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Conserved domains on  [gi|162287102|ref|NP_001104747|]
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translation initiation factor eIF2B subunit gamma isoform 1 [Mus musculus]

Protein Classification

translation initiation factor eIF-2B subunit gamma( domain architecture ID 10135962)

translation initiation factor eIF-2B subunit gamma is an essential component of the the translation initiation factor 2B (eIF-2B), a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex

CATH:  2.160.10.10
EC:  2.4.-.-
Gene Ontology:  GO:0005851|GO:0003743|GO:0005085
PubMed:  9438375|10521532|12691742|9445404|11747907|15500694|7893825
SCOP:  3000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-212 8.17e-102

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: 302.66  E-value: 8.17e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   3 FQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTKDVQKALCAEFKM-----KMKLDIVC 77
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSfplnlKQKLDEVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102  78 IPDEADMGTADSLRHIYPKLKTDVLVLSCDLITDVALHEVVDLFRAYDASLAMLMRKGQESIEPVPGqKGKKKPVEQRDF 157
Cdd:cd04198   81 IVLDEDMGTADSLRHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSEQKGG-KGKSKKADERDV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 162287102 158 IGVDSTGKRLLFMANEADLDEELVIKGSILQKHPRIHFHTGLVDAHLYCLKKYVV 212
Cdd:cd04198  160 IGLDEKTQRLLFITSEEDLDEDLELRKSLLKRHPRVTITTKLLDAHVYIFKRWVL 214
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 357-437 1.50e-32

eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


:

Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 118.45  E-value: 1.50e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102 357 LIGPDTQIGEKSSIKHSVIGSSCVIRDRTSITNCLLMNSVTVEEGSSIHGSVICNNAVIETGAEIKNCLVGSGQRIEAKA 436
Cdd:cd04652    1 LVGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAGT 80


                 .
gi 162287102 437 K 437
Cdd:cd04652   81 E 81
 
Name Accession Description Interval E-value
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-212 8.17e-102

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: 302.66  E-value: 8.17e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   3 FQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTKDVQKALCAEFKM-----KMKLDIVC 77
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSfplnlKQKLDEVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102  78 IPDEADMGTADSLRHIYPKLKTDVLVLSCDLITDVALHEVVDLFRAYDASLAMLMRKGQESIEPVPGqKGKKKPVEQRDF 157
Cdd:cd04198   81 IVLDEDMGTADSLRHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSEQKGG-KGKSKKADERDV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 162287102 158 IGVDSTGKRLLFMANEADLDEELVIKGSILQKHPRIHFHTGLVDAHLYCLKKYVV 212
Cdd:cd04198  160 IGLDEKTQRLLFITSEEDLDEDLELRKSLLKRHPRVTITTKLLDAHVYIFKRWVL 214
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 357-437 1.50e-32

eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 118.45  E-value: 1.50e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102 357 LIGPDTQIGEKSSIKHSVIGSSCVIRDRTSITNCLLMNSVTVEEGSSIHGSVICNNAVIETGAEIKNCLVGSGQRIEAKA 436
Cdd:cd04652    1 LVGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAGT 80


                 .
gi 162287102 437 K 437
Cdd:cd04652   81 E 81
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 4-134 2.15e-27

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: 109.47  E-value: 2.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   4 QAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTT--KDVQKALCAEFKmKMKLDIVCIPDE 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGylAEQIEEYFGDGS-RFGVRITYVDEG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 162287102  82 ADMGTADSLRHIYPKLKTD-VLVLSCDLITDVALHEVVDLFRAYDASLAMLMRK 134
Cdd:COG1208   80 EPLGTGGALKRALPLLGDEpFLVLNGDILTDLDLAALLAFHREKGADATLALVP 133
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 5-126 1.32e-15

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: 76.14  E-value: 1.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102    5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNK-PLIWYPLNLLERVGFEEVIVVTTKdvQKALCAEFKM----KMKLDIVCIP 79
Cdd:pfam00483   2 AIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQ--EHRFMLNELLgdgsKFGVQITYAL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 162287102   80 DEADMGTADSLRHIYPKL---KTDVLVLSCDLITDVALHEVVDLFRAYDA 126
Cdd:pfam00483  80 QPEGKGTAPAVALAADFLgdeKSDVLVLGGDHIYRMDLEQAVKFHIEKAA 129
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 336-446 4.63e-09

Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 55.42  E-value: 4.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102 336 EESMIHSSAQIVNKHLIGADSLIGPDT---------QIGEKSSIK-HSVI----GSSCVIRDRTSIT-NCLLmNSVTVEE 400
Cdd:COG0663   15 PSAFVAPTAVVIGDVTIGEDVSVWPGAvlrgdvgpiRIGEGSNIQdGVVLhvdpGYPLTIGDDVTIGhGAIL-HGCTIGD 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 162287102 401 GSSI-HGSVICNNAVIETGAEIK-NCLVGSGQRIEAkakrmNEVIVGN 446
Cdd:COG0663   94 NVLIgMGAIVLDGAVIGDGSIVGaGALVTEGKVVPP-----GSLVVGS 136
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 364-437 1.07e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 53.72  E-value: 1.07e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162287102 364 IGEKSSIKHSVIGSSCVIRDrtSITNCLLMNSVTVEEGSSIHGSVICNNAVIETGAEIKNCLVGSGQRIEAKAK 437
Cdd:PRK05293 285 IAENAKVKNSLVVEGCVVYG--TVEHSVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVI 356
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 4-56 8.68e-07

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 50.44  E-value: 8.68e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 162287102   4 QAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTT 56
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIIST 57
DUF4954 pfam16314
Domain of unknown function (DUF4954); This family consists of uncharacterized proteins around ...
 319-429 4.87e-03

Domain of unknown function (DUF4954); This family consists of uncharacterized proteins around 660 residues in length and is mainly found in various Bacteroides species. The function of this protein is unknown.


