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Conserved domains on  [gi|54291067|dbj|BAD61743|]
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putative eukaryotic translation initiation factor 2B, subunit 3 [Oryza sativa Japonica Group]

Protein Classification

translation initiation factor eIF-2B gamma subunit family protein( domain architecture ID 10302127)

translation initiation factor eIF-2B gamma subunit family protein contains N-terminal glycosyltransferase family 2 domain and a C-terminal Left-handed parallel beta-Helix (LbH) domain; 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

CATH:  2.160.10.10
EC:  2.4.-.-
Gene Ontology:  GO:0016757
PubMed:  10521532|12691742|9445404|7893825|11747907|15500694
SCOP:  3000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 3-220 8.80e-58

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases 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. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


The actual alignment was detected with superfamily member cd04198:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 214  Bit Score: 189.41  E-value: 8.80e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   3 FQVVVLAGGTSEKLSPLvSKDVPKALLPVANRPVLSYVLDLLEASDLKDIIVVVEGQEAARLVGAWASS--AYLDRLLVE 80
Cdd:cd04198   1 FQAVILAGGGGSRLYPL-TDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFplNLKQKLDEV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  81 VVAVPEDIGTAGALRAISKRLTaNDVLVISGDLVTDVLPGAVAATHRRNGAAVTALLCSVPISGPsdaaSSGGKDKAKKP 160
Cdd:cd04198  80 TIVLDEDMGTADSLRHIRKKIK-KDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSE----QKGGKGKSKKA 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067 161 TRLNIVGLDITRQFLLHIVSGTDVEKDVRVYKRKIRAVGEMEIRSDLMDAHLYAFKRTTL 220
Cdd:cd04198 155 DERDVIGLDEKTQRLLFITSEEDLDEDLELRKSLLKRHPRVTITTKLLDAHVYIFKRWVL 214
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 362-442 1.06e-35

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: 126.92  E-value: 1.06e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067 362 MLAEGSQLGDKCSVKRSVIGRHCRIGSNVKIVNSVVMNHVVIEDGCHIQGSVICNNVQLQERAVLKDCQVGAGYIVTASS 441
Cdd:cd04652   1 LVGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAGT 80


                .
gi 54291067 442 E 442
Cdd:cd04652  81 E 81
glmU super family cl33001
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 315-400 1.36e-03

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


The actual alignment was detected with superfamily member PRK14360:

Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 41.07  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  315 SIQAYCDINRDVVGDA-SHLSGysfsaqnniihpTSVLGSKTTIGPQCmLAEGSQLGDKCSVKRSV-------------- 379
Cdd:PRK14360 258 TISETVELGPDVIIEPqTHLRG------------NTVIGSGCRIGPGS-LIENSQIGENVTVLYSVvsdsqigdgvkigp 324

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 54291067  380 ---------IGRHCRIGSNVKIVNSVV-----MNH 400
Cdd:PRK14360 325 yahlrpeaqIGSNCRIGNFVEIKKSQLgegskVNH 359
 
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; ...
 3-220 8.80e-58

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: 189.41  E-value: 8.80e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   3 FQVVVLAGGTSEKLSPLvSKDVPKALLPVANRPVLSYVLDLLEASDLKDIIVVVEGQEAARLVGAWASS--AYLDRLLVE 80
Cdd:cd04198   1 FQAVILAGGGGSRLYPL-TDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFplNLKQKLDEV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  81 VVAVPEDIGTAGALRAISKRLTaNDVLVISGDLVTDVLPGAVAATHRRNGAAVTALLCSVPISGPsdaaSSGGKDKAKKP 160
Cdd:cd04198  80 TIVLDEDMGTADSLRHIRKKIK-KDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSE----QKGGKGKSKKA 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067 161 TRLNIVGLDITRQFLLHIVSGTDVEKDVRVYKRKIRAVGEMEIRSDLMDAHLYAFKRTTL 220
Cdd:cd04198 155 DERDVIGLDEKTQRLLFITSEEDLDEDLELRKSLLKRHPRVTITTKLLDAHVYIFKRWVL 214
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 362-442 1.06e-35

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: 126.92  E-value: 1.06e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067 362 MLAEGSQLGDKCSVKRSVIGRHCRIGSNVKIVNSVVMNHVVIEDGCHIQGSVICNNVQLQERAVLKDCQVGAGYIVTASS 441
Cdd:cd04652   1 LVGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAGT 80


                .
gi 54291067 442 E 442
Cdd:cd04652  81 E 81
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 4-147 7.76e-26

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: 105.23  E-value: 7.76e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   4 QVVVLAGGTSEKLSPLvSKDVPKALLPVANRPVLSYVLDLLEASDLKDIIVVVeGQEAARLVGAWASSAYLDrLLVEVVA 83
Cdd:COG1208   1 KAVILAGGLGTRLRPL-TDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINV-GYLAEQIEEYFGDGSRFG-VRITYVD 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 54291067  84 VPEDIGTAGALRAISKRLTANDVLVISGDLVTDVLPGAVAATHRRNGAAVTalLCSVPISGPSD 147
Cdd:COG1208  78 EGEPLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLAFHREKGADAT--LALVPVPDPSR 139
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 355-434 1.67e-11

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 65.48  E-value: 1.67e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067 355 TTIGPQCMlAEGSQLGDKC----SVKRSVIGRHCRIGSNVKIVNSVVMNHVVIEDGCHIqgsvicnnvqlqERAVL-KDC 429
Cdd:COG0448 278 AKFVRGGK-VKNSLVSNGCiisgTVENSVLFRGVRVESGAVVENSVIMPGVVIGEGAVI------------ENAIIdKNV 344


                ....*
gi 54291067 430 QVGAG 434
Cdd:COG0448 345 VIPPG 349
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 6-166 2.56e-10

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: 60.34  E-value: 2.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067     6 VVLAGGTSEKLSPLvSKDVPKALLPVANR-PVLSYVLDLLEASDLKDIIVVVEGQEAARLVGAWassAYLDRLLVEVVAV 84
Cdd:pfam00483   3 IILAGGSGTRLWPL-TRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELL---GDGSKFGVQITYA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067    85 --PEDIGTAGALRAISKRL--TANDVLVISGDLVTDVLPGAVAATHRRNGAAVTALLCSVPISGPSD----AASSGGK-- 154
Cdd:pfam00483  79 lqPEGKGTAPAVALAADFLgdEKSDVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEPPTGygvvEFDDNGRvi 158

                         170
                  ....*....|....*
gi 54291067   155 ---DKAKKPTRLNIV 166
Cdd:pfam00483 159 rfvEKPKLPKASNYA 173
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 344-414 1.18e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 59.77  E-value: 1.18e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 54291067  344 IIHPTSVLGSKTTIGPQCMLAEGSQLGDKCSV-KRSVIGRHCRIGSNVKI-VNSVVMNHVVIEDGCHIQ-GSVI 414
Cdd:PRK00892 108 VIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIgAGAVIGDGVKIGADCRLhANVTIYHAVRIGNRVIIHsGAVI 181
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-437 4.94e-08

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 54.84  E-value: 4.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067    1 MDFQVVVLAGG--TSEKlsplvSKdVPKALLPVANRPVLSYVLDLLEASDLKDIIVVVeGQEAARLVGAWASSayldrll 78
Cdd:PRK14354   1 MNRYAIILAAGkgTRMK-----SK-LPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVV-GHGAEEVKEVLGDR------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   79 VEVVAVPEDIGTAGALRAISKRLTAND--VLVISGD--LVTDVLPGAVAATHRRNGAAVTaLLCSVpisgpsdaassggk 154
Cdd:PRK14354  67 SEFALQEEQLGTGHAVMQAEEFLADKEgtTLVICGDtpLITAETLKNLIDFHEEHKAAAT-ILTAI-------------- 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  155 dkAKKPT---RlnIVGLDITRqfLLHIVSgtdvEKDVRVYKRKIRavgemEIRSDlmdahLYAFKRTTLQNILEE----- 226
Cdd:PRK14354 132 --AENPTgygR--IIRNENGE--VEKIVE----QKDATEEEKQIK-----EINTG-----TYCFDNKALFEALKKisndn 191

