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Conserved domains on  [gi|505228860|ref|WP_015415962|]
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cytidylyltransferase domain-containing protein [Pseudodesulfovibrio piezophilus]

Protein Classification

similar to acylneuraminate cytidylyltransferase( domain architecture ID 10787207)

protein similar to acylneuraminate cytidylyltransferase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NeuA COG1083
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ...
 1-234 3.93e-97

CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440700  Cd Length: 228  Bit Score: 282.82  E-value: 3.93e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505228860   1 MEILGLLTARGGSKGIPGKNYKEIAGKPLITWTAKEALKSSLLGRVVLSTDDLKIADIARSSGVEVpFMRPKYLAEDDSP 80
Cdd:COG1083    1 MKILAIIPARGGSKGIPGKNIRPLAGKPLIAYSIEAALKSGLFDRVVVSTDDEEIAEVAREYGAEV-FLRPAELAGDTAS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505228860  81 HIDCVLHALEWLKlEENYVPDLVCLLQPTSPLRLASDIDGALEmaitLFHEKGIASVVSVTDCVHHPFLVRKQEDDGSLT 160
Cdd:COG1083   80 TIDVILHALEWLE-EQGEEFDYVVLLQPTSPLRTAEDIDEAIE----LLLESGADSVVSVTEAHHPPYWALKLDEDGRLE 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505228860 161 PFIEHKISYERRQDLPVALMRNGAVYVSSTNSLLRDKTFFPDKYYGYYMPYERSLVIDTPIEFSFVEMLLQNQK 234
Cdd:COG1083  155 PLNPDPHNRPRRQDLPPAYRENGAIYIFKREALLENKSRFGGKTGAYEMPEERSVDIDTEEDFELAEALLKKRK 228
 
Name Accession Description Interval E-value
NeuA COG1083
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ...
 1-234 3.93e-97

CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440700  Cd Length: 228  Bit Score: 282.82  E-value: 3.93e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505228860   1 MEILGLLTARGGSKGIPGKNYKEIAGKPLITWTAKEALKSSLLGRVVLSTDDLKIADIARSSGVEVpFMRPKYLAEDDSP 80
Cdd:COG1083    1 MKILAIIPARGGSKGIPGKNIRPLAGKPLIAYSIEAALKSGLFDRVVVSTDDEEIAEVAREYGAEV-FLRPAELAGDTAS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505228860  81 HIDCVLHALEWLKlEENYVPDLVCLLQPTSPLRLASDIDGALEmaitLFHEKGIASVVSVTDCVHHPFLVRKQEDDGSLT 160
Cdd:COG1083   80 TIDVILHALEWLE-EQGEEFDYVVLLQPTSPLRTAEDIDEAIE----LLLESGADSVVSVTEAHHPPYWALKLDEDGRLE 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505228860 161 PFIEHKISYERRQDLPVALMRNGAVYVSSTNSLLRDKTFFPDKYYGYYMPYERSLVIDTPIEFSFVEMLLQNQK 234
Cdd:COG1083  155 PLNPDPHNRPRRQDLPPAYRENGAIYIFKREALLENKSRFGGKTGAYEMPEERSVDIDTEEDFELAEALLKKRK 228
CMP-NeuAc_Synthase cd02513
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ...
 3-230 2.06e-86

CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; CMP-N-acetylneuraminic acid synthetase (CMP-NeuAc synthetase) or acylneuraminate cytidylyltransferase catalyzes the transfer the CMP moiety of CTP to the anomeric hydroxyl group of NeuAc in the presence of Mg++. It is the second to last step in the sialylation of the oligosaccharide component of glycoconjugates by providing the activated sugar-nucleotide cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-Neu5Ac), the substrate for sialyltransferases. Eukaryotic CMP-NeuAc synthetases are predominantly located in the nucleus. The activated CMP-Neu5Ac diffuses from the nucleus into the cytoplasm.


