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Conserved domains on  [gi|2449300292|ref|NP_001403931|]
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translation initiation factor eIF2B subunit epsilon isoform 2 [Mus musculus]

Protein Classification

translation initiation factor eIF-2B subunit epsilon( domain architecture ID 10135942)

translation initiation factor eIF-2B subunit epsilon is one of the five subunits of the guanine nucleotide exchange factor for eIF-2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 39-253 3.36e-112

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: 338.04  E-value: 3.36e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292  39 LQAVLVADSFNRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLQKSKWC-HPTSPNVVR 117
Cdd:cd04197     1 LQAVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKSKWSkPKSSLMIVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 118 IITSELYRSLGDVLRDVDAKALVRSDFLLIYGDVISNINICRALEEHRLRRKLEKNVsVMTMVFKESSPSHPTRCHEDNV 197
Cdd:cd04197    81 IIMSEDCRSLGDALRDLDAKGLIRGDFILVSGDVVSNIDLKEILEEHKERRKKDKNA-IMTMVLKEASPPHRTRRTGEEF 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2449300292 198 VMAVDSATNRVLHFQKTQGLRRFSF--PLSLFQGSGDGVEIRYDLLDCHISICSPQVA 253
Cdd:cd04197   160 VIAVDPKTSRLLHYEELPGSKYRSItdLPSELLGSNSEVEIRHDLLDCHIDICSPDVL 217
W2_eIF2B_epsilon cd11558
C-terminal W2 domain of eukaryotic translation initiation factor 2B epsilon; eIF2B is a ...
 550-713 4.41e-54

C-terminal W2 domain of eukaryotic translation initiation factor 2B epsilon; eIF2B is a heteropentameric complex which functions as a guanine nucleotide exchange factor in the recycling of eIF-2 during the initiation of translation in eukaryotes. The epsilon and gamma subunits are sequence similar and both are essential in yeast. Epsilon appears to be the catalytically active subunit, with gamma enhancing its activity. The C-terminal domain of the eIF2B epsilon subunit contains bipartite motifs rich in acidic and aromatic residues, which are responsible for the interaction with eIF2. The structure of the domain resembles that of a set of concatenated HEAT repeats.


:

Pssm-ID: 211396  Cd Length: 169  Bit Score: 183.61  E-value: 4.41e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 550 DDIRVFQNEVLGTLQRGREENISCENLVLEINSLKHAYNISLKEVMQVLTLVVLEFPLQQVDglLDPNRYCALLLPLLKA 629
Cdd:cd11558     1 DDESDFHSEVVESLERALEENHSVDNAILEINSLRMAYNVTDHDVRRAVVKALLELILEVSS--TSTAELLEALKKLLSK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 630 WSPVLRNYIKRAADHLEALAAIEDFFLEHETLVTSMAKVLMAFYQLEILAEETILSWFSQRDTTDEGQQLRKNQQLQRFI 709
Cdd:cd11558    79 WGPLLENYVKSQDDQVELLLALEEFCLESEEGGPLFAKLLHALYDLDILEEEAILEWWEEPDAGADEEMKKVRELVKKFI 158


                  ....
gi 2449300292 710 QWLR 713
Cdd:cd11558   159 EWLE 162
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 357-435 6.64e-33

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: 121.53  E-value: 6.64e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2449300292 357 LLGAGTVIGSNCSITNSVIGPNCHIGDNVVLDQAYLWQGVRVAAGAQIHQSLLCDRAEVKERVKLKPYCVLTSQVVVGP 435
Cdd:cd05787     1 VIGRGTSIGEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPGSLISFGVVIGD 79
glgC super family cl32030
glucose-1-phosphate adenylyltransferase; Provisional
 318-392 4.33e-03

glucose-1-phosphate adenylyltransferase; Provisional


The actual alignment was detected with superfamily member PRK02862:

Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 40.25  E-value: 4.33e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2449300292 318 TPEVNFTDSTTQSYTHSRHNiyrgPEVSLGHGSVLEenVLLGAGTVIgSNCSITNSVIGPNCHIGDNVVLDQAYL 392
Cdd:PRK02862  277 NPPFSFYDEKAPIYTRARYL----PPSKLLDATITE--SIIAEGCII-KNCSIHHSVLGIRSRIESGCTIEDTLV 344
 
Name Accession Description Interval E-value
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 39-253 3.36e-112

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: 338.04  E-value: 3.36e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292  39 LQAVLVADSFNRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLQKSKWC-HPTSPNVVR 117
Cdd:cd04197     1 LQAVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKSKWSkPKSSLMIVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 118 IITSELYRSLGDVLRDVDAKALVRSDFLLIYGDVISNINICRALEEHRLRRKLEKNVsVMTMVFKESSPSHPTRCHEDNV 197
Cdd:cd04197    81 IIMSEDCRSLGDALRDLDAKGLIRGDFILVSGDVVSNIDLKEILEEHKERRKKDKNA-IMTMVLKEASPPHRTRRTGEEF 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2449300292 198 VMAVDSATNRVLHFQKTQGLRRFSF--PLSLFQGSGDGVEIRYDLLDCHISICSPQVA 253
Cdd:cd04197   160 VIAVDPKTSRLLHYEELPGSKYRSItdLPSELLGSNSEVEIRHDLLDCHIDICSPDVL 217
W2_eIF2B_epsilon cd11558
C-terminal W2 domain of eukaryotic translation initiation factor 2B epsilon; eIF2B is a ...
 550-713 4.41e-54

C-terminal W2 domain of eukaryotic translation initiation factor 2B epsilon; eIF2B is a heteropentameric complex which functions as a guanine nucleotide exchange factor in the recycling of eIF-2 during the initiation of translation in eukaryotes. The epsilon and gamma subunits are sequence similar and both are essential in yeast. Epsilon appears to be the catalytically active subunit, with gamma enhancing its activity. The C-terminal domain of the eIF2B epsilon subunit contains bipartite motifs rich in acidic and aromatic residues, which are responsible for the interaction with eIF2. The structure of the domain resembles that of a set of concatenated HEAT repeats.


