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Conserved domains on  [gi|644636269|ref|WP_025345200|]
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DVU_1551 family NTP transferase [Sulfurospirillum multivorans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-196 1.27e-66

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


:

Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 208.86  E-value: 1.27e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269   3 KSDMAVLIIAAGYSSRMHDFKPLLPFGETSALKRLIQTYQAHGLEHIYVVVGHRQDEIREVLKEENVTIVYNEEYDKGMF 82
Cdd:COG2068    1 MSKVAAIILAAGASSRMGRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLGVRVVVNPDWEEGMS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269  83 SSIQKGLRAMDEMIHAFYMQPVDIPLIKTQSLERLYEAYASTRKGVIYPTFLGHKGHPPLIDMKYKAQILASNGEGGLKK 162
Cdd:COG2068   81 SSLRAGLAALPADADAVLVLLGDQPLVTAETLRRLLAAFRESPASIVAPTYDGRRGHPVLFSRRLFPELLALTGDQGARA 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 644636269 163 VLEAFHADALHVNVCEQSVLMDMDTKEDYENLLR 196
Cdd:COG2068  161 LLRRHPDRVRLVPVDDPGVLLDIDTPEDLARLLA 194
PRK12703 super family cl28471
tRNA 2'-O-methylase; Reviewed
 203-324 1.38e-07

tRNA 2'-O-methylase; Reviewed


The actual alignment was detected with superfamily member PRK12703:

Pssm-ID: 237176 [Multi-domain]  Cd Length: 339  Bit Score: 52.56  E-value: 1.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269 203 PNKEECLAMMLQNEVPPHIIKHCEAVEKMASNLHEQIVCfgigiDKNALSAAAWVHDIARKEKN---HALVGAQKLRSMG 279
Cdd:PRK12703 170 PDEDQCLDLLKKYGASDLLIRHVKTVYKLAMRIADCINA-----DRRLVAAGALLHDIGRTKTNgidHAVAGAEILRKEN 244

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 644636269 280 -YGAIGEIVATHMDIEI------------DENVPLTANELLFL-ADKLVDEDEVCGFEK 324
Cdd:PRK12703 245 iDDRVVSIVERHIGAGItseeaqklglpvKDYVPETIEEMIVAhADNLFAGDKRLNLKQ 303
 
Name Accession Description Interval E-value
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-196 1.27e-66

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 208.86  E-value: 1.27e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269   3 KSDMAVLIIAAGYSSRMHDFKPLLPFGETSALKRLIQTYQAHGLEHIYVVVGHRQDEIREVLKEENVTIVYNEEYDKGMF 82
Cdd:COG2068    1 MSKVAAIILAAGASSRMGRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLGVRVVVNPDWEEGMS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269  83 SSIQKGLRAMDEMIHAFYMQPVDIPLIKTQSLERLYEAYASTRKGVIYPTFLGHKGHPPLIDMKYKAQILASNGEGGLKK 162
Cdd:COG2068   81 SSLRAGLAALPADADAVLVLLGDQPLVTAETLRRLLAAFRESPASIVAPTYDGRRGHPVLFSRRLFPELLALTGDQGARA 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 644636269 163 VLEAFHADALHVNVCEQSVLMDMDTKEDYENLLR 196
Cdd:COG2068  161 LLRRHPDRVRLVPVDDPGVLLDIDTPEDLARLLA 194
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 6-192 7.90e-53

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: 173.13  E-value: 7.90e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269   6 MAVLIIAAGYSSRMHDFKPLLPFGETSALKRLIQTYQAHGLEHIYVVVGHRQDEIREVLKEENVTIVYNEEYDKGMFSSI 85
Cdd:cd04182    1 IAAIILAAGRSSRMGGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDWEEGMSSSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269  86 QKGLRAMDEMIHAFYMQPVDIPLIKTQSLERLYEAYASTRKGVIYPTFLGHKGHPPLIDMKYKAQILASNGEGGLKKVLE 165
Cdd:cd04182   81 AAGLEALPADADAVLILLADQPLVTAETLRALIDAFREDGAGIVAPVYQGRRGHPVLFPRSLFPELLALSGDKGARSLLR 160

                        170       180
                 ....*....|....*....|....*..
gi 644636269 166 AfHADALHVNVCEQSVLMDMDTKEDYE 192
Cdd:cd04182  161 A-HPDRVVVEVDDPGVLIDIDTPEDLR 186
matur_MocA_YgfJ TIGR03310
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ...
 7-194 2.05e-38

