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Conserved domains on  [gi|756973937|ref|WP_042662255|]
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MULTISPECIES: sugar phosphate nucleotidyltransferase [unclassified Haloferax]

Protein Classification

NDP-sugar synthase; nucleotidyltransferase family protein( domain architecture ID 11440243)

NDP-sugar synthase such as mannose-1-phosphate guanyltransferase and UTP--glucose-1-phosphate uridylyltransferase, which catalyzes the formation of UDP-glucose from UTP and glucose 1-phosphate; nucleotidyltransferase family protein similar to Pseudomonas putida N-acetylmuramic acid alpha-1-phosphate (MurNAc-alpha1-P) uridylyltransferase MurU, which catalyzes the synthesis of uridine diphosphate (UDP)-MurNAc, a crucial precursor of the bacterial peptidoglycan cell wall

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-244 1.13e-64

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: 203.85  E-value: 1.13e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   2 KAVVLAGGYATRLWPITKHRPKMFLPVGDQTVIDTIFEDLEADDrVSEVFVSTNeRFAGAFEEYI-DESPFEkptLSVEd 80
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAG-ITEIVINVG-YLAEQIEEYFgDGSRFG---VRIT- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  81 TSEEDEKFGVVGALAQLIDREEvDEDLVVIAGDNLISFDVGDFVDFFYEKNA-PCLAAYDVgdkERAKSYGLVELDGD-R 158
Cdd:COG1208   75 YVDEGEPLGTGGALKRALPLLG-DEPFLVLNGDILTDLDLAALLAFHREKGAdATLALVPV---PDPSRYGVVELDGDgR 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 159 VINFQEKPEDPKSTLVSIACYAFPADDLpkfdEYLSGDNNPDEPGWFMQWLQQnGDVFAYTFDGAWFDIGTPQSYLDAVA 238
Cdd:COG1208  151 VTRFVEKPEEPPSNLINAGIYVLEPEIF----DYIPEGEPFDLEDLLPRLIAE-GRVYGYVHDGYWLDIGTPEDLLEANA 225


                 ....*.
gi 756973937 239 WYLGGE 244
Cdd:COG1208  226 LLLSGK 231
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 249-302 1.07e-07

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


The actual alignment was detected with superfamily member cd04651:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 104  Bit Score: 49.38  E-value: 1.07e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 756973937 249 ESATLTNTEVGTNVHVMANAVVEDsvleeSVVFPGAVI-RNAELKNSIVDEETHI 302
Cdd:cd04651   22 SGGTVENSVLFRGVRVGSGSVVED-----SVIMPNVGIgRNAVIRRAIIDKNVVI 71
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-244 1.13e-64

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: 203.85  E-value: 1.13e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   2 KAVVLAGGYATRLWPITKHRPKMFLPVGDQTVIDTIFEDLEADDrVSEVFVSTNeRFAGAFEEYI-DESPFEkptLSVEd 80
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAG-ITEIVINVG-YLAEQIEEYFgDGSRFG---VRIT- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  81 TSEEDEKFGVVGALAQLIDREEvDEDLVVIAGDNLISFDVGDFVDFFYEKNA-PCLAAYDVgdkERAKSYGLVELDGD-R 158
Cdd:COG1208   75 YVDEGEPLGTGGALKRALPLLG-DEPFLVLNGDILTDLDLAALLAFHREKGAdATLALVPV---PDPSRYGVVELDGDgR 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 159 VINFQEKPEDPKSTLVSIACYAFPADDLpkfdEYLSGDNNPDEPGWFMQWLQQnGDVFAYTFDGAWFDIGTPQSYLDAVA 238
Cdd:COG1208  151 VTRFVEKPEEPPSNLINAGIYVLEPEIF----DYIPEGEPFDLEDLLPRLIAE-GRVYGYVHDGYWLDIGTPEDLLEANA 225


                 ....*.
gi 756973937 239 WYLGGE 244
Cdd:COG1208  226 LLLSGK 231
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-228 1.93e-56

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: 182.01  E-value: 1.93e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   3 AVVLAGGYATRLWPITKHRPKMFLPVGDQTVIDTIFEDLEADDrVSEVFVSTNERfAGAFEEYIDESPFEKPTLsveDTS 82
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAG-IDEIILVVGYL-GEQIEEYFGDGSKFGVNI---EYV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  83 EEDEKFGVVGALAQLIDREEvDEDLVVIAGDNLISFDVGDFVDFFYEKNApcLAAYDVGDKERAKSYGLVELDGD-RVIN 161
Cdd:cd04181   76 VQEEPLGTAGAVRNAEDFLG-DDDFLVVNGDVLTDLDLSELLRFHREKGA--DATIAVKEVEDPSRYGVVELDDDgRVTR 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 756973937 162 FQEKPEDPKSTLVSIACYAFPADDLPKFDEYLSGdnNPDEPGWFMQWLQQNGDVFAYTFDGAWFDIG 228
Cdd:cd04181  153 FVEKPTLPESNLANAGIYIFEPEILDYIPEILPR--GEDELTDAIPLLIEEGKVYGYPVDGYWLDIG 217
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-236 2.14e-41

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 143.93  E-value: 2.14e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937    2 KAVVLAGGYATRLWPITKHRPK-MFLPVGDQTVIDTIFEDLEADDRVSEVFVSTNERFAGAFEEYIDESPFEkptLSVED 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKpLVPVGGKYPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFG---VQITY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   81 tSEEDEKFGVVGALAQ---LIDREevDEDLVVIAGDNLISFDVGDFVDFFYEKNAPCLAAYDVGDKERAKSYGLVELDGD 157
Cdd:pfam00483  78 -ALQPEGKGTAPAVALaadFLGDE--KSDVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEPPTGYGVVEFDDN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  158 -RVINFQEKPEDPK-STLVSIACYAFPADDLPKFDEYLSGDNN-PDEPGWFMQWLQQNGDVF-AYTFDG-AWFDIGTPQS 232
Cdd:pfam00483 155 gRVIRFVEKPKLPKaSNYASMGIYIFNSGVLDFLAKYLEELKRgEDEITDILPKALEDGKLAyAFIFKGyAWLDVGTWDS 234


                  ....
gi 756973937  233 YLDA 236
Cdd:pfam00483 235 LWEA 238
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 101-316 9.46e-22

