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Conserved domains on  [gi|83267879|ref|NP_003898|]
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translation initiation factor eIF2B subunit epsilon [Homo sapiens]

Protein Classification

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

translation initiation factor eIF-2B subunit epsilon acts as a catalytic component of the translation initiation factor 2B, which catalyzes the exchange of eukaryotic initiation factor 2 (eIF-2)-bound GDP for GTP and is regulated by phosphorylated eIF-2

CATH:  2.160.10.10
Gene Ontology:  GO:0005851|GO:0003743|GO:0005085|GO:0031369
PubMed:  9438375|10521532|12691742|9445404|11747907|15500694|7893825
SCOP:  3000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 43-257 2.63e-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: 2.63e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879  43 LQAVLVADSFDRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKWCRPTS-LNVVR 121
Cdd:cd04197   1 LQAVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKSKWSKPKSsLMIVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 122 IITSELYRSLGDVLRDVDAKALVRSDFLLVYGDVISNINITRALEEHRLRRKLEKNVsVMTMIFKESSPSHPTRCHEDNV 201
Cdd:cd04197  81 IIMSEDCRSLGDALRDLDAKGLIRGDFILVSGDVVSNIDLKEILEEHKERRKKDKNA-IMTMVLKEASPPHRTRRTGEEF 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 83267879 202 VVAVDSTTNRVLHFQKTQGLRRFAF--PLSLFQGSSDGVEVRYDLLDCHISICSPQVA 257
Cdd:cd04197 160 VIAVDPKTSRLLHYEELPGSKYRSItdLPSELLGSNSEVEIRHDLLDCHIDICSPDVL 217
W2_eIF2B_epsilon cd11558
C-terminal W2 domain of eukaryotic translation initiation factor 2B epsilon; eIF2B is a ...
 548-711 3.26e-56

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: 189.39  E-value: 3.26e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 548 DDIKVFQNEVLGTLQRGKEENISCDNLVLEINSLKYAYNISLKEVMQVLSHVVLEFPLQQMDspLDSSRYCALLLPLLKA 627
Cdd:cd11558   1 DDESDFHSEVVESLERALEENHSVDNAILEINSLRMAYNVTDHDVRRAVVKALLELILEVSS--TSTAELLEALKKLLSK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 628 WSPVFRNYIKRAADHLEALAAIEDFFLEHEALGISMAKVLMAFYQLEILAEETILSWFSQRDTTDKGQQLRKNQQLQRFI 707
Cdd:cd11558  79 WGPLLENYVKSQDDQVELLLALEEFCLESEEGGPLFAKLLHALYDLDILEEEAILEWWEEPDAGADEEMKKVRELVKKFI 158


                ....
gi 83267879 708 QWLK 711
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 ...
 361-439 5.78e-34

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: 124.23  E-value: 5.78e-34
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83267879 361 LLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVTLKPRSVLTSQVVVGP 439
Cdd:cd05787   1 VIGRGTSIGEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPGSLISFGVVIGD 79
 
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; ...
 43-257 2.63e-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: 2.63e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879  43 LQAVLVADSFDRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKWCRPTS-LNVVR 121
Cdd:cd04197   1 LQAVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKSKWSKPKSsLMIVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 122 IITSELYRSLGDVLRDVDAKALVRSDFLLVYGDVISNINITRALEEHRLRRKLEKNVsVMTMIFKESSPSHPTRCHEDNV 201
Cdd:cd04197  81 IIMSEDCRSLGDALRDLDAKGLIRGDFILVSGDVVSNIDLKEILEEHKERRKKDKNA-IMTMVLKEASPPHRTRRTGEEF 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 83267879 202 VVAVDSTTNRVLHFQKTQGLRRFAF--PLSLFQGSSDGVEVRYDLLDCHISICSPQVA 257
Cdd:cd04197 160 VIAVDPKTSRLLHYEELPGSKYRSItdLPSELLGSNSEVEIRHDLLDCHIDICSPDVL 217
W2_eIF2B_epsilon cd11558
C-terminal W2 domain of eukaryotic translation initiation factor 2B epsilon; eIF2B is a ...
 548-711 3.26e-56

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: 189.39  E-value: 3.26e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 548 DDIKVFQNEVLGTLQRGKEENISCDNLVLEINSLKYAYNISLKEVMQVLSHVVLEFPLQQMDspLDSSRYCALLLPLLKA 627
Cdd:cd11558   1 DDESDFHSEVVESLERALEENHSVDNAILEINSLRMAYNVTDHDVRRAVVKALLELILEVSS--TSTAELLEALKKLLSK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 628 WSPVFRNYIKRAADHLEALAAIEDFFLEHEALGISMAKVLMAFYQLEILAEETILSWFSQRDTTDKGQQLRKNQQLQRFI 707
Cdd:cd11558  79 WGPLLENYVKSQDDQVELLLALEEFCLESEEGGPLFAKLLHALYDLDILEEEAILEWWEEPDAGADEEMKKVRELVKKFI 158


                ....
gi 83267879 708 QWLK 711
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 ...
 361-439 5.78e-34

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: 124.23  E-value: 5.78e-34
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83267879 361 LLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVTLKPRSVLTSQVVVGP 439
Cdd:cd05787   1 VIGRGTSIGEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPGSLISFGVVIGD 79
eIF5C smart00515
Domain at the C-termini of GCD6, eIF-2B epsilon, eIF-4 gamma and eIF-5;
629-711 1.19e-27