Pssm-ID: 133006  Cd Length: 223  Bit Score: 255.54  E-value: 2.06e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505228860   3 ILGLLTARGGSKGIPGKNYKEIAGKPLITWTAKEALKSSLLGRVVLSTDDLKIADIARSSGVEVPFMRPKYLAEDDSPHI 82
Cdd:cd02513    2 ILAIIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLFDRVVVSTDDEEIAEVARKYGAEVPFLRPAELATDTASSI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505228860  83 DCVLHALEWLKlEENYVPDLVCLLQPTSPLRLASDIDGALEMaitlFHEKGIASVVSVTDCVHHPFLVRKQEDDGSLTPF 162
Cdd:cd02513   82 DVILHALDQLE-ELGRDFDIVVLLQPTSPLRSAEDIDEAIEL----LLSEGADSVFSVTEFHRFPWRALGLDDNGLEPVN 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505228860 163 I-EHKISyeRRQDLPVALMRNGAVYVSSTNSLLRDKTFFPDKYYGYYMPYERSLVIDTPIEFSFVEMLL 230
Cdd:cd02513  157 YpEDKRT--RRQDLPPAYHENGAIYIAKREALLESNSFFGGKTGPYEMPRERSIDIDTEEDFELAEALL 223
PseF TIGR03584
pseudaminic acid cytidylyltransferase; The sequences in this family include the pfam02348 ...
 4-231 5.51e-48

pseudaminic acid cytidylyltransferase; The sequences in this family include the pfam02348 (cytidyltransferase) domain and are homologous to the NeuA protein responsible for the transfer of CMP to neuraminic acid. According to, this gene is responsible for the transfer of CMP to the structurally related sugar, pseudaminic acid which is observed as a component of sugar modifications of flagellin in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci.


Pssm-ID: 274660  Cd Length: 222  Bit Score: 157.88  E-value: 5.51e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505228860    4 LGLLTARGGSKGIPGKNYKEIAGKPLITWTAKEALKSSLLGRVVLSTDDLKIADIARSSGVEVPFMRPKYLAEDDSPHID 83
Cdd:TIGR03584   1 IAIIPARGGSKRIPRKNIKPFCGKPMIAYSIEAALNSGLFDKVVVSTDDEEIAEVAKSYGASVPFLRPKELADDFTGTAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505228860   84 CVLHALEWLKLEENYvpDLVCLLQPTSPLRLASDidgaLEMAITLFHEKGIASVVSVTDCVHHPFLVRKQEDDGSLTPFI 163
Cdd:TIGR03584  81 VVKHAIEELKLQKQY--DHACCIYATAPFLQAKI----LKEAFELLKQPNAHFVFSVTSFAFPIQRAFKLKENGGVEMFQ 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505228860  164 -EHKISyeRRQDLPVALMRNGAVYVSSTNSLLRDKTFFPDKYYGYYMPYERSLVIDTPIEFSFVEMLLQ 231
Cdd:TIGR03584 155 pEHFNT--RSQDLEEAYHDAGQFYWGKSQAWLESGPIFSPHSIPIVLPRHLVQDIDTLEDWERAELLYK 221
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 4-232 8.63e-24

Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) 3-deoxy-manno-octulosonate cytidylyltransferase,, EC:2.7.7.38 catalysing the reaction:- CTP + 3-deoxy-D-manno-octulosonate <=> diphosphate + CMP-3-deoxy-D-manno-octulosonate, 2) acylneuraminate cytidylyltransferase EC:2.7.7.43,, catalysing the reaction:- CTP + N-acylneuraminate <=> diphosphate + CMP-N-acylneuraminate. NeuAc cytydilyltransferase of Mannheimia haemolytica has been characterized describing kinetics and regulation by substrate charge, energetic charge and amino-sugar demand.


Pssm-ID: 396773  Cd Length: 217  Bit Score: 94.71  E-value: 8.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505228860    4 LGLLTARGGSKGIPGKNYKEIAGKPLITWTAKEALKSSLLGRVVLSTDDLKIADIARSSGVEVPFMRPKYLAEDDSphid 83
Cdd:pfam02348   1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDR---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505228860   84 cvlhALEWLKLEENYVPDLVCLLQPTSPLRLASDIDGALEMAITLFhEKGIASVVSVTDCVHHPF------LVRKQEDDG 157
Cdd:pfam02348  77 ----FYEVVKAFLNDHDDIIVNIQGDNPLLQPEVILKAIETLLNNG-EPYMSTLVVPVGSAEEVLnanalkVVLDDDGYA 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505228860  158 SLtpFIEHKISYERRQDLPVALMRngavyvsstnslLRDKTFFPdkYYGYYMPYErsLVIDTPIEFSFVEMLLQN 232
Cdd:pfam02348 152 LY--FSRSVIPYIREHPAELYYVY------------LRHIGIYT--FRKNMPLIE--LVIDTPTALEYIEKLEQL 208
PRK05450 PRK05450
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 1-66 3.40e-12