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  227 --KESYRSIRLEVLpylvRSQlkssssgGE--GTTVDETGDTTVPSNSHLQcLSQ------HRILapsafkKDLLSSGGT 296
Cdd:PRK14354 192 aqGEYYLTDVIEIL----KNE-------GEkvGAYQTEDFEESLGVNDRVA-LAEaekvmrRRIN------EKHMVNGVT 253

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  297 yrccvYIATKSKYchrlnsIQAYCDINRDVVgdashlsgysfsaqnniIHPTSVLGSKTTIGPQCMLAEGS-----QLGD 371
Cdd:PRK14354 254 -----IIDPESTY------IDADVEIGSDTV-----------------IEPGVVIKGNTVIGEDCVIGPGSrivdsTIGD 305

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 54291067  372 KCSVKRSVIgRHCRIGSNVKI-------VNSVVMNHVVIEDGCHIQGSVICNNVQLQERA------VLKDCQVGAGYIV 437
Cdd:PRK14354 306 GVTITNSVI-EESKVGDNVTVgpfahlrPGSVIGEEVKIGNFVEIKKSTIGEGTKVSHLTyigdaeVGENVNIGCGTIT 383
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 315-400 1.36e-03

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 41.07  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  315 SIQAYCDINRDVVGDA-SHLSGysfsaqnniihpTSVLGSKTTIGPQCmLAEGSQLGDKCSVKRSV-------------- 379
Cdd:PRK14360 258 TISETVELGPDVIIEPqTHLRG------------NTVIGSGCRIGPGS-LIENSQIGENVTVLYSVvsdsqigdgvkigp 324

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 54291067  380 ---------IGRHCRIGSNVKIVNSVV-----MNH 400
Cdd:PRK14360 325 yahlrpeaqIGSNCRIGNFVEIKKSQLgegskVNH 359
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
383-409 3.06e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.01  E-value: 3.06e-03
                          10        20
                  ....*....|....*....|....*...
gi 54291067   383 HCRIGSNVKI-VNSVVMNHVVIEDGCHI 409
Cdd:pfam00132   1 GTVIGDNVLIgPNAVIGGGVIIGDNVII 28
 
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; ...
 3-220 8.80e-58

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: 189.41  E-value: 8.80e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   3 FQVVVLAGGTSEKLSPLvSKDVPKALLPVANRPVLSYVLDLLEASDLKDIIVVVEGQEAARLVGAWASS--AYLDRLLVE 80
Cdd:cd04198   1 FQAVILAGGGGSRLYPL-TDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFplNLKQKLDEV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  81 VVAVPEDIGTAGALRAISKRLTaNDVLVISGDLVTDVLPGAVAATHRRNGAAVTALLCSVPISGPsdaaSSGGKDKAKKP 160
Cdd:cd04198  80 TIVLDEDMGTADSLRHIRKKIK-KDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSE----QKGGKGKSKKA 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067 161 TRLNIVGLDITRQFLLHIVSGTDVEKDVRVYKRKIRAVGEMEIRSDLMDAHLYAFKRTTL 220
Cdd:cd04198 155 DERDVIGLDEKTQRLLFITSEEDLDEDLELRKSLLKRHPRVTITTKLLDAHVYIFKRWVL 214
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 3-220 1.01e-41

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: 147.40  E-value: 1.01e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   3 FQVVVLAGGTSEKLSPLvSKDVPKALLPVANRPVLSYVLDLLEASDLKDIIVVVEGQEAARLVGAWASSAYLDRLLVEVV 82
Cdd:cd02507   1 FQAVVLADGFGSRFLPL-TSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKWSSLSSKMIVD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  83 AVP----EDIGTAGALRAISKRLTaNDVLVISGDLVTDV-LPGAVAAT---HRRNGAAVTALLCSVPISGPSdaassggk 154
Cdd:cd02507  80 VITsdlcESAGDALRLRDIRGLIR-SDFLLLSCDLVSNIpLSELLEERrkkDKNAIATLTVLLASPPVSTEQ-------- 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 54291067 155 dkAKKPTRLNIVGLDITRQFLLHIVSGTDVEKDVRVYKRKI--RAVGEMEIRSDLMDAHLYAFKRTTL 220
Cdd:cd02507 151 --SKKTEEEDVIAVDSKTQRLLLLHYEEDLDEDLELIIRKSllSKHPNVTIRTDLLDCHIYICSPDVL 216
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 362-442 1.06e-35

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: 126.92  E-value: 1.06e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067 362 MLAEGSQLGDKCSVKRSVIGRHCRIGSNVKIVNSVVMNHVVIEDGCHIQGSVICNNVQLQERAVLKDCQVGAGYIVTASS 441
Cdd:cd04652   1 LVGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAGT 80


                .
gi 54291067 442 E 442
Cdd:cd04652  81 E 81
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 4-147 7.76e-26

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: 105.23  E-value: 7.76e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   4 QVVVLAGGTSEKLSPLvSKDVPKALLPVANRPVLSYVLDLLEASDLKDIIVVVeGQEAARLVGAWASSAYLDrLLVEVVA 83
Cdd:COG1208   1 KAVILAGGLGTRLRPL-TDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINV-GYLAEQIEEYFGDGSRFG-VRITYVD 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 54291067  84 VPEDIGTAGALRAISKRLTANDVLVISGDLVTDVLPGAVAATHRRNGAAVTalLCSVPISGPSD 147
Cdd:COG1208  78 EGEPLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLAFHREKGADAT--LALVPVPDPSR 139
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 5-141 1.53e-25

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: 103.81  E-value: 1.53e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   5 VVVLAGGTSEKLSPLvSKDVPKALLPVANRPVLSYVLDLLEASDLKDIIVVVegQEAARLVGAWASSAYLDRLLVEVVAV 84
Cdd:cd04181   1 AVILAAGKGTRLRPL-TDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVV--GYLGEQIEEYFGDGSKFGVNIEYVVQ 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 54291067  85 PEDIGTAGALRAISKRLTANDVLVISGDLVTDVLPGAVAATHRRNGAAVTALLCSVP 141
Cdd:cd04181  78 EEPLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVE 134
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 5-141 6.67e-21

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: 90.69  E-value: 6.67e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   5 VVVLAGGTSEKLSPLVsKDVPKALLPVANRPVLSYVLDLLEASDLKDIIVVVeGQEAArLVGAWASSAYLDRLLVEVVAV 84
Cdd:cd06915   1 AVILAGGLGTRLRSVV-KDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSV-GYLAE-QIEEYFGDGYRGGIRIYYVIE 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 54291067  85 PEDIGTAGALRAISKRLTANDVLVISGDLVTDVLPGAVAATHRRNGAAVTALLCSVP 141
Cdd:cd06915  78 PEPLGTGGAIKNALPKLPEDQFLVLNGDTYFDVDLLALLAALRASGADATMALRRVP 134
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 365-439 1.59e-20

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: 85.37  E-value: 1.59e-20
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 54291067 365 EGSQLGDKCSVKRSVIGRHCRIGSNVKIVNSVVMNHVVIEDGCHIQGSVICNNVQLQERAVLKDCQVgAGYIVTA 439
Cdd:cd03356   4 ESTVIGENAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNLCI-IGDDVVV 77
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 366-428 8.93e-19