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


Pssm-ID: 214705  Cd Length: 83  Bit Score: 106.60  E-value: 1.19e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879    629 SPVFRNYIKRAADHLEALAAIEDFFLEHEALGISMAKVLMAFYQLEILAEETILSWFSQRDTTDKGQQLRKNQQLqrFIQ 708
Cdd:smart00515   1 GPLLKFLAKDEEEQLELLYAIEEFCVELEKLGKLLPKILKSLYDADILEEEAILKWYEKAVSAEGKKKVRKNAKP--FVT 78


                   ...
gi 83267879    709 WLK 711
Cdd:smart00515  79 WLQ 81
W2 pfam02020
eIF4-gamma/eIF5/eIF2-epsilon; This domain of unknown function is found at the C-terminus of ...
 642-711 4.06e-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: 76.41  E-value: 4.06e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83267879   642 HLEALAAIEDFFLEHEALGISMAKVLMAFYQLEILAEETILSWFSQ-RDTTDKGQQLRKnqQLQRFIQWLK 711
Cdd:pfam02020   1 QVDLLLALQEFCAKLEELLKLLLKILKALYDLDIVEEEAILKWWEDvSSAEKGMKKVRK--QAKPFVEWLE 69
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 345-408 9.33e-11

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: 63.88  E-value: 9.33e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 83267879 345 GPEVSLGHGSILEENVLLGSGTVIGSNCfitnsVIGPGCHIGDNvvldqTYLWQGVRVAAGAQI 408
Cdd:COG1044 112 GEGVSIGPFAVIGAGVVIGDGVVIGPGV-----VIGDGVVIGDD-----CVLHPNVTIYERCVI 165
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 345-408 6.59e-10

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 61.31  E-value: 6.59e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 83267879  345 GPEVSLGHGSILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNVVL-DQTYLWQGVRVAAGAQI 408
Cdd:PRK00892 116 GEGVSIGPNAVIGAGVVIGDGVVIGAGAVIgDGVKIGADCRLHANVTIyHAVRIGNRVIIHSGAVI 181
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
44-156 3.18e-09

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 57.94  E-value: 3.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879  44 QAVLVADSFDRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKWCrptslnvVRII 123
Cdd:COG1213   1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARPGPD-------VTFV 73

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 83267879 124 TSELYR---SLGDVLRdvdAKALVRSDFLLVYGDVI 156
Cdd:COG1213  74 YNPDYDetnNIYSLWL---AREALDEDFLLLNGDVV 106
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
365-391 6.97e-06

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 43.09  E-value: 6.97e-06
                          10        20
                  ....*....|....*....|....*...
gi 83267879   365 GTVIGSNCFI-TNSVIGPGCHIGDNVVL 391
Cdd:pfam00132   1 GTVIGDNVLIgPNAVIGGGVIIGDNVII 28
 
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; ...
 43-257 2.63e-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: 2.63e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879  43 LQAVLVADSFDRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKWCRPTS-LNVVR 121
Cdd:cd04197   1 LQAVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKSKWSKPKSsLMIVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 122 IITSELYRSLGDVLRDVDAKALVRSDFLLVYGDVISNINITRALEEHRLRRKLEKNVsVMTMIFKESSPSHPTRCHEDNV 201
Cdd:cd04197  81 IIMSEDCRSLGDALRDLDAKGLIRGDFILVSGDVVSNIDLKEILEEHKERRKKDKNA-IMTMVLKEASPPHRTRRTGEEF 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 83267879 202 VVAVDSTTNRVLHFQKTQGLRRFAF--PLSLFQGSSDGVEVRYDLLDCHISICSPQVA 257
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; ...
 43-256 1.07e-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: 1.07e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879  43 LQAVLVADSFDRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKWCRPTSLNVVRI 122
Cdd:cd02507   1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKWSSLSSKMIVDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 123 ITSELYRSLGDVLRDVDAKALVRSDFLLVYGDVISNINITRALEEhrlRRKLEKNvSVMTMIFKESSPSHPT---RCHED 199
Cdd:cd02507  81 ITSDLCESAGDALRLRDIRGLIRSDFLLLSCDLVSNIPLSELLEE---RRKKDKN-AIATLTVLLASPPVSTeqsKKTEE 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 83267879 200 NVVVAVDSTTNR--VLHFQKTQGLRRFAFPLSLFQGSSDGVEVRYDLLDCHISICSPQV 256
Cdd:cd02507 157 EDVIAVDSKTQRllLLHYEEDLDEDLELIIRKSLLSKHPNVTIRTDLLDCHIYICSPDV 215
W2_eIF2B_epsilon cd11558
C-terminal W2 domain of eukaryotic translation initiation factor 2B epsilon; eIF2B is a ...
 548-711 3.26e-56

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: 189.39  E-value: 3.26e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 548 DDIKVFQNEVLGTLQRGKEENISCDNLVLEINSLKYAYNISLKEVMQVLSHVVLEFPLQQMDspLDSSRYCALLLPLLKA 627
Cdd:cd11558   1 DDESDFHSEVVESLERALEENHSVDNAILEINSLRMAYNVTDHDVRRAVVKALLELILEVSS--TSTAELLEALKKLLSK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 628 WSPVFRNYIKRAADHLEALAAIEDFFLEHEALGISMAKVLMAFYQLEILAEETILSWFSQRDTTDKGQQLRKNQQLQRFI 707
Cdd:cd11558  79 WGPLLENYVKSQDDQVELLLALEEFCLESEEGGPLFAKLLHALYDLDILEEEAILEWWEEPDAGADEEMKKVRELVKKFI 158


