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Conserved domains on  [gi|488285390|ref|WP_002356598|]
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MULTISPECIES: molybdenum cofactor cytidylyltransferase [Enterococcus]

Protein Classification

molybdenum cofactor cytidylyltransferase( domain architecture ID 10799133)

molybdenum cofactor cytidylyltransferase transfers a CMP moiety from CTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin cytosine dinucleotide (Mo-MCD) cofactor

EC:  2.7.7.76
Gene Ontology:  GO:0061602|GO:0000287|GO:0006777|GO:0000166

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
matur_MocA_YgfJ TIGR03310
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ...
 5-187 8.32e-84

molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which transfers cytosine from CTP to molybdopterin during molybdopterin cytosine dinucleotide (MCD) cofactor biosynthesis. It is distantly related to MobA, the GTP:molybdopterin guanylyltransferase. The MocA family is particularly closely related in phylogenetic distribution to other markers of selenium-dependent molybdenum hydroxylases (SDMH), suggesting most SDMH must use MCD rather than molybdopterin guanine dinucleotide.


:

Pssm-ID: 274516  Cd Length: 188  Bit Score: 245.71  E-value: 8.32e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390    5 SVIILASGNSQRMGQNKLFLKYQGKTFLEHTLTLVNQLDVLERILVVSPENQPAFPL---PKNIQLILNHQWQEGQSSSI 81
Cdd:TIGR03310   1 DAIILAAGLSSRMGQNKLLLPYKGKTILEHVVDNALRLFFDEVILVLGHEADELVALlanHSNITLVHNPQYAEGQSSSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390   82 RLGTE-QARGAGYLYLPSDQPLLTPKMLQPVLD--KCQRNKIVVPLQKDGCPsSPVLFGNQFRQELLTLTGEKGGRMIYE 158
Cdd:TIGR03310  81 KLGLElPVQSDGYLFLLGDQPFVTPDIIQLLLEafALKNDEIVVPLYKGKRG-HPVLFPRKLFPELLALTGDTGGRQILR 159

                         170       180
                  ....*....|....*....|....*....
gi 488285390  159 RFPEAVQMLRIATPGRLKDIDTPEEYRKL 187
Cdd:TIGR03310 160 ELPHEVKYVEVKDPGILFDIDTPEDYQAL 188
 
Name Accession Description Interval E-value
matur_MocA_YgfJ TIGR03310
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ...
 5-187 8.32e-84

molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which transfers cytosine from CTP to molybdopterin during molybdopterin cytosine dinucleotide (MCD) cofactor biosynthesis. It is distantly related to MobA, the GTP:molybdopterin guanylyltransferase. The MocA family is particularly closely related in phylogenetic distribution to other markers of selenium-dependent molybdenum hydroxylases (SDMH), suggesting most SDMH must use MCD rather than molybdopterin guanine dinucleotide.


Pssm-ID: 274516  Cd Length: 188  Bit Score: 245.71  E-value: 8.32e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390    5 SVIILASGNSQRMGQNKLFLKYQGKTFLEHTLTLVNQLDVLERILVVSPENQPAFPL---PKNIQLILNHQWQEGQSSSI 81
Cdd:TIGR03310   1 DAIILAAGLSSRMGQNKLLLPYKGKTILEHVVDNALRLFFDEVILVLGHEADELVALlanHSNITLVHNPQYAEGQSSSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390   82 RLGTE-QARGAGYLYLPSDQPLLTPKMLQPVLD--KCQRNKIVVPLQKDGCPsSPVLFGNQFRQELLTLTGEKGGRMIYE 158
Cdd:TIGR03310  81 KLGLElPVQSDGYLFLLGDQPFVTPDIIQLLLEafALKNDEIVVPLYKGKRG-HPVLFPRKLFPELLALTGDTGGRQILR 159

                         170       180
                  ....*....|....*....|....*....
gi 488285390  159 RFPEAVQMLRIATPGRLKDIDTPEEYRKL 187
Cdd:TIGR03310 160 ELPHEVKYVEVKDPGILFDIDTPEDYQAL 188
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 4-185 1.47e-59

