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Conserved domains on  [gi|767927902|ref|XP_011511567|]
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translation initiation factor eIF2B subunit epsilon isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
W2_eIF2B_epsilon cd11558
C-terminal W2 domain of eukaryotic translation initiation factor 2B epsilon; eIF2B is a ...
 298-461 1.25e-58

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: 190.55  E-value: 1.25e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902 298 DDIKVFQNEVLGTLQRGKEENISCDNLVLEINSLKYAYNISLKEVMQVLSHVVLEFPLQQMDspLDSSRYCALLLPLLKA 377
Cdd:cd11558    1 DDESDFHSEVVESLERALEENHSVDNAILEINSLRMAYNVTDHDVRRAVVKALLELILEVSS--TSTAELLEALKKLLSK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902 378 WSPVFRNYIKRAADHLEALAAIEDFFLEHEALGISMAKVLMAFYQLEILAEETILSWFSQRDTTDKGQQLRKNQQLQRFI 457
Cdd:cd11558   79 WGPLLENYVKSQDDQVELLLALEEFCLESEEGGPLFAKLLHALYDLDILEEEAILEWWEEPDAGADEEMKKVRELVKKFI 158


                 ....
gi 767927902 458 QWLK 461
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 ...
 111-189 3.15e-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: 123.07  E-value: 3.15e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767927902 111 LLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVTLKPRSVLTSQVVVGP 189
Cdd:cd05787    1 VIGRGTSIGEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPGSLISFGVVIGD 79
 
Name Accession Description Interval E-value
W2_eIF2B_epsilon cd11558
C-terminal W2 domain of eukaryotic translation initiation factor 2B epsilon; eIF2B is a ...
 298-461 1.25e-58

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: 190.55  E-value: 1.25e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902 298 DDIKVFQNEVLGTLQRGKEENISCDNLVLEINSLKYAYNISLKEVMQVLSHVVLEFPLQQMDspLDSSRYCALLLPLLKA 377
Cdd:cd11558    1 DDESDFHSEVVESLERALEENHSVDNAILEINSLRMAYNVTDHDVRRAVVKALLELILEVSS--TSTAELLEALKKLLSK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902 378 WSPVFRNYIKRAADHLEALAAIEDFFLEHEALGISMAKVLMAFYQLEILAEETILSWFSQRDTTDKGQQLRKNQQLQRFI 457
Cdd:cd11558   79 WGPLLENYVKSQDDQVELLLALEEFCLESEEGGPLFAKLLHALYDLDILEEEAILEWWEEPDAGADEEMKKVRELVKKFI 158


                 ....
gi 767927902 458 QWLK 461
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 ...
 111-189 3.15e-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: 123.07  E-value: 3.15e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767927902 111 LLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVTLKPRSVLTSQVVVGP 189
Cdd:cd05787    1 VIGRGTSIGEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPGSLISFGVVIGD 79
eIF5C smart00515
Domain at the C-termini of GCD6, eIF-2B epsilon, eIF-4 gamma and eIF-5;
379-461 7.86e-28

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


Pssm-ID: 214705  Cd Length: 83  Bit Score: 105.83  E-value: 7.86e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902   379 SPVFRNYIKRAADHLEALAAIEDFFLEHEALGISMAKVLMAFYQLEILAEETILSWFSQRDTTDKGQQLRKNQQLqrFIQ 458
Cdd:smart00515   1 GPLLKFLAKDEEEQLELLYAIEEFCVELEKLGKLLPKILKSLYDADILEEEAILKWYEKAVSAEGKKKVRKNAKP--FVT 78


                   ...
gi 767927902   459 WLK 461
Cdd:smart00515  79 WLQ 81
W2 pfam02020
eIF4-gamma/eIF5/eIF2-epsilon; This domain of unknown function is found at the C-terminus of ...
 392-461 3.97e-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: 75.64  E-value: 3.97e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767927902  392 HLEALAAIEDFFLEHEALGISMAKVLMAFYQLEILAEETILSWFSQ-RDTTDKGQQLRKnqQLQRFIQWLK 461
Cdd:pfam02020   1 QVDLLLALQEFCAKLEELLKLLLKILKALYDLDIVEEEAILKWWEDvSSAEKGMKKVRK--QAKPFVEWLE 69
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 95-158 4.80e-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: 4.80e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767927902  95 GPEVSLGHGSILEENVLLGSGTVIGSNCfitnsVIGPGCHIGDNvvldqTYLWQGVRVAAGAQI 158
Cdd:COG1044  112 GEGVSIGPFAVIGAGVVIGDGVVIGPGV-----VIGDGVVIGDD-----CVLHPNVTIYERCVI 165
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 95-158 3.41e-10