                ....
gi 83267879 708 QWLK 711
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 ...
 361-439 5.78e-34

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: 124.23  E-value: 5.78e-34
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83267879 361 LLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVTLKPRSVLTSQVVVGP 439
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 ...
 361-439 5.73e-29

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: 110.02  E-value: 5.73e-29
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83267879 361 LLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVTLKPRSVLTSQVVVGP 439
Cdd:cd03356   1 LIGESTVIGENAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNLCIIGDDVVVED 79
eIF5C smart00515
Domain at the C-termini of GCD6, eIF-2B epsilon, eIF-4 gamma and eIF-5;
629-711 1.19e-27

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


Pssm-ID: 214705  Cd Length: 83  Bit Score: 106.60  E-value: 1.19e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879    629 SPVFRNYIKRAADHLEALAAIEDFFLEHEALGISMAKVLMAFYQLEILAEETILSWFSQRDTTDKGQQLRKNQQLqrFIQ 708
Cdd:smart00515   1 GPLLKFLAKDEEEQLELLYAIEEFCVELEKLGKLLPKILKSLYDADILEEEAILKWYEKAVSAEGKKKVRKNAKP--FVT 78


                   ...
gi 83267879    709 WLK 711
Cdd:smart00515  79 WLQ 81
W2 cd11473
C-terminal domain of eIF4-gamma/eIF5/eIF2b-epsilon; This domain is found at the C-terminus of ...
 548-685 1.96e-22

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: 93.70  E-value: 1.96e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 548 DDIKVFQNEVLGTLqrgKEENISCDNLVLEINSLKYAYNISLKEVMQVLSHVVLEFPLQQmdsPLDSSRYCALLLPLLKA 627
Cdd:cd11473   1 EKNKKLRDSLLKEL---EEDKSSDVESVKAAKSKLDLDPISLEEVVKVLLTAVVNAVESA---DSISLTQKEQLVLVLKK 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83267879 628 WSPVFRNYIK-RAADHLEALAAIEDFFLEHE--ALGISMAKVLMAFYQLEILAEETILSWF 685
Cdd:cd11473  75 YGPVLRELLKlIKKDQLYLLLKIEKLCLQLKlsELISLLEKILDLLYDADVLSEEAILSWF 135
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 43-256 1.32e-20

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: 90.80  E-value: 1.32e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879  43 LQAVLVADSFDRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKWCRPTSLNVVRI 122
Cdd:cd04198   1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFPLNLKQKLDEVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 123 ITSELYRSLGDVLRDVDAKalVRSDFLLVYGDVISNINITRALEEHRlrrkleKNVSVMTMIFKESS------PSHPTRC 196
Cdd:cd04198  81 IVLDEDMGTADSLRHIRKK--IKKDFLVLSCDLITDLPLIELVDLHR------SHDASLTVLLYPPPvsseqkGGKGKSK 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 197 HEDN-VVVAVDSTTNRVLH------FQKTQGLRR---FAFPlslfqgssdGVEVRYDLLDCHISICSPQV 256
Cdd:cd04198 153 KADErDVIGLDEKTQRLLFitseedLDEDLELRKsllKRHP---------RVTITTKLLDAHVYIFKRWV 213
W2 pfam02020
eIF4-gamma/eIF5/eIF2-epsilon; This domain of unknown function is found at the C-terminus of ...
 642-711 4.06e-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: 76.41  E-value: 4.06e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83267879   642 HLEALAAIEDFFLEHEALGISMAKVLMAFYQLEILAEETILSWFSQ-RDTTDKGQQLRKnqQLQRFIQWLK 711
Cdd:pfam02020   1 QVDLLLALQEFCAKLEELLKLLLKILKALYDLDIVEEEAILKWWEDvSSAEKGMKKVRK--QAKPFVEWLE 69
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 55-216 6.59e-16

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: 77.24  E-value: 6.59e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879  55 RFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKWCRPTslnvVRIITSELYRSLGDV 134
Cdd:cd04181  11 RLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVN----IEYVVQEEPLGTAGA 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 135 LRDVdAKALVRSDFLLVYGDVISNINITRALEEHRLRRkleknvSVMTMIFKEssPSHPTRChednVVVAVDStTNRVLH 214
Cdd:cd04181  87 VRNA-EDFLGDDDFLVVNGDVLTDLDLSELLRFHREKG------ADATIAVKE--VEDPSRY----GVVELDD-DGRVTR 152


                ..
gi 83267879 215 FQ 216
Cdd:cd04181 153 FV 154
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 361-448 2.19e-12

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: 62.98  E-value: 2.19e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 361 LLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVTLKprsvltsQVVVGPN 440
Cdd:cd04652   1 LVGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLK-------DCLVGSG 73


                ....*...
gi 83267879 441 ITLPEGSV 448
Cdd:cd04652  74 YRVEAGTE 81
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 345-408 9.33e-11