Pssm-ID: 435270 [Multi-domain]  Cd Length: 653  Bit Score: 39.20  E-value: 4.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102  319 YMEA-NRQVPKLLSVLcpeESMIHSSAQIVnKHLIGAdslIGPDTQIGEKSSIKHSVIGSSCVIRDRTSITNcLLMNSvT 397
Cdd:pfam16314 142 YIMAlYRHRPELIEKL---KAMIDKYAESV-RSEMGT---IGDHVRILNCGTIRNVKIGDYCTIEGASRLEN-GSINS-N 212

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 162287102  398 VEEGSSIHGSVICNNAVIETGAEIKN------CLVGSG 429
Cdd:pfam16314 213 KEAPVLIGYGVIADDFIISSGSRITDgallsrCFVGQA 250
 
Name Accession Description Interval E-value
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-212 8.17e-102

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: 302.66  E-value: 8.17e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   3 FQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTKDVQKALCAEFKM-----KMKLDIVC 77
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSfplnlKQKLDEVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102  78 IPDEADMGTADSLRHIYPKLKTDVLVLSCDLITDVALHEVVDLFRAYDASLAMLMRKGQESIEPVPGqKGKKKPVEQRDF 157
Cdd:cd04198   81 IVLDEDMGTADSLRHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSEQKGG-KGKSKKADERDV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 162287102 158 IGVDSTGKRLLFMANEADLDEELVIKGSILQKHPRIHFHTGLVDAHLYCLKKYVV 212
Cdd:cd04198  160 IGLDEKTQRLLFITSEEDLDEDLELRKSLLKRHPRVTITTKLLDAHVYIFKRWVL 214
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 3-212 1.06e-72

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: 227.91  E-value: 1.06e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   3 FQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTKDVQKALCAEFKMK-------MKLDI 75
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKwsslsskMIVDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102  76 VCIPDEADMGTADSLRHIYPKLKTDVLVLSCDLITDVALHEVV----DLFRAYDASLAMLMRKGQESIEPvpgqkgkKKP 151
Cdd:cd02507   81 ITSDLCESAGDALRLRDIRGLIRSDFLLLSCDLVSNIPLSELLeerrKKDKNAIATLTVLLASPPVSTEQ-------SKK 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162287102 152 VEQRDFIGVDSTGKRLLFMANEADLDE--ELVIKGSILQKHPRIHFHTGLVDAHLYCLKKYVV 212
Cdd:cd02507  154 TEEEDVIAVDSKTQRLLLLHYEEDLDEdlELIIRKSLLSKHPNVTIRTDLLDCHIYICSPDVL 216
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 357-437 1.50e-32

eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 118.45  E-value: 1.50e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102 357 LIGPDTQIGEKSSIKHSVIGSSCVIRDRTSITNCLLMNSVTVEEGSSIHGSVICNNAVIETGAEIKNCLVGSGQRIEAKA 436
Cdd:cd04652    1 LVGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAGT 80


                 .
gi 162287102 437 K 437
Cdd:cd04652   81 E 81
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 4-134 2.15e-27

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: 109.47  E-value: 2.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   4 QAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTT--KDVQKALCAEFKmKMKLDIVCIPDE 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGylAEQIEEYFGDGS-RFGVRITYVDEG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 162287102  82 ADMGTADSLRHIYPKLKTD-VLVLSCDLITDVALHEVVDLFRAYDASLAMLMRK 134
Cdd:COG1208   80 EPLGTGGALKRALPLLGDEpFLVLNGDILTDLDLAALLAFHREKGADATLALVP 133
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 5-235 8.54e-27

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: 107.28  E-value: 8.54e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTKD---VQKALCAEFKMKMKLDIVciPDE 81
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLgeqIEEYFGDGSKFGVNIEYV--VQE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102  82 ADMGTADSLRHIYPKLKTD-VLVLSCDLITDVALHEVVDLFRAYDASLAMLMrkgqesiepvpgqkgkkKPVEQRDFIGV 160
Cdd:cd04181   79 EPLGTAGAVRNAEDFLGDDdFLVVNGDVLTDLDLSELLRFHREKGADATIAV-----------------KEVEDPSRYGV 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162287102 161 dstgkrllfmaneADLDEELVIKGsILQKhPRiHFHTGLVDAHLYCLKKYVVDFLMENR-SITSIRSELIPYLVRK 235
Cdd:cd04181  142 -------------VELDDDGRVTR-FVEK-PT-LPESNLANAGIYIFEPEILDYIPEILpRGEDELTDAIPLLIEE 201
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 357-434 1.38e-23

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: 93.85  E-value: 1.38e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162287102 357 LIGPDTQIGEKSSIKHSVIGSSCVIRDRTSITNCLLMNSVTVEEGSSIHGSVICNNAVIETGAEIKN-CLVGSGQRIEA 434
Cdd:cd03356    1 LIGESTVIGENAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNlCIIGDDVVVED 79
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
4-132 1.16e-16

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 79.13  E-value: 1.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   4 QAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT--TKDVQKALCAEFKMKMKldIVCIPDE 81
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTgyKAELIEEALARPGPDVT--FVYNPDY 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 162287102  82 ADMGTADSLRHIYPKLKTDVLVLSCDLITDvalHEVVDLFRAYDASLAMLM 132
Cdd:COG1213   79 DETNNIYSLWLAREALDEDFLLLNGDVVFD---PAILKRLLASDGDIVLLV 126
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 357-432 1.27e-16

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 74.54  E-value: 1.27e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162287102 357 LIGPDTQIGEKSSIKHSVIGSSCVIRDRTSITNCLLMNSVTVEEGSSIHGSVICNNAVIETGAEIKN-CLVGSGQRI 432
Cdd:cd05787    1 VIGRGTSIGEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPgSLISFGVVI 77
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 5-126 1.32e-15