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 61.31  E-value: 3.41e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767927902  95 GPEVSLGHGSILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNVVL-DQTYLWQGVRVAAGAQI 158
Cdd:PRK00892 116 GEGVSIGPNAVIGAGVVIGDGVVIGAGAVIgDGVKIGADCRLHANVTIyHAVRIGNRVIIHSGAVI 181
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
115-141 5.98e-06

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 42.71  E-value: 5.98e-06
                          10        20
                  ....*....|....*....|....*...
gi 767927902  115 GTVIGSNCFI-TNSVIGPGCHIGDNVVL 141
Cdd:pfam00132   1 GTVIGDNVLIgPNAVIGGGVIIGDNVII 28
 
Name Accession Description Interval E-value
W2_eIF2B_epsilon cd11558
C-terminal W2 domain of eukaryotic translation initiation factor 2B epsilon; eIF2B is a ...
 298-461 1.25e-58

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: 190.55  E-value: 1.25e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902 298 DDIKVFQNEVLGTLQRGKEENISCDNLVLEINSLKYAYNISLKEVMQVLSHVVLEFPLQQMDspLDSSRYCALLLPLLKA 377
Cdd:cd11558    1 DDESDFHSEVVESLERALEENHSVDNAILEINSLRMAYNVTDHDVRRAVVKALLELILEVSS--TSTAELLEALKKLLSK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902 378 WSPVFRNYIKRAADHLEALAAIEDFFLEHEALGISMAKVLMAFYQLEILAEETILSWFSQRDTTDKGQQLRKNQQLQRFI 457
Cdd:cd11558   79 WGPLLENYVKSQDDQVELLLALEEFCLESEEGGPLFAKLLHALYDLDILEEEAILEWWEEPDAGADEEMKKVRELVKKFI 158


                 ....
gi 767927902 458 QWLK 461
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 ...
 111-189 3.15e-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: 123.07  E-value: 3.15e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767927902 111 LLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVTLKPRSVLTSQVVVGP 189
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 ...
 111-189 1.92e-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: 1.92e-29
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767927902 111 LLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVTLKPRSVLTSQVVVGP 189
Cdd:cd03356    1 LIGESTVIGENAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNLCIIGDDVVVED 79
eIF5C smart00515
Domain at the C-termini of GCD6, eIF-2B epsilon, eIF-4 gamma and eIF-5;
379-461 7.86e-28

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


Pssm-ID: 214705  Cd Length: 83  Bit Score: 105.83  E-value: 7.86e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902   379 SPVFRNYIKRAADHLEALAAIEDFFLEHEALGISMAKVLMAFYQLEILAEETILSWFSQRDTTDKGQQLRKNQQLqrFIQ 458
Cdd:smart00515   1 GPLLKFLAKDEEEQLELLYAIEEFCVELEKLGKLLPKILKSLYDADILEEEAILKWYEKAVSAEGKKKVRKNAKP--FVT 78


                   ...
gi 767927902   459 WLK 461
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 ...
 298-435 7.80e-23

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: 7.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902 298 DDIKVFQNEVLGTLqrgKEENISCDNLVLEINSLKYAYNISLKEVMQVLSHVVLEFPLQQmdsPLDSSRYCALLLPLLKA 377
Cdd:cd11473    1 EKNKKLRDSLLKEL---EEDKSSDVESVKAAKSKLDLDPISLEEVVKVLLTAVVNAVESA---DSISLTQKEQLVLVLKK 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767927902 378 WSPVFRNYIK-RAADHLEALAAIEDFFLEHE--ALGISMAKVLMAFYQLEILAEETILSWF 435
Cdd:cd11473   75 YGPVLRELLKlIKKDQLYLLLKIEKLCLQLKlsELISLLEKILDLLYDADVLSEEAILSWF 135
W2 pfam02020
eIF4-gamma/eIF5/eIF2-epsilon; This domain of unknown function is found at the C-terminus of ...
 392-461 3.97e-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: 75.64  E-value: 3.97e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767927902  392 HLEALAAIEDFFLEHEALGISMAKVLMAFYQLEILAEETILSWFSQ-RDTTDKGQQLRKnqQLQRFIQWLK 461
Cdd:pfam02020   1 QVDLLLALQEFCAKLEELLKLLLKILKALYDLDIVEEEAILKWWEDvSSAEKGMKKVRK--QAKPFVEWLE 69
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 111-198 1.45e-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: 1.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902 111 LLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVTLKprsvltsQVVVGPN 190
Cdd:cd04652    1 LVGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLK-------DCLVGSG 73