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: 135.93  E-value: 2.05e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269    7 AVLIIAAGYSSRMHDFKPLLPFGETSALKRLIQTYQAHGLEHIYVVVGHRQDEIREVL-KEENVTIVYNEEYDKGMFSSI 85
Cdd:TIGR03310   1 DAIILAAGLSSRMGQNKLLLPYKGKTILEHVVDNALRLFFDEVILVLGHEADELVALLaNHSNITLVHNPQYAEGQSSSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269   86 QKGLRAMDEMIHAFYMqPVDIPLIKTQSLERLYEAYASTRKGVIYPTFLGHKGHPPLIDMKYKAQILASNGEGGLKKVLE 165
Cdd:TIGR03310  81 KLGLELPVQSDGYLFL-LGDQPFVTPDIIQLLLEAFALKNDEIVVPLYKGKRGHPVLFPRKLFPELLALTGDTGGRQILR 159

                         170       180
                  ....*....|....*....|....*....
gi 644636269  166 AFHADALHVNVCEQSVLMDMDTKEDYENL 194
Cdd:TIGR03310 160 ELPHEVKYVEVKDPGILFDIDTPEDYQAL 188
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 8-166 3.95e-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: 123.46  E-value: 3.95e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269    8 VLIIAAGYSSRMHDFKPLLPFGETSALKRLIQTYQAHGlEHIYVVVGHrqDEIREVLKEENVTIVYNEEYDKGMFSSIQK 87
Cdd:pfam12804   1 AVILAGGRSSRMGGDKALLPLGGKPLLERVLERLRPAG-DEVVVVAND--EEVLAALAGLGVPVVPDPDPGQGPLAGLLA 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 644636269   88 GLRAMDEmIHAFYMQPVDIPLIKTQSLERLYEAYASTRKGVIYPTFLGHKGHPPLIDMKYKAQILASNGEGGLKKVLEA 166
Cdd:pfam12804  78 ALRAAPG-ADAVLVLACDMPFLTPELLRRLLAAAEESGADIVVPVYDGGRGHPLLYRRRLLPALEALLGDRGLRRLLRR 155
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-120 3.83e-10

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 60.81  E-value: 3.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269   1 MTKSDMAVLIIAAGYSSRMHDFKP--LLPFGETSALKRLIQTYQAHGLEHIYVVVGHRQDEIREVLKEENVTIVYNEEyD 78
Cdd:PRK09451   1 MLNSAMSVVILAAGKGTRMYSDLPkvLHTLAGKPMVQHVIDAANELGAQHVHLVYGHGGDLLKQTLADEPLNWVLQAE-Q 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 644636269  79 KGMFSSIQKGLR--AMDEMIHAFYMqpvDIPLIKTQSLERLYEA 120
Cdd:PRK09451  80 LGTGHAMQQAAPffADDEDILMLYG---DVPLISVETLQRLRDA 120
PRK12703 PRK12703
tRNA 2'-O-methylase; Reviewed
 203-324 1.38e-07

tRNA 2'-O-methylase; Reviewed


Pssm-ID: 237176 [Multi-domain]  Cd Length: 339  Bit Score: 52.56  E-value: 1.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269 203 PNKEECLAMMLQNEVPPHIIKHCEAVEKMASNLHEQIVCfgigiDKNALSAAAWVHDIARKEKN---HALVGAQKLRSMG 279
Cdd:PRK12703 170 PDEDQCLDLLKKYGASDLLIRHVKTVYKLAMRIADCINA-----DRRLVAAGALLHDIGRTKTNgidHAVAGAEILRKEN 244

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 644636269 280 -YGAIGEIVATHMDIEI------------DENVPLTANELLFL-ADKLVDEDEVCGFEK 324
Cdd:PRK12703 245 iDDRVVSIVERHIGAGItseeaqklglpvKDYVPETIEEMIVAhADNLFAGDKRLNLKQ 303
RnaY COG1418
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ...
 218-313 3.60e-05

HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal structure and biogenesis, General function prediction only];