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 184.30  E-value: 1.47e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390   4 VSVIILASGNSQRMGQNKLFLKYQGKTFLEHTLTLVNQLDvLERILVVSPENQPAFPLPK---NIQLILNHQWQEGQSSS 80
Cdd:cd04182    1 IAAIILAAGRSSRMGGNKLLLPLDGKPLLRHALDAALAAG-LSRVIVVLGAEADAVRAALaglPVVVVINPDWEEGMSSS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390  81 IRLGTEQARG--AGYLYLPSDQPLLTPKMLQPVLDKCQRN--KIVVPLQKdGCPSSPVLFGNQFRQELLTLTGEKGGRMI 156
Cdd:cd04182   80 LAAGLEALPAdaDAVLILLADQPLVTAETLRALIDAFREDgaGIVAPVYQ-GRRGHPVLFPRSLFPELLALSGDKGARSL 158

                        170       180
                 ....*....|....*....|....*....
gi 488285390 157 YERFPEAVQmLRIATPGRLKDIDTPEEYR 185
Cdd:cd04182  159 LRAHPDRVV-VEVDDPGVLIDIDTPEDLR 186
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-190 8.57e-59

CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 182.67  E-value: 8.57e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390   1 MSLVSVIILASGNSQRMGQNKLFLKYQGKTFLEHTLTLVNQLDVLERILVVSPENQPAFPL--PKNIQLILNHQWQEGQS 78
Cdd:COG2068    1 MSKVAAIILAAGASSRMGRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAAlaGLGVRVVVNPDWEEGMS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390  79 SSIRLGTEQARGA--GYLYLPSDQPLLTPKMLQPVLDKCQRN--KIVVPlQKDGCPSSPVLFGNQFRQELLTLTGEKGGR 154
Cdd:COG2068   81 SSLRAGLAALPADadAVLVLLGDQPLVTAETLRRLLAAFRESpaSIVAP-TYDGRRGHPVLFSRRLFPELLALTGDQGAR 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 488285390 155 MIYERFPEAVQMLRIATPGRLKDIDTPEEYRKLIQE 190
Cdd:COG2068  160 ALLRRHPDRVRLVPVDDPGVLLDIDTPEDLARLLAR 195
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 6-163 2.17e-34

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 119.22  E-value: 2.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390    6 VIILASGNSQRMGQNKLFLKYQGKTFLEHTLTLVnqLDVLERILVVSPENQPAFPLPK-NIQLILNHQWQEGQSSSIRLG 84
Cdd:pfam12804   1 AVILAGGRSSRMGGDKALLPLGGKPLLERVLERL--RPAGDEVVVVANDEEVLAALAGlGVPVVPDPDPGQGPLAGLLAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390   85 TEQARGAGYLY-LPSDQPLLTPKMLQPVLDKCQRNK--IVVPlQKDGCPSSPVLFGNQFRQELLTLTGEKGGRMIYERFP 161
Cdd:pfam12804  79 LRAAPGADAVLvLACDMPFLTPELLRRLLAAAEESGadIVVP-VYDGGRGHPLLYRRRLLPALEALLGDRGLRRLLRRLD 157


                  ..
gi 488285390  162 EA 163
Cdd:pfam12804 158 EV 159
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
1-123 8.81e-10

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 55.91  E-value: 8.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390   1 MSLVSVIILASGNSQRMG--QNKLFLKYQGKTFLEHTLTLVNQLDVLERILVVSPENQPAFPLPKNIQLILNHQWQEGQS 78
Cdd:PRK00155   1 MMMVYAIIPAAGKGSRMGadRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAKDPKVTVVAGGA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488285390  79 S---SIRlgteqargAGYLYLPSDQ---------PLLTPKMLQPVLDKCQRNKIVVP 123
Cdd:PRK00155  81 ErqdSVL--------NGLQALPDDDwvlvhdaarPFLTPDDIDRLIEAAEETGAAIL 129
 
Name Accession Description Interval E-value
matur_MocA_YgfJ TIGR03310
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ...
 5-187 8.32e-84

molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which transfers cytosine from CTP to molybdopterin during molybdopterin cytosine dinucleotide (MCD) cofactor biosynthesis. It is distantly related to MobA, the GTP:molybdopterin guanylyltransferase. The MocA family is particularly closely related in phylogenetic distribution to other markers of selenium-dependent molybdenum hydroxylases (SDMH), suggesting most SDMH must use MCD rather than molybdopterin guanine dinucleotide.