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: 63.88  E-value: 9.33e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 83267879 345 GPEVSLGHGSILEENVLLGSGTVIGSNCfitnsVIGPGCHIGDNvvldqTYLWQGVRVAAGAQI 408
Cdd:COG1044 112 GEGVSIGPFAVIGAGVVIGDGVVIGPGV-----VIGDGVVIGDD-----CVLHPNVTIYERCVI 165
W2_eIF5 cd11561
C-terminal W2 domain of eukaryotic translation initiation factor 5; eIF5 functions as a GTPase ...
 632-711 4.52e-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: 58.78  E-value: 4.52e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 632 FRNYIKRAAD------HLeaLAAIEDFFLEHEALGIS-MAKVLMAFYQLEILAEETILSWFSQRD----TTDKGQQLRKN 700
Cdd:cd11561  64 RKALLLKLVTdekaqkAL--LGGIERFCGKHSPELLKkVPLILKALYDNDILEEEVILKWYEKVSkkyvSKEKSKKVRKA 141

                        90
                ....*....|.
gi 83267879 701 qqLQRFIQWLK 711
Cdd:cd11561 142 --AEPFVEWLE 150
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 345-408 4.92e-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: 59.73  E-value: 4.92e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 83267879 345 GPEVSLGHGSILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNVVL-DQTYLWQGVRVAAGAQI 408
Cdd:cd03352   5 GENVSIGPNAVIGEGVVIGDGVVIGPGVVIgDGVVIGDDCVIHPNVTIyEGCIIGDRVIIHSGAVI 70
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 345-408 6.59e-10

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 61.31  E-value: 6.59e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 83267879  345 GPEVSLGHGSILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNVVL-DQTYLWQGVRVAAGAQI 408
Cdd:PRK00892 116 GEGVSIGPNAVIGAGVVIGDGVVIGAGAVIgDGVKIGADCRLHANVTIyHAVRIGNRVIIHSGAVI 181
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 55-172 1.53e-09

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: 58.74  E-value: 1.53e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879  55 RFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKWcrptslnVVRIITSELYRSL--- 131
Cdd:cd06422  12 RMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDSRF-------GLRITISDEPDELlet 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 83267879 132 -GDVLRdvdAKALVRSD-FLLVYGDVISNINITRALEEHRLRR 172
Cdd:cd06422  85 gGGIKK---ALPLLGDEpFLVVNGDILWDGDLAPLLLLHAWRM 124
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 345-404 1.83e-09

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: 54.56  E-value: 1.83e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83267879 345 GPEVSLGHGSILEENVLLGsGTVIGSNCFITNSVIGPGCHIGDNV-VLDQTYLWQGVRVAA 404
Cdd:cd03356  20 GDNVRIGDGVTITNSILMD-NVTIGANSVIVDSIIGDNAVIGENVrVVNLCIIGDDVVVED 79
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 341-438 2.64e-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: 57.43  E-value: 2.64e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 341 NIYRGPEVSLGHGSILEENVLLGSGTVIGSNCfitnsVIGPGCHIGDNVvldqtylwqgvrVAAGAQIHQSLLCDNAEVK 420
Cdd:cd03353   9 TTYIDGDVEIGVDVVIDPGVILEGKTVIGEDC-----VIGPNCVIKDST------------IGDGVVIKASSVIEGAVIG 71

                        90       100
                ....*....|....*....|....
gi 83267879 421 ERVT------LKPRSVLTSQVVVG 438
Cdd:cd03353  72 NGATvgpfahLRPGTVLGEGVHIG 95
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
44-156 3.18e-09

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 57.94  E-value: 3.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879  44 QAVLVADSFDRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKWCrptslnvVRII 123
Cdd:COG1213   1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARPGPD-------VTFV 73

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 83267879 124 TSELYR---SLGDVLRdvdAKALVRSDFLLVYGDVI 156
Cdd:COG1213  74 YNPDYDetnNIYSLWL---AREALDEDFLLLNGDVV 106
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 350-408 4.12e-09

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


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 54.39  E-value: 4.12e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 83267879 350 LGHGSILE----ENVLLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQI 408
Cdd:cd04651  15 VSEGCIISggtvENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPDGVVI 77
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 341-408 9.00e-09

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: 58.50  E-value: 9.00e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 83267879 341 NIYRGPEVSLGH------GSILEENVLLGSGTVIGSNCFITNSVIGPGCHIgDNVVLDqtylwqGVRVAAGAQI 408
Cdd:COG1207 260 TTYIDGDVEIGRdvvidpNVILEGKTVIGEGVVIGPNCTLKDSTIGDGVVI-KYSVIE------DAVVGAGATV 326
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 345-449 1.08e-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: 55.57  E-value: 1.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 345 GPEVSLGHGSILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNVVLdqtylwqgvrvAAGAqihqsLLCDNAEVKERV 423
Cdd:cd03360  94 SPSAVIGEGCVIMAGAVINPDARIGDNVIInTGAVIGHDCVIGDFVHI-----------APGV-----VLSGGVTIGEGA 157

                        90       100
                ....*....|....*....|....*.
gi 83267879 424 TLKPRSVLTSQVVVGPNITLPEGSVI 449
Cdd:cd03360 158 FIGAGATIIQGVTIGAGAIIGAGAVV 183
W2_eIF5C_like cd11560
C-terminal W2 domain of the eukaryotic translation initiation factor 5C and similar proteins; ...
 556-711 1.24e-08