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: 76.14  E-value: 1.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102    5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNK-PLIWYPLNLLERVGFEEVIVVTTKdvQKALCAEFKM----KMKLDIVCIP 79
Cdd:pfam00483   2 AIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQ--EHRFMLNELLgdgsKFGVQITYAL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 162287102   80 DEADMGTADSLRHIYPKL---KTDVLVLSCDLITDVALHEVVDLFRAYDA 126
Cdd:pfam00483  80 QPEGKGTAPAVALAADFLgdeKSDVLVLGGDHIYRMDLEQAVKFHIEKAA 129
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 5-142 1.73e-15

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: 75.35  E-value: 1.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT--TKDVQKALCAEFkmkMKLDIVCIPDEA 82
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTgyKKEQIEELLKKY---PNIKFVYNPDYA 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162287102  83 DMGTADSLRHIYPKLKTDVLVLSCDLITDVA-LHEVVDlfraYDASLAML-MRKGQESIEPV 142
Cdd:cd02523   78 ETNNIYSLYLARDFLDEDFLLLEGDVVFDPSiLERLLS----SPADNAILvDKKTKEWEDEY 135
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 5-134 1.07e-14

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: 72.93  E-value: 1.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTT--KDVQKALCAEFKmKMKLDIVCIPDEA 82
Cdd:cd06426    1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNylAEMIEDYFGDGS-KFGVNISYVREDK 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 162287102  83 DMGTADSLRHIYPKLKTDVLVLSCDLITDVALHEVVDLFRAYDASLAMLMRK 134
Cdd:cd06426   80 PLGTAGALSLLPEKPTDPFLVMNGDILTNLNYEHLLDFHKENNADATVCVRE 131
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-229 2.82e-14

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: 71.83  E-value: 2.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   4 QAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT---TKDVQKALCAEFKmkmKLDIVcIPD 80
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNThhlADQIEAHLGDSRF---GLRIT-ISD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102  81 EAD--MGTADSLRHIYPKLKTD-VLVLSCDLITDVALHEVVDLFRAYDASLAMLMRKgqesiEPVPGQKGkkkpveQRDF 157
Cdd:cd06422   77 EPDelLETGGGIKKALPLLGDEpFLVVNGDILWDGDLAPLLLLHAWRMDALLLLLPL-----VRNPGHNG------VGDF 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162287102 158 igvdstgkrllfmaneaDLDEELVIKGSILQKHPRIHFhTGlvdahLYCLKKYVVDFLMENR-SITSIRSELI 229
Cdd:cd06422  146 -----------------SLDADGRLRRGGGGAVAPFTF-TG-----IQILSPELFAGIPPGKfSLNPLWDRAI 195
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 5-142 6.34e-14

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: 69.15  E-value: 6.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102    5 AVVMAVGGGSRMTDltssiPKPLLPVGNKPLIWYPLNLLERVgFEEVIVVTTKDVQKALCAEFkmkmklDIVCIPDE-AD 83
Cdd:pfam12804   1 AVILAGGRSSRMGG-----DKALLPLGGKPLLERVLERLRPA-GDEVVVVANDEEVLAALAGL------GVPVVPDPdPG 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162287102   84 MGTADSLRHIYPKLKTD--VLVLSCD--LITDVALHEVVDLFRAYDASLAMLMRKGQEsIEPV 142
Cdd:pfam12804  69 QGPLAGLLAALRAAPGAdaVLVLACDmpFLTPELLRRLLAAAEESGADIVVPVYDGGR-GHPL 130
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 5-134 2.39e-13

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: 69.12  E-value: 2.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIvvttkdvqkaLCAEFKMKM-----------KL 73
Cdd:cd06915    1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIV----------LSVGYLAEQieeyfgdgyrgGI 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162287102  74 DIVCIPDEADMGTADSLRHIYPKLKTD-VLVLSCDLITDVALHEVVDLFRAYDASLAMLMRK 134
Cdd:cd06915   71 RIYYVIEPEPLGTGGAIKNALPKLPEDqFLVLNGDTYFDVDLLALLAALRASGADATMALRR 132
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-205 3.61e-12

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: 65.32  E-value: 3.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   3 FQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTKDVQKAlcAEF-------KMKMKLDI 75
Cdd:cd04197    1 LQAVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQI--KEYiekskwsKPKSSLMI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102  76 V-CIPDEADMGTADSLRHIYPK--LKTDVLVLSCDLITDVALHEVVDLFRAY-----DASLAMLMRKGqesIEPVPGQKG 147
Cdd:cd04197   79 ViIIMSEDCRSLGDALRDLDAKglIRGDFILVSGDVVSNIDLKEILEEHKERrkkdkNAIMTMVLKEA---SPPHRTRRT 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102 148 KKKPVeqrdfIGVDSTGKRLLFMANEADLDEE--LVIKGSILQKHPRIHFHTGLVDAHLY 205
Cdd:cd04197  156 GEEFV-----IAVDPKTSRLLHYEELPGSKYRsiTDLPSELLGSNSEVEIRHDLLDCHID 210
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 5-126 6.10e-12

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: 65.31  E-value: 6.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTK--DVQKALCAEFKMKMKLDIVCIPDEA 82
Cdd:cd06425    3 ALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYrpEDMVPFLKEYEKKLGIKITFSIETE 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 162287102  83 DMGTADSLRHIYPKLKTDV---LVLSCDLITDVALHEVVDLFRAYDA 126
Cdd:cd06425   83 PLGTAGPLALARDLLGDDDepfFVLNSDVICDFPLAELLDFHKKHGA 129
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-136 1.03e-11

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 63.64  E-value: 1.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   1 MEFQAVVMAVGGGSRMtdltsSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT---TKDVQKALCAefkmkMKLDIVC 77
Cdd:COG2068    2 SKVAAIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLgadAEEVAAALAG-----LGVRVVV 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162287102  78 IPD-EADMGTadSLR----HIYPKLkTDVLVLSCD--LITDVALHEVVDLFRAYDASLAMLMRKGQ 136
Cdd:COG2068   72 NPDwEEGMSS--SLRaglaALPADA-DAVLVLLGDqpLVTAETLRRLLAAFRESPASIVAPTYDGR 134
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 5-131 1.07e-11