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 235473  Cd Length: 245  Bit Score: 63.98  E-value: 3.40e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505228860   1 MEILGLLTARGGSKGIPGKNYKEIAGKPLITWTAKEALKSSlLGRVVLSTDDLKIADIARSSGVEV 66
Cdd:PRK05450   1 MKFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKAG-ADRVVVATDDERIADAVEAFGGEV 65
 
Name Accession Description Interval E-value
NeuA COG1083
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ...
 1-234 3.93e-97

CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440700  Cd Length: 228  Bit Score: 282.82  E-value: 3.93e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505228860   1 MEILGLLTARGGSKGIPGKNYKEIAGKPLITWTAKEALKSSLLGRVVLSTDDLKIADIARSSGVEVpFMRPKYLAEDDSP 80
Cdd:COG1083    1 MKILAIIPARGGSKGIPGKNIRPLAGKPLIAYSIEAALKSGLFDRVVVSTDDEEIAEVAREYGAEV-FLRPAELAGDTAS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505228860  81 HIDCVLHALEWLKlEENYVPDLVCLLQPTSPLRLASDIDGALEmaitLFHEKGIASVVSVTDCVHHPFLVRKQEDDGSLT 160
Cdd:COG1083   80 TIDVILHALEWLE-EQGEEFDYVVLLQPTSPLRTAEDIDEAIE----LLLESGADSVVSVTEAHHPPYWALKLDEDGRLE 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505228860 161 PFIEHKISYERRQDLPVALMRNGAVYVSSTNSLLRDKTFFPDKYYGYYMPYERSLVIDTPIEFSFVEMLLQNQK 234
Cdd:COG1083  155 PLNPDPHNRPRRQDLPPAYRENGAIYIFKREALLENKSRFGGKTGAYEMPEERSVDIDTEEDFELAEALLKKRK 228
CMP-NeuAc_Synthase cd02513
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ...
 3-230 2.06e-86

CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; CMP-N-acetylneuraminic acid synthetase (CMP-NeuAc synthetase) or acylneuraminate cytidylyltransferase catalyzes the transfer the CMP moiety of CTP to the anomeric hydroxyl group of NeuAc in the presence of Mg++. It is the second to last step in the sialylation of the oligosaccharide component of glycoconjugates by providing the activated sugar-nucleotide cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-Neu5Ac), the substrate for sialyltransferases. Eukaryotic CMP-NeuAc synthetases are predominantly located in the nucleus. The activated CMP-Neu5Ac diffuses from the nucleus into the cytoplasm.


Pssm-ID: 133006  Cd Length: 223  Bit Score: 255.54  E-value: 2.06e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505228860   3 ILGLLTARGGSKGIPGKNYKEIAGKPLITWTAKEALKSSLLGRVVLSTDDLKIADIARSSGVEVPFMRPKYLAEDDSPHI 82
Cdd:cd02513    2 ILAIIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLFDRVVVSTDDEEIAEVARKYGAEVPFLRPAELATDTASSI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505228860  83 DCVLHALEWLKlEENYVPDLVCLLQPTSPLRLASDIDGALEMaitlFHEKGIASVVSVTDCVHHPFLVRKQEDDGSLTPF 162
Cdd:cd02513   82 DVILHALDQLE-ELGRDFDIVVLLQPTSPLRSAEDIDEAIEL----LLSEGADSVFSVTEFHRFPWRALGLDDNGLEPVN 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505228860 163 I-EHKISyeRRQDLPVALMRNGAVYVSSTNSLLRDKTFFPDKYYGYYMPYERSLVIDTPIEFSFVEMLL 230
Cdd:cd02513  157 YpEDKRT--RRQDLPPAYHENGAIYIAKREALLESNSFFGGKTGPYEMPRERSIDIDTEEDFELAEALL 223
PseF TIGR03584
pseudaminic acid cytidylyltransferase; The sequences in this family include the pfam02348 ...
 4-231 5.51e-48

pseudaminic acid cytidylyltransferase; The sequences in this family include the pfam02348 (cytidyltransferase) domain and are homologous to the NeuA protein responsible for the transfer of CMP to neuraminic acid. According to, this gene is responsible for the transfer of CMP to the structurally related sugar, pseudaminic acid which is observed as a component of sugar modifications of flagellin in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci.