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: 55.30  E-value: 1.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 556 EVLGTLQRGKEENISCDNLVLEINSLKYAYNISLKEVMQVLSHVVlefplqqMDSPLDSSR---YCALLLPLLKAWSPVF 632
Cdd:cd11560  40 ELQQELKEMIAEEEPVKEIIAAVKEQMKKSSLPEHEVVGLLWTAL-------MDAVEWSKKedqIAEQALRHLKKYAPLL 112

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83267879 633 RNYIKRAADHLEALAAIEDFFLEHEALGISMAKVLMAFYQLEILAEETILSWFSQrDTTDKGQQLRkNQQLQRFIQWLK 711
Cdd:cd11560 113 AAFCTTARAELALLNKIQEYCYENMKFMKVFQKIVKLLYKADVLSEDAILKWYKK-GHSPKGKQVF-LKQMEPFVEWLQ 189
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 45-168 2.27e-08

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 55.32  E-value: 2.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879  45 AVLVADSFDRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKwcrptslnVVRIIT 124
Cdd:cd02523   1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYP--------NIKFVY 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 83267879 125 SELYRSLGDVLRDVDAKALVRSDFLLVYGDVISNINITRALEEH 168
Cdd:cd02523  73 NPDYAETNNIYSLYLARDFLDEDFLLLEGDVVFDPSILERLLSS 116
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 340-391 2.82e-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: 2.82e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 83267879 340 HNIYRGPEVSLGHGSILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNVVL 391
Cdd:cd03352  12 PNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIhPNVTIYEGCIIGDRVII 64
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 355-438 2.93e-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: 2.93e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 355 ILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDnvvldqtylwqGVRVAAGAQIHqsllcDNAEVKERVTLKPRSVLTS 433
Cdd:cd03352   3 KIGENVSIGPNAVIGEGVVIgDGVVIGPGVVIGD-----------GVVIGDDCVIH-----PNVTIYEGCIIGDRVIIHS 66


                ....*
gi 83267879 434 QVVVG 438
Cdd:cd03352  67 GAVIG 71
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 343-450 7.31e-08

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 55.52  E-value: 7.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879  343 YRGPEVSLGHGSILEENVLLGSGTVIGSNCFITNSVIGPGCHIGDNVVldqtylwqgvrVAAGAQIHQSLLCDNAEVKER 422
Cdd:PRK14355 264 YIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKGCRIGDDVT-----------VKAGSVLEDSVVGDDVAIGPM 332

                         90       100       110
                 ....*....|....*....|....*....|...
gi 83267879  423 VTLKPRSVLTSQVVVG-----PNITLPEGSVIS 450
Cdd:PRK14355 333 AHLRPGTELSAHVKIGnfvetKKIVMGEGSKAS 365
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 336-408 7.70e-08

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 55.08  E-value: 7.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 336 THSRHN----IYRGPEVS---LGHGSILE---ENVLLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAG 405
Cdd:COG0448 270 TKQKDLppakFVRGGKVKnslVSNGCIISgtvENSVLFRGVRVESGAVVENSVIMPGVVIGEGAVIENAIIDKNVVIPPG 349


                ...
gi 83267879 406 AQI 408
Cdd:COG0448 350 VVI 352
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 368-449 9.55e-08

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: 50.54  E-value: 9.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 368 IGSNCFITNSVIGPGCHIGDNVVlDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVTLKprsvltsQVVVGPNITLPEGS 447
Cdd:cd04651   4 IGRRGEVKNSLVSEGCIISGGTV-ENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIR-------RAIIDKNVVIPDGV 75


                ..
gi 83267879 448 VI 449
Cdd:cd04651  76 VI 77
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 345-408 1.06e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 54.37  E-value: 1.06e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 83267879  345 GPEVSLGHGSILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNvvldqTYLWQGVRVAAGAQI 408
Cdd:PRK00892 110 DPSAKIGEGVSIGPNAVIGAGVVIGDGVVIgAGAVIGDGVKIGAD-----CRLHANVTIYHAVRI 169
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 342-446 2.28e-07

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: 51.09  E-value: 2.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 342 IYRGPEVSLGHGSILEENVLLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSllcDNAEVKE 421
Cdd:cd00710  65 VWIGKNVSIAHGAIVHGPAYIGDNCFIGFRSVVFNAKVGDNCVIGHNAVVDGVEIPPGRYVPAGAVITSQ---TQADALP 141

                        90       100
                ....*....|....*....|....*
gi 83267879 422 RVTLKPRsvLTSQVVVGPNITLPEG 446
Cdd:cd00710 142 DVTDSAR--EFNEKVITVNNELAEG 164
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
354-449 3.08e-07

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 50.25  E-value: 3.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 354 SILEENVLLGSGTVIGSNCFI--TNSVIGPGCHIGDNVVLdqtYLWQGVRVAAGAQIHQ--SLLCDN---------AEVK 420
Cdd:COG0110   3 LLLLFGARIGDGVVIGPGVRIygGNITIGDNVYIGPGVTI---DDPGGITIGDNVLIGPgvTILTGNhpiddpatfPLRT 79