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 94.16  E-value: 9.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 101 EEVDEDLVVI-AGDNLISFDVGDFVDFFYEKNAP-CLAAYDVGDKErAKSYGLVELD-GDRVINFQEKPEDPKSTLVSIA 177
Cdd:PRK05293 113 DQYDPEYVLIlSGDHIYKMDYDKMLDYHKEKEADvTIAVIEVPWEE-ASRFGIMNTDeNMRIVEFEEKPKNPKSNLASMG 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 178 CYAFPADDLPKFDEYLSGDNNPDE-------PgwfmQWLQQNGDVFAYTFDGAWFDIGTPQSYLDAVAWYLGGEN----- 245
Cdd:PRK05293 192 IYIFNWKRLKEYLIEDEKNPNSSHdfgknviP----LYLEEGEKLYAYPFKGYWKDVGTIESLWEANMELLRPENplnlf 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 246 ----------------FVHESATLTNTEVG---------------TNVHVMANAVVEDsvleeSVVFPGAVI-RNAELKN 293
Cdd:PRK05293 268 drnwriysvnpnlppqYIAENAKVKNSLVVegcvvygtvehsvlfQGVQVGEGSVVKD-----SVIMPGAKIgENVVIER 342

                        250       260
                 ....*....|....*....|....*....
gi 756973937 294 SIVDEET------HIESLDLSNALIGAHS 316
Cdd:PRK05293 343 AIIGENAvigdgvIIGGGKEVITVIGENE 371
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 249-302 1.07e-07

Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 49.38  E-value: 1.07e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 756973937 249 ESATLTNTEVGTNVHVMANAVVEDsvleeSVVFPGAVI-RNAELKNSIVDEETHI 302
Cdd:cd04651   22 SGGTVENSVLFRGVRVGSGSVVED-----SVIMPNVGIgRNAVIRRAIIDKNVVI 71
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 230-302 1.13e-04

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 43.44  E-value: 1.13e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 756973937 230 PQS-YLDAVAWYLGgENFVHESATLTNTEVGTNVHVMANAVVEDSVLEESVVFPGAVIR-NAELKNsivdeeTHI 302
Cdd:PRK14359 251 PETiYIESGVEFEG-ECELEEGVRILGKSKIENSHIKAHSVIEESIIENSDVGPLAHIRpKSEIKN------THI 318
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 246-318 2.47e-04

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 42.31  E-value: 2.47e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 756973937 246 FVHESAtltntEVGTNVHVMANAVVEDSVL--EESVVFPGAVIrnaeLKNSIVDEETHIEsldlSNALIGAHSRL 318
Cdd:COG1044  104 VIDPSA-----KIGEGVSIGPFAVIGAGVVigDGVVIGPGVVI----GDGVVIGDDCVLH----PNVTIYERCVI 165
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-244 1.13e-64

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: 203.85  E-value: 1.13e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   2 KAVVLAGGYATRLWPITKHRPKMFLPVGDQTVIDTIFEDLEADDrVSEVFVSTNeRFAGAFEEYI-DESPFEkptLSVEd 80
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAG-ITEIVINVG-YLAEQIEEYFgDGSRFG---VRIT- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  81 TSEEDEKFGVVGALAQLIDREEvDEDLVVIAGDNLISFDVGDFVDFFYEKNA-PCLAAYDVgdkERAKSYGLVELDGD-R 158
Cdd:COG1208   75 YVDEGEPLGTGGALKRALPLLG-DEPFLVLNGDILTDLDLAALLAFHREKGAdATLALVPV---PDPSRYGVVELDGDgR 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 159 VINFQEKPEDPKSTLVSIACYAFPADDLpkfdEYLSGDNNPDEPGWFMQWLQQnGDVFAYTFDGAWFDIGTPQSYLDAVA 238
Cdd:COG1208  151 VTRFVEKPEEPPSNLINAGIYVLEPEIF----DYIPEGEPFDLEDLLPRLIAE-GRVYGYVHDGYWLDIGTPEDLLEANA 225


                 ....*.
gi 756973937 239 WYLGGE 244
Cdd:COG1208  226 LLLSGK 231
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-228 1.93e-56

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: 182.01  E-value: 1.93e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   3 AVVLAGGYATRLWPITKHRPKMFLPVGDQTVIDTIFEDLEADDrVSEVFVSTNERfAGAFEEYIDESPFEKPTLsveDTS 82
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAG-IDEIILVVGYL-GEQIEEYFGDGSKFGVNI---EYV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  83 EEDEKFGVVGALAQLIDREEvDEDLVVIAGDNLISFDVGDFVDFFYEKNApcLAAYDVGDKERAKSYGLVELDGD-RVIN 161
Cdd:cd04181   76 VQEEPLGTAGAVRNAEDFLG-DDDFLVVNGDVLTDLDLSELLRFHREKGA--DATIAVKEVEDPSRYGVVELDDDgRVTR 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 756973937 162 FQEKPEDPKSTLVSIACYAFPADDLPKFDEYLSGdnNPDEPGWFMQWLQQNGDVFAYTFDGAWFDIG 228
Cdd:cd04181  153 FVEKPTLPESNLANAGIYIFEPEILDYIPEILPR--GEDELTDAIPLLIEEGKVYGYPVDGYWLDIG 217
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-236 2.14e-41

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 143.93  E-value: 2.14e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937    2 KAVVLAGGYATRLWPITKHRPK-MFLPVGDQTVIDTIFEDLEADDRVSEVFVSTNERFAGAFEEYIDESPFEkptLSVED 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKpLVPVGGKYPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFG---VQITY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   81 tSEEDEKFGVVGALAQ---LIDREevDEDLVVIAGDNLISFDVGDFVDFFYEKNAPCLAAYDVGDKERAKSYGLVELDGD 157
Cdd:pfam00483  78 -ALQPEGKGTAPAVALaadFLGDE--KSDVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEPPTGYGVVEFDDN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  158 -RVINFQEKPEDPK-STLVSIACYAFPADDLPKFDEYLSGDNN-PDEPGWFMQWLQQNGDVF-AYTFDG-AWFDIGTPQS 232
Cdd:pfam00483 155 gRVIRFVEKPKLPKaSNYASMGIYIFNSGVLDFLAKYLEELKRgEDEITDILPKALEDGKLAyAFIFKGyAWLDVGTWDS 234