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: 80.31  E-value: 8.93e-19
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 54291067 366 GSQLGDKCSVKRSVIGRHCRIGSNVKIVNSVVMNHVVIEDGCHIQGSVICNNVQLQERAVLKD 428
Cdd:cd05787   5 GTSIGEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPP 67
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-213 8.79e-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: 64.55  E-value: 8.79e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   3 FQVVVLAGGTSEKLSPLvSKDVPKALLPVANRPVLSYVLDLLEASDLKDIIVVV---EGQEAARLVGAWASSAYLDRLLV 79
Cdd:cd04197   1 LQAVVLADSFNRRFRPL-TKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCcshSDQIKEYIEKSKWSKPKSSLMIV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  80 EVVAVPEDIGTAGALRAI-SKRLTANDVLVISGDLVTDV-LPGAVAAtHRRN-----GAAVTALLCSvpiSGPSDAASSG 152
Cdd:cd04197  80 IIIMSEDCRSLGDALRDLdAKGLIRGDFILVSGDVVSNIdLKEILEE-HKERrkkdkNAIMTMVLKE---ASPPHRTRRT 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 54291067 153 GKDkakkptrLNIVgLDITRQFLLHI--VSGTDVEKDVRVYKRKIRAVGEMEIRSDLMDAHLY 213
Cdd:cd04197 156 GEE-------FVIA-VDPKTSRLLHYeeLPGSKYRSITDLPSELLGSNSEVEIRHDLLDCHID 210
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 7-144 9.68e-12

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: 64.51  E-value: 9.68e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   7 VLAGGTSEKLSPLvSKDVPKALLPVANRPVLSYVLDLLEASDLKDIIVVVEGQeAARLVGAWASSAYLDRLLV--EvvaV 84
Cdd:cd06422   4 ILAAGLGTRMRPL-TDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHL-ADQIEAHLGDSRFGLRITIsdE---P 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  85 PEDIGTAGALRAISKRLTANDVLVISGDLVTDVLPGAVAATHRRNGAAVTALLCSVPISG 144
Cdd:cd06422  79 DELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLLHAWRMDALLLLLPLVRNPG 138
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 355-434 1.67e-11

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 65.48  E-value: 1.67e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067 355 TTIGPQCMlAEGSQLGDKC----SVKRSVIGRHCRIGSNVKIVNSVVMNHVVIEDGCHIqgsvicnnvqlqERAVL-KDC 429
Cdd:COG0448 278 AKFVRGGK-VKNSLVSNGCiisgTVENSVLFRGVRVESGAVVENSVIMPGVVIGEGAVI------------ENAIIdKNV 344


                ....*
gi 54291067 430 QVGAG 434
Cdd:COG0448 345 VIPPG 349
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 362-427 3.47e-11

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: 59.78  E-value: 3.47e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 54291067 362 MLAEGSQLgDKCSVKRSVIGRHCRIGSNVKIVNSVVMNHVVIEDGCHIQGSVICNNVQLQERAVLK 427
Cdd:cd04651  14 LVSEGCII-SGGTVENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPDGVVIG 78
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 5-134 3.79e-11

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: 62.53  E-value: 3.79e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   5 VVVLAGGTSEKLSPLvSKDVPKALLPVANRPVLSYVLDLLEASDLKDIIVVVEgqeaarlvgawassaYL---------- 74
Cdd:cd06426   1 VVIMAGGKGTRLRPL-TENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVN---------------YLaemiedyfgd 64

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 54291067  75 -DRLLVEVVAVPED--IGTAGALRAISKRLTaNDVLVISGDLVTDVLPGAVAATHRRNGAAVT 134
Cdd:cd06426  65 gSKFGVNISYVREDkpLGTAGALSLLPEKPT-DPFLVMNGDILTNLNYEHLLDFHKENNADAT 126
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1-419 1.18e-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: 63.12  E-value: 1.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   1 MDFQVVVLAGG--T---SEKlsplvskdvPKALLPVANRPVLSYVLDLLEASDLKDIIVVVeGQEAARLvgawasSAYLD 75
Cdd:COG1207   1 SPLAVVILAAGkgTrmkSKL---------PKVLHPLAGKPMLEHVLDAARALGPDRIVVVV-GHGAEQV------RAALA 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  76 RLLVEVVAVPEDIGTAGALRAISKRLTAND--VLVISGD--LVTDVLPGAVAATHRRNGAAVTALLCSVPisgpsdaass 151
Cdd:COG1207  65 DLDVEFVLQEEQLGTGHAVQQALPALPGDDgtVLVLYGDvpLIRAETLKALLAAHRAAGAAATVLTAELD---------- 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067 152 ggkdkakKPT---RlnivgldITRQ---FLLHIVSgtdvEKDVRVYKRKIRavgemEIRSDlmdahLYAFKRTTLQNILE 225
Cdd:COG1207 135 -------DPTgygR-------IVRDedgRVLRIVE----EKDATEEQRAIR-----EINTG-----IYAFDAAALREALP 186

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067 226 E-------KESYrsirL-EVLPYLVRsqlkssssggEGTTVdetgDTTVPS--------NSHLQcLS------QHRILap 283
Cdd:COG1207 187 KlsndnaqGEYY----LtDVIAIARA----------DGLKV----AAVQPEdpwevlgvNDRVQ-LAeaerilQRRIA-- 245

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067 284 safkKDLLSSGgtyrccVYIAtkskychrlnsiqaycDINRdvvgdashlsgysfsaqnNIIHPTSVLGSKTTIGPQCML 363
Cdd:COG1207 246 ----ERLMRAG------VTII----------------DPAT------------------TYIDGDVEIGRDVVIDPNVIL 281

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 54291067 364 aEGsqlgdkcsvkRSVIGRHCRIGSNVKIVNSVVMNHVVIEdGCHIQGSVICNNVQ 419
Cdd:COG1207 282 -EG----------KTVIGEGVVIGPNCTLKDSTIGDGVVIK-YSVIEDAVVGAGAT 325
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 343-440 1.72e-10

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: 60.19  E-value: 1.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067 343 NIIHPTSVLGSKTTIGPQCMLAEGS------QLGDKCSVK-RSVIGRHCRIGSNVKIVNSVVMN-HVVIEDGCHI-QGSV 413
Cdd:cd03360  85 TLIHPSAVVSPSAVIGEGCVIMAGAvinpdaRIGDNVIINtGAVIGHDCVIGDFVHIAPGVVLSgGVTIGEGAFIgAGAT 164

                        90       100
                ....*....|....*....|....*..
gi 54291067 414 ICNNVQLQERAVlkdcqVGAGYIVTAS 440
Cdd:cd03360 165 IIQGVTIGAGAI-----IGAGAVVTKD 186
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 5-141 1.78e-10

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: 60.61  E-value: 1.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   5 VVVL-AG-GTSEKlSPLvskdvPKALLPVANRPVLSYVLDLLEASDLKDIIVVV-EGQEAARlvgawassAYLDRLLVEV 81
Cdd:cd02540   1 AVILaAGkGTRMK-SDL-----PKVLHPLAGKPMLEHVLDAARALGPDRIVVVVgHGAEQVK--------KALANPNVEF 66

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 54291067  82 VAVPEDIGTAGALRAISKRLT--ANDVLVISGD--LVTDVLPGAVAATHRRNGAAVTALLCSVP 141
Cdd:cd02540  67 VLQEEQLGTGHAVKQALPALKdfEGDVLVLYGDvpLITPETLQRLLEAHREAGADVTVLTAELE 130
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 6-166 2.56e-10

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: 60.34  E-value: 2.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067     6 VVLAGGTSEKLSPLvSKDVPKALLPVANR-PVLSYVLDLLEASDLKDIIVVVEGQEAARLVGAWassAYLDRLLVEVVAV 84
Cdd:pfam00483   3 IILAGGSGTRLWPL-TRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELL---GDGSKFGVQITYA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067    85 --PEDIGTAGALRAISKRL--TANDVLVISGDLVTDVLPGAVAATHRRNGAAVTALLCSVPISGPSD----AASSGGK-- 154
Cdd:pfam00483  79 lqPEGKGTAPAVALAADFLgdEKSDVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEPPTGygvvEFDDNGRvi 158

                         170
                  ....*....|....*
gi 54291067   155 ---DKAKKPTRLNIV 166
Cdd:pfam00483 159 rfvEKPKLPKASNYA 173
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-135 8.43e-10

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 58.25  E-value: 8.43e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   1 MDFQVVVLAGGTSEKLsplvskDVPKALLPVANRPVLSYVLDLLEASDLKDIIVVVeGQEAARLvgawasSAYLDRLLVE 80
Cdd:COG2068   2 SKVAAIILAAGASSRM------GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVL-GADAEEV------AAALAGLGVR 68

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 54291067  81 VVAVP---EDIGT--AGALRAISKRLTAndVLVISGD--LVT-DVLpGAVAATHRRNGAAVTA 135
Cdd:COG2068  69 VVVNPdweEGMSSslRAGLAALPADADA--VLVLLGDqpLVTaETL-RRLLAAFRESPASIVA 128
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 344-414 9.75e-10

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: 59.65  E-value: 9.75e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 54291067 344 IIHPTSVLGSKTTIGPQCMLAEGSQLGDKCSVK-RSVIGRHCRIGSNVKIV-NSVVMNHVVIEDGCHIQ-GSVI 414
Cdd:COG1044 104 VIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGpGVVIGDGVVIGDDCVLHpNVTIYERCVIGDRVIIHsGAVI 177
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
4-114 1.04e-09

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 58.71  E-value: 1.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   4 QVVVLAGGTSEKLSPLvSKDVPKALLPVANRPVLSYVLDLLEASDLKDIIVVVeGQEAARLVgawassAYLDRLLVEVVA 83
Cdd:COG1213   1 KAVILAAGRGSRLGPL-TDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVT-GYKAELIE------EALARPGPDVTF 72

                        90       100       110
                ....*....|....*....|....*....|....*
gi 54291067  84 V----PEDIGTAGALrAISKRLTANDVLVISGDLV 114
Cdd:COG1213  73 VynpdYDETNNIYSL-WLAREALDEDFLLLNGDVV 106
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 344-414 1.18e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 59.77  E-value: 1.18e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 54291067  344 IIHPTSVLGSKTTIGPQCMLAEGSQLGDKCSV-KRSVIGRHCRIGSNVKI-VNSVVMNHVVIEDGCHIQ-GSVI 414
Cdd:PRK00892 108 VIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIgAGAVIGDGVKIGADCRLhANVTIYHAVRIGNRVIIHsGAVI 181
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 345-419 2.51e-09

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: 56.66  E-value: 2.51e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 54291067 345 IHPTSVLGSKTTIGPQCMLaEGsqlgdkcsvkRSVIGRHCRIGSNVKIVNSVVMNHVVIEDGCHIQGSVICNNVQ 419
Cdd:cd03353  12 IDGDVEIGVDVVIDPGVIL-EG----------KTVIGEDCVIGPNCVIKDSTIGDGVVIKASSVIEGAVIGNGAT 75
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 6-141 5.92e-09

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: 56.42  E-value: 5.92e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   6 VVLAGGTSEKLSPLvSKDVPKALLPVANRPVLSYVLDLLEASDLKDIIVVV--EGQEAARLVGAWasSAYldRLLVEVVA 83
Cdd:cd04189   4 LILAGGKGTRLRPL-TYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVgpTGEEIKEALGDG--SRF--GVRITYIL 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 54291067  84 VPEDIGTAGALRAISKRLTANDVLVISGD-LVTDVLPGAVAAtHRRNGAAVTALLCSVP 141
Cdd:cd04189  79 QEEPLGLAHAVLAARDFLGDEPFVVYLGDnLIQEGISPLVRD-FLEEDADASILLAEVE 136
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 342-405 1.27e-08

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: 51.86  E-value: 1.27e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067 342 NNIIHPtSVLGSKTTIGP-----QCMLAEGSQLGDKCSVKRSVIGRHCRIGSNVKIVN-SVVMNHVVIED 405
Cdd:cd03356  11 NAIIKN-SVIGDNVRIGDgvtitNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNlCIIGDDVVVED 79
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 348-414 1.87e-08

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: 54.34  E-value: 1.87e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067 348 TSVLGSKTTIGPQCMLAEGSQLGDKCSVK-RSVIGRHCRIGSNVKI-VNSVVMNHVVIEDGCHIQ-GSVI 414
Cdd:cd03352   1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGpGVVIGDGVVIGDDCVIhPNVTIYEGCIIGDRVIIHsGAVI 70
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 5-135 4.91e-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: 52.95  E-value: 4.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   5 VVVLAGGTSEKLsplvskDVPKALLPVANRPVLSYVLDLLEASDLKDIIVVVeGQEAARLvgawasSAYLDRLLVEVVAV 84
Cdd:cd04182   3 AIILAAGRSSRM------GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVL-GAEADAV------RAALAGLPVVVVIN 69

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  85 P---EDIGT--AGALRAISKRLTAndVLVISGD--LVT--DVLpgAVAATHRRNGAAVTA 135
Cdd:cd04182  70 PdweEGMSSslAAGLEALPADADA--VLILLADqpLVTaeTLR--ALIDAFREDGAGIVA 125
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-437 4.94e-08

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 54.84  E-value: 4.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067    1 MDFQVVVLAGG--TSEKlsplvSKdVPKALLPVANRPVLSYVLDLLEASDLKDIIVVVeGQEAARLVGAWASSayldrll 78
Cdd:PRK14354   1 MNRYAIILAAGkgTRMK-----SK-LPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVV-GHGAEEVKEVLGDR------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   79 VEVVAVPEDIGTAGALRAISKRLTAND--VLVISGD--LVTDVLPGAVAATHRRNGAAVTaLLCSVpisgpsdaassggk 154
Cdd:PRK14354  67 SEFALQEEQLGTGHAVMQAEEFLADKEgtTLVICGDtpLITAETLKNLIDFHEEHKAAAT-ILTAI-------------- 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  155 dkAKKPT---RlnIVGLDITRqfLLHIVSgtdvEKDVRVYKRKIRavgemEIRSDlmdahLYAFKRTTLQNILEE----- 226
Cdd:PRK14354 132 --AENPTgygR--IIRNENGE--VEKIVE----QKDATEEEKQIK-----EINTG-----TYCFDNKALFEALKKisndn 191

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  227 --KESYRSIRLEVLpylvRSQlkssssgGE--GTTVDETGDTTVPSNSHLQcLSQ------HRILapsafkKDLLSSGGT 296
Cdd:PRK14354 192 aqGEYYLTDVIEIL----KNE-------GEkvGAYQTEDFEESLGVNDRVA-LAEaekvmrRRIN------EKHMVNGVT 253

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  297 yrccvYIATKSKYchrlnsIQAYCDINRDVVgdashlsgysfsaqnniIHPTSVLGSKTTIGPQCMLAEGS-----QLGD 371
Cdd:PRK14354 254 -----IIDPESTY------IDADVEIGSDTV-----------------IEPGVVIKGNTVIGEDCVIGPGSrivdsTIGD 305

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 54291067  372 KCSVKRSVIgRHCRIGSNVKI-------VNSVVMNHVVIEDGCHIQGSVICNNVQLQERA------VLKDCQVGAGYIV 437
Cdd:PRK14354 306 GVTITNSVI-EESKVGDNVTVgpfahlrPGSVIGEEVKIGNFVEIKKSTIGEGTKVSHLTyigdaeVGENVNIGCGTIT 383
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
344-438 6.70e-08