Pssm-ID: 274660  Cd Length: 222  Bit Score: 157.88  E-value: 5.51e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505228860    4 LGLLTARGGSKGIPGKNYKEIAGKPLITWTAKEALKSSLLGRVVLSTDDLKIADIARSSGVEVPFMRPKYLAEDDSPHID 83
Cdd:TIGR03584   1 IAIIPARGGSKRIPRKNIKPFCGKPMIAYSIEAALNSGLFDKVVVSTDDEEIAEVAKSYGASVPFLRPKELADDFTGTAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505228860   84 CVLHALEWLKLEENYvpDLVCLLQPTSPLRLASDidgaLEMAITLFHEKGIASVVSVTDCVHHPFLVRKQEDDGSLTPFI 163
Cdd:TIGR03584  81 VVKHAIEELKLQKQY--DHACCIYATAPFLQAKI----LKEAFELLKQPNAHFVFSVTSFAFPIQRAFKLKENGGVEMFQ 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505228860  164 -EHKISyeRRQDLPVALMRNGAVYVSSTNSLLRDKTFFPDKYYGYYMPYERSLVIDTPIEFSFVEMLLQ 231
Cdd:TIGR03584 155 pEHFNT--RSQDLEEAYHDAGQFYWGKSQAWLESGPIFSPHSIPIVLPRHLVQDIDTLEDWERAELLYK 221
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 4-232 8.63e-24

Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) 3-deoxy-manno-octulosonate cytidylyltransferase,, EC:2.7.7.38 catalysing the reaction:- CTP + 3-deoxy-D-manno-octulosonate <=> diphosphate + CMP-3-deoxy-D-manno-octulosonate, 2) acylneuraminate cytidylyltransferase EC:2.7.7.43,, catalysing the reaction:- CTP + N-acylneuraminate <=> diphosphate + CMP-N-acylneuraminate. NeuAc cytydilyltransferase of Mannheimia haemolytica has been characterized describing kinetics and regulation by substrate charge, energetic charge and amino-sugar demand.


Pssm-ID: 396773  Cd Length: 217  Bit Score: 94.71  E-value: 8.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505228860    4 LGLLTARGGSKGIPGKNYKEIAGKPLITWTAKEALKSSLLGRVVLSTDDLKIADIARSSGVEVPFMRPKYLAEDDSphid 83
Cdd:pfam02348   1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDR---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505228860   84 cvlhALEWLKLEENYVPDLVCLLQPTSPLRLASDIDGALEMAITLFhEKGIASVVSVTDCVHHPF------LVRKQEDDG 157
Cdd:pfam02348  77 ----FYEVVKAFLNDHDDIIVNIQGDNPLLQPEVILKAIETLLNNG-EPYMSTLVVPVGSAEEVLnanalkVVLDDDGYA 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505228860  158 SLtpFIEHKISYERRQDLPVALMRngavyvsstnslLRDKTFFPdkYYGYYMPYErsLVIDTPIEFSFVEMLLQN 232
Cdd:pfam02348 152 LY--FSRSVIPYIREHPAELYYVY------------LRHIGIYT--FRKNMPLIE--LVIDTPTALEYIEKLEQL 208
KdsB COG1212
CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; ...
 1-66 2.32e-12

CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; CMP-2-keto-3-deoxyoctulosonic acid synthetase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440825  Cd Length: 242  Bit Score: 64.31  E-value: 2.32e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505228860   1 MEILGLLTARGGSKGIPGKNYKEIAGKPLITWTAKEALKSSLLGRVVLSTDDLKIADIARSSGVEV 66
Cdd:COG1212    1 MKFIVVIPARYASTRLPGKPLADIAGKPMIQRVYERALASKGADRVVVATDDERIADAVEAFGGEV 66
PRK05450 PRK05450
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 1-66 3.40e-12

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 235473  Cd Length: 245  Bit Score: 63.98  E-value: 3.40e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505228860   1 MEILGLLTARGGSKGIPGKNYKEIAGKPLITWTAKEALKSSlLGRVVLSTDDLKIADIARSSGVEV 66
Cdd:PRK05450   1 MKFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKAG-ADRVVVATDDERIADAVEAFGGEV 65
CMP-KDO-Synthetase cd02517
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ...
 3-66 4.74e-12

CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the lipopolysaccharide; CMP-KDO Synthetase: 3-Deoxy-D-manno-octulosonate cytidylyltransferase (CMP-KDO synthetase) catalyzes the conversion of CTP and 3-deoxy-D-manno-octulosonate into CMP-3-deoxy-D-manno-octulosonate (CMP-KDO) and pyrophosphate. KDO is an essential component of the lipopolysaccharide found in the outer surface of gram-negative eubacteria. It is also a constituent of the capsular polysaccharides of some gram-negative eubacteria. Its presence in the cell wall polysaccharides of green algae and plant were also discovered. However, they have not been found in yeast and animals. The absence of the enzyme in mammalian cells makes it an attractive target molecule for drug design.