                 ....*...
gi 767927902 191 ITLPEGSV 198
Cdd:cd04652   74 YRVEAGTE 81
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 95-158 4.80e-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: 4.80e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767927902  95 GPEVSLGHGSILEENVLLGSGTVIGSNCfitnsVIGPGCHIGDNvvldqTYLWQGVRVAAGAQI 158
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 ...
 382-461 2.72e-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: 2.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902 382 FRNYIKRAAD------HLeaLAAIEDFFLEHEALGIS-MAKVLMAFYQLEILAEETILSWFSQRD----TTDKGQQLRKN 450
Cdd:cd11561   64 RKALLLKLVTdekaqkAL--LGGIERFCGKHSPELLKkVPLILKALYDNDILEEEVILKWYEKVSkkyvSKEKSKKVRKA 141

                         90
                 ....*....|.
gi 767927902 451 qqLQRFIQWLK 461
Cdd:cd11561  142 --AEPFVEWLE 150
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 95-158 3.40e-10

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 59.34  E-value: 3.40e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767927902  95 GPEVSLGHGSILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNVVL-DQTYLWQGVRVAAGAQI 158
Cdd:cd03352    5 GENVSIGPNAVIGEGVVIGDGVVIGPGVVIgDGVVIGDDCVIHPNVTIyEGCIIGDRVIIHSGAVI 70
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 95-158 3.41e-10

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 61.31  E-value: 3.41e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767927902  95 GPEVSLGHGSILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNVVL-DQTYLWQGVRVAAGAQI 158
Cdd:PRK00892 116 GEGVSIGPNAVIGAGVVIGDGVVIGAGAVIgDGVKIGADCRLHANVTIyHAVRIGNRVIIHSGAVI 181
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 95-154 1.24e-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: 1.24e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767927902  95 GPEVSLGHGSILEENVLLGsGTVIGSNCFITNSVIGPGCHIGDNV-VLDQTYLWQGVRVAA 154
Cdd:cd03356   20 GDNVRIGDGVTITNSILMD-NVTIGANSVIVDSIIGDNAVIGENVrVVNLCIIGDDVVVED 79
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 91-188 1.55e-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: 1.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902  91 NIYRGPEVSLGHGSILEENVLLGSGTVIGSNCfitnsVIGPGCHIGDNVvldqtylwqgvrVAAGAQIHQSLLCDNAEVK 170
Cdd:cd03353    9 TTYIDGDVEIGVDVVIDPGVILEGKTVIGEDC-----VIGPNCVIKDST------------IGDGVVIKASSVIEGAVIG 71

                         90       100
                 ....*....|....*....|....
gi 767927902 171 ERVT------LKPRSVLTSQVVVG 188
Cdd:cd03353   72 NGATvgpfahLRPGTVLGEGVHIG 95
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 100-158 2.03e-09

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


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 54.78  E-value: 2.03e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767927902 100 LGHGSILE----ENVLLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQI 158
Cdd:cd04651   15 VSEGCIISggtvENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPDGVVI 77
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 91-158 5.02e-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: 58.11  E-value: 5.02e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767927902  91 NIYRGPEVSLGH------GSILEENVLLGSGTVIGSNCFITNSVIGPGCHIgDNVVLDqtylwqGVRVAAGAQI 158
Cdd:COG1207  260 TTYIDGDVEIGRdvvidpNVILEGKTVIGEGVVIGPNCTLKDSTIGDGVVI-KYSVIE------DAVVGAGATV 326
W2_eIF5C_like cd11560
C-terminal W2 domain of the eukaryotic translation initiation factor 5C and similar proteins; ...
 306-461 8.15e-09