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 51.41  E-value: 6.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067 344 IIHPTSVLGSKTTIGPQCMLAEGSQLGDKCSVKrsvIGRHCRIGSNVKIVNS-----------VVMNHVVIEDGCHI-QG 411
Cdd:COG0110  17 IGPGVRIYGGNITIGDNVYIGPGVTIDDPGGIT---IGDNVLIGPGVTILTGnhpiddpatfpLRTGPVTIGDDVWIgAG 93

                        90       100
                ....*....|....*....|....*..
gi 54291067 412 SVICNNVQLQERAVlkdcqVGAGYIVT 438
Cdd:COG0110  94 ATILPGVTIGDGAV-----VGAGSVVT 115
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 5-136 7.71e-08

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: 51.81  E-value: 7.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067     5 VVVLAGGTSEKLsplvskDVPKALLPVANRPVLSYVLDLLEASdLKDIIVVVEGQEAArlvgawassAYLDRLLVEVVAV 84
Cdd:pfam12804   1 AVILAGGRSSRM------GGDKALLPLGGKPLLERVLERLRPA-GDEVVVVANDEEVL---------AALAGLGVPVVPD 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 54291067    85 P-EDIGTAGALRAISKRLTAND-VLVISGD--LVTDVLPGAVAATHRRNGAAVTAL 136
Cdd:pfam12804  65 PdPGQGPLAGLLAALRAAPGADaVLVLACDmpFLTPELLRRLLAAAEESGADIVVP 120
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 5-136 1.89e-07

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: 51.76  E-value: 1.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   5 VVVLAGGTSEKLSPlvskDVPKALLPVANRPVLSYVLDLLEASDL-KDIIVVVEGQEAARlvgAWASSAYLDRLLVEVVA 83
Cdd:cd02516   3 AIILAAGSGSRMGA----DIPKQFLELGGKPVLEHTLEAFLAHPAiDEIVVVVPPDDIDL---AKELAKYGLSKVVKIVE 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 54291067  84 vpedigtAGALRAIS-----KRLTAND---VLV-------ISGDLVTDVLpgAVAATHrrnGAAVTAL 136
Cdd:cd02516  76 -------GGATRQDSvlnglKALPDADpdiVLIhdaarpfVSPELIDRLI--DALKEY---GAAIPAV 131
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 6-136 1.90e-07

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: 51.67  E-value: 1.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   6 VVLAGGTSEKLSplvsKDVPKALLPVANRPVLSYVLDLLEAS-DLKDIIVVVEGQEAARLVGAWAssAYLDRLLVEVVAv 84
Cdd:COG1211   1 IIPAAGSGSRMG----AGIPKQFLPLGGKPVLEHTLEAFLAHpRIDEIVVVVPPDDIEYFEELLA--KYGIDKPVRVVA- 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 54291067  85 pediGtaGALRAIS-----KRLTAND--VLV-------ISGDLVTDVLpgAVAATHrrnGAAVTAL 136
Cdd:COG1211  74 ----G--GATRQDSvrnglEALPDDDdwVLVhdaarplVSPELIDRVI--EAAREY---GAAIPAL 128
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
6-56 2.09e-07

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 52.40  E-value: 2.09e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 54291067   6 VVLAGGTSEKLSPLvSKDVPKALLPVANRPVLSYVLDLLEASDLKDIIVVV 56
Cdd:COG1209   4 IILAGGSGTRLRPL-TLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIIS 53
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 5-140 3.33e-07

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: 51.06  E-value: 3.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   5 VVVLAGGTSEKLSPLVSKdVPKALLPVANRPVLSYVLDLLEASDLKDIIVVVEgQEAARLVGawASSAYLDRLLVEVVAV 84
Cdd:cd06425   3 ALILVGGYGTRLRPLTLT-VPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVN-YRPEDMVP--FLKEYEKKLGIKITFS 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  85 PED--IGTAGALRAISKRLTAND--VLVISGDLVTDVLPGAVAATHRRNGAAVTALLCSV 140
Cdd:cd06425  79 IETepLGTAGPLALARDLLGDDDepFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKV 138
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 5-56 3.89e-07

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: 50.69  E-value: 3.89e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 54291067   5 VVVLAGGTSEKLSPLvSKDVPKALLPVANRPVLSYVLDLLEASDLKDIIVVV 56
Cdd:cd02523   1 AIILAAGRGSRLRPL-TEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVT 51
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-113 4.42e-07

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: 50.19  E-value: 4.42e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   1 MDFQVVVLAGGTSEKLSplvskdVPKALLPVANRPVLSYVLDLLeASDLKDIIVVVEGQEAARLVGawassayldrllVE 80
Cdd:COG0746   3 MPITGVILAGGRSRRMG------QDKALLPLGGRPLLERVLERL-RPQVDEVVIVANRPERYAALG------------VP 63

                        90       100       110
                ....*....|....*....|....*....|....
gi 54291067  81 VVA-VPEDIGTAGALRAISKRLTANDVLVISGDL 113
Cdd:COG0746  64 VVPdDPPGAGPLAGILAALEAAPAEWVLVLACDM 97
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-136 5.75e-07

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 51.79  E-value: 5.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067    6 VVLAGGTSEKL-SPLvskdvPKALLPVANRPVLSYVLDLLEASDLKDIIVVV-EGQEAarlVGAWASSAYLDrllVEVVA 83
Cdd:PRK14353   9 IILAAGEGTRMkSSL-----PKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVgPGAEA---VAAAAAKIAPD---AEIFV 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 54291067   84 VPEDIGTAGALRAISKRLT--ANDVLVISGD--LVT-DVLPGAVAatHRRNGAAVTAL 136
Cdd:PRK14353  78 QKERLGTAHAVLAAREALAggYGDVLVLYGDtpLITaETLARLRE--RLADGADVVVL 133
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 3-141 6.69e-07

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 51.52  E-value: 6.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067    3 FQVVVLAGGTSEKLSplvsKDVPKALLPVANRPVLSYVLDLLEASDLKDiIVVVEGQEAARLVGAWASSAyldrllVEVV 82
Cdd:PRK14358   8 LDVVILAAGQGTRMK----SALPKVLHPVAGRPMVAWAVKAARDLGARK-IVVVTGHGAEQVEAALQGSG------VAFA 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 54291067   83 AVPEDIGTAGALRAISKRLTAN--DVLVISGD---LVTDVLPgAVAATHRRNGAAVTALLCSVP 141
Cdd:PRK14358  77 RQEQQLGTGDAFLSGASALTEGdaDILVLYGDtplLRPDTLR-ALVADHRAQGSAMTILTGELP 139
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-141 1.56e-06

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 50.32  E-value: 1.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067    5 VVVLAGGTSEKLSplvsKDVPKALLPVANRPVLSYVLDLLEASDLKDIIVVV--EGQEAARLVGAWASSAyldrllveVV 82
Cdd:PRK14352   7 VIVLAAGAGTRMR----SDTPKVLHTLAGRSMLGHVLHAAAGLAPQHLVVVVghDRERVAPAVAELAPEV--------DI 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 54291067   83 AVPEDI-GTAGALRAISKRLTAN---DVLVISGD--LVTDVLPGAVAATHRRNGAAVTALLCSVP 141
Cdd:PRK14352  75 AVQDEQpGTGHAVQCALEALPADfdgTVVVTAGDvpLLDGETLADLVATHTAEGNAVTVLTTTLD 139
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 347-418 3.02e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 49.11  E-value: 3.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  347 PTSVLGSKTTigpQCMLAEGSQLgDKCSVKRSVIGRHCRIGSNVKIVNSVVMN-------------------HVVIEDGC 407
Cdd:PRK02862 298 PSKLLDATIT---ESIIAEGCII-KNCSIHHSVLGIRSRIESGCTIEDTLVMGadfyesseereelrkegkpPLGIGEGT 373