Pssm-ID: 211396  Cd Length: 169  Bit Score: 183.61  E-value: 4.41e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 550 DDIRVFQNEVLGTLQRGREENISCENLVLEINSLKHAYNISLKEVMQVLTLVVLEFPLQQVDglLDPNRYCALLLPLLKA 629
Cdd:cd11558     1 DDESDFHSEVVESLERALEENHSVDNAILEINSLRMAYNVTDHDVRRAVVKALLELILEVSS--TSTAELLEALKKLLSK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 630 WSPVLRNYIKRAADHLEALAAIEDFFLEHETLVTSMAKVLMAFYQLEILAEETILSWFSQRDTTDEGQQLRKNQQLQRFI 709
Cdd:cd11558    79 WGPLLENYVKSQDDQVELLLALEEFCLESEEGGPLFAKLLHALYDLDILEEEAILEWWEEPDAGADEEMKKVRELVKKFI 158


                  ....
gi 2449300292 710 QWLR 713
Cdd:cd11558   159 EWLE 162
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 357-435 6.64e-33

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: 121.53  E-value: 6.64e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2449300292 357 LLGAGTVIGSNCSITNSVIGPNCHIGDNVVLDQAYLWQGVRVAAGAQIHQSLLCDRAEVKERVKLKPYCVLTSQVVVGP 435
Cdd:cd05787     1 VIGRGTSIGEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPGSLISFGVVIGD 79
eIF5C smart00515
Domain at the C-termini of GCD6, eIF-2B epsilon, eIF-4 gamma and eIF-5;
631-713 2.56e-25

Domain at the C-termini of GCD6, eIF-2B epsilon, eIF-4 gamma and eIF-5;


Pssm-ID: 214705  Cd Length: 83  Bit Score: 100.06  E-value: 2.56e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292  631 SPVLRNYIKRAADHLEALAAIEDFFLEHETLVTSMAKVLMAFYQLEILAEETILSWFSQRDTTDEGQQLRKNQQLqrFIQ 710
Cdd:smart00515   1 GPLLKFLAKDEEEQLELLYAIEEFCVELEKLGKLLPKILKSLYDADILEEEAILKWYEKAVSAEGKKKVRKNAKP--FVT 78


                   ...
gi 2449300292  711 WLR 713
Cdd:smart00515  79 WLQ 81
W2 pfam02020
eIF4-gamma/eIF5/eIF2-epsilon; This domain of unknown function is found at the C-terminus of ...
 644-713 5.05e-17

eIF4-gamma/eIF5/eIF2-epsilon; This domain of unknown function is found at the C-terminus of several translation initiation factors.


Pssm-ID: 460415  Cd Length: 76  Bit Score: 76.03  E-value: 5.05e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2449300292 644 HLEALAAIEDFFLEHETLVTSMAKVLMAFYQLEILAEETILSWFSQRDTTDEG-QQLRKnqQLQRFIQWLR 713
Cdd:pfam02020   1 QVDLLLALQEFCAKLEELLKLLLKILKALYDLDIVEEEAILKWWEDVSSAEKGmKKVRK--QAKPFVEWLE 69
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 341-436 4.30e-12

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: 68.12  E-value: 4.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 341 GPEVSLGHGSVLEENVLLGAGTVIGSNCsitnsVIGPNCHIGDNVVldqayLWQGVRVAAGAQIHqsllcDRaevkervk 420
Cdd:COG1044   112 GEGVSIGPFAVIGAGVVIGDGVVIGPGV-----VIGDGVVIGDDCV-----LHPNVTIYERCVIG-----DR-------- 168

                          90
                  ....*....|....*.
gi 2449300292 421 lkpyCVLTSQVVVGPD 436
Cdd:COG1044   169 ----VIIHSGAVIGAD 180
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 341-404 4.75e-10

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 61.69  E-value: 4.75e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2449300292 341 GPEVSLGHGSVLEENVLLGAGTVIGSNCSI-TNSVIGPNCHIGDNVVLDQA-YLWQGVRVAAGAQI 404
Cdd:PRK00892  116 GEGVSIGPNAVIGAGVVIGDGVVIGAGAVIgDGVKIGADCRLHANVTIYHAvRIGNRVIIHSGAVI 181
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
40-152 5.54e-10

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 60.25  E-value: 5.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292  40 QAVLVADSFNRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLQKSkwchptSPNvVRII 119
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARP------GPD-VTFV 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2449300292 120 TSELYR---SLGDVLRdvdAKALVRSDFLLIYGDVI 152
Cdd:COG1213    74 YNPDYDetnNIYSLWL---AREALDEDFLLLNGDVV 106
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
361-387 3.56e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 41.17  E-value: 3.56e-05
                          10        20
                  ....*....|....*....|....*...
gi 2449300292 361 GTVIGSNCSI-TNSVIGPNCHIGDNVVL 387
Cdd:pfam00132   1 GTVIGDNVLIgPNAVIGGGVIIGDNVII 28
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 318-392 4.33e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 40.25  E-value: 4.33e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2449300292 318 TPEVNFTDSTTQSYTHSRHNiyrgPEVSLGHGSVLEenVLLGAGTVIgSNCSITNSVIGPNCHIGDNVVLDQAYL 392
Cdd:PRK02862  277 NPPFSFYDEKAPIYTRARYL----PPSKLLDATITE--SIIAEGCII-KNCSIHHSVLGIRSRIESGCTIEDTLV 344
 
Name Accession Description Interval E-value
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 39-253 3.36e-112

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: 338.04  E-value: 3.36e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292  39 LQAVLVADSFNRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLQKSKWC-HPTSPNVVR 117
Cdd:cd04197     1 LQAVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKSKWSkPKSSLMIVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 118 IITSELYRSLGDVLRDVDAKALVRSDFLLIYGDVISNINICRALEEHRLRRKLEKNVsVMTMVFKESSPSHPTRCHEDNV 197
Cdd:cd04197    81 IIMSEDCRSLGDALRDLDAKGLIRGDFILVSGDVVSNIDLKEILEEHKERRKKDKNA-IMTMVLKEASPPHRTRRTGEEF 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2449300292 198 VMAVDSATNRVLHFQKTQGLRRFSF--PLSLFQGSGDGVEIRYDLLDCHISICSPQVA 253
Cdd:cd04197   160 VIAVDPKTSRLLHYEELPGSKYRSItdLPSELLGSNSEVEIRHDLLDCHIDICSPDVL 217
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 39-252 1.41e-78

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: 250.63  E-value: 1.41e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292  39 LQAVLVADSFNRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLQKSKWCHPTSPNVVRI 118
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKWSSLSSKMIVDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 119 ITSELYRSLGDVLRDVDAKALVRSDFLLIYGDVISNINICRALEEhrlRRKLEKNvSVMTMVFKESSPSHPT---RCHED 195
Cdd:cd02507    81 ITSDLCESAGDALRLRDIRGLIRSDFLLLSCDLVSNIPLSELLEE---RRKKDKN-AIATLTVLLASPPVSTeqsKKTEE 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2449300292 196 NVVMAVDSATNR--VLHFQKTQGLRRFSFPLSLFQGSGDGVEIRYDLLDCHISICSPQV 252
Cdd:cd02507   157 EDVIAVDSKTQRllLLHYEEDLDEDLELIIRKSLLSKHPNVTIRTDLLDCHIYICSPDV 215
W2_eIF2B_epsilon cd11558
C-terminal W2 domain of eukaryotic translation initiation factor 2B epsilon; eIF2B is a ...
 550-713 4.41e-54

C-terminal W2 domain of eukaryotic translation initiation factor 2B epsilon; eIF2B is a heteropentameric complex which functions as a guanine nucleotide exchange factor in the recycling of eIF-2 during the initiation of translation in eukaryotes. The epsilon and gamma subunits are sequence similar and both are essential in yeast. Epsilon appears to be the catalytically active subunit, with gamma enhancing its activity. The C-terminal domain of the eIF2B epsilon subunit contains bipartite motifs rich in acidic and aromatic residues, which are responsible for the interaction with eIF2. The structure of the domain resembles that of a set of concatenated HEAT repeats.