                        90       100
                ....*....|....*....|....*....
gi 83267879 421 ERVTLKPRSVLTSQVVVGPNITLPEGSVI 449
Cdd:COG0110  80 GPVTIGDDVWIGAGATILPGVTIGDGAVV 108
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 340-391 6.95e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 52.06  E-value: 6.95e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 83267879  340 HNIYRGPEVSLGHGSILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNVVL 391
Cdd:PRK00892 123 PNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLhANVTIYHAVRIGNRVII 175
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 341-450 8.23e-07

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 50.10  E-value: 8.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 341 NIYRGPEVSLGHGSILEENVLLGSGTVIGSNCFI-TNSVIG---------PGCH----------IGDNV----------- 389
Cdd:cd03352  31 GVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIhSGAVIGsdgfgfapdGGGWvkipqlggviIGDDVeiganttidrg 110

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83267879 390 VLDQTYLWQGVR------VAAGAQI--HqSLLCDNAEVKERVTLKPRSVLTSQVVVGPNITLPEGSVIS 450
Cdd:cd03352 111 ALGDTVIGDGTKidnlvqIAHNVRIgeN-CLIAAQVGIAGSTTIGDNVIIGGQVGIAGHLTIGDGVVIG 178
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 368-449 1.76e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 50.64  E-value: 1.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879  368 IGSNCFITNSVIGPGCHIGDNVvlDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVTLKprsvltsQVVVGPNITLPEGS 447
Cdd:PRK05293 285 IAENAKVKNSLVVEGCVVYGTV--EHSVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIE-------RAIIGENAVIGDGV 355


                 ..
gi 83267879  448 VI 449
Cdd:PRK05293 356 II 357
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 340-392 2.91e-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: 45.70  E-value: 2.91e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 83267879 340 HNIYRGPEVSLGHGSILEENVLLG--------SGTVIGSNCFI-TNSVIGPGCHIGDNVVLD 392
Cdd:cd00208  11 PKAVIRGPVVIGDNVNIGPGAVIGaatgpnekNPTIIGDNVEIgANAVIHGGVKIGDNAVIG 72
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 344-419 4.05e-06

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: 47.58  E-value: 4.05e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 83267879 344 RGPEVSLGHGSILEENVLLGSGTVIGSNCfitnsVIGPGCHIGDNVVLDqtylwQGVRVAAGAQIHQSLLCDNAEV 419
Cdd:cd05636  14 IKGPVWIGEGAIVRSGAYIEGPVIIGKGC-----EIGPNAYIRGYTVLG-----DGCVVGNSVEVKNSIIMDGTKV 79
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 341-438 6.31e-06

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 49.44  E-value: 6.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879  341 NIYRGPEVSLGHGSILEENVLLGSGTVIGSNCFIT------NSVIGPGCHIGDNVVLDqtylwqgvrvaagaqihqsllc 414
Cdd:PRK14354 259 STYIDADVEIGSDTVIEPGVVIKGNTVIGEDCVIGpgsrivDSTIGDGVTITNSVIEE---------------------- 316

                         90       100       110
                 ....*....|....*....|....*....|
gi 83267879  415 dnAEVKERVT------LKPRSVLTSQVVVG 438
Cdd:PRK14354 317 --SKVGDNVTvgpfahLRPGSVIGEEVKIG 344
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
365-391 6.97e-06

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 43.09  E-value: 6.97e-06
                          10        20
                  ....*....|....*....|....*...
gi 83267879   365 GTVIGSNCFI-TNSVIGPGCHIGDNVVL 391
Cdd:pfam00132   1 GTVIGDNVLIgPNAVIGGGVIIGDNVII 28
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
338-406 9.24e-06

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 46.02  E-value: 9.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 338 SRHNIYRGPEVSLGHGSIL----------EENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNVVldqtylwqgvrVAAGA 406
Cdd:COG0110  44 DPGGITIGDNVLIGPGVTIltgnhpiddpATFPLRTGPVTIGDDVWIgAGATILPGVTIGDGAV-----------VGAGS 112
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 55-172 1.25e-05

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


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 47.18  E-value: 1.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879  55 RFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLK-SKWcrptSLNVVRIITSELyRSLGD 133
Cdd:cd04189  13 RLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDgSRF----GVRITYILQEEP-LGLAH 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 83267879 134 -VLRdvdAKALV-RSDFLLVYGDVISNINITRALEEHRLRR 172
Cdd:cd04189  88 aVLA---ARDFLgDEPFVVYLGDNLIQEGISPLVRDFLEED 125
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 365-406 1.76e-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: 44.37  E-value: 1.76e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 83267879 365 GTVIGSNCFI-TNSVIGPGCHIGDNVVldqtylwqgvrVAAGA 406
Cdd:cd04647  58 PIVIGDDVWIgANVVILPGVTIGDGAV-----------VGAGS 89
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 345-408 2.28e-05

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


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 44.03  E-value: 2.28e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 83267879 345 GPEVSLGHGSILEENVLLGSGTVIGSNCFIT-NSVIGPGCHIGDNVVL----------DQTYLWQGVRVAAGAQI 408
Cdd:cd03358   2 GDNCIIGTNVFIENDVKIGDNVKIQSNVSIYeGVTIEDDVFIGPNVVFtndlyprskiYRKWELKGTTVKRGASI 76
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 359-449 3.83e-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: 43.21  E-value: 3.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 359 NVLLGSGTVIGSNCFITNS---VIGPGCHIGDNVVLdqtylwqgvrVAAGAQIH-QSLLCDNAEVKERVTLKPRSVLTSQ 434
Cdd:cd04647   1 NISIGDNVYIGPGCVISAGggiTIGDNVLIGPNVTI----------YDHNHDIDdPERPIEQGVTSAPIVIGDDVWIGAN 70