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: 8.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902 306 EVLGTLQRGKEENISCDNLVLEINSLKYAYNISLKEVMQVLSHVVlefplqqMDSPLDSSR---YCALLLPLLKAWSPVF 382
Cdd:cd11560   40 ELQQELKEMIAEEEPVKEIIAAVKEQMKKSSLPEHEVVGLLWTAL-------MDAVEWSKKedqIAEQALRHLKKYAPLL 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767927902 383 RNYIKRAADHLEALAAIEDFFLEHEALGISMAKVLMAFYQLEILAEETILSWFSQrDTTDKGQQLRkNQQLQRFIQWLK 461
Cdd:cd11560  113 AAFCTTARAELALLNKIQEYCYENMKFMKVFQKIVKLLYKADVLSEDAILKWYKK-GHSPKGKQVF-LKQMEPFVEWLQ 189
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 95-199 9.49e-09

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: 55.18  E-value: 9.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902  95 GPEVSLGHGSILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNVVLdqtylwqgvrvAAGAqihqsLLCDNAEVKERV 173
Cdd:cd03360   94 SPSAVIGEGCVIMAGAVINPDARIGDNVIInTGAVIGHDCVIGDFVHI-----------APGV-----VLSGGVTIGEGA 157

                         90       100
                 ....*....|....*....|....*.
gi 767927902 174 TLKPRSVLTSQVVVGPNITLPEGSVI 199
Cdd:cd03360  158 FIGAGATIIQGVTIGAGAIIGAGAVV 183
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 90-141 1.83e-08

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 54.34  E-value: 1.83e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767927902  90 HNIYRGPEVSLGHGSILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNVVL 141
Cdd:cd03352   12 PNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIhPNVTIYEGCIIGDRVII 64
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 105-188 2.02e-08

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 54.34  E-value: 2.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902 105 ILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDnvvldqtylwqGVRVAAGAQIHqsllcDNAEVKERVTLKPRSVLTS 183
Cdd:cd03352    3 KIGENVSIGPNAVIGEGVVIgDGVVIGPGVVIGD-----------GVVIGDDCVIH-----PNVTIYEGCIIGDRVIIHS 66


                 ....*
gi 767927902 184 QVVVG 188
Cdd:cd03352   67 GAVIG 71
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 93-200 3.76e-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: 3.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902  93 YRGPEVSLGHGSILEENVLLGSGTVIGSNCFITNSVIGPGCHIGDNVVldqtylwqgvrVAAGAQIHQSLLCDNAEVKER 172
Cdd:PRK14355 264 YIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKGCRIGDDVT-----------VKAGSVLEDSVVGDDVAIGPM 332

                         90       100       110
                 ....*....|....*....|....*....|...
gi 767927902 173 VTLKPRSVLTSQVVVG-----PNITLPEGSVIS 200
Cdd:PRK14355 333 AHLRPGTELSAHVKIGnfvetKKIVMGEGSKAS 365
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 103-158 4.22e-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: 4.22e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767927902 103 GSILE---ENVLLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQI 158
Cdd:COG0448  294 GCIISgtvENSVLFRGVRVESGAVVENSVIMPGVVIGEGAVIENAIIDKNVVIPPGVVI 352
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 118-199 4.93e-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: 50.92  E-value: 4.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902 118 IGSNCFITNSVIGPGCHIGDNVVlDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVTLKprsvltsQVVVGPNITLPEGS 197
Cdd:cd04651    4 IGRRGEVKNSLVSEGCIISGGTV-ENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIR-------RAIIDKNVVIPDGV 75


                 ..
gi 767927902 198 VI 199
Cdd:cd04651   76 VI 77
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 95-158 5.66e-08

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 54.37  E-value: 5.66e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767927902  95 GPEVSLGHGSILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNvvldqTYLWQGVRVAAGAQI 158
Cdd:PRK00892 110 DPSAKIGEGVSIGPNAVIGAGVVIGDGVVIgAGAVIGDGVKIGAD-----CRLHANVTIYHAVRI 169
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 92-196 1.65e-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: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902  92 IYRGPEVSLGHGSILEENVLLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSllcDNAEVKE 171
Cdd:cd00710   65 VWIGKNVSIAHGAIVHGPAYIGDNCFIGFRSVVFNAKVGDNCVIGHNAVVDGVEIPPGRYVPAGAVITSQ---TQADALP 141