Pssm-ID: 211396  Cd Length: 169  Bit Score: 183.61  E-value: 4.41e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 550 DDIRVFQNEVLGTLQRGREENISCENLVLEINSLKHAYNISLKEVMQVLTLVVLEFPLQQVDglLDPNRYCALLLPLLKA 629
Cdd:cd11558     1 DDESDFHSEVVESLERALEENHSVDNAILEINSLRMAYNVTDHDVRRAVVKALLELILEVSS--TSTAELLEALKKLLSK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 630 WSPVLRNYIKRAADHLEALAAIEDFFLEHETLVTSMAKVLMAFYQLEILAEETILSWFSQRDTTDEGQQLRKNQQLQRFI 709
Cdd:cd11558    79 WGPLLENYVKSQDDQVELLLALEEFCLESEEGGPLFAKLLHALYDLDILEEEAILEWWEEPDAGADEEMKKVRELVKKFI 158


                  ....
gi 2449300292 710 QWLR 713
Cdd:cd11558   159 EWLE 162
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 357-435 6.64e-33

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: 121.53  E-value: 6.64e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2449300292 357 LLGAGTVIGSNCSITNSVIGPNCHIGDNVVLDQAYLWQGVRVAAGAQIHQSLLCDRAEVKERVKLKPYCVLTSQVVVGP 435
Cdd:cd05787     1 VIGRGTSIGEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPGSLISFGVVIGD 79
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 357-435 1.94e-28

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: 108.48  E-value: 1.94e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2449300292 357 LLGAGTVIGSNCSITNSVIGPNCHIGDNVVLDQAYLWQGVRVAAGAQIHQSLLCDRAEVKERVKLKPYCVLTSQVVVGP 435
Cdd:cd03356     1 LIGESTVIGENAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNLCIIGDDVVVED 79
eIF5C smart00515
Domain at the C-termini of GCD6, eIF-2B epsilon, eIF-4 gamma and eIF-5;
631-713 2.56e-25

Domain at the C-termini of GCD6, eIF-2B epsilon, eIF-4 gamma and eIF-5;


Pssm-ID: 214705  Cd Length: 83  Bit Score: 100.06  E-value: 2.56e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292  631 SPVLRNYIKRAADHLEALAAIEDFFLEHETLVTSMAKVLMAFYQLEILAEETILSWFSQRDTTDEGQQLRKNQQLqrFIQ 710
Cdd:smart00515   1 GPLLKFLAKDEEEQLELLYAIEEFCVELEKLGKLLPKILKSLYDADILEEEAILKWYEKAVSAEGKKKVRKNAKP--FVT 78


                   ...
gi 2449300292  711 WLR 713
Cdd:smart00515  79 WLQ 81
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 39-252 5.42e-22

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: 94.65  E-value: 5.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292  39 LQAVLVADSFNRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLQKSKWCHPTSPNVVRI 118
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFPLNLKQKLDEVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 119 ITSELYRSLGDVLRDVDAKalVRSDFLLIYGDVISNINICRALEEHRlrrkleKNVSVMTMVFKESS------PSHPTRC 192
Cdd:cd04198    81 IVLDEDMGTADSLRHIRKK--IKKDFLVLSCDLITDLPLIELVDLHR------SHDASLTVLLYPPPvsseqkGGKGKSK 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 193 HEDN-VVMAVDSATNRVLH------FQKTQGLRR---FSFPlslfqgsgdGVEIRYDLLDCHISICSPQV 252
Cdd:cd04198   153 KADErDVIGLDEKTQRLLFitseedLDEDLELRKsllKRHP---------RVTITTKLLDAHVYIFKRWV 213
W2 cd11473
C-terminal domain of eIF4-gamma/eIF5/eIF2b-epsilon; This domain is found at the C-terminus of ...
 550-687 4.49e-21

C-terminal domain of eIF4-gamma/eIF5/eIF2b-epsilon; This domain is found at the C-terminus of several translation initiation factors, including the epsilon chain of eIF2b, where it has been found to catalyze the conversion of eIF2.GDP to its active eIF2.GTP form. The structure of the domain resembles that of a set of concatenated HEAT repeats.


Pssm-ID: 211395  Cd Length: 135  Bit Score: 89.84  E-value: 4.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 550 DDIRVFQNEVLGTLQrgrEENISCENLVLEINSLKHAYNISLKEVMQVLTLVVLEFPLQQVDGLLDpnrYCALLLPLLKA 629
Cdd:cd11473     1 EKNKKLRDSLLKELE---EDKSSDVESVKAAKSKLDLDPISLEEVVKVLLTAVVNAVESADSISLT---QKEQLVLVLKK 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2449300292 630 WSPVLRNYIK-RAADHLEALAAIEDFFLEHET--LVTSMAKVLMAFYQLEILAEETILSWF 687
Cdd:cd11473    75 YGPVLRELLKlIKKDQLYLLLKIEKLCLQLKLseLISLLEKILDLLYDADVLSEEAILSWF 135
W2 pfam02020
eIF4-gamma/eIF5/eIF2-epsilon; This domain of unknown function is found at the C-terminus of ...
 644-713 5.05e-17

eIF4-gamma/eIF5/eIF2-epsilon; This domain of unknown function is found at the C-terminus of several translation initiation factors.


Pssm-ID: 460415  Cd Length: 76  Bit Score: 76.03  E-value: 5.05e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2449300292 644 HLEALAAIEDFFLEHETLVTSMAKVLMAFYQLEILAEETILSWFSQRDTTDEG-QQLRKnqQLQRFIQWLR 713
Cdd:pfam02020   1 QVDLLLALQEFCAKLEELLKLLLKILKALYDLDIVEEEAILKWWEDVSSAEKGmKKVRK--QAKPFVEWLE 69
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 357-444 1.93e-15

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: 71.84  E-value: 1.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 357 LLGAGTVIGSNCSITNSVIGPNCHIGDNVVLDQAYLWQGVRVAAGAQIHQSLLCDRAEVKERVKLKpYCvltsqvVVGPD 436
Cdd:cd04652     1 LVGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLK-DC------LVGSG 73


                  ....*...
gi 2449300292 437 ITLPEGSV 444
Cdd:cd04652    74 YRVEAGTE 81
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 51-212 2.39e-15