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: 64.46  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   5 AVVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT---TKDVQKALCaefkmkmKLDIVCIPDE 81
Cdd:cd02540    1 AVILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVghgAEQVKKALA-------NPNVEFVLQE 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 162287102  82 ADMGTADSLRHIYPKLKT---DVLVLSCD--LITDVALHEVVDLFRAYDASLAML 131
Cdd:cd02540   71 EQLGTGHAVKQALPALKDfegDVLVLYGDvpLITPETLQRLLEAHREAGADVTVL 125
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 5-128 2.02e-11

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: 63.74  E-value: 2.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVV---TTKDVQKALCAEFKMKMKldIVCIPDE 81
Cdd:cd04189    3 GLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVvgpTGEEIKEALGDGSRFGVR--ITYILQE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 162287102  82 ADMGTADSLRHIYPKLKTD--VLVLSCDLITDvALHEVVDLFRA--YDASL 128
Cdd:cd04189   81 EPLGLAHAVLAARDFLGDEpfVVYLGDNLIQE-GISPLVRDFLEedADASI 130
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
5-63 1.27e-10

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 62.03  E-value: 1.27e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162287102   5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTKD----VQKAL 63
Cdd:COG1209    3 GIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEdgpqFERLL 65
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1-131 3.22e-10

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: 61.97  E-value: 3.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   1 MEFQAVVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT---TKDVQKALCAEfkmkmklDIVC 77
Cdd:COG1207    1 SPLAVVILAAGKGTRMK---SKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVghgAEQVRAALADL-------DVEF 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 162287102  78 IPDEADMGTADSLRHIYPKLKTD---VLVLSCD--LITDVALHEVVDLFRAYDASLAML 131
Cdd:COG1207   71 VLQEEQLGTGHAVQQALPALPGDdgtVLVLYGDvpLIRAETLKALLAAHRAAGAAATVL 129
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 8-182 1.05e-09

GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 57.59  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   8 MAVGGGSRMTDltssIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTKDVQKAlcAEFKMKMKLDIVCIPDE---ADM 84
Cdd:COG2266    1 MAGGKGTRLGG----GEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSPNTPKT--REYLKERGVEVIETPGEgyvEDL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102  85 GTAdsLRHIypklKTDVLVLSCDL--ITDVALHEVVDLFRAYDA-SLAM-----LMRKGQESIEPVPGQKGKKKPVeqrd 156
Cdd:COG2266   75 NEA--LESI----SGPVLVVPADLplLTPEIIDDIIDAYLESGKpSLTVvvpaaLKRELGVSPDTTFEIDGELVPT---- 144

                        170       180
                 ....*....|....*....|....*.
gi 162287102 157 fiGVDstgkrlLFMANEADLDEELVI 182
Cdd:COG2266  145 --GIN------IVDGSDGEQEETNLV 162
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 5-57 1.77e-09

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: 57.97  E-value: 1.77e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 162287102   5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTK 57
Cdd:cd02538    3 GIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTP 55
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 364-451 1.79e-09

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: 54.78  E-value: 1.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102 364 IGEKSSIKHSVIGSSCVIRDrTSITNCLLMNSVTVEEGSSIHGSVICNNAVIETGAEIKNCLVGSGQRIEAkakrmNEVI 443
Cdd:cd04651    4 IGRRGEVKNSLVSEGCIISG-GTVENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPD-----GVVI 77


                 ....*...
gi 162287102 444 VGNDQLME 451
Cdd:cd04651   78 GGDPEEDR 85
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 355-423 1.92e-09

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: 54.78  E-value: 1.92e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162287102 355 DSLIGPDTQIgEKSSIKHSVIGSSCVIRDRTSITNCLLMNSVTVEEGSSIHGSVICNNAVIETGAEIKN 423
Cdd:cd04651   12 NSLVSEGCII-SGGTVENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPDGVVIGG 79
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 336-446 4.63e-09

Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 55.42  E-value: 4.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102 336 EESMIHSSAQIVNKHLIGADSLIGPDT---------QIGEKSSIK-HSVI----GSSCVIRDRTSIT-NCLLmNSVTVEE 400
Cdd:COG0663   15 PSAFVAPTAVVIGDVTIGEDVSVWPGAvlrgdvgpiRIGEGSNIQdGVVLhvdpGYPLTIGDDVTIGhGAIL-HGCTIGD 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 162287102 401 GSSI-HGSVICNNAVIETGAEIK-NCLVGSGQRIEAkakrmNEVIVGN 446
Cdd:COG0663   94 NVLIgMGAIVLDGAVIGDGSIVGaGALVTEGKVVPP-----GSLVVGS 136
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-144 1.16e-08

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: 54.81  E-value: 1.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   1 MEFQAVVMAVGGGSRM-TDltssipKPLLPVGNKPLIWYPLNLLERVgFEEVIVVTTKDVQKAlcaefkmkmKLDIVCIP 79
Cdd:COG0746    3 MPITGVILAGGRSRRMgQD------KALLPLGGRPLLERVLERLRPQ-VDEVVIVANRPERYA---------ALGVPVVP 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162287102  80 DE-ADMG------TAdsLRHIypklKTD-VLVLSCD--LITDvalhEVVD-LFRAYDASLAMLMRKGQESIEPVPG 144
Cdd:COG0746   67 DDpPGAGplagilAA--LEAA----PAEwVLVLACDmpFLPP----DLVRrLLEALEEGADAVVPRSGGRLEPLFA 132
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 5-131 1.57e-08

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: 55.34  E-value: 1.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   5 AVVMaVGG---GSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERV-GFEEVIVVT--TKDVQKALCAEFKMKMKLDIVCI 78
Cdd:cd06428    1 AVIL-VGGpqkGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVpDLKEVLLIGfyPESVFSDFISDAQQEFNVPIRYL 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 162287102  79 PDEADMGTADSLRH----IYPKLKTDVLVLSCDLITDVALHEVVDLFRAYDASLAML 131
Cdd:cd06428   80 QEYKPLGTAGGLYHfrdqILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTIL 136
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 5-129 1.87e-08