                         90       100
                 ....*....|....*....|....*
gi 767927902 172 RVTLKPRsvLTSQVVVGPNITLPEG 196
Cdd:cd00710  142 DVTDSAR--EFNEKVITVNNELAEG 164
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
104-199 1.88e-07

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 50.25  E-value: 1.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902 104 SILEENVLLGSGTVIGSNCFI--TNSVIGPGCHIGDNVVLdqtYLWQGVRVAAGAQIHQ--SLLCDN---------AEVK 170
Cdd:COG0110    3 LLLLFGARIGDGVVIGPGVRIygGNITIGDNVYIGPGVTI---DDPGGITIGDNVLIGPgvTILTGNhpiddpatfPLRT 79

                         90       100
                 ....*....|....*....|....*....
gi 767927902 171 ERVTLKPRSVLTSQVVVGPNITLPEGSVI 199
Cdd:COG0110   80 GPVTIGDDVWIGAGATILPGVTIGDGAVV 108
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 90-141 3.75e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 52.06  E-value: 3.75e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767927902  90 HNIYRGPEVSLGHGSILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNVVL 141
Cdd:PRK00892 123 PNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLhANVTIYHAVRIGNRVII 175
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 91-200 6.35e-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: 49.71  E-value: 6.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902  91 NIYRGPEVSLGHGSILEENVLLGSGTVIGSNCFI-TNSVIG---------PGCH----------IGDNV----------- 139
Cdd:cd03352   31 GVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIhSGAVIGsdgfgfapdGGGWvkipqlggviIGDDVeiganttidrg 110

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767927902 140 VLDQTYLWQGVR------VAAGAQI--HqSLLCDNAEVKERVTLKPRSVLTSQVVVGPNITLPEGSVIS 200
Cdd:cd03352  111 ALGDTVIGDGTKidnlvqIAHNVRIgeN-CLIAAQVGIAGSTTIGDNVIIGGQVGIAGHLTIGDGVVIG 178
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 118-199 1.11e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 50.64  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902 118 IGSNCFITNSVIGPGCHIGDNVvlDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVTLKprsvltsQVVVGPNITLPEGS 197
Cdd:PRK05293 285 IAENAKVKNSLVVEGCVVYGTV--EHSVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIE-------RAIIGENAVIGDGV 355


                 ..
gi 767927902 198 VI 199
Cdd:PRK05293 356 II 357
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 94-169 2.89e-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: 47.20  E-value: 2.89e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767927902  94 RGPEVSLGHGSILEENVLLGSGTVIGSNCfitnsVIGPGCHIGDNVVLDqtylwQGVRVAAGAQIHQSLLCDNAEV 169
Cdd:cd05636   14 IKGPVWIGEGAIVRSGAYIEGPVIIGKGC-----EIGPNAYIRGYTVLG-----DGCVVGNSVEVKNSIIMDGTKV 79
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 91-188 3.38e-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: 3.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902  91 NIYRGPEVSLGHGSILEENVLLGSGTVIGSNCFIT------NSVIGPGCHIGDNVVLDqtylwqgvrvaagaqihqsllc 164
Cdd:PRK14354 259 STYIDADVEIGSDTVIEPGVVIKGNTVIGEDCVIGpgsrivDSTIGDGVTITNSVIEE---------------------- 316

                         90       100       110
                 ....*....|....*....|....*....|
gi 767927902 165 dnAEVKERVT------LKPRSVLTSQVVVG 188
Cdd:PRK14354 317 --SKVGDNVTvgpfahLRPGSVIGEEVKIG 344
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 90-142 3.55e-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: 44.93  E-value: 3.55e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767927902  90 HNIYRGPEVSLGHGSILEENVLLG--------SGTVIGSNCFI-TNSVIGPGCHIGDNVVLD 142
Cdd:cd00208   11 PKAVIRGPVVIGDNVNIGPGAVIGaatgpnekNPTIIGDNVEIgANAVIHGGVKIGDNAVIG 72
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
88-156 5.66e-06

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 46.02  E-value: 5.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902  88 SRHNIYRGPEVSLGHGSIL----------EENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNVVldqtylwqgvrVAAGA 156
Cdd:COG0110   44 DPGGITIGDNVLIGPGVTIltgnhpiddpATFPLRTGPVTIGDDVWIgAGATILPGVTIGDGAV-----------VGAGS 112
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
115-141 5.98e-06