Pssm-ID: 274516  Cd Length: 188  Bit Score: 245.71  E-value: 8.32e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390    5 SVIILASGNSQRMGQNKLFLKYQGKTFLEHTLTLVNQLDVLERILVVSPENQPAFPL---PKNIQLILNHQWQEGQSSSI 81
Cdd:TIGR03310   1 DAIILAAGLSSRMGQNKLLLPYKGKTILEHVVDNALRLFFDEVILVLGHEADELVALlanHSNITLVHNPQYAEGQSSSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390   82 RLGTE-QARGAGYLYLPSDQPLLTPKMLQPVLD--KCQRNKIVVPLQKDGCPsSPVLFGNQFRQELLTLTGEKGGRMIYE 158
Cdd:TIGR03310  81 KLGLElPVQSDGYLFLLGDQPFVTPDIIQLLLEafALKNDEIVVPLYKGKRG-HPVLFPRKLFPELLALTGDTGGRQILR 159

                         170       180
                  ....*....|....*....|....*....
gi 488285390  159 RFPEAVQMLRIATPGRLKDIDTPEEYRKL 187
Cdd:TIGR03310 160 ELPHEVKYVEVKDPGILFDIDTPEDYQAL 188
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 4-185 1.47e-59

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 184.30  E-value: 1.47e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390   4 VSVIILASGNSQRMGQNKLFLKYQGKTFLEHTLTLVNQLDvLERILVVSPENQPAFPLPK---NIQLILNHQWQEGQSSS 80
Cdd:cd04182    1 IAAIILAAGRSSRMGGNKLLLPLDGKPLLRHALDAALAAG-LSRVIVVLGAEADAVRAALaglPVVVVINPDWEEGMSSS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390  81 IRLGTEQARG--AGYLYLPSDQPLLTPKMLQPVLDKCQRN--KIVVPLQKdGCPSSPVLFGNQFRQELLTLTGEKGGRMI 156
Cdd:cd04182   80 LAAGLEALPAdaDAVLILLADQPLVTAETLRALIDAFREDgaGIVAPVYQ-GRRGHPVLFPRSLFPELLALSGDKGARSL 158

                        170       180
                 ....*....|....*....|....*....
gi 488285390 157 YERFPEAVQmLRIATPGRLKDIDTPEEYR 185
Cdd:cd04182  159 LRAHPDRVV-VEVDDPGVLIDIDTPEDLR 186
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-190 8.57e-59

CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 182.67  E-value: 8.57e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390   1 MSLVSVIILASGNSQRMGQNKLFLKYQGKTFLEHTLTLVNQLDVLERILVVSPENQPAFPL--PKNIQLILNHQWQEGQS 78
Cdd:COG2068    1 MSKVAAIILAAGASSRMGRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAAlaGLGVRVVVNPDWEEGMS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390  79 SSIRLGTEQARGA--GYLYLPSDQPLLTPKMLQPVLDKCQRN--KIVVPlQKDGCPSSPVLFGNQFRQELLTLTGEKGGR 154
Cdd:COG2068   81 SSLRAGLAALPADadAVLVLLGDQPLVTAETLRRLLAAFRESpaSIVAP-TYDGRRGHPVLFSRRLFPELLALTGDQGAR 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 488285390 155 MIYERFPEAVQMLRIATPGRLKDIDTPEEYRKLIQE 190
Cdd:COG2068  160 ALLRRHPDRVRLVPVDDPGVLLDIDTPEDLARLLAR 195
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 6-163 2.17e-34

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 119.22  E-value: 2.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390    6 VIILASGNSQRMGQNKLFLKYQGKTFLEHTLTLVnqLDVLERILVVSPENQPAFPLPK-NIQLILNHQWQEGQSSSIRLG 84
Cdd:pfam12804   1 AVILAGGRSSRMGGDKALLPLGGKPLLERVLERL--RPAGDEVVVVANDEEVLAALAGlGVPVVPDPDPGQGPLAGLLAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390   85 TEQARGAGYLY-LPSDQPLLTPKMLQPVLDKCQRNK--IVVPlQKDGCPSSPVLFGNQFRQELLTLTGEKGGRMIYERFP 161
Cdd:pfam12804  79 LRAAPGADAVLvLACDMPFLTPELLRRLLAAAEESGadIVVP-VYDGGRGHPLLYRRRLLPALEALLGDRGLRRLLRRLD 157


                  ..
gi 488285390  162 EA 163
Cdd:pfam12804 158 EV 159
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 4-184 4.86e-17

MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 74.92  E-value: 4.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390   4 VSVIILASGNSQRMGQNKLFLKYQGKTFLEHTLTLVNQLDvlERILVVSPENQPAFPLPkNIQLILNHQWQEGQSSSIRL 83
Cdd:cd02503    1 ITGVILAGGKSRRMGGDKALLELGGKPLLEHVLERLKPLV--DEVVISANRDQERYALL-GVPVIPDEPPGKGPLAGILA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390  84 GTEQARGAGYLYLPSDQPLLTPKMLQPVLDK-CQRNKIVVPLQKDGcpSSPvLFG---NQFRQELLTLTGEKGGRMIyeR 159
Cdd:cd02503   78 ALRAAPADWVLVLACDMPFLPPELLERLLAAaEEGADAVVPKSGGR--LQP-LHAlyhKSLLPALEELLEAGERRLR--R 152

                        170       180
                 ....*....|....*....|....*....
gi 488285390 160 FPEAVQMLRIATPGRLKD----IDTPEEY 184
Cdd:cd02503  153 LLEKLGVQYVEFEDERLDaffnINTPEDL 181
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 4-189 4.26e-16

Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 72.53  E-value: 4.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390   4 VSVIILASGNSQRMGQNKLFLKYQGKTFLEHTLTLVNQldVLERILVVSPENQ--PAFPLPkniqLILNHQWQEGQSSSI 81
Cdd:COG0746    5 ITGVILAGGRSRRMGQDKALLPLGGRPLLERVLERLRP--QVDEVVIVANRPEryAALGVP----VVPDDPPGAGPLAGI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390  82 RLGTEQARGAGYLYLPSDQPLLTPKMLQPVLDKCQRN-KIVVPLQKDGC-PsspvLFG---NQFRQELLTLTGEKGGRMI 156
Cdd:COG0746   79 LAALEAAPAEWVLVLACDMPFLPPDLVRRLLEALEEGaDAVVPRSGGRLeP----LFAlyrRSLLPALEAALAEGERSLR 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 488285390 157 yeRFPEAVQMLRIATP---GRLKDIDTPEEYRKLIQ 189
Cdd:COG0746  155 --ALLERLDVVYVPFEdldDAFFNVNTPEDLARAEE 188
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 7-123 6.30e-10

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440824  Cd Length: 224  Bit Score: 56.29  E-value: 6.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390   7 IILASGNSQRMGQ--NKLFLKYQGKTFLEHTLTLVNQLDVLERILVVSPENQPA--------FPLPKNIQLIlnhqwqEG 76
Cdd:COG1211    1 IIPAAGSGSRMGAgiPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEyfeellakYGIDKPVRVV------AG 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390  77 QSS---SIRlgteqargAGYLYLPSDQ----------PLLTPKMLQPVLDKCQRNKIVVP 123
Cdd:COG1211   75 GATrqdSVR--------NGLEALPDDDdwvlvhdaarPLVSPELIDRVIEAAREYGAAIP 126
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
1-123 8.81e-10

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 55.91  E-value: 8.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390   1 MSLVSVIILASGNSQRMG--QNKLFLKYQGKTFLEHTLTLVNQLDVLERILVVSPENQPAFPLPKNIQLILNHQWQEGQS 78
Cdd:PRK00155   1 MMMVYAIIPAAGKGSRMGadRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAKDPKVTVVAGGA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488285390  79 S---SIRlgteqargAGYLYLPSDQ---------PLLTPKMLQPVLDKCQRNKIVVP 123
Cdd:PRK00155  81 ErqdSVL--------NGLQALPDDDwvlvhdaarPFLTPDDIDRLIEAAEETGAAIL 129
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 4-123 9.94e-10

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 55.61  E-value: 9.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390   4 VSVIILASGNSQRMGQ--NKLFLKYQGKTFLEHTLTLVNQLDVLERILVVSPE-------NQPAFPLPKNIQLIlnhqwq 74
Cdd:cd02516    1 VAAIILAAGSGSRMGAdiPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPddidlakELAKYGLSKVVKIV------ 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488285390  75 EGQSS---SIRLGTEQARGAGYLY-LPSD--QPLLTPKMLQPVLDKCQRNKIVVP 123
Cdd:cd02516   75 EGGATrqdSVLNGLKALPDADPDIvLIHDaaRPFVSPELIDRLIDALKEYGAAIP 129
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 1-187 1.68e-08