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: 54.10  E-value: 1.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   5 AVVMAVGGGSRMTDltssiPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT--TKDVQKALCAEFkmkmKLDIVCIPDeA 82
Cdd:cd04182    3 AIILAAGRSSRMGG-----NKLLLPLDGKPLLRHALDAALAAGLSRVIVVLgaEADAVRAALAGL----PVVVVINPD-W 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 162287102  83 DMGTADSLRHIYPKLKTD---VLVLSCD--LITDVALHEVVDLFRAYDASLA 129
Cdd:cd04182   73 EEGMSSSLAAGLEALPADadaVLILLADqpLVTAETLRALIDAFREDGAGIV 124
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 5-53 6.00e-08

G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.


Pssm-ID: 133015 [Multi-domain]  Cd Length: 253  Bit Score: 53.73  E-value: 6.00e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 162287102   5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIV 53
Cdd:cd02524    1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFIL 49
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 5-58 6.97e-08

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


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 52.91  E-value: 6.97e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 162287102   5 AVVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVG-FEEVIVVTTKD 58
Cdd:cd02516    3 AIILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVVVVPPD 54
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 6-77 7.93e-08

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: 52.82  E-value: 7.93e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162287102   6 VVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVG-FEEVIVVTTKDVQ---KALCAEFKMKMKLDIVC 77
Cdd:COG1211    1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIeyfEELLAKYGIDKPVRVVA 73
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 364-437 1.07e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 53.72  E-value: 1.07e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162287102 364 IGEKSSIKHSVIGSSCVIRDrtSITNCLLMNSVTVEEGSSIHGSVICNNAVIETGAEIKNCLVGSGQRIEAKAK 437
Cdd:PRK05293 285 IAENAKVKNSLVVEGCVVYG--TVEHSVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVI 356
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 313-421 1.78e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 52.91  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102 313 VSTLGLYMEANRQvpkLLSVlCPEESM------IHSS------AQIVNKHL---IGADSLIGPDTQIgEKSSIKHSVIGS 377
Cdd:PRK00844 262 VGTIDAYYDAHMD---LLSV-HPVFNLynrewpIYTSspnlppAKFVDGGGrvgSAQDSLVSAGSII-SGATVRNSVLSP 336

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 162287102 378 SCVIRDRTSITNCLLMNSVTVEEGSSIHGSVICNNAVIETGAEI 421
Cdd:PRK00844 337 NVVVESGAEVEDSVLMDGVRIGRGAVVRRAILDKNVVVPPGATI 380
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 352-420 2.03e-07

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 51.25  E-value: 2.03e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162287102 352 IGADSLIGPDTQIGEkssikHSVIGSSCVIRDRTSI-TNCLLMNSVTVEEGSSI-HGSVICNNAVIetGAE 420
Cdd:cd03352   10 IGPNAVIGEGVVIGD-----GVVIGPGVVIGDGVVIgDDCVIHPNVTIYEGCIIgDRVIIHSGAVI--GSD 73
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 335-437 4.78e-07

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: 50.11  E-value: 4.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102 335 PEESMIHSSAQI-------VNKHLIGaDSLIGPDTQIGEKSSIKHSVIGSSCVIRDRTSITNCllmnsvTVEEGSSI--- 404
Cdd:cd03353    7 PETTYIDGDVEIgvdvvidPGVILEG-KTVIGEDCVIGPNCVIKDSTIGDGVVIKASSVIEGA------VIGNGATVgpf 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 162287102 405 ----HGSVICNNAVIETGAEIKNCLVGSGqrieAKAK 437
Cdd:cd03353   80 ahlrPGTVLGEGVHIGNFVEIKKSTIGEG----SKAN 112
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 340-421 6.60e-07

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 50.91  E-value: 6.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102 340 IHSSAQIVNKHLIGADSLIGPDTQIGEkssikHSVIGSSCVIRDRTSI-TNCLLMNSVTVeegssIHGSVICNNAVIETG 418
Cdd:PRK00892 109 IDPSAKIGEGVSIGPNAVIGAGVVIGD-----GVVIGAGAVIGDGVKIgADCRLHANVTI-----YHAVRIGNRVIIHSG 178


                 ...
gi 162287102 419 AEI 421
Cdd:PRK00892 179 AVI 181
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 5-108 6.81e-07

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: 49.50  E-value: 6.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   5 AVVMAvGG-GSRMTDltssiPKPLLPVGNKPLIWYPLNLLERVgFEEVIVVTTKDVQKALcaefkmkmKLDIVCIPDEA- 82
Cdd:cd02503    3 GVILA-GGkSRRMGG-----DKALLELGGKPLLEHVLERLKPL-VDEVVISANRDQERYA--------LLGVPVIPDEPp 67

                         90       100
                 ....*....|....*....|....*..
gi 162287102  83 DMGTADSLRHIYPKLKTD-VLVLSCDL 108
Cdd:cd02503   68 GKGPLAGILAALRAAPADwVLVLACDM 94
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 4-56 8.68e-07

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 50.44  E-value: 8.68e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 162287102   4 QAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTT 56
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIIST 57
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 4-96 1.04e-06

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: 49.84  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   4 QAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTK---------DVQKALCAEFKMKMKLD 74
Cdd:cd02541    2 KAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRgkraiedhfDRSYELEETLEKKGKTD 81

                         90       100
                 ....*....|....*....|...
gi 162287102  75 IVCIPDE-ADMGTADSLRHIYPK 96
Cdd:cd02541   82 LLEEVRIiSDLANIHYVRQKEPL 104
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 340-432 1.81e-06