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 42.71  E-value: 5.98e-06
                          10        20
                  ....*....|....*....|....*...
gi 767927902  115 GTVIGSNCFI-TNSVIGPGCHIGDNVVL 141
Cdd:pfam00132   1 GTVIGDNVLIgPNAVIGGGVIIGDNVII 28
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 95-158 1.41e-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: 1.41e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767927902  95 GPEVSLGHGSILEENVLLGSGTVIGSNCFIT-NSVIGPGCHIGDNVVL----------DQTYLWQGVRVAAGAQI 158
Cdd:cd03358    2 GDNCIIGTNVFIENDVKIGDNVKIQSNVSIYeGVTIEDDVFIGPNVVFtndlyprskiYRKWELKGTTVKRGASI 76
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 115-156 1.55e-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: 43.98  E-value: 1.55e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 767927902 115 GTVIGSNCFI-TNSVIGPGCHIGDNVVldqtylwqgvrVAAGA 156
Cdd:cd04647   58 PIVIGDDVWIgANVVILPGVTIGDGAV-----------VGAGS 89
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 109-199 3.54e-05

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


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 42.83  E-value: 3.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902 109 NVLLGSGTVIGSNCFITNS---VIGPGCHIGDNVVLdqtylwqgvrVAAGAQIH-QSLLCDNAEVKERVTLKPRSVLTSQ 184
Cdd:cd04647    1 NISIGDNVYIGPGCVISAGggiTIGDNVLIGPNVTI----------YDHNHDIDdPERPIEQGVTSAPIVIGDDVWIGAN 70

                         90
                 ....*....|....*
gi 767927902 185 VVVGPNITLPEGSVI 199
Cdd:cd04647   71 VVILPGVTIGDGAVV 85
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 95-141 4.24e-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: 45.01  E-value: 4.24e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 767927902  95 GPEVSLGHGSILEENVLLGSGTVIGSNCFIT-NSVIGPGCHIGDNVVL 141
Cdd:COG1043   17 GENVEIGPFCVIGPDVEIGDGTVIGSHVVIEgPTTIGKNNRIFPFASI 64
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 65-158 4.89e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 45.59  E-value: 4.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902  65 RRW----VYPLTPEANFTDSTTQSCtHSRHNIyrgpeVSLG---HGSILEENVLlGSGTVIGSNCFITNSVIGPGCHIGD 137
Cdd:PRK00844 287 REWpiytSSPNLPPAKFVDGGGRVG-SAQDSL-----VSAGsiiSGATVRNSVL-SPNVVVESGAEVEDSVLMDGVRIGR 359

                         90       100
                 ....*....|....*....|.
gi 767927902 138 NVVLDQTYLWQGVRVAAGAQI 158
Cdd:PRK00844 360 GAVVRRAILDKNVVVPPGATI 380
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 108-174 7.26e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 44.82  E-value: 7.26e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767927902 108 ENVLLGSGTVIgSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVT 174
Cdd:PRK00844 314 QDSLVSAGSII-SGATVRNSVLSPNVVVESGAEVEDSVLMDGVRIGRGAVVRRAILDKNVVVPPGAT 379
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 98-199 8.07e-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: 43.63  E-value: 8.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902  98 VSLGHGS-ILEENVLLGSGTVIGSNCfitnsVIGPGCHIGDNVVldqtyLWQGVRVAagaqiHQSLLCDNaevkerVTLK 176
Cdd:cd03360   84 ATLIHPSaVVSPSAVIGEGCVIMAGA-----VINPDARIGDNVI-----INTGAVIG-----HDCVIGDF------VHIA 142

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767927902 177 PRSVLTSQVVVG------------PNITLPEGSVI 199
Cdd:cd03360  143 PGVVLSGGVTIGegafigagatiiQGVTIGAGAII 177
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 126-199 8.74e-05