                  ....
gi 756973937  233 YLDA 236
Cdd:pfam00483 235 LWEA 238
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-241 4.91e-34

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: 124.60  E-value: 4.91e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   1 MKAVVLAGGYATRLWPITKHRPKMFLPVGDQTVIDTIFEDLeADDRVSEVFVSTNErFAGAFEEYI-DESPFEKPTLSVe 79
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDL-REAGIEDIGIVVGP-TGEEIKEALgDGSRFGVRITYI- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  80 dtsEEDEKFGVvgALAQLIDREEV-DEDLVVIAGDNLISFDVGDFVDFFYEKNApclAAY----DVGDKERaksYGLVEL 154
Cdd:cd04189   78 ---LQEEPLGL--AHAVLAARDFLgDEPFVVYLGDNLIQEGISPLVRDFLEEDA---DASillaEVEDPRR---FGVAVV 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 155 DGDRVINFQEKPEDPKSTLVSIACYAFPADDLPKFDEYlsgdnnpdEPGW--------FMQWL-QQNGDVFAYTFDGAWF 225
Cdd:cd04189  147 DDGRIVRLVEKPKEPPSNLALVGVYAFTPAIFDAISRL--------KPSWrgeleitdAIQWLiDRGRRVGYSIVTGWWK 218

                        250
                 ....*....|....*.
gi 756973937 226 DIGTPQSYLDAVAWYL 241
Cdd:cd04189  219 DTGTPEDLLEANRLLL 234
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-313 1.72e-31

Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 121.34  E-value: 1.72e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   3 AVVLAGGYATRLWPITKHRPKMFLPVG------DQTV-------IDTIFedleaddrvseVFV-----STNE-------- 56
Cdd:COG0448    4 AIILAGGRGSRLGPLTKDRAKPAVPFGgkyriiDFPLsncvnsgIRRVG-----------VLTqykshSLNDhigsgkpw 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  57 ----RFAGAFeeyidespfekpTLSVEDTSEEDEKF-GVVGALAQLIDR-EEVDEDLVVI-AGDNLISFDVGDFVDFFYE 129
Cdd:COG0448   73 dldrKRGGVF------------ILPPYQQREGEDWYqGTADAVYQNLDFiERSDPDYVLIlSGDHIYKMDYRQMLDFHIE 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 130 KNAPC-LAAYDVgDKERAKSYGLVELDGD-RVINFQEKPEDPKSTLVSIACYAFPADDLpkfDEYLSGDNNPDEPGwF-- 205
Cdd:COG0448  141 SGADItVACIEV-PREEASRFGVMEVDEDgRITEFEEKPKDPKSALASMGIYVFNKDVL---IELLEEDAPNSSHD-Fgk 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 206 --MQWLQQNGDVFAYTFDGAWFDIGTPQSYLDA---------------VAW------------YLGGENFVHES------ 250
Cdd:COG0448  216 diIPRLLDRGKVYAYEFDGYWRDVGTIDSYYEAnmdlldpepefnlydPEWpiytkqkdlppaKFVRGGKVKNSlvsngc 295

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 756973937 251 ---ATLTNTEVGTNVHVMANAVVEDSVLeesvvFPGAVI-RNAELKNSIVDEETHIEsldlSNALIG 313
Cdd:COG0448  296 iisGTVENSVLFRGVRVESGAVVENSVI-----MPGVVIgEGAVIENAIIDKNVVIP----PGVVIG 353
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 3-233 7.97e-30

WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars.


Pssm-ID: 133065 [Multi-domain]  Cd Length: 223  Bit Score: 113.03  E-value: 7.97e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   3 AVVLAGGYATRLWPITKHRPKMFLPVGDQTVIDTIFEDLEADDrVSEVFVSTNERfAGAFEEYIDESPFEKPTLSVEDts 82
Cdd:cd06915    1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQG-ISRIVLSVGYL-AEQIEEYFGDGYRGGIRIYYVI-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  83 eEDEKFGVVGALAQLIDREEvDEDLVVIAGDNLISFDVGDFVDFFYEKNAP-CLAAYDVGDKERaksYGLVELDGD-RVI 160
Cdd:cd06915   77 -EPEPLGTGGAIKNALPKLP-EDQFLVLNGDTYFDVDLLALLAALRASGADaTMALRRVPDASR---YGNVTVDGDgRVI 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 756973937 161 NFQEKPEDPKSTLVSIACYAFPADDLpkfdEYLSGDNNPDEPGWFMQWLqQNGDVFAYTFDGAWFDIGTPQSY 233
Cdd:cd06915  152 AFVEKGPGAAPGLINGGVYLLRKEIL----AEIPADAFSLEADVLPALV-KRGRLYGFEVDGYFIDIGIPEDY 219
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-268 4.44e-27

dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 107.48  E-value: 4.44e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   1 MKAVVLAGGYATRLWPITKHRPKMFLPVGDQTVIDTIFEDL-EADDRvsEV-FVSTNErFAGAFEEYIDESPFEKPTLSV 78
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLmLAGIR--EIlIISTPE-DGPQFERLLGDGSQLGIKISY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  79 EdtsEEDEKFGvvgaLAQ--LIDREEVDEDLVVIA-GDNLisFDVGDFVDFFYEKNAP----CLAAYDVGDKERaksYGL 151
Cdd:COG1209   78 A---VQPEPLG----LAHafIIAEDFIGGDPVALVlGDNI--FYGDGLSELLREAAAResgaTIFGYKVEDPER---YGV 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 152 VELDGD-RVINFQEKPEDPKSTLVSIACYAFPADdLPKFDEYLsgdnnpdEPGW--------FMQWLQQNGDVFAYTF-D 221
Cdd:COG1209  146 VEFDEDgRVVSLEEKPKEPKSNLAVTGLYFYDND-VVEIAKNL-------KPSArgeleitdANQAYLERGKLVVELLgR 217

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 756973937 222 G-AWFDIGTPQSYLDA--------------------VAWYLG---GENFVHESATLTNTEVGTNVHVMANA 268
Cdd:COG1209  218 GfAWLDTGTHESLLEAnrfvltiekrqglkiacpeeIAYRMGwidAEQLAKLANSLEKSGYGPYLLRLLDS 288
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 3-236 7.43e-24

NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133048 [Multi-domain]  Cd Length: 220  Bit Score: 97.20  E-value: 7.43e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   3 AVVLAGGYATRLWPITKHRPKMFLPVGDQTVIDTIFEDLeADDRVSEVFVSTNERfAGAFEEYI-DESPFekptlSVE-D 80
Cdd:cd06426    1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRF-IAQGFRNFYISVNYL-AEMIEDYFgDGSKF-----GVNiS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  81 TSEEDEKFGVVGALAQLidREEVDEDLVVIAGDNLISFDVGDFVDFFYEKNAP---CLAAYDVgdkerAKSYGLVELDGD 157
Cdd:cd06426   74 YVREDKPLGTAGALSLL--PEKPTDPFLVMNGDILTNLNYEHLLDFHKENNADatvCVREYEV-----QVPYGVVETEGG 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 158 RVINFQEKPEdpKSTLVSIACYAF-PA--DDLPKfDEYLsgdnnpDEPGWFMQWLQQNGDVFAYTFDGAWFDIGTPQSYL 234
Cdd:cd06426  147 RITSIEEKPT--HSFLVNAGIYVLePEvlDLIPK-NEFF------DMPDLIEKLIKEGKKVGVFPIHEYWLDIGRPEDYE 217


                 ..
gi 756973937 235 DA 236
Cdd:cd06426  218 KA 219
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 101-316 9.46e-22

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 94.16  E-value: 9.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 101 EEVDEDLVVI-AGDNLISFDVGDFVDFFYEKNAP-CLAAYDVGDKErAKSYGLVELD-GDRVINFQEKPEDPKSTLVSIA 177
Cdd:PRK05293 113 DQYDPEYVLIlSGDHIYKMDYDKMLDYHKEKEADvTIAVIEVPWEE-ASRFGIMNTDeNMRIVEFEEKPKNPKSNLASMG 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 178 CYAFPADDLPKFDEYLSGDNNPDE-------PgwfmQWLQQNGDVFAYTFDGAWFDIGTPQSYLDAVAWYLGGEN----- 245
Cdd:PRK05293 192 IYIFNWKRLKEYLIEDEKNPNSSHdfgknviP----LYLEEGEKLYAYPFKGYWKDVGTIESLWEANMELLRPENplnlf 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 246 ----------------FVHESATLTNTEVG---------------TNVHVMANAVVEDsvleeSVVFPGAVI-RNAELKN 293
Cdd:PRK05293 268 drnwriysvnpnlppqYIAENAKVKNSLVVegcvvygtvehsvlfQGVQVGEGSVVKD-----SVIMPGAKIgENVVIER 342

                        250       260
                 ....*....|....*....|....*....
gi 756973937 294 SIVDEET------HIESLDLSNALIGAHS 316
Cdd:PRK05293 343 AIIGENAvigdgvIIGGGKEVITVIGENE 371
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-237 1.51e-19

Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity.


Pssm-ID: 133021 [Multi-domain]  Cd Length: 267  Bit Score: 86.43  E-value: 1.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   1 MKAVVLAGGYATRLWPITKHRPKMFLPVGDQTVIDTIFEdlEA-DDRVSEVFVSTNERfAGAFEEYIDESPFekptlsVE 79
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVE--EAvAAGIEDIIIVTGRG-KRAIEDHFDRSYE------LE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  80 DTSEEDEKFG---VVGALAQLID-------------------REEV-DEDLVVIAGDNLISFDVG---DFVDFFYEKNAP 133
Cdd:cd02541   72 ETLEKKGKTDlleEVRIISDLANihyvrqkeplglghavlcaKPFIgDEPFAVLLGDDLIDSKEPclkQLIEAYEKTGAS 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 134 CLAAYDVgDKERAKSYGLVELDGD-----RVINFQEKP--EDPKSTLVSIACYAFPaddlPKFDEYLSgDNNPDEPGWF- 205
Cdd:cd02541  152 VIAVEEV-PPEDVSKYGIVKGEKIdgdvfKVKGLVEKPkpEEAPSNLAIVGRYVLT----PDIFDILE-NTKPGKGGEIq 225

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 756973937 206 ----MQWLQQNGDVFAYTFDGAWFDIGTPQSYLDAV 237
Cdd:cd02541  226 ltdaIAKLLEEEPVYAYVFEGKRYDCGNKLGYLKAT 261
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-248 7.70e-18

G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short 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 homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. 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.


Pssm-ID: 133019 [Multi-domain]  Cd Length: 240  Bit Score: 81.08  E-value: 7.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   1 MKAVVLAGGYATRLWPITKHRPKMFLPVGDQTVI-DTIFEDLEADDRvsEVFVSTNERFAGAFEEYI-DESPFekptlSV 78
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIyYPLSTLMLAGIR--EILIISTPEDLPLFKELLgDGSDL-----GI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  79 EDTSEEDEKfgvVGALAQ--LIDREEV-DEDLVVIAGDNLIsFDVG--DFVDFFYEKNA-PCLAAYDVGDKERaksYGLV 152
Cdd:cd02538   74 RITYAVQPK---PGGLAQafIIGEEFIgDDPVCLILGDNIF-YGQGlsPILQRAAAQKEgATVFGYEVNDPER---YGVV 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 153 ELDGD-RVINFQEKPEDPKSTLVSIACYAFPAD--DLPKfdeylsgDNNPDEPGWF------MQWLQQNG-DVFAYTFDG 222
Cdd:cd02538  147 EFDENgRVLSIEEKPKKPKSNYAVTGLYFYDNDvfEIAK-------QLKPSARGELeitdvnNEYLEKGKlSVELLGRGF 219

                        250       260
                 ....*....|....*....|....*.
gi 756973937 223 AWFDIGTPQSYLDAVawylggeNFVH 248
Cdd:cd02538  220 AWLDTGTHESLLEAS-------NFVQ 238
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-241 1.43e-17