Pssm-ID: 441028 [Multi-domain]  Cd Length: 191  Bit Score: 44.12  E-value: 3.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269 218 PPHIIKHCEAVEKMASNLHEQIvcfgiGIDKNALSAAAWVHDIAR-----KEKNHALVGAQK----LRSMGYG-----AI 283
Cdd:COG1418   16 GQHDLQHSLRVAKLAGLIAAEE-----GADVEVAKRAALLHDIGKakdheVEGSHAEIGAELarkyLESLGFPeeeieAV 90

                         90       100       110
                 ....*....|....*....|....*....|
gi 644636269 284 GEIVATHMDIEIDENVPLTAnELLFLADKL 313
Cdd:COG1418   91 VHAIEAHSFSGGIEPESLEA-KIVQDADRL 119
HDIG TIGR00277
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ...
 221-290 8.54e-04

HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number of uncharacterized proteins. It contains four widely separated His residues, the second of which is part of an invariant dipeptide His-Asp in a region matched approximately by the motif HDIG. This model may annotate homologous domains in which one or more of the His residues is conserved but misaligned, and some probable false-positive hits.


Pssm-ID: 272994 [Multi-domain]  Cd Length: 80  Bit Score: 37.70  E-value: 8.54e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 644636269  221 IIKHCEAVEKMASNLHEQIvcfgiGIDKNALSAAAWVHDIAR-------KEKNHALVGAQKLRSMGYG-AIGEIVATH 290
Cdd:TIGR00277   5 VLQHSLEVAKLAEALAREL-----GLDVELARRGALLHDIGKpitregvIFESHVVVGAEIARKYGEPlEVIDIIAEH 77
 
Name Accession Description Interval E-value
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-196 1.27e-66

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 208.86  E-value: 1.27e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269   3 KSDMAVLIIAAGYSSRMHDFKPLLPFGETSALKRLIQTYQAHGLEHIYVVVGHRQDEIREVLKEENVTIVYNEEYDKGMF 82
Cdd:COG2068    1 MSKVAAIILAAGASSRMGRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLGVRVVVNPDWEEGMS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269  83 SSIQKGLRAMDEMIHAFYMQPVDIPLIKTQSLERLYEAYASTRKGVIYPTFLGHKGHPPLIDMKYKAQILASNGEGGLKK 162
Cdd:COG2068   81 SSLRAGLAALPADADAVLVLLGDQPLVTAETLRRLLAAFRESPASIVAPTYDGRRGHPVLFSRRLFPELLALTGDQGARA 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 644636269 163 VLEAFHADALHVNVCEQSVLMDMDTKEDYENLLR 196
Cdd:COG2068  161 LLRRHPDRVRLVPVDDPGVLLDIDTPEDLARLLA 194
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 6-192 7.90e-53

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: 173.13  E-value: 7.90e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269   6 MAVLIIAAGYSSRMHDFKPLLPFGETSALKRLIQTYQAHGLEHIYVVVGHRQDEIREVLKEENVTIVYNEEYDKGMFSSI 85
Cdd:cd04182    1 IAAIILAAGRSSRMGGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDWEEGMSSSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269  86 QKGLRAMDEMIHAFYMQPVDIPLIKTQSLERLYEAYASTRKGVIYPTFLGHKGHPPLIDMKYKAQILASNGEGGLKKVLE 165
Cdd:cd04182   81 AAGLEALPADADAVLILLADQPLVTAETLRALIDAFREDGAGIVAPVYQGRRGHPVLFPRSLFPELLALSGDKGARSLLR 160

                        170       180
                 ....*....|....*....|....*..
gi 644636269 166 AfHADALHVNVCEQSVLMDMDTKEDYE 192
Cdd:cd04182  161 A-HPDRVVVEVDDPGVLIDIDTPEDLR 186
matur_MocA_YgfJ TIGR03310
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ...
 7-194 2.05e-38

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: 135.93  E-value: 2.05e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269    7 AVLIIAAGYSSRMHDFKPLLPFGETSALKRLIQTYQAHGLEHIYVVVGHRQDEIREVL-KEENVTIVYNEEYDKGMFSSI 85
Cdd:TIGR03310   1 DAIILAAGLSSRMGQNKLLLPYKGKTILEHVVDNALRLFFDEVILVLGHEADELVALLaNHSNITLVHNPQYAEGQSSSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269   86 QKGLRAMDEMIHAFYMqPVDIPLIKTQSLERLYEAYASTRKGVIYPTFLGHKGHPPLIDMKYKAQILASNGEGGLKKVLE 165
Cdd:TIGR03310  81 KLGLELPVQSDGYLFL-LGDQPFVTPDIIQLLLEAFALKNDEIVVPLYKGKRGHPVLFPRKLFPELLALTGDTGGRQILR 159