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: 49.63  E-value: 1.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102 340 IHSSAQIvnkhliGADSLIGPDTQIGEkssikHSVIGSSCVIRDRTSI-TNCLLMNSVTVEEGSSIHgsvicNNAVIETG 418
Cdd:COG1044   99 IHPSAVI------DPSAKIGEGVSIGP-----FAVIGAGVVIGDGVVIgPGVVIGDGVVIGDDCVLH-----PNVTIYER 162

                         90
                 ....*....|....*
gi 162287102 419 AEI-KNCLVGSGQRI 432
Cdd:COG1044  163 CVIgDRVIIHSGAVI 177
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-131 2.57e-06

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 49.48  E-value: 2.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   5 AVVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTKDVQkALCAEFKMKMKLDIVCIPDEaDM 84
Cdd:PRK14353   8 AIILAAGEGTRMK---SSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAE-AVAAAAAKIAPDAEIFVQKE-RL 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 162287102  85 GTADSLRHIYPKLKT---DVLVLSCD--LITDVALHEVVDLfRAYDASLAML 131
Cdd:PRK14353  83 GTAHAVLAAREALAGgygDVLVLYGDtpLITAETLARLRER-LADGADVVVL 133
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 336-446 4.24e-06

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 46.25  E-value: 4.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102 336 EESMIHSSAQIVNKHLIGADSLIGPDTQI-GEKSSIkhsVIGSSCVIRDRTSI-----TNCLLMNSVTVEEGSSIHGSVI 409
Cdd:cd04645    4 PSAFIAPNATVIGDVTLGEGSSVWFGAVLrGDVNPI---RIGERTNIQDGSVLhvdpgYPTIIGDNVTVGHGAVLHGCTI 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 162287102 410 CNNAVIETGAEI-------KNCLVGSG------QRIEAkakrmNEVIVGN 446
Cdd:cd04645   81 GDNCLIGMGAIIldgavigKGSIVAAGslvppgKVIPP-----GSLVAGS 125
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
5-77 5.04e-06

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 47.44  E-value: 5.04e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162287102   5 AVVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVG-FEEVIVVT----TKDVQKALCAEFKmkmKLDIVC 77
Cdd:PRK00155   6 AIIPAAGKGSRMG---ADRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVppddRPDFAELLLAKDP---KVTVVA 77
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 352-446 6.68e-06

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: 46.64  E-value: 6.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102 352 IGADSLIGPDTQIGEKSSIK-HSVIGSSCVIRDRTSITNCllmnsvTVEEGSSIHGSVICNNAVIEtgaeiKNCLVGSGQ 430
Cdd:cd03353   12 IDGDVEIGVDVVIDPGVILEgKTVIGEDCVIGPNCVIKDS------TIGDGVVIKASSVIEGAVIG-----NGATVGPFA 80

                         90
                 ....*....|....*.
gi 162287102 431 RIEAKAKRMNEVIVGN 446
Cdd:cd03353   81 HLRPGTVLGEGVHIGN 96
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 328-429 1.50e-05

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 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. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 45.55  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102 328 KLLSVLCPEESMIHSSAqIVNKH-------LIGADSLIGPDTQIGEKSSIK-HSVIGSSCVIRDRTSIT-NCLLMNSVTV 398
Cdd:cd03360   75 KLLAAGYRFATLIHPSA-VVSPSavigegcVIMAGAVINPDARIGDNVIINtGAVIGHDCVIGDFVHIApGVVLSGGVTI 153

                         90       100       110
                 ....*....|....*....|....*....|..
gi 162287102 399 EEGSSIHGsvicnNAVIETGAEI-KNCLVGSG 429
Cdd:cd03360  154 GEGAFIGA-----GATIIQGVTIgAGAIIGAG 180
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 335-446 1.55e-05

paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity.


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 45.05  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102 335 PEESMIHSSAQIVNKHLIGADSLIGPDTQI-GEKSSIkhsVIGSSCVIRDrtsitNCLLMN----SVTVEEGSSI-HGSV 408
Cdd:cd04745    4 DPSSFVHPTAVLIGDVIIGKNCYIGPHASLrGDFGRI---VIRDGANVQD-----NCVIHGfpgqDTVLEENGHIgHGAI 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 162287102 409 I--CN---------NAVIETGAEI-KNCLVGSGQRIEAKAK-RMNEVIVGN 446
Cdd:cd04745   76 LhgCTigrnalvgmNAVVMDGAVIgEESIVGAMAFVKAGTViPPRSLIAGS 126
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 352-432 1.70e-05

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 47.13  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102 352 IGADSLIGPDTQIGEKSSIK-HSVIGSSCVIRDRTSITNCLLMNSVTVEEgSSIHGSVICNNAVIETGAEIK-NCLVGSG 429
Cdd:PRK14354 262 IDADVEIGSDTVIEPGVVIKgNTVIGEDCVIGPGSRIVDSTIGDGVTITN-SVIEESKVGDNVTVGPFAHLRpGSVIGEE 340


                 ...
gi 162287102 430 QRI 432
Cdd:PRK14354 341 VKI 343
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
4-55 1.80e-05

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 46.44  E-value: 1.80e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 162287102   4 QAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT 55
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVT 61
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-220 4.35e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 45.87  E-value: 4.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   5 AVVMAVGGGSRMtdlTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT---TKDVQKALCAEfkmkmklDIVCIPDE 81
Cdd:PRK14356   8 ALILAAGKGTRM---HSDKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVghrADMVRAAFPDE-------DARFVLQE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102  82 ADMGTADSLRHIYPKLK----TDVLVLSCD--LITDVALHEVVDlfRAYDASLAMLmrkgqeSIE-PVPGQKGKkkpveq 154
Cdd:PRK14356  78 QQLGTGHALQCAWPSLTaaglDRVLVVNGDtpLVTTDTIDDFLK--EAAGADLAFM------TLTlPDPGAYGR------ 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162287102 155 rdfigVDSTGKRLLFMANEADLDEELvikgsilqKHPRihfhTGLVDAHLYCLKKYVVDFLM-----ENRS 220
Cdd:PRK14356 144 -----VVRRNGHVAAIVEAKDYDEAL--------HGPE----TGEVNAGIYYLRLDAVESLLprltnANKS 197
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 340-444 4.75e-05

Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 43.77  E-value: 4.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102 340 IHSSAQIVNKHLIGADSLIGPDT----------QIGEKSSIKHSVI-----GSSCVIRDRTSITNCLLMNS-VTVEE--- 400
Cdd:cd00710   11 VHPTAVVIGDVIIGDNVFVGPGAsiradegtpiIIGANVNIQDGVVihaleGYSVWIGKNVSIAHGAIVHGpAYIGDncf 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 162287102 401 ---GSSIHGSVICNNAVIETGAEIKNC------LVGSGQRI--EAKAKRMNEVIV 444
Cdd:cd00710   91 igfRSVVFNAKVGDNCVIGHNAVVDGVeippgrYVPAGAVItsQTQADALPDVTD 145
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 352-415 6.84e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 45.12  E-value: 6.84e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162287102 352 IGADSLIGPDTQIGekssiKHSVIGSSCVIRDRTSITNCLLMNSVTVEEGSSIHGSVICNNAVI 415
Cdd:PRK14355 271 IGRDTTIYPGVCIS-----GDTRIGEGCTIEQGVVIKGCRIGDDVTVKAGSVLEDSVVGDDVAI 329
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 1-58 1.28e-04

bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 44.07  E-value: 1.28e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 162287102   1 MEFQAVVMAVGGGSRmtdLTSSIPKPLLPVGNKPLIWYPL-NLLERVGFEEVIVVTTKD 58
Cdd:PRK09382   4 SDISLVIVAAGRSTR---FSAEVKKQWLRIGGKPLWLHVLeNLSSAPAFKEIVVVIHPD 59
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 8-122 1.47e-04

GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which 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.


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 43.01  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   8 MAvGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVttkdVQKALCAEFKMKMKL-------DIVCIPD 80
Cdd:cd04183    5 MA-GLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFI----CRDEHNTKFHLDESLkllapnaTVVELDG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 162287102  81 EADmGTADSLRHIYPKLKTD--VLVLSCDLITDVALHEVVDLFR 122
Cdd:cd04183   80 ETL-GAACTVLLAADLIDNDdpLLIFNCDQIVESDLLAFLAAFR 122
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 6-131 1.54e-04

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 43.81  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   6 VVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT---TKDVQKALCAEfkmkmklDIVCIPDEA 82
Cdd:PRK14358  11 VILAAGQGTRMK---SALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTghgAEQVEAALQGS-------GVAFARQEQ 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 162287102  83 DMGTADSLRHIYPKLKT---DVLVLSCD--LITDVALHEVVDLFRAYDASLAML 131
Cdd:PRK14358  81 QLGTGDAFLSGASALTEgdaDILVLYGDtpLLRPDTLRALVADHRAQGSAMTIL 134
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 352-429 1.59e-04

WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 40.95  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102 352 IGADSLIGPDTQIGEKSSIK-------HSVIGSSCVIRDRTSITNCLLMNS----------VTVEEGSSIhGSvicnNAV 414
Cdd:cd03358    7 IGTNVFIENDVKIGDNVKIQsnvsiyeGVTIEDDVFIGPNVVFTNDLYPRSkiyrkwelkgTTVKRGASI-GA----NAT 81

                         90
                 ....*....|....*.
gi 162287102 415 IETGAEI-KNCLVGSG 429
Cdd:cd03358   82 ILPGVTIgEYALVGAG 97
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 355-400 1.78e-04

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: 39.92  E-value: 1.78e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 162287102 355 DSLIGPDTQIGEKSSIKHSVIGSSCVIRDRTSITN-CLLMNSVTVEE 400
Cdd:cd03356   33 NSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNlCIIGDDVVVED 79
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 373-432 2.24e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 43.29  E-value: 2.24e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102 373 SVIGSSCVIRDrTSITNCLLMNSVTVEEGSSIHGSVICNNAVIETGAEIKNCLVGSGQRI 432
Cdd:PRK00725 328 SLVSGGCIISG-AVVRRSVLFSRVRVNSFSNVEDSVLLPDVNVGRSCRLRRCVIDRGCVI 386
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-131 2.36e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 43.19  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   5 AVVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTKDvQKALCAEFKMKMklDIVCIPDEADM 84
Cdd:PRK14355   6 AIILAAGKGTRMK---SDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQ-AEKVREHFAGDG--DVSFALQEEQL 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 162287102  85 GTADSLRHIYPKLKT---DVLVLSCD--LITDVALHEVVDLFRAYDASLAML 131
Cdd:PRK14355  80 GTGHAVACAAPALDGfsgTVLILCGDvpLLRAETLQGMLAAHRATGAAVTVL 131
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
3-55 2.95e-04

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 42.57  E-value: 2.95e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 162287102   3 FQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT 55
Cdd:PRK10122   4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVT 56
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-110 3.03e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 42.90  E-value: 3.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102   1 MEFQAVVMAVGGGSRMtdlTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT---TKDVQKALC--AEFKMKmkldi 75
Cdd:PRK14354   1 MNRYAIILAAGKGTRM---KSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVghgAEEVKEVLGdrSEFALQ----- 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 162287102  76 vcipdEADMGTADSLRHIYPKLKT---DVLVLSCD--LIT 110
Cdd:PRK14354  73 -----EEQLGTGHAVMQAEEFLADkegTTLVICGDtpLIT 107
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 335-423 3.14e-04

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple 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.