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 43.55  E-value: 8.74e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767927902 126 NSVIGPGCHIGDNVVLDqtylwQGVRVAAGAQIH-QSLLCDNAEVKERVTLKPRSVLTSQVVVGPNITLPEGSVI 199
Cdd:cd03352    1 SAKIGENVSIGPNAVIG-----EGVVIGDGVVIGpGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 97-199 1.17e-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: 42.40  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902  97 EVSLGHGSILEENVLL----GSGTVIGSNCFITNSVIGPGCHIGDNVVldqtylwqgvrVAAGAQIhqsllCDNAEVKER 172
Cdd:cd04645   38 PIRIGERTNIQDGSVLhvdpGYPTIIGDNVTVGHGAVLHGCTIGDNCL-----------IGMGAII-----LDGAVIGKG 101

                         90       100
                 ....*....|....*....|....*..
gi 767927902 173 VTLKPRSVLTsqvvvgPNITLPEGSVI 199
Cdd:cd04645  102 SIVAAGSLVP------PGKVIPPGSLV 122
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
95-141 1.63e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 43.16  E-value: 1.63e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 767927902  95 GPEVSLGHGSILEENVLLGSGTVIGSNCFIT-NSVIGPGCHIGDNVVL 141
Cdd:PRK05289  18 GENVEIGPFCVIGPNVVIGDGTVIGSHVVIDgHTTIGKNNRIFPFASI 65
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 95-141 1.94e-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: 42.80  E-value: 1.94e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 767927902  95 GPEVSLGHGSILEENVLLGSGTVIGSNCFIT-NSVIGPGCHIGDNVVL 141
Cdd:cd03351   15 GENVEIGPFCVIGPNVEIGDGTVIGSHVVIDgPTTIGKNNRIFPFASI 62
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 92-199 3.25e-04

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


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 41.03  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902  92 IYRGPEVSLGHGSILEENVLLGSGTVIGSNCFITNSVIGPGCHI------GDNVvldqtyLWQGVRVAAGAQIhQSLLCD 165
Cdd:cd05636   36 VIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKVphlnyvGDSV------LGENVNLGAGTIT-ANLRFD 108

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 767927902 166 NAEVKerVTLKPRSVLTSQ----------VVVGPNITLPEGSVI 199
Cdd:cd05636  109 DKPVK--VRLKGERVDTGRrklgaiigdgVKTGINVSLNPGVKI 150
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 95-140 3.26e-04

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 41.17  E-value: 3.26e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767927902  95 GPEVSLGHGSIL-----EENVLLGSG------TVIGSNCFIT-NSVIGPGCHIGDNVV 140
Cdd:COG0663   75 GDDVTIGHGAILhgctiGDNVLIGMGaivldgAVIGDGSIVGaGALVTEGKVVPPGSL 132
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 104-199 4.51e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 42.55  E-value: 4.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902 104 SILEENVLLGSGTVIgsncfiTNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIhqsllcdnAEVKERVTlkprsvlts 183
Cdd:PRK05293 309 SVLFQGVQVGEGSVV------KDSVIMPGAKIGENVVIERAIIGENAVIGDGVII--------GGGKEVIT--------- 365

                         90
                 ....*....|....*.
gi 767927902 184 qvVVGPNITLPEGSVI 199
Cdd:PRK05293 366 --VIGENEVIGVGTVI 379
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 128-199 6.55e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 41.66  E-value: 6.55e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767927902 128 VIGPGCHIGDNVVLD-QTYLWQGVRVAAGAQIH-QSLLCDNAEVKERVTLKPRSVLTSQVVVGPNITLPEGSVI 199
Cdd:PRK00892 108 VIDPSAKIGEGVSIGpNAVIGAGVVIGDGVVIGaGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVI 181
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 94-158 7.52e-04