                         170       180
                  ....*....|....*....|....*....
gi 644636269  166 AFHADALHVNVCEQSVLMDMDTKEDYENL 194
Cdd:TIGR03310 160 ELPHEVKYVEVKDPGILFDIDTPEDYQAL 188
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 8-166 3.95e-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: 123.46  E-value: 3.95e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269    8 VLIIAAGYSSRMHDFKPLLPFGETSALKRLIQTYQAHGlEHIYVVVGHrqDEIREVLKEENVTIVYNEEYDKGMFSSIQK 87
Cdd:pfam12804   1 AVILAGGRSSRMGGDKALLPLGGKPLLERVLERLRPAG-DEVVVVAND--EEVLAALAGLGVPVVPDPDPGQGPLAGLLA 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 644636269   88 GLRAMDEmIHAFYMQPVDIPLIKTQSLERLYEAYASTRKGVIYPTFLGHKGHPPLIDMKYKAQILASNGEGGLKKVLEA 166
Cdd:pfam12804  78 ALRAAPG-ADAVLVLACDMPFLTPELLRRLLAAAEESGADIVVPVYDGGRGHPLLYRRRLLPALEALLGDRGLRRLLRR 155
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
8-94 8.00e-17

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 78.74  E-value: 8.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269   8 VLIIAAGYSSRMHDF-----KPLLPFGETSALKRLIQTYQAHGLEHIYVVVGHRQDEIREVLKEE--NVTIVYNEEYDK- 79
Cdd:COG1213    2 AVILAAGRGSRLGPLtddipKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARPgpDVTFVYNPDYDEt 81

                         90
                 ....*....|....*
gi 644636269  80 GMFSSIQKGLRAMDE 94
Cdd:COG1213   82 NNIYSLWLAREALDE 96
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 8-94 3.88e-16

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: 76.50  E-value: 3.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269   8 VLIIAAGYSSRMHDF-----KPLLPFGETSALKRLIQTYQAHGLEHIYVVVGHRQDEIREVL-KEENVTIVYNEEYDK-G 80
Cdd:cd02523    1 AIILAAGRGSRLRPLtedrpKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLkKYPNIKFVYNPDYAEtN 80

                         90
                 ....*....|....
gi 644636269  81 MFSSIQKGLRAMDE 94
Cdd:cd02523   81 NIYSLYLARDFLDE 94
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 4-128 1.78e-12

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 68.13  E-value: 1.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269   4 SDMAVLIIAAGYSSRMHDFKP--LLPFGETSALKRLIQTYQAHGLEHIYVVVGHRQDEIREVLKEENVTIVYNEEydkgm 81
Cdd:COG1207    1 SPLAVVILAAGKGTRMKSKLPkvLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALADLDVEFVLQEE----- 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 644636269  82 fssiQKG-----LRAMDEMihAFYMQPV-----DIPLIKTQSLERLYEAYASTRKGV 128
Cdd:COG1207   76 ----QLGtghavQQALPAL--PGDDGTVlvlygDVPLIRAETLKALLAAHRAAGAAA 126
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 8-128 4.85e-12

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: 64.84  E-value: 4.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269   8 VLIIAAGYSSRMHDFKP--LLPFGETSALKRLIQTYQAHGLEHIYVVVGHRQDEIREVLKEENVTIVYNEEydkgmfssi 85
Cdd:cd02540    1 AVILAAGKGTRMKSDLPkvLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANPNVEFVLQEE--------- 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 644636269  86 QKG-----LRAMDEmIHAFY----MQPVDIPLIKTQSLERLYEAYASTRKGV 128
Cdd:cd02540   72 QLGtghavKQALPA-LKDFEgdvlVLYGDVPLITPETLQRLLEAHREAGADV 122
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 6-191 1.07e-11