                         90
                 ....*....|.
gi 54291067  408 HIQGSVICNNV 418
Cdd:PRK02862 374 TIKRAIIDKNA 384
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 344-414 3.98e-06

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: 48.09  E-value: 3.98e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 54291067 344 IIHPTSVLGSKTTIGPQCmlaegsqlgdkcsvkrsVIGRHCRIGSNVKIV-NSVVMNHVVIEDGCHI-QGSVI 414
Cdd:COG1043   9 IVDPGAKLGENVEIGPFC-----------------VIGPDVEIGDGTVIGsHVVIEGPTTIGKNNRIfPFASI 64
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 1-139 7.63e-06

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: 47.92  E-value: 7.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067    1 MDFQVVVLAGGTSEKLSPlvskDVPKALLPVANRPVLSYVLD-LLEASDLKDIIVVV-EGQEAArlvgawASSAYLDRLL 78
Cdd:PRK09382   4 SDISLVIVAAGRSTRFSA----EVKKQWLRIGGKPLWLHVLEnLSSAPAFKEIVVVIhPDDIAY------MKKALPEIKF 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 54291067   79 VEVVavpedigTAGALRAISKRltaNDVLVISGD--LVTDV----LPGAV----AATHRRNGAAVTALLCS 139
Cdd:PRK09382  74 VTLV-------TGGATRQESVR---NALEALDSEyvLIHDAarpfVPKELidrlIEALDKADCVLPALPVA 134
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 322-434 9.26e-06

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 47.82  E-value: 9.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  322 INRDVVgdashLSGYSF-SAQNNIIHPTSVLGSKTTIGPQCMLAEGSQLGDKCSVKRSVIGRHCRIGSNVKI------VN 394
Cdd:PRK14355 246 INRELM-----LAGVTLiDPETTYIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKGCRIGDDVTVkagsvlED 320

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 54291067  395 SVVMNHVVIEDGCHIQ-GSVICNNVQLQERAVLKDCQVGAG 434
Cdd:PRK14355 321 SVVGDDVAIGPMAHLRpGTELSAHVKIGNFVETKKIVMGEG 361
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 6-113 9.28e-06

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: 46.03  E-value: 9.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   6 VVLAGGTSEKLSPlvskdvPKALLPVANRPVLSYVLDLLEASDLKDIIVVVEGQEAARLVGawassayldrllVEVVA-V 84
Cdd:cd02503   4 VILAGGKSRRMGG------DKALLELGGKPLLEHVLERLKPLVDEVVISANRDQERYALLG------------VPVIPdE 65

                        90       100
                ....*....|....*....|....*....
gi 54291067  85 PEDIGTAGALRAISKRLTANDVLVISGDL 113
Cdd:cd02503  66 PPGKGPLAGILAALRAAPADWVLVLACDM 94
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 320-418 1.80e-05

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 45.49  E-value: 1.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067 320 CDINRDVVgdashlsgysfSAQNNIIHPTSVLGSKTTIGPQCMLAEGSQLGDkcsvkrSVIGRHCRIGSNVKIVNSVVMN 399
Cdd:cd03353  10 TYIDGDVE-----------IGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKD------STIGDGVVIKASSVIEGAVIGN 72

                        90       100
                ....*....|....*....|
gi 54291067 400 HVVIEDGCHIQ-GSVICNNV 418
Cdd:cd03353  73 GATVGPFAHLRpGTVLGEGV 92
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 369-438 2.86e-05

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: 43.26  E-value: 2.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067 369 LGDKCSVKRSV-IGRHCRIGSNVKIVNSV-VMNHVVIEDGCHI----------------------QGSVICNNVQLQERA 424
Cdd:cd03358   1 IGDNCIIGTNVfIENDVKIGDNVKIQSNVsIYEGVTIEDDVFIgpnvvftndlyprskiyrkwelKGTTVKRGASIGANA 80

                        90       100
                ....*....|....*....|.
gi 54291067 425 VL-------KDCQVGAGYIVT 438
Cdd:cd03358  81 TIlpgvtigEYALVGAGAVVT 101
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 6-112 2.95e-05

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: 45.26  E-value: 2.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   6 VVLAGGTSEKLSPLvSKDVPKALLPVANRPVLSYVLDLLEASDLKDIIVVVEGQEAARLVgawassayldRLL------- 78
Cdd:cd02538   4 IILAGGSGTRLYPL-TKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFK----------ELLgdgsdlg 72

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 54291067  79 --VEVVAVPEDIGTAGALrAISKRLTAND-VLVISGD 112
Cdd:cd02538  73 irITYAVQPKPGGLAQAF-IIGEEFIGDDpVCLILGD 108
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
1-136 3.09e-05

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 45.12  E-value: 3.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067    1 MDFQVVVLAGGTSEKLSPlvskDVPKALLPVANRPVLSYVLD-LLEASDLKDIIVVVEGQEAARLVGawASSAYLDRllV 79
Cdd:PRK00155   2 MMVYAIIPAAGKGSRMGA----DRPKQYLPLGGKPILEHTLEaFLAHPRIDEIIVVVPPDDRPDFAE--LLLAKDPK--V 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   80 EVVAvpediGtaGALRAIS-----KRLTAND-VLV-------ISGDLVTDVLpgAVAATHrrnGAAVTAL 136
Cdd:PRK00155  74 TVVA-----G--GAERQDSvlnglQALPDDDwVLVhdaarpfLTPDDIDRLI--EAAEET---GAAILAV 131
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 8-180 3.80e-05

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: 44.11  E-value: 3.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   8 LAGGTSEKLsplvsKDVPKALLPVANRPVLSYVLDLLEASDLKDIIVVV-EGQEAARlvgawassAYLDRLLVEVVAVP- 85
Cdd:COG2266   1 MAGGKGTRL-----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVsPNTPKTR--------EYLKERGVEVIETPg 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  86 ----EDIGTagALRAISKRltandVLVISGDL---VTDVLPGAVAATHRRNGAAVT-----ALLCSVPISgPSDAASSGG 153
Cdd:COG2266  68 egyvEDLNE--ALESISGP-----VLVVPADLpllTPEIIDDIIDAYLESGKPSLTvvvpaALKRELGVS-PDTTFEIDG 139

                       170       180
                ....*....|....*....|....*...
gi 54291067 154 KdkaKKPTRLNIV-GLDITRQFLLHIVS 180
Cdd:COG2266 140 E---LVPTGINIVdGSDGEQEETNLVLD 164
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 349-409 4.19e-05

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 45.45  E-value: 4.19e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 54291067 349 SVLGSKTTIGpqcmlaEGSQlgdkcsVKRSVIGRHCRIGSNVKIVNSVVMNHVVIEDGCHI 409
Cdd:COG0448 304 SVLFRGVRVE------SGAV------VENSVIMPGVVIGEGAVIENAIIDKNVVIPPGVVI 352
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 316-442 4.64e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 45.24  E-value: 4.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  316 IQAYCDINRDVVGDASHLSGYS-----FSaqNNIIHPTSVLGSKTTIgpqcmlaEGSQLGDKC----SVKRSVIGRHCRI 386
Cdd:PRK05293 247 IESLWEANMELLRPENPLNLFDrnwriYS--VNPNLPPQYIAENAKV-------KNSLVVEGCvvygTVEHSVLFQGVQV 317

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 54291067  387 GSNVKIVNSVVMNHVVIEDGCHIQGSVICNNVQLQERAVLKDCQ-----VGAGYIVTASSE 442
Cdd:PRK05293 318 GEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIGGGKevitvIGENEVIGVGTV 378
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
344-414 4.99e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 44.70  E-value: 4.99e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 54291067  344 IIHPTSVLGSKTTIGPQCmlaegsqlgdkcsvkrsVIGRHCRIGSNVKIV-NSVVMNHVVIEDGCHI-QGSVI 414
Cdd:PRK05289  10 IVEPGAKIGENVEIGPFC-----------------VIGPNVVIGDGTVIGsHVVIDGHTTIGKNNRIfPFASI 65
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 5-136 6.25e-05