Pssm-ID: 133010  Cd Length: 239  Bit Score: 63.65  E-value: 4.74e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505228860   3 ILGLLTARGGSKGIPGKNYKEIAGKPLITWTAKEALKSSLLGRVVLSTDDLKIADIARSSGVEV 66
Cdd:cd02517    2 VIVVIPARYASSRLPGKPLADIAGKPMIQHVYERAKKAKGLDEVVVATDDERIADAVESFGGKV 65
SpsF COG1861
Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall ...
 1-66 2.83e-08

Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441466  Cd Length: 245  Bit Score: 52.90  E-value: 2.83e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505228860   1 MEILGLLTARGGSKGIPGKNYKEIAGKPLITWTAKEALKSSLLGRVVLST----DDLKIADIARSSGVEV 66
Cdd:COG1861    2 MKIVAIIQARMGSTRLPGKVLKPLGGKPVLEHVIERLKRSKLIDEVVVATttdpADDPLVDLAKELGVPV 71
PRK13368 PRK13368
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 1-66 6.73e-08

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 184007  Cd Length: 238  Bit Score: 51.50  E-value: 6.73e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505228860   1 MEILGLLTARGGSKGIPGKNYKEIAGKPLITWTAKEALKSSLLGRVVLSTDDLKIADIARSSGVEV 66
Cdd:PRK13368   1 MKVVVVIPARYGSSRLPGKPLLDILGKPMIQHVYERAAQAAGVEEVYVATDDQRIEDAVEAFGGKV 66
PLN02917 PLN02917
CMP-KDO synthetase
 3-125 3.70e-07

CMP-KDO synthetase


Pssm-ID: 215495  Cd Length: 293  Bit Score: 49.83  E-value: 3.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505228860   3 ILGLLTARGGSKGIPGKNYKEIAGKPLITWTAKEALKSSLLGRVVLSTDDLKIADIARSSGVEVPFMrpkylAEDDSPHI 82
Cdd:PLN02917  48 VVGIIPARFASSRFEGKPLVHILGKPMIQRTWERAKLATTLDHIVVATDDERIAECCRGFGADVIMT-----SESCRNGT 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 505228860  83 DCVLHALEwlKLEENYvpDLVCLLQPTSPLRLASDIDG---ALEMA 125
Cdd:PLN02917 123 ERCNEALK--KLEKKY--DIVVNIQGDEPLIEPEIIDGvvkALQAA 164
GT2_SpsF cd02518
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat ...
 4-66 1.39e-06

SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat polysaccharide biosynthesis protein F (spsF) is a glycosyltransferase implicated in the synthesis of the spore coat in a variety of bacteria challenged by stress as starvation. The spsF gene is expressed in the late stage of coat development responsible for a terminal step in coat formation that involves the glycosylation of the coat. SpsF gene mutation resulted in spores that appeared normal. But, the spores tended to aggregate and had abnormal adsorption properties, indicating a surface alteration.


Pssm-ID: 133011  Cd Length: 233  Bit Score: 47.57  E-value: 1.39e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505228860   4 LGLLTARGGSKGIPGKNYKEIAGKPLITWTAKEALKSSLLGRVVLST----DDLKIADIARSSGVEV 66
Cdd:cd02518    1 VAIIQARMGSTRLPGKVLKPLGGKPLLEHLLDRLKRSKLIDEIVIATstneEDDPLEALAKKLGVKV 67
kdsB TIGR00466
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and ...
 6-66 8.93e-06

3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 129558  Cd Length: 238  Bit Score: 45.29  E-value: 8.93e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505228860    6 LLTARGGSKGIPGKNYKEIAGKPLITWTAKEALKsSLLGRVVLSTDDLKIADIARSSGVEV 66
Cdd:TIGR00466   3 IIPARLASSRLPGKPLEDIFGKPMIVHVAENANE-SGADRCIVATDDESVAQTCQKFGIEV 62
 
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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