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 52.11  E-value: 1.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390   1 MSLVSVIILASGNSQRM-GQNKLFLKYQGKTFLEHTL-TLVNQLDvleRILVVSPENQPAF----------PLPKNIqli 68
Cdd:PRK00317   1 MPPITGVILAGGRSRRMgGVDKGLQELNGKPLIQHVIeRLAPQVD---EIVINANRNLARYaafglpvipdSLADFP--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390  69 lnhqwqeGQSSSIRLGTEQARGAGYLYLPSDQPLLTPKMLQPVLDKCQRNKIVVPLQKDGCPSSPV--LFGNQFRQELLT 146
Cdd:PRK00317  75 -------GPLAGILAGLKQARTEWVLVVPCDTPFIPPDLVARLAQAAGKDDADVAWAHDGGRLHPTfaLYSVALLPDLEA 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 488285390 147 LTgEKGGRMIyERFPEAVQMLRIATPG---RLKDIDTPEEYRKL 187
Cdd:PRK00317 148 YL-AAGERKV-MAFYARHGGVAVDFSDpkdAFFNINTPEDLAQL 189
PRK02726 PRK02726
molybdenum cofactor guanylyltransferase;
1-109 6.51e-08

molybdenum cofactor guanylyltransferase;


Pssm-ID: 235063  Cd Length: 200  Bit Score: 50.42  E-value: 6.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390   1 MSLVSVIILASGNSQRMGQNKLFLKYQGKTFLEHTLTLVNQldVLERILVVSPEN---QPAfpLPKNIQLILNHQWQEGQ 77
Cdd:PRK02726   5 KNNLVALILAGGKSSRMGQDKALLPWQGVPLLQRVARIAAA--CADEVYIITPWPeryQSL--LPPGCHWLREPPPSQGP 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 488285390  78 SSSIRLGTEQARGAGYLYLPSDQPLLTPKMLQ 109
Cdd:PRK02726  81 LVAFAQGLPQIKTEWVLLLACDLPRLTVDVLQ 112
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 6-68 2.25e-07

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes which catalyze the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP).


Pssm-ID: 460075  Cd Length: 219  Bit Score: 48.99  E-value: 2.25e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488285390    6 VIILASGNSQRM--GQNKLFLKYQGKTFLEHTLTLVNQLDVLERI-LVVSPENQPAF---PLPKNIQLI 68
Cdd:pfam01128   1 AVIPAAGSGKRMgaGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIvVAVSPDDTPEFrqlLGDPSIQLV 69
PRK14490 PRK14490
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; ...
 7-190 3.64e-05

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; Provisional


Pssm-ID: 237728 [Multi-domain]  Cd Length: 369  Bit Score: 43.11  E-value: 3.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390   7 IILASGNSQRMGQNKLFLKYQGKTFLEHTLTLVNQldVLERILVVSPENQPAFPLPKNIQLILNHQWQEGQSSSIRLGTE 86
Cdd:PRK14490 178 LVLAGGRSSRMGSDKALLSYHESNQLVHTAALLRP--HCQEVFISCRAEQAEQYRSFGIPLITDSYLDIGPLGGLLSAQR 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390  87 QARGAGYLYLPSDQPLLTPKMLQPVLDkcQRNkivvplqkdgcpssPVLFGNQFRQE-------LLTLTGEKGGRMIYER 159
Cdd:PRK14490 256 HHPDAAWLVVACDLPFLDEATLQQLVE--GRN--------------PFRFATAFRHPdsgrpepLCAIYEPKSRLRLLLR 319

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 488285390 160 FPEA------------VQMLRIATPGRLKDIDTPEEYRKLIQE 190
Cdd:PRK14490 320 HAAGnnslrsflatsrIEELEPTDPEALQNINDPEEMDRAERA 362
PRK14489 PRK14489
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ...
 1-183 8.50e-05