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: 80.33  E-value: 1.43e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   1 MKAVVLAGGYATRLWPITKHRPKMFLPVGDQTVIDTIFEDLeADDRVSEVFVSTNERfAGAFEEYIDEspFEKpTLSVE- 79
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEAL-AKAGVKEIILAVNYR-PEDMVPFLKE--YEK-KLGIKi 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  80 DTSEEDEKFGVVGALAQLIDR-EEVDEDLVVIAGDNLISFDVGDFVDFfyEKNAPCLAAYDVGDKERAKSYGLVELDGD- 157
Cdd:cd06425   76 TFSIETEPLGTAGPLALARDLlGDDDEPFFVLNSDVICDFPLAELLDF--HKKHGAEGTILVTKVEDPSKYGVVVHDENt 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 158 -RVINFQEKPEDPKSTLVSIACYAFPADDLpkfdeylsgDNNPDEP----GWFMQWLQQNGDVFAYTFDGAWFDIGTPQS 232
Cdd:cd06425  154 gRIERFVEKPKVFVGNKINAGIYILNPSVL---------DRIPLRPtsieKEIFPKMASEGQLYAYELPGFWMDIGQPKD 224


                 ....*....
gi 756973937 233 YLDAVAWYL 241
Cdd:cd06425  225 FLKGMSLYL 233
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-236 2.74e-16

NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 76.46  E-value: 2.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   2 KAVVLAGGYATRLWPITKHRPKMFLPVGDQTVIDTIFEDLeADDRVSEVFVSTNeRFAGAFEEYIDESpFEKPTLSVEDt 81
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRL-AAAGIRRIVVNTH-HLADQIEAHLGDS-RFGLRITISD- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  82 sEEDEKFGVVGALAQ---LIDreevDEDLVVIAGDNLISFDVGDFVDFFYEKNAPCLAAYDVGDKERAKSYGLVELDGDR 158
Cdd:cd06422   77 -EPDELLETGGGIKKalpLLG----DEPFLVVNGDILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFSLDADG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 159 VINFQEKPEDPKSTLVSIACYAfPA--DDLPkfDEYLSgdNNPdepgWFMQWLQQnGDVFAYTFDGAWFDIGTPQSYLDA 236
Cdd:cd06422  152 RLRRGGGGAVAPFTFTGIQILS-PElfAGIP--PGKFS--LNP----LWDRAIAA-GRLFGLVYDGLWFDVGTPERLLAA 221
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 3-302 3.34e-16

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 78.71  E-value: 3.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   3 AVVLAGGYATRLWPITKHRPKMFLPVGDQ-TVIDTIFEDLeADDRVSEVFV-------------STNERFAGAFEEYIDE 68
Cdd:PRK00844   8 AIVLAGGEGKRLMPLTADRAKPAVPFGGSyRLIDFVLSNL-VNSGYLRIYVltqykshsldrhiSQTWRLSGLLGNYITP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  69 SP---------FEkptlsvedtseedekfGVVGALAQ---LIDREevDEDLVVIAG-DNLISFDVGDFVDFFYEKNAPC- 134
Cdd:PRK00844  87 VPaqqrlgkrwYL----------------GSADAIYQslnLIEDE--DPDYVVVFGaDHVYRMDPRQMVDFHIESGAGVt 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 135 LAAYDVgDKERAKSYGLVELDGD-RVINFQEKPEDPKS-------TLVSIACYAFPADDLpkFDEYLSGDNNPDEP---- 202
Cdd:PRK00844 149 VAAIRV-PREEASAFGVIEVDPDgRIRGFLEKPADPPGlpddpdeALASMGNYVFTTDAL--VDALRRDAADEDSShdmg 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 203 GWFMQWLQQNGDVFAYTFD------------GAWFDIGTPQSYLDA----------------------------VAWYLG 242
Cdd:PRK00844 226 GDIIPRLVERGRAYVYDFStnevpgaterdrGYWRDVGTIDAYYDAhmdllsvhpvfnlynrewpiytsspnlpPAKFVD 305

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 756973937 243 GENFV---HES----------ATLTNTEVGTNVHVMANAVVEDSVLEESVVF-PGAVIRNAEL-KNSIVDEETHI 302
Cdd:PRK00844 306 GGGRVgsaQDSlvsagsiisgATVRNSVLSPNVVVESGAEVEDSVLMDGVRIgRGAVVRRAILdKNVVVPPGATI 380
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 3-304 3.36e-15

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 75.69  E-value: 3.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   3 AVVLAGGYATRLWPITKHRPKMFLPVG------DQTVIDTIFEDLEaddrvsEVFVSTN----------------ERFAG 60
Cdd:PRK02862   6 AIILGGGAGTRLYPLTKLRAKPAVPLAgkyrliDIPISNCINSGIN------KIYVLTQfnsaslnrhisqtynfDGFSG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  61 AFEEyidespfekpTLSVEDTSEEDEKF-GVVGALAQ---LIDREEVDEDLVvIAGDNLISFDVGDFVDFFYEKNAP-CL 135
Cdd:PRK02862  80 GFVE----------VLAAQQTPENPSWFqGTADAVRKylwHFQEWDVDEYLI-LSGDQLYRMDYRLFVQHHRETGADiTL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 136 AAYDVgDKERAKSYGLVELDGD-RVINFQEKPEDP---------------------KSTLVSIACYAFPADDLPKFdeyL 193
Cdd:PRK02862 149 AVLPV-DEKDASGFGLMKTDDDgRITEFSEKPKGDelkamavdtsrlglspeeakgKPYLASMGIYVFSRDVLFDL---L 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 194 sgDNNPDE--------PgwfmqwlQQNGD--VFAYTFDGAWFDIGTPQSYLDA-VAwyLGGE-----NFVHESATLTnte 257
Cdd:PRK02862 225 --NKNPEYtdfgkeiiP-------EAIRDykVQSYLFDGYWEDIGTIEAFYEAnLA--LTQQpnppfSFYDEKAPIY--- 290

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 756973937 258 vgTNVHVMANAVVEDSVLEESVVFPGAVIRNAELKNSIVDEETHIES 304
Cdd:PRK02862 291 --TRARYLPPSKLLDATITESIIAEGCIIKNCSIHHSVLGIRSRIES 335
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 3-302 3.51e-15