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: 44.55  E-value: 6.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   5 VVVLAGGTSE--KLSPLvSKDVPKALLPVANRPVLSYVLDLL-EASDLKDIIvvvegqeaarLVGAWASSAYLD------ 75
Cdd:cd06428   1 AVILVGGPQKgtRFRPL-SLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVL----------LIGFYPESVFSDfisdaq 69

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 54291067  76 -------RLLVEvvavPEDIGTAGALRAISKRLTAND---VLVISGDLVTDVLPGAVAATHRRNGAAVTAL 136
Cdd:cd06428  70 qefnvpiRYLQE----YKPLGTAGGLYHFRDQILAGNpsaFFVLNADVCCDFPLQELLEFHKKHGASGTIL 136
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 374-440 6.42e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 45.20  E-value: 6.42e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 54291067  374 SVKRSVIGRHCRIGSNVKIVNSVVMNHVVIEDGCHIQGSVICNNVQLQERAvlkdcQVG-------AGYIVTAS 440
Cdd:PRK00844 328 TVRNSVLSPNVVVESGAEVEDSVLMDGVRIGRGAVVRRAILDKNVVVPPGA-----TIGvdleedrRRFTVSEG 396
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 6-135 9.92e-05

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 44.28  E-value: 9.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067    6 VVLAGGTSEKLSPlVSKDVPKALLPVANRPVLSYVLDLLEASDLKDIIVVVEGQEAAR---LVGawASSAYLDRLLVEVV 82
Cdd:PRK15480   7 IILAGGSGTRLYP-VTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRfqqLLG--DGSQWGLNLQYKVQ 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 54291067   83 AVPEdiGTAGALRAISKRLTANDVLVISGDLV---TDVLPGAVAATHRRNGAAVTA 135
Cdd:PRK15480  84 PSPD--GLAQAFIIGEEFIGGDDCALVLGDNIfygHDLPKLMEAAVNKESGATVFA 137
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 321-414 1.06e-04

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 42.71  E-value: 1.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067 321 DINRDVVGDASHLsgysfsaQNN-IIH-----PTsVLGSKTTIGPQCMLaegsqlgdkcsvkrsvigrH-CRIGSNVKI- 392
Cdd:COG0663  46 DVGPIRIGEGSNI-------QDGvVLHvdpgyPL-TIGDDVTIGHGAIL-------------------HgCTIGDNVLIg 98

                        90       100
                ....*....|....*....|...
gi 54291067 393 VNSVVMNHVVIEDGCHIQ-GSVI 414
Cdd:COG0663  99 MGAIVLDGAVIGDGSIVGaGALV 121
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 370-446 1.12e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 44.43  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  370 GDKCSVKRSVIGRHCRIgSNVKIVNSVVMNHVVIEDGCHIQGSVICNNVQLQERAVL------KDCQVGAGYIVTASSEH 443
Cdd:PRK00844 308 GRVGSAQDSLVSAGSII-SGATVRNSVLSPNVVVESGAEVEDSVLMDGVRIGRGAVVrraildKNVVVPPGATIGVDLEE 386


                 ...
gi 54291067  444 KAE 446
Cdd:PRK00844 387 DRR 389
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 344-409 1.61e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 43.09  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  344 IIHPTSVLGSKTTIGPQCMLAEGSQLGDKCSV-KRSVIGRHCRIGSNVKIVNSVVM-------------NHVVIEDGCHI 409
Cdd:PRK12461   7 VIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIgPHAVILGPTRIGKNNKIHQGAVVgdepqdftykgeeSRLEIGDRNVI 86
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 344-420 2.55e-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: 41.42  E-value: 2.55e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 54291067 344 IIHPTSVLGSKTTIGPQCMLAEGSQLGDKCSVKRSV-IGRHCRIGSNVKIVNSVVMNHVVIEDGCHIQGSVICNNVQL 420
Cdd:cd05636  19 WIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTvLGDGCVVGNSVEVKNSIIMDGTKVPHLNYVGDSVLGENVNL 96
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 321-414 3.32e-04

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: 40.86  E-value: 3.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067 321 DINRDVVGDASHLsgysfsaQNN-IIHPTS----VLGSKTTIGPQCMLaegsqlgdkcsvkrsvigrH-CRIGSNVKI-V 393
Cdd:cd04645  35 DVNPIRIGERTNI-------QDGsVLHVDPgyptIIGDNVTVGHGAVL-------------------HgCTIGDNCLIgM 88

                        90       100
                ....*....|....*....|..
gi 54291067 394 NSVVMNHVVIEDGCHIQ-GSVI 414
Cdd:cd04645  89 GAIILDGAVIGKGSIVAaGSLV 110
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 344-414 4.77e-04

UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this family catalyze the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc. It is the first enzyme in the lipid A biosynthetic pathway and is also referred to as LpxA. Lipid A is essential for the growth of Escherichia coli and related bacteria. It is also essential for maintaining the integrity of the outer membrane. UDP-GlcNAc acyltransferase is a homotrimer of left-handed parallel beta helix (LbH) subunits. Each subunit contains an N-terminal LbH region with 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal alpha-helical region.


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 41.65  E-value: 4.77e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 54291067 344 IIHPTSVLGSKTTIGPQCmlaegsqlgdkcsvkrsVIGRHCRIGSNVKIvnsvvMNHVVIE------DGCHI-QGSVI 414
Cdd:cd03351   7 IVDPGAKIGENVEIGPFC-----------------VIGPNVEIGDGTVI-----GSHVVIDgpttigKNNRIfPFASI 62
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 316-438 7.90e-04

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: 40.48  E-value: 7.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067 316 IQAYCDINRDVVGDASHLSGYSfsaqnnIIHpTSVLGSKTTIGP------QCMLAEGSQLGDKCSVKRSVIGRH------ 383
Cdd:cd03353  42 IGPNCVIKDSTIGDGVVIKASS------VIE-GAVIGNGATVGPfahlrpGTVLGEGVHIGNFVEIKKSTIGEGskanhl 114

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 54291067 384 -----CRIGSNVKI------VN--SVVMNHVVIEDGCHIqGSvicnNVQLqeRA---VLKDCQVGAGYIVT 438
Cdd:cd03353 115 sylgdAEIGEGVNIgagtitCNydGVNKHRTVIGDNVFI-GS----NSQL--VApvtIGDGATIAAGSTIT 178
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 22-56 8.29e-04

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: 40.98  E-value: 8.29e-04
                        10        20        30
                ....*....|....*....|....*....|....*
gi 54291067  22 KDVPKALLPVANRPVLSYVLDLLEASDLKDIIVVV 56
Cdd:cd02541  19 KAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVT 53
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 315-400 1.36e-03

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 41.07  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  315 SIQAYCDINRDVVGDA-SHLSGysfsaqnniihpTSVLGSKTTIGPQCmLAEGSQLGDKCSVKRSV-------------- 379
Cdd:PRK14360 258 TISETVELGPDVIIEPqTHLRG------------NTVIGSGCRIGPGS-LIENSQIGENVTVLYSVvsdsqigdgvkigp 324

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 54291067  380 ---------IGRHCRIGSNVKIVNSVV-----MNH 400
Cdd:PRK14360 325 yahlrpeaqIGSNCRIGNFVEIKKSQLgegskVNH 359
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 315-411 1.49e-03

UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this family catalyze the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc. It is the first enzyme in the lipid A biosynthetic pathway and is also referred to as LpxA. Lipid A is essential for the growth of Escherichia coli and related bacteria. It is also essential for maintaining the integrity of the outer membrane. UDP-GlcNAc acyltransferase is a homotrimer of left-handed parallel beta helix (LbH) subunits. Each subunit contains an N-terminal LbH region with 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal alpha-helical region.