                        90
                ....*....|....*
gi 83267879 435 VVVGPNITLPEGSVI 449
Cdd:cd04647  71 VVILPGVTIGDGAVV 85
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 345-391 6.35e-05

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: 45.39  E-value: 6.35e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 83267879 345 GPEVSLGHGSILEENVLLGSGTVIGSNCFIT-NSVIGPGCHIGDNVVL 391
Cdd:COG1043  17 GENVEIGPFCVIGPDVEIGDGTVIGSHVVIEgPTTIGKNNRIFPFASI 64
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 315-408 8.95e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 45.59  E-value: 8.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879  315 RRW----VYPLTPEANFTDSTTQSCtHSRHNIyrgpeVSLG---HGSILEENVLlGSGTVIGSNCFITNSVIGPGCHIGD 387
Cdd:PRK00844 287 REWpiytSSPNLPPAKFVDGGGRVG-SAQDSL-----VSAGsiiSGATVRNSVL-SPNVVVESGAEVEDSVLMDGVRIGR 359

                         90       100
                 ....*....|....*....|.
gi 83267879  388 NVVLDQTYLWQGVRVAAGAQI 408
Cdd:PRK00844 360 GAVVRRAILDKNVVVPPGATI 380
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 348-449 9.15e-05

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 44.01  E-value: 9.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 348 VSLGHGS-ILEENVLLGSGTVIGSNCfitnsVIGPGCHIGDNVVldqtyLWQGVRVAagaqiHQSLLCDNaevkerVTLK 426
Cdd:cd03360  84 ATLIHPSaVVSPSAVIGEGCVIMAGA-----VINPDARIGDNVI-----INTGAVIG-----HDCVIGDF------VHIA 142

                        90       100       110
                ....*....|....*....|....*....|....*
gi 83267879 427 PRSVLTSQVVVG------------PNITLPEGSVI 449
Cdd:cd03360 143 PGVVLSGGVTIGegafigagatiiQGVTIGAGAII 177
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 347-449 1.27e-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: 1.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 347 EVSLGHGSILEENVLL----GSGTVIGSNCFITNSVIGPGCHIGDNVVldqtylwqgvrVAAGAQIhqsllCDNAEVKER 422
Cdd:cd04645  38 PIRIGERTNIQDGSVLhvdpGYPTIIGDNVTVGHGAVLHGCTIGDNCL-----------IGMGAII-----LDGAVIGKG 101

                        90       100
                ....*....|....*....|....*..
gi 83267879 423 VTLKPRSVLTsqvvvgPNITLPEGSVI 449
Cdd:cd04645 102 SIVAAGSLVP------PGKVIPPGSLV 122
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 376-449 1.29e-04

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: 43.55  E-value: 1.29e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 83267879 376 NSVIGPGCHIGDNVVLDqtylwQGVRVAAGAQIH-QSLLCDNAEVKERVTLKPRSVLTSQVVVGPNITLPEGSVI 449
Cdd:cd03352   1 SAKIGENVSIGPNAVIG-----EGVVIGDGVVIGpGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 358-424 1.35e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 44.82  E-value: 1.35e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 83267879  358 ENVLLGSGTVIgSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVT 424
Cdd:PRK00844 314 QDSLVSAGSII-SGATVRNSVLSPNVVVESGAEVEDSVLMDGVRIGRGAVVRRAILDKNVVVPPGAT 379
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
345-391 2.74e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 43.16  E-value: 2.74e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 83267879  345 GPEVSLGHGSILEENVLLGSGTVIGSNCFIT-NSVIGPGCHIGDNVVL 391
Cdd:PRK05289  18 GENVEIGPFCVIGPNVVIGDGTVIGSHVVIDgHTTIGKNNRIFPFASI 65
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 345-391 2.81e-04

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 43.19  E-value: 2.81e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 83267879 345 GPEVSLGHGSILEENVLLGSGTVIGSNCFIT-NSVIGPGCHIGDNVVL 391
Cdd:cd03351  15 GENVEIGPFCVIGPNVEIGDGTVIGSHVVIDgPTTIGKNNRIFPFASI 62
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 345-390 3.97e-04

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 41.55  E-value: 3.97e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 83267879 345 GPEVSLGHGSIL-----EENVLLGSG------TVIGSNCFIT-NSVIGPGCHIGDNVV 390
Cdd:COG0663  75 GDDVTIGHGAILhgctiGDNVLIGMGaivldgAVIGDGSIVGaGALVTEGKVVPPGSL 132
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 342-449 4.66e-04

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 41.42  E-value: 4.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 342 IYRGPEVSLGHGSILEENVLLGSGTVIGSNCFITNSVIGPGCHI------GDNVvldqtyLWQGVRVAAGAQIhQSLLCD 415
Cdd:cd05636  36 VIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKVphlnyvGDSV------LGENVNLGAGTIT-ANLRFD 108