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 75.65  E-value: 3.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   3 AVVLAGGYATRLWPITKHRPKMFLPVGDQT-VIDtifedleaddrvsevFVSTN------------------------ER 57
Cdd:PRK00725  18 ALILAGGRGSRLKELTDKRAKPAVYFGGKFrIID---------------FALSNcinsgirrigvltqykahslirhiQR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  58 ----FAGAFEEYIDESPFEKptlsveDTSEEDEKFGVVGALAQLID--REEVDEDLVVIAGDNLISFDVGDFVDFFYEKN 131
Cdd:PRK00725  83 gwsfFREELGEFVDLLPAQQ------RVDEENWYRGTADAVYQNLDiiRRYDPKYVVILAGDHIYKMDYSRMLADHVESG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 132 APC-LAAYDVgDKERAKSYGLVELDGD-RVINFQEKPEDPKS-------TLVSIACYAFPADDLpkFDEYLSGDNNPDEP 202
Cdd:PRK00725 157 ADCtVACLEV-PREEASAFGVMAVDENdRITAFVEKPANPPAmpgdpdkSLASMGIYVFNADYL--YELLEEDAEDPNSS 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 203 GWF----MQWLQQNGDVFAYTFDGA-----------WFDIGTPQSY----LDAVA-----------W----YlgGEN--- 245
Cdd:PRK00725 234 HDFgkdiIPKIVEEGKVYAHPFSDScvrsdpeeepyWRDVGTLDAYwqanLDLASvtpeldlydrnWpiwtY--QEQlpp 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 246 --FVHES--------------------ATLTNTEVGTNVHVMANAVVEDSVLeesvvFPGAVI-RNAELKNSIVDEETHI 302
Cdd:PRK00725 312 akFVFDRsgrrgmainslvsggciisgAVVRRSVLFSRVRVNSFSNVEDSVL-----LPDVNVgRSCRLRRCVIDRGCVI 386
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-174 1.68e-12

The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 65.37  E-value: 1.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   1 MKAVVLAGGYATRLWPITKHRPKMFLPVGDQTVIDTIFEDLEADDrVSEVFVSTNERFAGAFEEYIDESPFEKPTLSVED 80
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAG-FEDVIVVVPEEEQAEISTYLRSFPLNLKQKLDEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  81 TSEEDEKFGVVGALaQLIdREEVDEDLVVIAGDNLISFDVGDFVDFFYEKNAPCLAAYD-----------VGDKERAKSY 149
Cdd:cd04198   80 TIVLDEDMGTADSL-RHI-RKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYpppvsseqkggKGKSKKADER 157

                        170       180
                 ....*....|....*....|....*.
gi 756973937 150 GLVELDG-DRVINFQEKPEDPKSTLV 174
Cdd:cd04198  158 DVIGLDEkTQRLLFITSEEDLDEDLE 183
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 1-117 8.32e-12

The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 63.43  E-value: 8.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   1 MKAVVLAGGYATRLWPITKHRPKMFLPVGDQTVIDTIFEDLEADDrVSEVFVSTNERFAGAFEEYIDESPFEKPTLSVED 80
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAG-VEEVFVVCCEHSQAIIEHLLKSKWSSLSSKMIVD 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 756973937  81 --TSEEDEKFGvvGALAQLIDREEVDEDLVVIAGDnLIS 117
Cdd:cd02507   80 viTSDLCESAG--DALRLRDIRGLIRSDFLLLSCD-LVS 115
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 3-304 2.01e-11

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 64.49  E-value: 2.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   3 AVVLAGGYATRLWPITKHRPKMFLPVG-DQTVIDTIFEDLEADDrVSEVFV-------STNERFAGAFEeYIDESPFEKP 74
Cdd:PLN02241   6 AIILGGGAGTRLFPLTKRRAKPAVPIGgNYRLIDIPMSNCINSG-INKIYVltqfnsaSLNRHLSRAYN-FGNGGNFGDG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  75 tlSVE-----DTSEEDEKF-GVVGALAQLI-----DREEVDEDLVVIAGDNLISFDVGDFVDFFYEKNAP-CLAAYDVGD 142
Cdd:PLN02241  84 --FVEvlaatQTPGEKGWFqGTADAVRQFLwlfedAKNKNVEEVLILSGDHLYRMDYMDFVQKHRESGADiTIACLPVDE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 143 kERAKSYGLVELDGD-RVINFQEKPE----------------DP-----KSTLVSIACYAFPADDLPKF-DEYLSGDNN- 198
Cdd:PLN02241 162 -SRASDFGLMKIDDTgRIIEFSEKPKgdelkamqvdttvlglSPeeakeKPYIASMGIYVFKKDVLLKLlRWRFPTANDf 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 199 -----PdepgwfmQWLQQNGDVFAYTFDGAWFDIGTPQSYLDA---VAWYLGGENFvHESATLTNTevgtnvhvMAN--- 267
Cdd:PLN02241 241 gseiiP-------GAIKEGYNVQAYLFDGYWEDIGTIKSFYEAnlaLTKQPPKFSF-YDPDAPIYT--------SPRflp 304

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 756973937 268 -AVVEDSVLEESVVFPGAVIRNAELKNSIVDEETHIES 304
Cdd:PLN02241 305 pSKIEDCRITDSIISHGCFLRECKIEHSVVGLRSRIGE 342
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-237 8.01e-11

UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 61.59  E-value: 8.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   2 KAVVLAGGYATRLWPITKHRPKMFLPVGDQTVIDTIFEdlEAD----DRVseVFV-STNERfagAFEEYIDESPfekptl 76
Cdd:COG1210    5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVE--EAVaagiEEI--IFVtGRGKR---AIEDHFDRSY------ 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  77 SVEDTSEE---DEKFGVVGALAQLID-------------------REEV-DEDLVVIAGDNLISFDVGDF---VDFFYEK 130
Cdd:COG1210   72 ELEATLEAkgkEELLEEVRSISPLANihyvrqkeplglghavlcaRPFVgDEPFAVLLGDDLIDSEKPCLkqmIEVYEET 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 131 NAPCLAAYDVgDKERAKSYGLVELDGD-----RVINFQEKP--EDPKSTLVSIACYAFPaddlPKFDEYLsgDNNPdePG 203
Cdd:COG1210  152 GGSVIAVQEV-PPEEVSKYGIVDGEEIeggvyRVTGLVEKPapEEAPSNLAIVGRYILT----PEIFDIL--EKTK--PG 222

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 756973937 204 -----WF---MQWLQQNGDVFAYTFDGAWFDIGTPQSYLDAV 237
Cdd:COG1210  223 aggeiQLtdaIAALAKEEPVYAYEFEGKRYDCGDKLGYLKAT 264
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-240 5.17e-10