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional


Pssm-ID: 237727 [Multi-domain]  Cd Length: 366  Bit Score: 42.05  E-value: 8.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390   1 MSLVSVIILASGNSQRM-GQNKLFLKYQGKTFLEHTL-TLVNQLDVLERILVVSPE--NQPAFPLPKNIQLILNHQwqeG 76
Cdd:PRK14489   3 ISQIAGVILAGGLSRRMnGRDKALILLGGKPLIERVVdRLRPQFARIHLNINRDPAryQDLFPGLPVYPDILPGFQ---G 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390  77 QSSSIRLGTEQARGAGYLYLPSDQPLLTPKMLQPVLDKCQRN--KIVVPlqKDGCPSSPvLFGNQFRQELLTLTG--EKG 152
Cdd:PRK14489  80 PLSGILAGLEHADSEYLFVVACDTPFLPENLVKRLSKALAIEgaDIAVP--HDGERAHP-LFALYHRSCLPALRRylAEG 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 488285390 153 GRMIYERFPEA-VQMLRIATPGR-LKDIDTPEE 183
Cdd:PRK14489 157 ERRLFDFFQRQrVRYVDLSTQKDaFFNVNTPED 189
PLN02728 PLN02728
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
 4-59 7.90e-04

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase


Pssm-ID: 215387  Cd Length: 252  Bit Score: 38.94  E-value: 7.90e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488285390   4 VSVIILASGNSQRMGQN--KLFLKYQGKTFLEHTL-TLVNQLDVLERILVVSPENQPAF 59
Cdd:PLN02728  25 VSVILLAGGVGKRMGANmpKQYLPLLGQPIALYSLyTFARMPEVKEIVVVCDPSYRDVF 83
PRK14500 PRK14500
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MoaC/MobA; ...
 7-120 8.75e-04

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MoaC/MobA; Provisional


Pssm-ID: 237734 [Multi-domain]  Cd Length: 346  Bit Score: 39.11  E-value: 8.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390   7 IILASGNSQRMGQNKLFLKYQGKTFLEHTLTLVNQldVLERILVVSPENQPAFPLPKNIQLILNHQWQEGQSSSIRLGTE 86
Cdd:PRK14500 164 LVLTGGKSRRMGKDKALLNYQGQPHAQYLYDLLAK--YCEQVFLSARPSQWQGTPLENLPTLPDRGESVGPISGILTALQ 241

                         90       100       110
                 ....*....|....*....|....*....|....
gi 488285390  87 QARGAGYLYLPSDQPLLTPKMLQPVLDKCQRNKI 120
Cdd:PRK14500 242 SYPGVNWLVVACDLAYLNSETVEKLLAHYRQDLV 275
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
6-186 2.47e-03

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 37.53  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390   6 VIILASGNSQRMGQN-----KLFLKYQGKTFLEHTLTLVNQLDVLERILVVSPEN----QPAFPLPKNIQLILNHQWQE- 75
Cdd:COG1213    2 AVILAAGRGSRLGPLtddipKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAelieEALARPGPDVTFVYNPDYDEt 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390  76 GQSSSIRLGTEQARGaGYLYLPSDQpLLTPKMLQPVLDKCQRNKIVVP--------------LQKDGC--------PSSP 133
Cdd:COG1213   82 NNIYSLWLAREALDE-DFLLLNGDV-VFDPAILKRLLASDGDIVLLVDrkwekpldeevkvrVDEDGRiveigkklPPEE 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488285390 134 VL------------FGNQFRQELLTLTGEKGGRMIYERfpeAVQMLrIATPGRLK----------DIDTPEEYRK 186
Cdd:COG1213  160 ADgeyigifkfsaeGAAALREALEALIDEGGPNLYYED---ALQEL-IDEGGPVKavdigglpwvEIDTPEDLER 230
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 6-122 6.41e-03

N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 36.34  E-value: 6.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285390   6 VIILASGNSQRMGQN--KLFLKYQGKTFLEHTLTLVNQLDVlERILVV----SPENQPAFPLPkNIQLILnhqwQEGQss 79
Cdd:cd02540    1 AVILAAGKGTRMKSDlpKVLHPLAGKPMLEHVLDAARALGP-DRIVVVvghgAEQVKKALANP-NVEFVL----QEEQ-- 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488285390  80 sirLGT----EQARGA--GY----LYLPSDQPLLTPKMLQPVLDK--CQRNKIVV 122
Cdd:cd02540   73 ---LGTghavKQALPAlkDFegdvLVLYGDVPLITPETLQRLLEAhrEAGADVTV 124
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 6-75 7.26e-03

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 36.06  E-value: 7.26e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488285390   6 VIILASGNSQRMG---QN--KLFLKYQGKTFLEHTLTLVNQLDVLERILVVSPEN---QPAFPLPKNIQLILNHQWQE 75
Cdd:cd02523    1 AIILAAGRGSRLRpltEDrpKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKeqiEELLKKYPNIKFVYNPDYAE 78
 
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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