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 83267879 416 NAEVKerVTLKPRSVLTSQ----------VVVGPNITLPEGSVI 449
Cdd:cd05636 109 DKPVK--VRLKGERVDTGRrklgaiigdgVKTGINVSLNPGVKI 150
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 354-449 6.85e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 42.55  E-value: 6.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879  354 SILEENVLLGSGTVIgsncfiTNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIhqsllcdnAEVKERVTlkprsvlts 433
Cdd:PRK05293 309 SVLFQGVQVGEGSVV------KDSVIMPGAKIGENVVIERAIIGENAVIGDGVII--------GGGKEVIT--------- 365

                         90
                 ....*....|....*.
gi 83267879  434 qvVVGPNITLPEGSVI 449
Cdd:PRK05293 366 --VIGENEVIGVGTVI 379
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 378-449 1.16e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 41.66  E-value: 1.16e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 83267879  378 VIGPGCHIGDNVVLD-QTYLWQGVRVAAGAQIH-QSLLCDNAEVKERVTLKPRSVLTSQVVVGPNITLPEGSVI 449
Cdd:PRK00892 108 VIDPSAKIGEGVSIGpNAVIGAGVVIGDGVVIGaGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVI 181
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 344-408 1.34e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 41.94  E-value: 1.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 83267879  344 RGpevSLGHGS--------ILEENVLLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDqtylwqGVRVAAGAQI 408
Cdd:PRK09451 263 RG---TLTHGRdveidtnvIIEGNVTLGNRVKIGAGCVLKNCVIGDDCEISPYSVVE------DANLGAACTI 326
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
353-386 1.50e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.55  E-value: 1.50e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 83267879   353 GSILEENVLLGSGTVIGSNCfitnsVIGPGCHIG 386
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGV-----IIGDNVIIG 29
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 367-449 3.28e-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: 36.84  E-value: 3.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 367 VIGSNCFI-TNSVIGPGCHIGDNVvldqtylwqgvRVAAGAQIHqSLLCDN----AEVKERVTLKPRSVLTSQVVVGPNI 441
Cdd:cd00208   2 FIGEGVKIhPKAVIRGPVVIGDNV-----------NIGPGAVIG-AATGPNeknpTIIGDNVEIGANAVIHGGVKIGDNA 69


                ....*...
gi 83267879 442 TLPEGSVI 449
Cdd:cd00208  70 VIGAGAVV 77
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 343-391 3.35e-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: 39.72  E-value: 3.35e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 83267879 343 YRGPEVSL--GHGSILEENVLLGSG-------TVIGSNCFI-TNSVIGPGCHIGDNVVL 391
Cdd:cd03351  71 YKGEPTRLeiGDNNTIREFVTIHRGtaqgggvTRIGNNNLLmAYVHVAHDCVIGNNVIL 129
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
343-391 5.40e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 39.31  E-value: 5.40e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 83267879  343 YRGPEVSL--GHGSILEENVLLGSGTV-------IGSNCFI-TNSVIGPGCHIGDNVVL 391
Cdd:PRK05289  74 YKGEPTRLviGDNNTIREFVTINRGTVqgggvtrIGDNNLLmAYVHVAHDCVVGNHVIL 132
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 355-449 5.70e-03

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 38.47  E-value: 5.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 355 ILEENVLLGSGTVI-GSNCFITnsvIGPGCHIGDNVVL--DQTY-LW--QGVRVAAGAQIH------------QSLLCDN 416
Cdd:COG0663  30 TIGEDVSVWPGAVLrGDVGPIR---IGEGSNIQDGVVLhvDPGYpLTigDDVTIGHGAILHgctigdnvligmGAIVLDG 106

                        90       100       110
                ....*....|....*....|....*....|...
gi 83267879 417 AEVKERVTLKPRSvltsqvVVGPNITLPEGSVI 449
Cdd:COG0663 107 AVIGDGSIVGAGA------LVTEGKVVPPGSLV 133
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
353-410 5.85e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 39.31  E-value: 5.85e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 83267879  353 GSILEENVLLGSGTVIGSNCfitnsVIGPGCHIGDNVVLDqtylwQGVRVAAGAQIHQ 410
Cdd:PRK05289  14 GAKIGENVEIGPFCVIGPNV-----VIGDGTVIGSHVVID-----GHTTIGKNNRIFP 61
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 359-406 6.54e-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: 36.02  E-value: 6.54e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 83267879 359 NVLLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGA 406
Cdd:cd04652  33 NCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAGT 80
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 354-443 7.35e-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: 36.07  E-value: 7.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83267879 354 SILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNvvldqtylwQGVRVAAGAQIHqsllcDNAEVKERVTLKPRSVLT 432
Cdd:cd00208   1 VFIGEGVKIHPKAVIRGPVVIgDNVNIGPGAVIGAA---------TGPNEKNPTIIG-----DNVEIGANAVIHGGVKIG 66

                        90
                ....*....|.
gi 83267879 433 SQVVVGPNITL 443
Cdd:cd00208  67 DNAVIGAGAVV 77
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 354-410 9.48e-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: 38.46  E-value: 9.48e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 83267879 354 SILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNVVLDqtylwQGVRVAAGAQIHQ 410
Cdd:COG1043   8 AIVDPGAKLGENVEIGPFCVIgPDVEIGDGTVIGSHVVIE-----GPTTIGKNNRIFP 60
 
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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