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: 75.69  E-value: 2.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292  51 RFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLQKSKWCHPTspnvVRIITSELYRSLGDV 130
Cdd:cd04181    11 RLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVN----IEYVVQEEPLGTAGA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 131 LRDVdAKALVRSDFLLIYGDVISNINICRALEEHRLRRkleknvSVMTMVFKEssPSHPTRChednVVMAVDsATNRVLH 210
Cdd:cd04181    87 VRNA-EDFLGDDDFLVVNGDVLTDLDLSELLRFHREKG------ADATIAVKE--VEDPSRY----GVVELD-DDGRVTR 152


                  ..
gi 2449300292 211 FQ 212
Cdd:cd04181   153 FV 154
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 341-436 4.30e-12

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: 68.12  E-value: 4.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 341 GPEVSLGHGSVLEENVLLGAGTVIGSNCsitnsVIGPNCHIGDNVVldqayLWQGVRVAAGAQIHqsllcDRaevkervk 420
Cdd:COG1044   112 GEGVSIGPFAVIGAGVVIGDGVVIGPGV-----VIGDGVVIGDDCV-----LHPNVTIYERCVIG-----DR-------- 168

                          90
                  ....*....|....*.
gi 2449300292 421 lkpyCVLTSQVVVGPD 436
Cdd:COG1044   169 ----VIIHSGAVIGAD 180
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 341-400 1.21e-10

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: 58.02  E-value: 1.21e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2449300292 341 GPEVSLGHGSVLEENVLLGaGTVIGSNCSITNSVIGPNCHIGDNV-VLDQAYLWQGVRVAA 400
Cdd:cd03356    20 GDNVRIGDGVTITNSILMD-NVTIGANSVIVDSIIGDNAVIGENVrVVNLCIIGDDVVVED 79
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 51-168 2.28e-10

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: 61.05  E-value: 2.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292  51 RFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLQKSKWchptspnVVRIITSELYRSL--- 127
Cdd:cd06422    12 RMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDSRF-------GLRITISDEPDELlet 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2449300292 128 -GDVLRdvdAKALVRSD-FLLIYGDVISNINICRALEEHRLRR 168
Cdd:cd06422    85 gGGIKK---ALPLLGDEpFLVVNGDILWDGDLAPLLLLHAWRM 124
W2_eIF5 cd11561
C-terminal W2 domain of eukaryotic translation initiation factor 5; eIF5 functions as a GTPase ...
 591-713 2.94e-10

C-terminal W2 domain of eukaryotic translation initiation factor 5; eIF5 functions as a GTPase acceleration protein (GAP), as well as a GDP dissociation inhibitor (GDI) during translational initiation in eukaryotes. The structure of this C-terminal domain resembles that of a set of concatenated HEAT repeats.


Pssm-ID: 211399  Cd Length: 157  Bit Score: 59.17  E-value: 2.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 591 LKEVMQVLTLVVLefplqqVDGLLDPNrycalLLPLLKAWSPVLRNYI--KRAADHLeaLAAIEDFF-LEHETLVTSMAK 667
Cdd:cd11561    36 RLDVVKDKAVLVL------AEVLFDEN-----IVKEIKKRKALLLKLVtdEKAQKAL--LGGIERFCgKHSPELLKKVPL 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2449300292 668 VLMAFYQLEILAEETILSWF---SQRDTTDEG-QQLRKNqqLQRFIQWLR 713
Cdd:cd11561   103 ILKALYDNDILEEEVILKWYekvSKKYVSKEKsKKVRKA--AEPFVEWLE 150
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 341-404 4.75e-10

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 61.69  E-value: 4.75e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2449300292 341 GPEVSLGHGSVLEENVLLGAGTVIGSNCSI-TNSVIGPNCHIGDNVVLDQA-YLWQGVRVAAGAQI 404
Cdd:PRK00892  116 GEGVSIGPNAVIGAGVVIGDGVVIGAGAVIgDGVKIGADCRLHANVTIYHAvRIGNRVIIHSGAVI 181
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
40-152 5.54e-10

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 60.25  E-value: 5.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292  40 QAVLVADSFNRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLQKSkwchptSPNvVRII 119
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARP------GPD-VTFV 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2449300292 120 TSELYR---SLGDVLRdvdAKALVRSDFLLIYGDVI 152
Cdd:COG1213    74 YNPDYDetnNIYSLWL---AREALDEDFLLLNGDVV 106
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 341-404 6.13e-10

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: 59.34  E-value: 6.13e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2449300292 341 GPEVSLGHGSVLEENVLLGAGTVIGSNCSI-TNSVIGPNCHIGDNVVL-DQAYLWQGVRVAAGAQI 404
Cdd:cd03352     5 GENVSIGPNAVIGEGVVIGDGVVIGPGVVIgDGVVIGDDCVIHPNVTIyEGCIIGDRVIIHSGAVI 70
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 354-464 1.79e-09

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


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 55.55  E-value: 1.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 354 ENVLLGAGTVIgSNCSITNSVIGPNCHIGDNVVLDQAYLWQGVRVAAGAQIHqsllcdraevkervklkpycvltsQVVV 433
Cdd:cd04651    11 KNSLVSEGCII-SGGTVENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIR------------------------RAII 65

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2449300292 434 GPDITLPEGSVISlhpPDAEEDEDDGQFSDD 464
Cdd:cd04651    66 DKNVVIPDGVVIG---GDPEEDRARFYVTED 93
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 346-404 1.97e-09

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


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 55.55  E-value: 1.97e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2449300292 346 LGHGSVLE----ENVLLGAGTVIGSNCSITNSVIGPNCHIGDNVVLDQAYLWQGVRVAAGAQI 404
Cdd:cd04651    15 VSEGCIISggtvENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPDGVVI 77
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 337-434 3.33e-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: 57.04  E-value: 3.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 337 NIYRGPEVSLGHGSVLEENVLLGAGTVIGSNCsitnsVIGPNCHIGDNVVLDqaylwqGVRVAAGAQIHQSLLCDRAEVK 416
Cdd:cd03353     9 TTYIDGDVEIGVDVVIDPGVILEGKTVIGEDC-----VIGPNCVIKDSTIGD------GVVIKASSVIEGAVIGNGATVG 77

                          90
                  ....*....|....*...
gi 2449300292 417 ERVKLKPYCVLTSQVVVG 434
Cdd:cd03353    78 PFAHLRPGTVLGEGVHIG 95
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 318-404 3.46e-09

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 59.32  E-value: 3.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 318 TPEVNFTDSTTQSYTHSRHN----IYRGPEVS---LGHGSVLE---ENVLLGAGTVIGSNCSITNSVIGPNCHIGDNVVL 387
Cdd:COG0448   256 EPEFNLYDPEWPIYTKQKDLppakFVRGGKVKnslVSNGCIISgtvENSVLFRGVRVESGAVVENSVIMPGVVIGEGAVI 335

                          90
                  ....*....|....*..
gi 2449300292 388 DQAYLWQGVRVAAGAQI 404
Cdd:COG0448   336 ENAIIDKNVVIPPGVVI 352
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 41-164 5.09e-09