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: 7.52e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767927902  94 RGpevSLGHGS--------ILEENVLLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDqtylwqGVRVAAGAQI 158
Cdd:PRK09451 263 RG---TLTHGRdveidtnvIIEGNVTLGNRVKIGAGCVLKNCVIGDDCEISPYSVVE------DANLGAACTI 326
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
103-136 1.27e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.16  E-value: 1.27e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767927902  103 GSILEENVLLGSGTVIGSNCfitnsVIGPGCHIG 136
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGV-----IIGDNVIIG 29
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 93-141 2.46e-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: 2.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767927902  93 YRGPEVSL--GHGSILEENVLLGSG-------TVIGSNCFI-TNSVIGPGCHIGDNVVL 141
Cdd:cd03351   71 YKGEPTRLeiGDNNTIREFVTIHRGtaqgggvTRIGNNNLLmAYVHVAHDCVIGNNVIL 129
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
93-141 3.35e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 39.31  E-value: 3.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767927902  93 YRGPEVSL--GHGSILEENVLLGSGTV-------IGSNCFI-TNSVIGPGCHIGDNVVL 141
Cdd:PRK05289  74 YKGEPTRLviGDNNTIREFVTINRGTVqgggvtrIGDNNLLmAYVHVAHDCVVGNHVIL 132
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
103-160 3.66e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 38.93  E-value: 3.66e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767927902 103 GSILEENVLLGSGTVIGSNCfitnsVIGPGCHIGDNVVLDqtylwQGVRVAAGAQIHQ 160
Cdd:PRK05289  14 GAKIGENVEIGPFCVIGPNV-----VIGDGTVIGSHVVID-----GHTTIGKNNRIFP 61
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 117-199 3.97e-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: 3.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902 117 VIGSNCFI-TNSVIGPGCHIGDNVvldqtylwqgvRVAAGAQIHqSLLCDN----AEVKERVTLKPRSVLTSQVVVGPNI 191
Cdd:cd00208    2 FIGEGVKIhPKAVIRGPVVIGDNV-----------NIGPGAVIG-AATGPNeknpTIIGDNVEIGANAVIHGGVKIGDNA 69


                 ....*...
gi 767927902 192 TLPEGSVI 199
Cdd:cd00208   70 VIGAGAVV 77
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 109-156 4.21e-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: 4.21e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 767927902 109 NVLLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGA 156
Cdd:cd04652   33 NCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAGT 80
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 105-199 4.82e-03

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 37.70  E-value: 4.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902 105 ILEENVLLGSGTVI-GSNCFITnsvIGPGCHIGDNVVL--DQTY-LW--QGVRVAAGAQIH------------QSLLCDN 166
Cdd:COG0663   30 TIGEDVSVWPGAVLrGDVGPIR---IGEGSNIQDGVVLhvDPGYpLTigDDVTIGHGAILHgctigdnvligmGAIVLDG 106

                         90       100       110
                 ....*....|....*....|....*....|...
gi 767927902 167 AEVKERVTLKPRSvltsqvVVGPNITLPEGSVI 199
Cdd:COG0663  107 AVIGDGSIVGAGA------LVTEGKVVPPGSLV 133
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 104-160 6.69e-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: 38.08  E-value: 6.69e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767927902 104 SILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNVVLDqtylwQGVRVAAGAQIHQ 160
Cdd:COG1043    8 AIVDPGAKLGENVEIGPFCVIgPDVEIGDGTVIGSHVVIE-----GPTTIGKNNRIFP 60
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 118-188 6.90e-03

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


Pssm-ID: 100062 [Multi-domain]  Cd Length: 80  Bit Score: 35.59  E-value: 6.90e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767927902 118 IGSNCFI-TNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVTLKPRSVLTSQVVVG 188
Cdd:cd05824    8 IGKTAKIgPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLENVTVLGDDVTIK 79
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 104-160 7.85e-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: 38.18  E-value: 7.85e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767927902 104 SILEENVLLGSGTVIGSNCFIT-NSVIGPGCHIGDNVVLDqtylwQGVRVAAGAQIHQ 160
Cdd:cd03351    6 AIVDPGAKIGENVEIGPFCVIGpNVEIGDGTVIGSHVVID-----GPTTIGKNNRIFP 58
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 84-158 8.10e-03

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 38.37  E-value: 8.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902  84 SCTHSRhniyrgpEVSLGHGSILEENVLL------GSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTylwqgvrVAAGAQ 157
Cdd:PRK14360 256 SCTISE-------TVELGPDVIIEPQTHLrgntviGSGCRIGPGSLIENSQIGENVTVLYSVVSDSQ-------IGDGVK 321


                 .
gi 767927902 158 I 158
Cdd:PRK14360 322 I 322
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 104-193 8.88e-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: 35.30  E-value: 8.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927902 104 SILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNvvldqtylwQGVRVAAGAQIHqsllcDNAEVKERVTLKPRSVLT 182
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIgDNVNIGPGAVIGAA---------TGPNEKNPTIIG-----DNVEIGANAVIHGGVKIG 66

                         90
                 ....*....|.
gi 767927902 183 SQVVVGPNITL 193
Cdd:cd00208   67 DNAVIGAGAVV 77
 
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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