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 41.03  E-value: 3.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102 335 PEESMIHSSAQIVNKHLIGADSLIGPDTQIGEKSSIK-HSVIGSSCVIRDRTSITNCLLMNSVTVEEGSSIHGSVICNNA 413
Cdd:cd05636   15 KGPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRgYTVLGDGCVVGNSVEVKNSIIMDGTKVPHLNYVGDSVLGENV 94

                         90
                 ....*....|
gi 162287102 414 VIETGAEIKN 423
Cdd:cd05636   95 NLGAGTITAN 104
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 355-422 4.68e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 42.16  E-value: 4.68e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162287102 355 DSLIGPDTQIGEKSSIKHSVIGSSCVIRDRTSITNCLLMNSVTVEEGSSIHG-----SVICNNAVIETGAEIK 422
Cdd:PRK05293 308 HSVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIGGgkeviTVIGENEVIGVGTVIG 380
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 355-432 1.03e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 41.41  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102 355 DSLIGpDTQIGEKSSIKHSVIGSSCVIRDRTSITNCLLM-----NSVTVEEGSSIHGSV---ICNNAVIEtGAEI-KNCL 425
Cdd:PRK02862 308 ESIIA-EGCIIKNCSIHHSVLGIRSRIESGCTIEDTLVMgadfyESSEEREELRKEGKPplgIGEGTTIK-RAIIdKNAR 385


                 ....*..
gi 162287102 426 VGSGQRI 432
Cdd:PRK02862 386 IGNNVRI 392
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 337-387 1.08e-03

Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane/envelope biogenesis]; Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 40.77  E-value: 1.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 162287102 337 ESMIHSSAQIVNKHLIGAD------SLIGPDTQIGEkssikHSVIGSSCVIRDRTSI 387
Cdd:COG1043    1 MAMIHPTAIVDPGAKLGENveigpfCVIGPDVEIGD-----GTVIGSHVVIEGPTTI 52
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 5-69 1.65e-03

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


Pssm-ID: 396773  Cd Length: 217  Bit Score: 39.63  E-value: 1.65e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102    5 AVVMAVGGGSRMTDltssipKPLLPVGNKPLIWYPL-NLLERVGFEEVIVVT----TKDVQKALCAEFKM 69
Cdd:pfam02348   2 AIIPARLGSKRLPG------KNLLDLGGKPLIHHVLeAALKSGAFEKVIVATdseeIADVAKEFGAGVVM 65
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
352-446 4.01e-03

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 37.54  E-value: 4.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102 352 IGADSLIGPDTQI-GEKSSI-KHSVIGSSCVIRDRTSIT---NCLLMNSVTV----------EEGSSIHGSV-------I 409
Cdd:COG0110   11 IGDGVVIGPGVRIyGGNITIgDNVYIGPGVTIDDPGGITigdNVLIGPGVTIltgnhpiddpATFPLRTGPVtigddvwI 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 162287102 410 CNNAVIETGAEI-KNCLVGSG----QRIEAkakrmNEVIVGN 446
Cdd:COG0110   91 GAGATILPGVTIgDGAVVGAGsvvtKDVPP-----YAIVAGN 127
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
336-387 4.03e-03

acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 38.93  E-value: 4.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 162287102 336 EESMIHSSAQIVNKHLIGAD------SLIGPDTQIGEkssikHSVIGSSCVIRDRTSI 387
Cdd:PRK05289   1 MMAKIHPTAIVEPGAKIGENveigpfCVIGPNVVIGD-----GTVIGSHVVIDGHTTI 53
DUF4954 pfam16314
Domain of unknown function (DUF4954); This family consists of uncharacterized proteins around ...
 319-429 4.87e-03

Domain of unknown function (DUF4954); This family consists of uncharacterized proteins around 660 residues in length and is mainly found in various Bacteroides species. The function of this protein is unknown.


Pssm-ID: 435270 [Multi-domain]  Cd Length: 653  Bit Score: 39.20  E-value: 4.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102  319 YMEA-NRQVPKLLSVLcpeESMIHSSAQIVnKHLIGAdslIGPDTQIGEKSSIKHSVIGSSCVIRDRTSITNcLLMNSvT 397
Cdd:pfam16314 142 YIMAlYRHRPELIEKL---KAMIDKYAESV-RSEMGT---IGDHVRILNCGTIRNVKIGDYCTIEGASRLEN-GSINS-N 212

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 162287102  398 VEEGSSIHGSVICNNAVIETGAEIKN------CLVGSG 429
Cdd:pfam16314 213 KEAPVLIGYGVIADDFIISSGSRITDgallsrCFVGQA 250
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 336-429 7.22e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 38.66  E-value: 7.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287102 336 EESMIHSSAQIVNKHLIGADSLIGP-----DTQIGEKSSIKHSVIGSScVIRDRTSItncllmnsvtveeGSSIH---GS 407
Cdd:PRK14354 270 SDTVIEPGVVIKGNTVIGEDCVIGPgsrivDSTIGDGVTITNSVIEES-KVGDNVTV-------------GPFAHlrpGS 335

                         90       100
                 ....*....|....*....|..
gi 162287102 408 VICNNAVIETGAEIKNCLVGSG 429
Cdd:PRK14354 336 VIGEEVKIGNFVEIKKSTIGEG 357
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 339-415 7.72e-03

Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Mannose-1-phosphate guanylyltransferase is also known as GDP-mannose pyrophosphorylase. It catalyzes the synthesis of GDP-mannose from GTP and mannose-1-phosphate, and is involved in the maintenance of cell wall integrity and glycosylation. Similar to ADP-glucose pyrophosphorylase, it contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain, presumably with 4 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.


Pssm-ID: 100062 [Multi-domain]  Cd Length: 80  Bit Score: 35.21  E-value: 7.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162287102 339 MIHSSAQIVNKHLIGADSLIGPDTQIGEKSSIKHSVIGSSCVIRDRTSITNCLLMNSVTVEEGSSIHG-SVICNNAVI 415
Cdd:cd05824    1 LIDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLENvTVLGDDVTI 78
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
5-55 9.27e-03

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 37.70  E-value: 9.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 162287102   5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNllERV--GFEEVIVVT 55
Cdd:COG1210    6 AVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVE--EAVaaGIEEIIFVT 56
 
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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