes related to cytidylate kinase.
7-186 1.56e-03

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


Pssm-ID: 433023 [Multi-domain]  Cd Length: 176  Bit Score: 37.99  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669    7 VITIDGPSGAGKGTLCKAMAETLQWHLLDSGAIYRVlalaalhhhvdvaSEEALVPLAahldvrfvaqqgELEVILEGED 86
Cdd:pfam13189   1 VITISRQYGSGGTTIAKKLAEKLGYPFYDREILDEI-------------AKELGISEE------------EFELFDEKSR 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669   87 VSAEIRTQEVANAASQIAAFPRVREALLRRQRAFREAPGLIADGRDmGTVVFPDAP--VKIFLDASSEERAhRRMLQLQE 164
Cdd:pfam13189  56 LSSFLYSLAGGRVRGDALSDDRLFDAQSKVIRELAAEDNCVIVGRG-ADYILKDIPnvLRVFLTAPLEDRV-KRVMEREG 133
                         170       180
                  ....*....|....*....|..
gi 495141669  165 KGfsvnfERLLAEIKERDDRDR 186
Cdd:pfam13189 134 LS-----EEEARELIKETDKRR 150
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
8-113 3.66e-03

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 37.62  E-value: 3.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495141669   8 ITIDGPSGAGKGTLCKAMA--ETlqwhlLDSGAIY----RVLALAALHHHVD-VASEEALVPlaaHLDVRfvaqqgelev 80
Cdd:PRK09452  43 LTLLGPSGCGKTTVLRLIAgfET-----PDSGRIMldgqDITHVPAENRHVNtVFQSYALFP---HMTVF---------- 104
                         90       100       110
                 ....*....|....*....|....*....|...
gi 495141669  81 ilegEDVSAEIRTQEVANAasQIAafPRVREAL 113
Cdd:PRK09452 105 ----ENVAFGLRMQKTPAA--EIT--PRVMEAL 129
TMPK cd01672
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
8-66 4.13e-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: 37.25  E-value: 4.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495141669   8 ITIDGPSGAGKGTLCKAMAETLQWHLLD--------SGAIYRVLALAALHHHVDVASE--EALVPLAAH 66
Cdd:cd01672    3 IVFEGIDGAGKTTLIELLAERLEARGYEvvltrepgGTPIGEAIRELLLDPEDEKMDPraELLLFAADR 71
PRK06547 PRK06547
hypothetical protein; Provisional
6-33 4.40e-03

hypothetical protein; Provisional


Pssm-ID: 235825  Cd Length: 172  Bit Score: 36.64  E-value: 4.40e-03
                         10        20
                 ....*....|....*....|....*...
gi 495141669   6 PVITIDGPSGAGKGTLCKAMAETLQWHL 33
Cdd:PRK06547  16 ITVLIDGRSGSGKTTLAGALAARTGFQL 43
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
1-29 5.74e-03

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: 36.74  E-value: 5.74e-03
                         10        20
                 ....*....|....*....|....*....
gi 495141669   1 MTASVPVITIDGPSGAGKGTLCKAMAETL 29
Cdd:COG0572    3 RSGKPRIIGIAGPSGSGKTTFARRLAEQL 31
 
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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