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: 62.98  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269   6 MAVLIIAAGYSSRM-HDfKPLLPFGETSALKRLIQTYQAHGlEHIYVVVGHRQdeirEVLKEENVTIVYNEEYDKGMFSS 84
Cdd:cd02503    1 ITGVILAGGKSRRMgGD-KALLELGGKPLLEHVLERLKPLV-DEVVISANRDQ----ERYALLGVPVIPDEPPGKGPLAG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269  85 IQKGLRAMDEMiHAFYMqPVDIPLIKTQSLERLYEAYASTRKGVIYPtflgHKGHP-PLIdMKYKAQILAS------NGE 157
Cdd:cd02503   75 ILAALRAAPAD-WVLVL-ACDMPFLPPELLERLLAAAEEGADAVVPK----SGGRLqPLH-ALYHKSLLPAleelleAGE 147

                        170       180       190
                 ....*....|....*....|....*....|....
gi 644636269 158 GGLKKVLEAFHADALHVNVCEQSVLMDMDTKEDY 191
Cdd:cd02503  148 RRLRRLLEKLGVQYVEFEDERLDAFFNINTPEDL 181
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-196 2.85e-11

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: 61.75  E-value: 2.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269   1 MTkSDMAVLIIAAGYSSRMHDFKPLLPFGETSALKRLIQTYQAHgLEHIYVVVghRQDEIREVLkeeNVTIVYNEEYDKG 80
Cdd:COG0746    1 MT-MPITGVILAGGRSRRMGQDKALLPLGGRPLLERVLERLRPQ-VDEVVIVA--NRPERYAAL---GVPVVPDDPPGAG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269  81 MFSSIQKGLRAMDEmiHAFYMQPVDIPLIKTQSLERLYEAYASTRKGVIYPTflghKGHP-PLIdMKYKAQILAS----- 154
Cdd:COG0746   74 PLAGILAALEAAPA--EWVLVLACDMPFLPPDLVRRLLEALEEGADAVVPRS----GGRLePLF-ALYRRSLLPAleaal 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 644636269 155 -NGEGGLKKVLEAFHADALHVNVCEQSvLMDMDTKEDYENLLR 196
Cdd:COG0746  147 aEGERSLRALLERLDVVYVPFEDLDDA-FFNVNTPEDLARAEE 188
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-120 3.83e-10

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 60.81  E-value: 3.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269   1 MTKSDMAVLIIAAGYSSRMHDFKP--LLPFGETSALKRLIQTYQAHGLEHIYVVVGHRQDEIREVLKEENVTIVYNEEyD 78
Cdd:PRK09451   1 MLNSAMSVVILAAGKGTRMYSDLPkvLHTLAGKPMVQHVIDAANELGAQHVHLVYGHGGDLLKQTLADEPLNWVLQAE-Q 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 644636269  79 KGMFSSIQKGLR--AMDEMIHAFYMqpvDIPLIKTQSLERLYEA 120
Cdd:PRK09451  80 LGTGHAMQQAAPffADDEDILMLYG---DVPLISVETLQRLRDA 120
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 8-76 1.52e-08

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 54.77  E-value: 1.52e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 644636269   8 VLIIAAGYSSRMHDF-----KPLLPFGETSALKRLIQTYQAHGLEHIYVVVGHRQDEIREVL---KEENVTIVYNEE 76
Cdd:COG1208    2 AVILAGGLGTRLRPLtdtrpKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFgdgSRFGVRITYVDE 78
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-128 4.08e-08

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 54.56  E-value: 4.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269   4 SDMAVLIIAAGYSSRMHDFKP--LLPFGETSALKRLIQTYQAHGLEHIYVVVGHRQDEIREVLKE--ENVTIVYNEEyDK 79
Cdd:PRK14352   3 RPTAVIVLAAGAGTRMRSDTPkvLHTLAGRSMLGHVLHAAAGLAPQHLVVVVGHDRERVAPAVAElaPEVDIAVQDE-QP 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 644636269  80 GMFSSIQKGLRAMDEMIH-AFYMQPVDIPLIKTQSLERLYEAYASTRKGV 128
Cdd:PRK14352  82 GTGHAVQCALEALPADFDgTVVVTAGDVPLLDGETLADLVATHTAEGNAV 131
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 8-76 6.76e-08

NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 52.58  E-value: 6.76e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 644636269   8 VLIIAAGYSSRM----HDF-KPLLPFGETSALKRLIQTYQAHGLEHIYVVVGHRQDEIREVLKEE-----NVTIVYNEE 76
Cdd:cd04181    1 AVILAAGKGTRLrpltDTRpKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGskfgvNIEYVVQEE 79
PRK12703 PRK12703
tRNA 2'-O-methylase; Reviewed
 203-324 1.38e-07

tRNA 2'-O-methylase; Reviewed


Pssm-ID: 237176 [Multi-domain]  Cd Length: 339  Bit Score: 52.56  E-value: 1.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269 203 PNKEECLAMMLQNEVPPHIIKHCEAVEKMASNLHEQIVCfgigiDKNALSAAAWVHDIARKEKN---HALVGAQKLRSMG 279
Cdd:PRK12703 170 PDEDQCLDLLKKYGASDLLIRHVKTVYKLAMRIADCINA-----DRRLVAAGALLHDIGRTKTNgidHAVAGAEILRKEN 244

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 644636269 280 -YGAIGEIVATHMDIEI------------DENVPLTANELLFL-ADKLVDEDEVCGFEK 324
Cdd:PRK12703 245 iDDRVVSIVERHIGAGItseeaqklglpvKDYVPETIEEMIVAhADNLFAGDKRLNLKQ 303
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-128 2.08e-06

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 49.36  E-value: 2.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269   5 DMAVLIIAAGYSSRMHD--FKPLLPFGETSALKRLIQTYQAHGLEHIYVVVGHRQDEIREVLKE-ENVTIVYNEEyDKGM 81
Cdd:PRK14355   3 NLAAIILAAGKGTRMKSdlVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGdGDVSFALQEE-QLGT 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 644636269  82 FSSIQKGLRAMDEMIHAFYMQPVDIPLIKTQSLERLYEAYASTRKGV 128
Cdd:PRK14355  82 GHAVACAAPALDGFSGTVLILCGDVPLLRAETLQGMLAAHRATGAAV 128
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 7-117 8.48e-06

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 47.41  E-value: 8.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269   7 AVLIIAAGYSSRMHDFKP-----LLpfGET------SALKRLIQtyqahglEHIYVVVGHRQDEIREVLKEENVTIVYNE 75
Cdd:PRK14356   7 GALILAAGKGTRMHSDKPkvlqtLL--GEPmlrfvyRALRPLFG-------DNVWTVVGHRADMVRAAFPDEDARFVLQE 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 644636269  76 EyDKGMFSSIQKglrAMDEMIHAFYMQPV----DIPLIKTQSLERL 117
Cdd:PRK14356  78 Q-QLGTGHALQC---AWPSLTAAGLDRVLvvngDTPLVTTDTIDDF 119
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 6-76 1.26e-05

G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 46.02  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269   6 MAVLIIAAGYSSRMHDF-----KPLLPFGETSALKRLIQTYQAHGLEHIYVVVGHRQDEIREVLKEE-----NVTIVYNE 75
Cdd:cd04189    1 MKGLILAGGKGTRLRPLtytrpKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGsrfgvRITYILQE 80


                 .
gi 644636269  76 E 76
Cdd:cd04189   81 E 81
RnaY COG1418
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ...
 218-313 3.60e-05

HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal structure and biogenesis, General function prediction only];


Pssm-ID: 441028 [Multi-domain]  Cd Length: 191  Bit Score: 44.12  E-value: 3.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269 218 PPHIIKHCEAVEKMASNLHEQIvcfgiGIDKNALSAAAWVHDIAR-----KEKNHALVGAQK----LRSMGYG-----AI 283
Cdd:COG1418   16 GQHDLQHSLRVAKLAGLIAAEE-----GADVEVAKRAALLHDIGKakdheVEGSHAEIGAELarkyLESLGFPeeeieAV 90

                         90       100       110
                 ....*....|....*....|....*....|
gi 644636269 284 GEIVATHMDIEIDENVPLTAnELLFLADKL 313
Cdd:COG1418   91 VHAIEAHSFSGGIEPESLEA-KIVQDADRL 119
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 7-117 6.58e-05

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 44.53  E-value: 6.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269   7 AVLIIAAGYSSRMHDFKP--LLPFGETSALKRLIQTyqAHGL--EHIYVVVGHRQDEIREVLKE-ENVTIVYNEEyDKGM 81
Cdd:PRK14360   3 AVAILAAGKGTRMKSSLPkvLHPLGGKSLVERVLDS--CEELkpDRRLVIVGHQAEEVEQSLAHlPGLEFVEQQP-QLGT 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 644636269  82 FSSIQKGLRAMDEMIHAFYMQPVDIPLIKTQSLERL 117
Cdd:PRK14360  80 GHAVQQLLPVLKGFEGDLLVLNGDVPLLRPETLEAL 115
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-122 2.08e-04