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: 57.24  E-value: 5.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292  41 AVLVADSFNRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLQKSKwchptspnVVRIIT 120
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYP--------NIKFVY 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2449300292 121 SELYRSLGDVLRDVDAKALVRSDFLLIYGDVISNINICRALEEH 164
Cdd:cd02523    73 NPDYAETNNIYSLYLARDFLDEDFLLLEGDVVFDPSILERLLSS 116
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 351-404 1.17e-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: 55.88  E-value: 1.17e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2449300292 351 VLEENVLLGAGTVIGSNCSI-TNSVIGPNCHIGDNVVL-DQAYLWQGVRVAAGAQI 404
Cdd:cd03352     3 KIGENVSIGPNAVIGEGVVIgDGVVIGPGVVIGDGVVIgDDCVIHPNVTIYEGCII 58
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 337-404 1.62e-08

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: 57.73  E-value: 1.62e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2449300292 337 NIYRGPEVSLGH------GSVLEENVLLGAGTVIGSNCSITNSVIGPNCHIgDNVVLDQAylwqgvRVAAGAQI 404
Cdd:COG1207   260 TTYIDGDVEIGRdvvidpNVILEGKTVIGEGVVIGPNCTLKDSTIGDGVVI-KYSVIEDA------VVGAGATV 326
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 337-387 1.86e-08

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: 56.95  E-value: 1.86e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2449300292 337 NIYRGPEVSLGHGSVLEENVLLGAGTVIGSNCSI-TNSVIGPN------CHIGDNVVL 387
Cdd:COG1044   114 GVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIgDDCVLHPNvtiyerCVIGDRVII 171
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 336-387 2.12e-08

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 56.69  E-value: 2.12e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2449300292 336 HNIYRGPEVSLGHGSVLEENVLLGAGTVIGSNCSI-TNSVIGPN------CHIGDNVVL 387
Cdd:PRK00892  117 EGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIgADCRLHANvtiyhaVRIGNRVII 175
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 337-387 2.94e-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: 54.72  E-value: 2.94e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2449300292 337 NIYRGPEVSLGHGSVLEENVLLGAGTVIGSNCSI-TNSVIGPN------CHIGDNVVL 387
Cdd:cd03352     7 NVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIgDDCVIHPNvtiyegCIIGDRVII 64
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 330-387 5.05e-08

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: 53.64  E-value: 5.05e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2449300292 330 SYTHSRHNIyrGPEVSLGHGSVLEENVLLGAGTVIGSNCSI-TNSVIGPNCHIGDNVVL 387
Cdd:cd03360    85 TLIHPSAVV--SPSAVIGEGCVIMAGAVINPDARIGDNVIInTGAVIGHDCVIGDFVHI 141
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 341-387 1.21e-07

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


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 50.15  E-value: 1.21e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2449300292 341 GPEVSLGHGSVLEENVLLGaGTVIGSNCSITNSVIGPNCHIGDNVVL 387
Cdd:cd04651    32 FRGVRVGSGSVVEDSVIMP-NVGIGRNAVIRRAIIDKNVVIPDGVVI 77
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 341-404 2.27e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 53.60  E-value: 2.27e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2449300292 341 GPEVSLGHGSVLEENVLLGAGTVIGSNCSI-TNSVIGPNCHIGDNVvldqaYLWQGVRVAAGAQI 404
Cdd:PRK00892  110 DPSAKIGEGVSIGPNAVIGAGVVIGDGVVIgAGAVIGDGVKIGADC-----RLHANVTIYHAVRI 169
W2_eIF5C_like cd11560
C-terminal W2 domain of the eukaryotic translation initiation factor 5C and similar proteins; ...
 627-712 3.25e-07

C-terminal W2 domain of the eukaryotic translation initiation factor 5C and similar proteins; eIF5C appears to be essential for the initiation of protein translation; its actual function, and specifically that of the C-terminal W2 domain, are not well understood. The Drosophila ortholog, kra (krasavietz) or exba (extra bases), may be involved in translational inhibition in neural development. The structure of this C-terminal domain resembles that of a set of concatenated HEAT repeats.


Pssm-ID: 211398 [Multi-domain]  Cd Length: 194  Bit Score: 51.44  E-value: 3.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 627 LKAWSPVLRNYIKRAADHLEALAAIEDFFLEHETLVTSMAKVLMAFYQLEILAEETILSWFSQRDTTDEGQQLrkNQQLQ 706
Cdd:cd11560   105 LKKYAPLLAAFCTTARAELALLNKIQEYCYENMKFMKVFQKIVKLLYKADVLSEDAILKWYKKGHSPKGKQVF--LKQME 182


                  ....*.
gi 2449300292 707 RFIQWL 712
Cdd:cd11560   183 PFVEWL 188
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 339-446 4.79e-07

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 52.82  E-value: 4.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 339 YRGPEVSLGHGSVLEENVLLGAGTVIGSNCSITNSVIGPNCHIGDNVVldqaylwqgvrVAAGAQIHQSLLCDRAEVKER 418
Cdd:PRK14355  264 YIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKGCRIGDDVT-----------VKAGSVLEDSVVGDDVAIGPM 332

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2449300292 419 VKLKPYCVLTSQVVVG-----PDITLPEGSVIS 446
Cdd:PRK14355  333 AHLRPGTELSAHVKIGnfvetKKIVMGEGSKAS 365
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
350-445 6.60e-07

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 49.10  E-value: 6.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 350 SVLEENVLLGAGTVIGSNCSI--TNSVIGPNCHIGDNVVLdqaYLWQGVRVAAGAQI-HQSLLCD----------RAEVK 416
Cdd:COG0110     3 LLLLFGARIGDGVVIGPGVRIygGNITIGDNVYIGPGVTI---DDPGGITIGDNVLIgPGVTILTgnhpiddpatFPLRT 79

                          90       100
                  ....*....|....*....|....*....
gi 2449300292 417 ERVKLKPYCVLTSQVVVGPDITLPEGSVI 445
Cdd:COG0110    80 GPVTIGDDVWIGAGATILPGVTIGDGAVV 108
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 349-436 1.16e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 51.29  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 349 GSVLEENVLLGAGTVIGSNCsitnsVIGPNCHIGDNVVLD-QAYLWQGVRVAAGAQIHQsllcdRAEVKERVKLKPYCVL 427
Cdd:PRK00892  106 SAVIDPSAKIGEGVSIGPNA-----VIGAGVVIGDGVVIGaGAVIGDGVKIGADCRLHA-----NVTIYHAVRIGNRVII 175


                  ....*....
gi 2449300292 428 TSQVVVGPD 436
Cdd:PRK00892  176 HSGAVIGSD 184
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 336-388 1.64e-06