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 40.11  E-value: 1.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067 315 SIQAYCDINRDVV-GD----ASH--LSGYSFSAQNNIIHPTSVLG------------SKTTIGPQCMLAEGsqlgdkCSV 375
Cdd:cd03351  19 EIGPFCVIGPNVEiGDgtviGSHvvIDGPTTIGKNNRIFPFASIGeapqdlkykgepTRLEIGDNNTIREF------VTI 92

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 54291067 376 KRS--------VIGRH------------CRIGSNVKIVNSVVM-NHVVIEDGCHIQG 411
Cdd:cd03351  93 HRGtaqgggvtRIGNNnllmayvhvahdCVIGNNVILANNATLaGHVEIGDYAIIGG 149
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 319-394 1.50e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 40.64  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  319 YCDINRDVVGDASHLsgysfsaQNNIIHpTSVLGSKTTIGPQCML---------------------AEGSQ---LGDKCS 374
Cdd:PRK02862 303 DATITESIIAEGCII-------KNCSIH-HSVLGIRSRIESGCTIedtlvmgadfyesseereelrKEGKPplgIGEGTT 374

                         90       100
                 ....*....|....*....|
gi 54291067  375 VKRSVIGRHCRIGSNVKIVN 394
Cdd:PRK02862 375 IKRAIIDKNARIGNNVRIVN 394
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 347-398 1.57e-03

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 40.61  E-value: 1.57e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 54291067  347 PTSVLGSK---TTIGPQCMLAEgsqlgdkCSVKRSVIGRHCRIGSNVKIVNSVVM 398
Cdd:PLN02241 305 PSKIEDCRitdSIISHGCFLRE-------CKIEHSVVGLRSRIGEGVEIEDTVMM 352
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 374-422 1.59e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 40.59  E-value: 1.59e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 54291067  374 SVKRSVIGRHCRIGSNVKIVNSVVMNHVVIEDGCHIQGSVICNNVQLQE 422
Cdd:PRK00725 340 VVRRSVLFSRVRVNSFSNVEDSVLLPDVNVGRSCRLRRCVIDRGCVIPE 388
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 341-418 2.45e-03

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: 39.00  E-value: 2.45e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 54291067 341 QNNIIHPTSVLGSKTTIGPQCMLAEGSQLGDKCsvkrsVIGRHCRIGSnvkivNSVVMNHVVIEDGCHI-QGSVICNNV 418
Cdd:cd03360 119 DNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGV-----TIGEGAFIGA-----GATIIQGVTIGAGAIIgAGAVVTKDV 187
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
383-409 3.06e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.01  E-value: 3.06e-03
                          10        20
                  ....*....|....*....|....*...
gi 54291067   383 HCRIGSNVKI-VNSVVMNHVVIEDGCHI 409
Cdd:pfam00132   1 GTVIGDNVLIgPNAVIGGGVIIGDNVII 28
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 345-448 3.38e-03

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: 38.12  E-value: 3.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067 345 IHPTSVLGSKTTIGPQC---------------MLAEGSQLGDKCsVKRSVIGRHCRIGSNVKIvnsvvmNHVVIEDGCHI 409
Cdd:cd04745   9 VHPTAVLIGDVIIGKNCyigphaslrgdfgriVIRDGANVQDNC-VIHGFPGQDTVLEENGHI------GHGAILHGCTI 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 54291067 410 -QGSVICNNVQLQERAVL-KDCQVGAGYIVTASSEHKAESL 448
Cdd:cd04745  82 gRNALVGMNAVVMDGAVIgEESIVGAMAFVKAGTVIPPRSL 122
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 334-429 4.10e-03

Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p25 is part of the pointed-end subcomplex in dynactin that also includes p26, p27, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 37.96  E-value: 4.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067 334 SGYSFSAQNNIIHPTS-VLGSKTTIGPQCMLAegsqlGDKCSVKrsvIGRHCRIGSNVKIV------------------- 393
Cdd:cd03359   6 SGNKVSRKSVICGSQNiVLNGKTIIQSDVIIR-----GDLATVS---IGRYCILSEGCVIRppfkkfskgvaffplhigd 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 54291067 394 ------NSVVM-----NHVVIEDGCHIqgsvicnnvqlQERAVLKDC 429
Cdd:cd03359  78 yvfigeNCVVNaaqigSYVHIGKNCVI-----------GRRCIIKDC 113
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 342-411 4.50e-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: 38.85  E-value: 4.50e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 54291067 342 NNII------HP-TSVLGSKTTIGPQCMLAEGSQLGdkcsvkrsvigrH-CRIGSNVKIVNSVVM-NHVVIEDGCHIQG 411
Cdd:COG1043  85 NNTIrefvtiHRgTVQGGGVTRIGDDNLLMAYVHVA------------HdCVVGNNVILANNATLaGHVEVGDHAIIGG 151
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 315-414 4.73e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 38.85  E-value: 4.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  315 SIQAYCDINRDV-------VGDASHLSGYSFSAQNNIIHPTSVLG------------SKTTIGPQCMLAEG--------- 366
Cdd:PRK12461  19 EIGPFAVIGANVeigdgtwIGPHAVILGPTRIGKNNKIHQGAVVGdepqdftykgeeSRLEIGDRNVIREGvtihrgtkg 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 54291067  367 ---SQLGDKCS-VKRSVIGRHCRIGSNVKIVNSVVM-NHVVIEDGCHIQGSVI 414
Cdd:PRK12461  99 ggvTRIGNDNLlMAYSHVAHDCQIGNNVILVNGALLaGHVTVGDRAIISGNCL 151
PRK01346 PRK01346
enhanced intracellular survival protein Eis;
65-137 5.30e-03

enhanced intracellular survival protein Eis;


Pssm-ID: 234945 [Multi-domain]  Cd Length: 411  Bit Score: 39.14  E-value: 5.30e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 54291067   65 VGAWASSAYLDRLLVeVVAVPEDIGTAGAlraISKRLTANDVLVISGDLVTDVlpgAVAATHRRNGAAvTALL 137
Cdd:PRK01346  37 LEAWRALVEPDRTLG-AFDGDEVVGTAGA---FDLRLTVPGGAVLPAAGVTAV---TVAPTHRRRGLL-TALM 101
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 320-428 6.05e-03

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 38.68  E-value: 6.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067  320 CDINRDVVGDASHLSGYSfsaqnnIIHptSVLGSKTTIGPQC---------------------MLAEGS---QLGDKCSV 375
Cdd:PLN02241 311 CRITDSIISHGCFLRECK------IEH--SVVGLRSRIGEGVeiedtvmmgadyyeteeeiasLLAEGKvpiGIGENTKI 382

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 54291067  376 KRSVIGRHCRIGSNVKIVNSV-VMNHVVIEDGCHIQGSVIcnnVQLQErAVLKD 428
Cdd:PLN02241 383 RNAIIDKNARIGKNVVIINKDgVQEADREEEGYYIRSGIV---VILKN-AVIPD 432
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
21-135 6.67e-03

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 38.33  E-value: 6.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291067   21 SKDVPKALLPVANRPVLSYVLDLLEASDLKDIIVVVEGQEAA---RLVGAWASSAYLD-----RLLVEVVAV-------- 84
Cdd:PRK10122  21 TKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAvenHFDTSYELESLLEqrvkrQLLAEVQSIcppgvtim 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 54291067   85 ----PEDIGTAGALRAISKRLTANDVLVISGDLVTDvlpGAVAATHRRNGAAVTA 135
Cdd:PRK10122 101 nvrqGQPLGLGHSILCARPAIGDNPFVVVLPDVVID---DASADPLRYNLAAMIA 152
 
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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