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 58.71  E-value: 5.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   2 KAVVLAGGYATRLWPITKHRPKMFLPVGDQTVIDTIFEDLEADDrVSEVFVSTNERfAGAFEEYIDESPFEKPTLSVEDT 81
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAG-IKDIVVVTGYK-AELIEEALARPGPDVTFVYNPDY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  82 seedEKFGVVGALAQLidREEVDEDLVVIAGDnlISFDVGDFVDFFYEKNAPCLA---AYDVGDKERAKsyglVELD-GD 157
Cdd:COG1213   79 ----DETNNIYSLWLA--REALDEDFLLLNGD--VVFDPAILKRLLASDGDIVLLvdrKWEKPLDEEVK----VRVDeDG 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 158 RVINFQEKPEDPKSTLVSIACYAFPADDLPKFDEYLSGDNNPDEPGWFM-----QWLQQNGDVFA-YTFDGAWFDIGTPQ 231
Cdd:COG1213  147 RIVEIGKKLPPEEADGEYIGIFKFSAEGAAALREALEALIDEGGPNLYYedalqELIDEGGPVKAvDIGGLPWVEIDTPE 226


                 ....*....
gi 756973937 232 SYLDAVAWY 240
Cdd:COG1213  227 DLERAEELF 235
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-125 1.11e-09

GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 58.36  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   1 MKAVVLAGGYATRLWPI-TKHRPKMFLPV-GDQTVIDTIFEDLEADDRVSEVFVSTNERFAGAFEEYIDESpFEKPTLSV 78
Cdd:cd02509    1 IYPVILAGGSGTRLWPLsRESYPKQFLKLfGDKSLLQQTLDRLKGLVPPDRILVVTNEEYRFLVREQLPEG-LPEENIIL 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 756973937  79 E----DTseedekFGVVGALAQLIDREEVDEDLVVIAGDNLISfDVGDFVD 125
Cdd:cd02509   80 EpegrNT------APAIALAALYLAKRDPDAVLLVLPSDHLIE-DVEAFLK 123
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-240 3.06e-09

N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. 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 that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH 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 including cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 56.88  E-value: 3.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   3 AVVLAGG--YATRLWPITKHRPKMFLPVGDQTVIDTIFEDLEADDRVSEVFVstnerfAGAFEEyidespfEKPTLSVED 80
Cdd:cd06428    1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLL------IGFYPE-------SVFSDFISD 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  81 TSE----------EDEKFGVVGALAQLID--REEVDEDLVVIAGDNLISFDVGDFVDFFYEKNAPCLAAYDVGDKERAKS 148
Cdd:cd06428   68 AQQefnvpirylqEYKPLGTAGGLYHFRDqiLAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASREQASN 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 149 YG-LVE-LDGDRVINFQEKPEDPKSTLVSIACYAFPAD-----DLPKFDEYLSGDNNPDEPGWFMQ---WLQQ------- 211
Cdd:cd06428  148 YGcIVEdPSTGEVLHYVEKPETFVSDLINCGVYLFSPEifdtiKKAFQSRQQEAQLGDDNNREGRAeviRLEQdvltpla 227

                        250       260       270
                 ....*....|....*....|....*....|
gi 756973937 212 -NGDVFAYTFDGAWFDIGTPQSYLDAVAWY 240
Cdd:cd06428  228 gSGKLYVYKTDDFWSQIKTAGSAIYANRLY 257
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-70 7.21e-09

Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 56.23  E-value: 7.21e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 756973937   1 MKAVVLAGGYATRLWPI-TKHRPKMFLP-VGDQTVIDTIFEDLEADDRVSEVFVSTNERFAGAFEEYIDESP 70
Cdd:COG0836    3 IYPVILAGGSGTRLWPLsRESYPKQFLPlLGEKSLLQQTVERLAGLVPPENILVVTNEEHRFLVAEQLPELG 74
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 3-231 3.20e-08

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: 53.39  E-value: 3.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   3 AVVLAGGYATRLWPITKHRPKMFLPVGDQTVIDTIFEDLEADDrVSEVFVSTNERFAgAFEEYIDESPfeKPTLsVEdtS 82
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAG-IDDIVIVTGYKKE-QIEELLKKYP--NIKF-VY--N 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  83 EEDEKFGVVGALAQLidREEVDEDLVVIAGDNLisFDVgDFVDFFYEKNAPCLAAYDVGDKERAKSYGLVELDGDRVINF 162
Cdd:cd02523   74 PDYAETNNIYSLYLA--RDFLDEDFLLLEGDVV--FDP-SILERLLSSPADNAILVDKKTKEWEDEYVKDLDDAGVLLGI 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 756973937 163 QEKPEDPKSTL-VSIACYAFPADDLPKFDEYLSGDNNPDEPGWFM----QWLQQNGDVFAYT-FDGAWFDIGTPQ 231
Cdd:cd02523  149 ISKAKNLEEIQgEYVGISKFSPEDADRLAEALEELIEAGRVNLYYedalQRLISEEGVKVKDiSDGFWYEIDDLE 223
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-176 4.55e-08

The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of epsilon subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133040 [Multi-domain]  Cd Length: 217  Bit Score: 52.61  E-value: 4.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   3 AVVLAGGYATRLWPITKHRPKMFLPVGDQTVIDTIFEDLEADDrVSEVFVstnerFAGA----FEEYIDESPFEKPTLSV 78
Cdd:cd04197    3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNG-VEEVFV-----FCCShsdqIKEYIEKSKWSKPKSSL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  79 ED----TSEEDEKFGvvGALAQLIDREEVDEDLVVIAGDNLISFDVGDFVDFFYE-----KNAPCLAAY-DVGDKERAKS 148
Cdd:cd04197   77 MIviiiMSEDCRSLG--DALRDLDAKGLIRGDFILVSGDVVSNIDLKEILEEHKErrkkdKNAIMTMVLkEASPPHRTRR 154

                        170       180       190
                 ....*....|....*....|....*....|...
gi 756973937 149 YG---LVELD--GDRVINFQEKPEDPKSTLVSI 176
Cdd:cd04197  155 TGeefVIAVDpkTSRLLHYEELPGSKYRSITDL 187
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 249-302 1.07e-07

Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 49.38  E-value: 1.07e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 756973937 249 ESATLTNTEVGTNVHVMANAVVEDsvleeSVVFPGAVI-RNAELKNSIVDEETHI 302
Cdd:cd04651   22 SGGTVENSVLFRGVRVGSGSVVED-----SVIMPNVGIgRNAVIRRAIIDKNVVI 71
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-113 1.31e-06

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: 47.57  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937    3 AVVLAGGYATRLwpitkHRPKMFLPVGDQTVIDTIFEDLEAddRVSEVFVSTNERfagAFEEYIDESPFEKptlsVEDTS 82
Cdd:pfam12804   1 AVILAGGRSSRM-----GGDKALLPLGGKPLLERVLERLRP--AGDEVVVVANDE---EVLAALAGLGVPV----VPDPD 66

                          90       100       110
                  ....*....|....*....|....*....|.
gi 756973937   83 EEDekfGVVGALAQLIDREEVDEDLVVIAGD 113
Cdd:pfam12804  67 PGQ---GPLAGLLAALRAAPGADAVLVLACD 94
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-57 4.32e-06

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: 46.34  E-value: 4.32e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 756973937   1 MKAVVLAGGYATRLWpitkhRPKMFLPVGDQTVIDTIFEDLEADdrVSEVFVSTNER 57
Cdd:COG0746    5 ITGVILAGGRSRRMG-----QDKALLPLGGRPLLERVLERLRPQ--VDEVVIVANRP 54
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 3-227 5.22e-06

ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2.


Pssm-ID: 133002 [Multi-domain]  Cd Length: 200  Bit Score: 46.38  E-value: 5.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937   3 AVVLAGGYATRLWPITKHRPKMFLPVG------DQTV-------IDTIFedleaddrvseVFVSTNER------------ 57
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFGgryrliDFPLsnmvnsgIRNVG-----------VLTQYKSRslndhlgsgkew 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937  58 FAGAFEEYIDESPFekptlsvEDTSEEDEKFGVVGALAQLIDR-EEVDEDLVVIA-GDNLISFDVGDFVDFFYEKNAPCL 135
Cdd:cd02508   70 DLDRKNGGLFILPP-------QQRKGGDWYRGTADAIYQNLDYiERSDPEYVLILsGDHIYNMDYREMLDFHIESGADIT 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 136 AAYdvgdkeraksyglveldgdrvinfqekpedpkstLVSIACYAFPADDLPKFDEYLSGDNNPDEPGWFMQWLQQNGDV 215
Cdd:cd02508  143 VVY----------------------------------KASMGIYIFSKDLLIELLEEDAADGSHDFGKDIIPAMLKKLKI 188

                        250
                 ....*....|..
gi 756973937 216 FAYTFDGAWFDI 227
Cdd:cd02508  189 YAYEFNGYWADI 200
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 241-316 2.88e-05

N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 43.95  E-value: 2.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 241 LGGENFVHESATLTNTEVGTNVHVMANAVVEDSVLEESVV---F----PGAVIRNA-------ELKNSIVDEETHIESLD 306
Cdd:cd03353   36 IGEDCVIGPNCVIKDSTIGDGVVIKASSVIEGAVIGNGATvgpFahlrPGTVLGEGvhignfvEIKKSTIGEGSKANHLS 115

                         90
                 ....*....|.
gi 756973937 307 -LSNALIGAHS 316
Cdd:cd03353  116 yLGDAEIGEGV 126
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 230-302 1.13e-04

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 43.44  E-value: 1.13e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 756973937 230 PQS-YLDAVAWYLGgENFVHESATLTNTEVGTNVHVMANAVVEDSVLEESVVFPGAVIR-NAELKNsivdeeTHI 302
Cdd:PRK14359 251 PETiYIESGVEFEG-ECELEEGVRILGKSKIENSHIKAHSVIEESIIENSDVGPLAHIRpKSEIKN------THI 318
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 1-74 1.98e-04

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: 41.41  E-value: 1.98e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 756973937   1 MKAVVLAGGYATRLwpitkHRPKMFLPVGDQTVIDTIFEDLEAddRVSEVFVSTNERFAGAFEEYI----DESPFEKP 74
Cdd:cd02503    1 ITGVILAGGKSRRM-----GGDKALLELGGKPLLEHVLERLKP--LVDEVVISANRDQERYALLGVpvipDEPPGKGP 71
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 246-318 2.47e-04

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 42.31  E-value: 2.47e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 756973937 246 FVHESAtltntEVGTNVHVMANAVVEDSVL--EESVVFPGAVIrnaeLKNSIVDEETHIEsldlSNALIGAHSRL 318
Cdd:COG1044  104 VIDPSA-----KIGEGVSIGPFAVIGAGVVigDGVVIGPGVVI----GDGVVIGDDCVLH----PNVTIYERCVI 165
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 4-79 2.89e-04

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: 41.27  E-value: 2.89e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 756973937   4 VVLAGGYATRLwpiTKHRPKMFLPVGDQTVID-TIfEDLEADDRVSEVFVSTNERFAGAFEEYIDESPFEKPTLSVE 79
Cdd:COG1211    1 IIPAAGSGSRM---GAGIPKQFLPLGGKPVLEhTL-EAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGIDKPVRVVA 73
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 269-320 7.84e-04

Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 38.21  E-value: 7.84e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 756973937 269 VVEDSVLEESVVFPGAVI-RNAELKNSIVdeethiesldLSNALIGAHSRLTN 320
Cdd:cd04651   20 IISGGTVENSVLFRGVRVgSGSVVEDSVI----------MPNVGIGRNAVIRR 62
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 240-322 1.65e-03

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 36.84  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973937 240 YLGGENFVHESATLTNTEVGTNVHVMANAVVEDSVLEESVVfpgaVIRNAELKNSIVDEethiesldlsNALIGAHSRLT 319
Cdd:cd03356    1 LIGESTVIGENAIIKNSVIGDNVRIGDGVTITNSILMDNVT----IGANSVIVDSIIGD----------NAVIGENVRVV 66


                 ...
gi 756973937 320 NGQ 322
Cdd:cd03356   67 NLC 69
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 255-302 6.83e-03

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: 38.08  E-value: 6.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 756973937 255 NTEVGTNVHVMANAVVEDSVLEEsvvfpGAVIRNAELKNSIVDEETHI 302
Cdd:COG1207  284 KTVIGEGVVIGPNCTLKDSTIGD-----GVVIKYSVIEDAVVGAGATV 326
 
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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