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 46.09  E-value: 1.64e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2449300292 336 HNIYRGPEVSLGHGSVLEENVLLGA--------GTVIGSNCSI-TNSVIGPNCHIGDNVVLD 388
Cdd:cd00208    11 PKAVIRGPVVIGDNVNIGPGAVIGAatgpneknPTIIGDNVEIgANAVIHGGVKIGDNAVIG 72
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 341-387 2.04e-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: 49.63  E-value: 2.04e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2449300292 341 GPEVSLGHGSVLEENVLLGAGTVIGSNCSIT-NSVIGPNCHIGDNVVL 387
Cdd:COG1043    17 GENVEIGPFCVIGPDVEIGDGTVIGSHVVIEgPTTIGKNNRIFPFASI 64
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 355-445 3.92e-06

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 46.30  E-value: 3.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 355 NVLLGAGTVIGSNCSITNS---VIGPNCHIGDNVVLdqaylwqgvrVAAGAQIH-QSLLCDRAEVKERVKLKPYCVLTSQ 430
Cdd:cd04647     1 NISIGDNVYIGPGCVISAGggiTIGDNVLIGPNVTI----------YDHNHDIDdPERPIEQGVTSAPIVIGDDVWIGAN 70

                          90
                  ....*....|....*
gi 2449300292 431 VVVGPDITLPEGSVI 445
Cdd:cd04647    71 VVILPGVTIGDGAVV 85
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 341-387 1.06e-05

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: 47.43  E-value: 1.06e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2449300292 341 GPEVSLGHGSVLEENVLLGAGTVIGSNCSIT-NSVIGPNCHIGDNVVL 387
Cdd:cd03351    15 GENVEIGPFCVIGPNVEIGDGTVIGSHVVIDgPTTIGKNNRIFPFASI 62
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 340-415 1.09e-05

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: 46.04  E-value: 1.09e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2449300292 340 RGPEVSLGHGSVLEENVLLGAGTVIGSNCsitnsVIGPNCHIGDNVVLDqaylwQGVRVAAGAQIHQSLLCDRAEV 415
Cdd:cd05636    14 IKGPVWIGEGAIVRSGAYIEGPVIIGKGC-----EIGPNAYIRGYTVLG-----DGCVVGNSVEVKNSIIMDGTKV 79
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
341-387 1.10e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 47.79  E-value: 1.10e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2449300292 341 GPEVSLGHGSVLEENVLLGAGTVIGSNCSIT-NSVIGPNCHIGDNVVL 387
Cdd:PRK05289   18 GENVEIGPFCVIGPNVVIGDGTVIGSHVVIDgHTTIGKNNRIFPFASI 65
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 347-455 1.22e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 48.28  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 347 GHGSVLEENVLLGAGTVIgSNCSITNSVIGPNCHIGDNVVLDQAYLWQGVRVAAGAQIHQsllcdraevkervklkpyCV 426
Cdd:PRK00844  307 GGRVGSAQDSLVSAGSII-SGATVRNSVLSPNVVVESGAEVEDSVLMDGVRIGRGAVVRR------------------AI 367

                          90       100
                  ....*....|....*....|....*....
gi 2449300292 427 LTSQVVVgpditlPEGSVISLhppDAEED 455
Cdd:PRK00844  368 LDKNVVV------PPGATIGV---DLEED 387
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 337-388 2.30e-05

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 47.52  E-value: 2.30e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2449300292 337 NIYRGPEVSLGHGSVLEENVLLGAGTVIGSNC------SITNSVIGPNCHIGDNVVLD 388
Cdd:PRK14354  259 STYIDADVEIGSDTVIEPGVVIKGNTVIGEDCvigpgsRIVDSTIGDGVTITNSVIEE 316
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
361-387 3.56e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 41.17  E-value: 3.56e-05
                          10        20
                  ....*....|....*....|....*...
gi 2449300292 361 GTVIGSNCSI-TNSVIGPNCHIGDNVVL 387
Cdd:pfam00132   1 GTVIGDNVLIgPNAVIGGGVIIGDNVII 28
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 341-402 4.90e-05

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 42.83  E-value: 4.90e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 341 GPEVSL---GHG----SVLEENVLLGAGTVIGSNCSI-TNSVIGPNCHIGDNVVldqaylwqgvrVAAGA 402
Cdd:cd04647    31 GPNVTIydhNHDiddpERPIEQGVTSAPIVIGDDVWIgANVVILPGVTIGDGAV-----------VGAGS 89
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 341-446 9.47e-05

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: 43.94  E-value: 9.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 341 GPEVSLGHGSVLEENVLLGAGTVIGSNC--------------SITNSVIGPNCHIGDNVVLDQAylWQG----------- 395
Cdd:cd03352    47 HPNVTIYEGCIIGDRVIIHSGAVIGSDGfgfapdgggwvkipQLGGVIIGDDVEIGANTTIDRG--ALGdtvigdgtkid 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2449300292 396 --VRVAAGAQI--HqSLLCDRAEVKERVKLKPYCVLTSQVVVGPDITLPEGSVIS 446
Cdd:cd03352   125 nlVQIAHNVRIgeN-CLIAAQVGIAGSTTIGDNVIIGGQVGIAGHLTIGDGVVIG 178
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 364-445 1.02e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 45.24  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 364 IGSNCSITNSVIGPNCHIGDNVvlDQAYLWQGVRVAAGAQIHQSLLCDRAEVKERVKLKpycvltsQVVVGPDITLPEGS 443
Cdd:PRK05293  285 IAENAKVKNSLVVEGCVVYGTV--EHSVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIE-------RAIIGENAVIGDGV 355


                  ..
gi 2449300292 444 VI 445
Cdd:PRK05293  356 II 357
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 344-404 1.08e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 45.20  E-value: 1.08e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2449300292 344 VSLG---HGSVLEENVLlGAGTVIGSNCSITNSVIGPNCHIGDNVVLDQAYLWQGVRVAAGAQI 404
Cdd:PRK00844  318 VSAGsiiSGATVRNSVL-SPNVVVESGAEVEDSVLMDGVRIGRGAVVRRAILDKNVVVPPGATI 380
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 355-445 1.47e-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: 42.78  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 355 NVLLGAGTVIGSNCSI---TNSV-IGPNCHIGDNVVLDQAYLW-----QGVRVAAGAQIH------------QSLLCDRA 413
Cdd:cd04645    17 DVTLGEGSSVWFGAVLrgdVNPIrIGERTNIQDGSVLHVDPGYptiigDNVTVGHGAVLHgctigdncligmGAIILDGA 96

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2449300292 414 EVKErvklkpYCVLTSQVVVGPDITLPEGSVI 445
Cdd:cd04645    97 VIGK------GSIVAAGSLVPPGKVIPPGSLV 122
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 342-388 1.50e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 44.86  E-value: 1.50e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2449300292 342 PEVSLGHGSVLEENVLLgAGTVIGSNCSITNSVIGPNCHIGDNVVLD 388
Cdd:PRK05293  313 QGVQVGEGSVVKDSVIM-PGAKIGENVVIERAIIGENAVIGDGVIIG 358
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 338-442 1.55e-04