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 42.93  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269   1 MTKSDMAVLIIAAGYSSRMHDFKP--LLPFGETSALKRLIQTYQAHGLEHIYVVVGHRQDEIREVLK--EENVTIVYNEE 76
Cdd:PRK14353   1 MTDRTCLAIILAAGEGTRMKSSLPkvLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAAAAkiAPDAEIFVQKE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 644636269  77 ydkgmfssiQKG----LRAMDEMIHAFYMQPV----DIPLIKTQSLERLYEAYA 122
Cdd:PRK14353  81 ---------RLGtahaVLAAREALAGGYGDVLvlygDTPLITAETLARLRERLA 125
HDIG TIGR00277
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ...
 221-290 8.54e-04

HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number of uncharacterized proteins. It contains four widely separated His residues, the second of which is part of an invariant dipeptide His-Asp in a region matched approximately by the motif HDIG. This model may annotate homologous domains in which one or more of the His residues is conserved but misaligned, and some probable false-positive hits.


Pssm-ID: 272994 [Multi-domain]  Cd Length: 80  Bit Score: 37.70  E-value: 8.54e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 644636269  221 IIKHCEAVEKMASNLHEQIvcfgiGIDKNALSAAAWVHDIAR-------KEKNHALVGAQKLRSMGYG-AIGEIVATH 290
Cdd:TIGR00277   5 VLQHSLEVAKLAEALAREL-----GLDVELARRGALLHDIGKpitregvIFESHVVVGAEIARKYGEPlEVIDIIAEH 77
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 9-129 1.31e-03

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: 39.73  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269   9 LIIAAGYSSRMHDFKP--LLPFGETSALKRLIQTYQAHGL-EHIYVVVG-HRQDEIREVLKEEN----VTIVYNEE--YD 78
Cdd:COG1211    1 IIPAAGSGSRMGAGIPkqFLPLGGKPVLEHTLEAFLAHPRiDEIVVVVPpDDIEYFEELLAKYGidkpVRVVAGGAtrQD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 644636269  79 kgmfsSIQKGLRAMDE-----MIHafymqpvDI--PLIKTQSLERLYEAyASTRKGVI 129
Cdd:COG1211   81 -----SVRNGLEALPDdddwvLVH-------DAarPLVSPELIDRVIEA-AREYGAAI 125
PRK00560 PRK00560
molybdenum cofactor guanylyltransferase MobA;
3-196 4.03e-03

molybdenum cofactor guanylyltransferase MobA;


Pssm-ID: 167003  Cd Length: 196  Bit Score: 38.20  E-value: 4.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269   3 KSDMAVLIIAAGYSSRMHDFKPLLPFGETSALKRliqtYQAHGLEHIYVVVghrqdEIREVLKEENVTIVYNEEYDKGMF 82
Cdd:PRK00560   6 IDNIPCVILAGGKSSRMGENKALLPFGSYSSLLE----YQYTRLLKLFKKV-----YISTKDKKFEFNAPFLLEKESDLF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269  83 SSIQKGLRAMDEM-IHAFYMQPVDIPLIKTQSLERLYE------AYASTRKGVIYPTFLGHKGHPPLIDMKYKAQILAsn 155
Cdd:PRK00560  77 SPLFGIINAFLTLqTPEIFFISVDTPFVSFESIKKLCGkenfsvTYAKSPTKEHYLISLWHQSLLNALIYALKTQNYR-- 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 644636269 156 geggLKKVLEAFHADALHVNVCEQsvLMDMDTKEDYENLLR 196
Cdd:PRK00560 155 ----LSDLVKNTSSQAVHFEDEEE--FLNLNTLKDYELALQ 189
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 6-76 4.67e-03

N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 37.96  E-value: 4.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644636269   6 MAVLIIAAGYSSRMHDF-----KPLLPFGETSALKRLIQTYQAHGLEHIYVVVGHRQDEIREVLKEE----NVTIVYNEE 76
Cdd:cd06425    1 MKALILVGGYGTRLRPLtltvpKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYekklGIKITFSIE 80
 
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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