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


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 43.00  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 338 IYRGPEVSLGHGSVLEENVLLGAGTVIGSNCSITNSVIGPNCHIGDNVVLDQAYLWQGVRVAAGAQIHQSLLCDRAE--- 414
Cdd:cd00710    65 VWIGKNVSIAHGAIVHGPAYIGDNCFIGFRSVVFNAKVGDNCVIGHNAVVDGVEIPPGRYVPAGAVITSQTQADALPdvt 144

                          90       100
                  ....*....|....*....|....*...
gi 2449300292 415 VKERvklkpycvLTSQVVVGPDITLPEG 442
Cdd:cd00710   145 DSAR--------EFNEKVITVNNELAEG 164
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 344-402 1.62e-04

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: 43.24  E-value: 1.62e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2449300292 344 VSLGHGSVLEENVLLGAGTVIGSNCSI-------TNSVIGPNCHIGDNVVldqaylwqgvrVAAGA 402
Cdd:cd03360   127 AVIGHDCVIGDFVHIAPGVVLSGGVTIgegafigAGATIIQGVTIGAGAI-----------IGAGA 181
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 348-404 1.65e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 44.47  E-value: 1.65e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2449300292 348 HGSVleENVLLGAGTVIGSNCSITNSVIGPNCHIGDNVVLDQAYLWQGVRVAAGAQI 404
Cdd:PRK05293  303 YGTV--EHSVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVII 357
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 338-420 1.96e-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: 42.58  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 338 IYRGPEVSLGHGSVLEENVLLGAGTVIGSNCSITNSVIGPNCHI------GDNVvldqayLWQGVRVAAGAQIhQSLLCD 411
Cdd:cd05636    36 VIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKVphlnyvGDSV------LGENVNLGAGTIT-ANLRFD 108


                  ....*....
gi 2449300292 412 RAEVKERVK 420
Cdd:cd05636   109 DKPVKVRLK 117
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 51-168 1.96e-04

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: 43.71  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292  51 RFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLQK-SKWChptspnvVRI--ITSELYRSL 127
Cdd:cd04189    13 RLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDgSRFG-------VRItyILQEEPLGL 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2449300292 128 GD-VLRdvdAKALV-RSDFLLIYGDVISNINICRALEEHRLRR 168
Cdd:cd04189    86 AHaVLA---ARDFLgDEPFVVYLGDNLIQEGISPLVRDFLEED 125
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
349-382 2.08e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 38.86  E-value: 2.08e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2449300292 349 GSVLEENVLLGAGTVIGSNCsitnsVIGPNCHIG 382
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGV-----IIGDNVIIG 29
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 355-449 2.73e-04

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: 42.20  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 355 NVLLGAGTVIGSNCSITNSVIGPNCHIGDNVVLDQaylwqgvrvaagaqihqsllcdRAEVKERVKLKPYCvltsqvVVG 434
Cdd:cd03359    72 PLHIGDYVFIGENCVVNAAQIGSYVHIGKNCVIGR----------------------RCIIKDCVKILDGT------VVP 123

                          90
                  ....*....|....*
gi 2449300292 435 PDITLPEGSVISLHP 449
Cdd:cd03359   124 PDTVIPPYSVVSGRP 138
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 339-446 5.34e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 42.32  E-value: 5.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 339 YRGPEVSL--GHGSVLEENVLL------GAGTVIGSNCS-ITNSVIGPNCHIGDNVVLdqaylwqgvrvAAGAqihqsLL 409
Cdd:PRK12461   71 YKGEESRLeiGDRNVIREGVTIhrgtkgGGVTRIGNDNLlMAYSHVAHDCQIGNNVIL-----------VNGA-----LL 134

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2449300292 410 CDRAEVKERVKLKPYCVLTSQVVVGPDITLPEGSVIS 446
Cdd:PRK12461  135 AGHVTVGDRAIISGNCLVHQFCRIGALAMMAGGSRIS 171
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 332-451 5.75e-04

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 42.99  E-value: 5.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 332 THSRHNIYRGPEVSLGHGSVLEEnvllgagTVIGSNCSITNSV-----------IGP------------NCHIGDNVVLD 388
Cdd:PRK14360  275 THLRGNTVIGSGCRIGPGSLIEN-------SQIGENVTVLYSVvsdsqigdgvkIGPyahlrpeaqigsNCRIGNFVEIK 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 389 QAYLWQGVRVAagaqiHQSLLCD------------------------RAEVKERVKLKPYCVLTSQVVVGPDITLPEGSV 444
Cdd:PRK14360  348 KSQLGEGSKVN-----HLSYIGDatlgeqvnigagtitanydgvkkhRTVIGDRSKTGANSVLVAPITLGEDVTVAAGST 422


                  ....*..
gi 2449300292 445 ISLHPPD 451
Cdd:PRK14360  423 ITKDVPD 429
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 356-435 1.27e-03

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 38.00  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 356 VLLGAGTVIGSNCSI-TNSVIGPNCHIGDNVVLDQAylwQGVRVAAGAQIHqsllcDRAEVKERVKLKPYCVLTSQVVVG 434
Cdd:cd00208     1 VFIGEGVKIHPKAVIrGPVVIGDNVNIGPGAVIGAA---TGPNEKNPTIIG-----DNVEIGANAVIHGGVKIGDNAVIG 72


                  .
gi 2449300292 435 P 435
Cdd:cd00208    73 A 73
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 340-404 2.12e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 41.17  E-value: 2.12e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2449300292 340 RGpevSLGHGS--------VLEENVLLGAGTVIGSNCSITNSVIGPNCHIGDNVVLDQAylwqgvRVAAGAQI 404
Cdd:PRK09451  263 RG---TLTHGRdveidtnvIIEGNVTLGNRVKIGAGCVLKNCVIGDDCEISPYSVVEDA------NLGAACTI 326
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
349-406 2.30e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 40.47  E-value: 2.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2449300292 349 GSVLEENVLLGAGTVIGSNCsitnsVIGPNCHIGDNVVLDqaylwQGVRVAAGAQIHQ 406
Cdd:PRK05289   14 GAKIGENVEIGPFCVIGPNV-----VIGDGTVIGSHVVID-----GHTTIGKNNRIFP 61
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 339-387 2.39e-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: 40.49  E-value: 2.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2449300292 339 YRGPEVSL--GHGSVLEENVLLGAG-------TVIGSNCSI-TNSVIGPNCHIGDNVVL 387
Cdd:cd03351    71 YKGEPTRLeiGDNNTIREFVTIHRGtaqgggvTRIGNNNLLmAYVHVAHDCVIGNNVIL 129
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 372-445 3.35e-03

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: 39.31  E-value: 3.35e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2449300292 372 NSVIGPNCHIGDNVVLDqaylwQGVRVAAGAQIH-QSLLCDRAEVKERVKLKPYCVLTSQVVVGPDITLPEGSVI 445
Cdd:cd03352     1 SAKIGENVSIGPNAVIG-----EGVVIGDGVVIGpGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 375-445 3.44e-03

wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 37.59  E-value: 3.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 375 IGPNCHIGDNVVLDQaylwQG-VRVAAGAQIHQ-SLLC---------DRAEVKERVKLKPYCVLTSQVVVGPDITLPEGS 443
Cdd:cd05825     6 IGDNSWIGEGVWIYN----LApVTIGSDACISQgAYLCtgshdyrspAFPLITAPIVIGDGAWVAAEAFVGPGVTIGEGA 81


                  ..
gi 2449300292 444 VI 445
Cdd:cd05825    82 VV 83
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 374-445 3.52e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 40.12  E-value: 3.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2449300292 374 VIGPNCHIGDNVVLD-QAYLWQGVRVAAGAQIH-QSLLCDRAEVKERVKLKPYCVLTSQVVVGPDITLPEGSVI 445
Cdd:PRK00892  108 VIDPSAKIGEGVSIGpNAVIGAGVVIGDGVVIGaGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVI 181
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 374-445 3.76e-03

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: 40.00  E-value: 3.76e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2449300292 374 VIGPNCHIGDNVVLDqaylwQGVRVAAGAQIH-QSLLCDRAEVKERVKLKPYCVLTSQVVVGPDITLPEGSVI 445
Cdd:COG1044   110 KIGEGVSIGPFAVIG-----AGVVIGDGVVIGpGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVI 177
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 318-392 4.33e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 40.25  E-value: 4.33e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2449300292 318 TPEVNFTDSTTQSYTHSRHNiyrgPEVSLGHGSVLEenVLLGAGTVIgSNCSITNSVIGPNCHIGDNVVLDQAYL 392
Cdd:PRK02862  277 NPPFSFYDEKAPIYTRARYL----PPSKLLDATITE--SIIAEGCII-KNCSIHHSVLGIRSRIESGCTIEDTLV 344
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 364-434 4.71e-03

Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Mannose-1-phosphate guanylyltransferase is also known as GDP-mannose pyrophosphorylase. It catalyzes the synthesis of GDP-mannose from GTP and mannose-1-phosphate, and is involved in the maintenance of cell wall integrity and glycosylation. Similar to ADP-glucose pyrophosphorylase, it contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain, presumably with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100062 [Multi-domain]  Cd Length: 80  Bit Score: 36.75  E-value: 4.71e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2449300292 364 IGSNCSI-TNSVIGPNCHIGDNVVLDQAYLWQGVRVAAGAQIHQSLLCDRAEVKERVKLKPYCVLTSQVVVG 434
Cdd:cd05824     8 IGKTAKIgPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLENVTVLGDDVTIK 79
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 349-402 4.89e-03

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: 36.40  E-value: 4.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2449300292 349 GSVLEENVllgagtVIGSNCSITNSVIGPNCHIGDNVVLDQAYLWQGVRVAAGA 402
Cdd:cd04652    33 NCVIMDNV------TIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAGT 80
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 341-396 5.49e-03

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: 38.16  E-value: 5.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2449300292 341 GPEVSLGHGSVL-----EENVLLG------AGTVIGSNCSIT-NSVIGPNCHIGDNvvldqaYLWQGV 396
Cdd:cd04645    64 GDNVTVGHGAVLhgctiGDNCLIGmgaiilDGAVIGKGSIVAaGSLVPPGKVIPPG------SLVAGS 125
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 341-445 5.82e-03

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 38.08  E-value: 5.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 341 GPEVSLGHGSVL---EENVLLGAGTVIGSNCSI-----TNSVIGPNCHIGDNVVLDQAYLWQGVRVAAGAqihqsLLCDR 412
Cdd:COG0663    32 GEDVSVWPGAVLrgdVGPIRIGEGSNIQDGVVLhvdpgYPLTIGDDVTIGHGAILHGCTIGDNVLIGMGA-----IVLDG 106

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2449300292 413 AEVKErvklkpYCVLTSQVVVGPDITLPEGSVI 445
Cdd:COG0663   107 AVIGD------GSIVGAGALVTEGKVVPPGSLV 133
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 349-406 7.41e-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: 7.41e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2449300292 349 GSVLEENVLLGAGTVIGSNCsitnsVIGPNCHIGDNVVLDqaylwQGVRVAAGAQIHQ 406
Cdd:COG1043    13 GAKLGENVEIGPFCVIGPDV-----EIGDGTVIGSHVVIE-----GPTTIGKNNRIFP 60
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
339-387 8.16e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 38.93  E-value: 8.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2449300292 339 YRGPEVSL--GHGSVLEENVLLGAGTV-------IGSNCSI-TNSVIGPNCHIGDNVVL 387
Cdd:PRK05289   74 YKGEPTRLviGDNNTIREFVTINRGTVqgggvtrIGDNNLLmAYVHVAHDCVVGNHVIL 132
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 344-402 8.35e-03

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: 36.71  E-value: 8.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 344 VSLGHGSVLEENVLLG---------------------AGTVIGSNCSI-TNSVIGPNCHIGDNVVldqaylwqgvrVAAG 401
Cdd:cd03358    29 VSIYEGVTIEDDVFIGpnvvftndlyprskiyrkwelKGTTVKRGASIgANATILPGVTIGEYAL-----------VGAG 97


                  .
gi 2449300292 402 A 402
Cdd:cd03358    98 A 98
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 351-446 8.88e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 38.97  E-value: 8.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 351 VLEENVLLGAG----------TVIGSNCSITNSV-IGPNCHIGDNVVldqaylwqgvrVAAGAQIHQSllcdraevkerV 419
Cdd:PRK00892  205 IIGDDVEIGANttidrgalddTVIGEGVKIDNLVqIAHNVVIGRHTA-----------IAAQVGIAGS-----------T 262

                          90       100
                  ....*....|....*....|....*..
gi 2449300292 420 KLKPYCVLTSQVVVGPDITLPEGSVIS 446
Cdd:PRK00892  263 KIGRYCMIGGQVGIAGHLEIGDGVTIT 289
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 341-404 9.46e-03

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: 36.71  E-value: 9.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300292 341 GPEVSLGHGSVLEENVllgagtVIGSNCSI-------TNSVIGPNCHIGDNVVL----------DQAYLWQGVRVAAGAQ 403
Cdd:cd03358     2 GDNCIIGTNVFIENDV------KIGDNVKIqsnvsiyEGVTIEDDVFIGPNVVFtndlyprskiYRKWELKGTTVKRGAS 75


                  .
gi 2449300292 404 I 404
Cdd:cd03358    76 I 76
 
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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