NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|398366139|ref|NP_010497|]
View 

Gcd6p [Saccharomyces cerevisiae S288c]

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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; ...
27-243 4.88e-103

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  Cd Length: 217  Bit Score: 316.86  E-value: 4.88e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  27 LQAVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIENSKWNLP-WSPFKIT 105
Cdd:cd04197    1 LQAVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKSKWSKPkSSLMIVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 106 TIMSPEARCTGDVMRDLDNRGIITGDFILVSGDVLTNIDFSKMLEFHKKMHLQDKDHISTMCLSKASTYPKTR-TIEPAA 184
Cdd:cd04197   81 IIMSEDCRSLGDALRDLDAKGLIRGDFILVSGDVVSNIDLKEILEEHKERRKKDKNAIMTMVLKEASPPHRTRrTGEEFV 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 398366139 185 FVLDKSTSRCIYYQDLPLPSSREKTsiQIDPELLDNVDEFVIRNDLIDCRIDICTSHVP 243
Cdd:cd04197  161 IAVDPKTSRLLHYEELPGSKYRSIT--DLPSELLGSNSEVEIRHDLLDCHIDICSPDVL 217
W2_eIF2B_epsilon cd11558
C-terminal W2 domain of eukaryotic translation initiation factor 2B epsilon; eIF2B is a ...
550-704 1.66e-50

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: 173.98  E-value: 1.66e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 550 IATVERAMENNHDLDTALLELNTLRMSMNVTYHEVRIATITALLRRVYHFIATQTLGPKDAVVKVFNQWGLLFKRQAFDE 629
Cdd:cd11558   11 VESLERALEENHSVDNAILEINSLRMAYNVTDHDVRRAVVKALLELILEVSSTSTAELLEALKKLLSKWGPLLENYVKSQ 90
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366139 630 EEYIDLMNIIMEKIVEqsFDKPDLILFSALVSLYDNDIIEEDVIYKWWDNVST--DPRYDEVKKLTVKWVEWLQNAD 704
Cdd:cd11558   91 DDQVELLLALEEFCLE--SEEGGPLFAKLLHALYDLDILEEEAILEWWEEPDAgaDEEMKKVRELVKKFIEWLEEAE 165
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
344-422 5.85e-37

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: 133.47  E-value: 5.85e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366139 344 AIGSGTKIGEGTKIENSVIGRNCQIGENIRIKNSFIWDDCIIGNNSIIDHSLIASNATLGSNVRLNDGCIIGFNVKIDD 422
Cdd:cd05787    1 VIGRGTSIGEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPGSLISFGVVIGD 79
GCD1 COG1208
Nucleoside-diphosphate-sugar pyrophosphorylase involved in lipopolysaccharide biosynthesis ...
28-420 1.04e-66

Nucleoside-diphosphate-sugar pyrophosphorylase involved in lipopolysaccharide biosynthesis/translation initiation factor 2B, gamma/epsilon subunits (eIF-2Bgamma/eIF-2Bepsilon) [Cell envelope biogenesis, outer membrane / Translation, ribosomal structure and biogenesis]


:

Pssm-ID: 224129 [Multi-domain]  Cd Length: 358  Bit Score: 225.68  E-value: 1.04e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  28 QAVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIENSKwnlpWSPFKITTI 107
Cdd:COG1208    3 KAVILAGGYGTRLRPLTDDRPKPLLPIAGKPLIEYVLEALAAAGVEEIVLVVGYLGEQIEEYFGDGE----GLGVRITYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 108 MSPEARCTGDVMRDLDNRgIITGDFILVSGDVLTNIDFSKMLEFHKKmHLQDKDHISTMCLSKasTYPKTRTIEPAAFVL 187
Cdd:COG1208   79 VEKEPLGTAGALKNALDL-LGGDDFLVLNGDVLTDLDLSELLEFHKK-KGALATIALTRVLDP--SEFGVVETDDGDGRV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 188 DKSTSRCIYYQdlPLPSSREKTSIQIDPELLDNVdEFVIRNDLIDcridictSHVPLIFQENFDYQSLRTDfvkgvissd 267
Cdd:COG1208  155 VEFREKPGPEE--PPSNLINAGIYIFDPEVFDYI-EKGERFDFEE-------ELLPALAAKGEDVYGYVFE--------- 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 268 ilgKHIYAYLTDE-YAVRVESWQTYDTISQdfLGRWCYPLVLDsniqddqtysyesRHIYKEKDVVLAQSCKIGKCTAIG 346
Cdd:COG1208  216 ---GYWLDIGTPEdLLEANELLLRGDGKSP--LGPIEEPVVII-------------RSAYIIGPVVIGPGAKIGPGALIG 277
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366139 347 SGTkigegtkiensVIGRNCQIGENIRIKNSFIWDDCIIGNNSIIDHSLIASNATLGSNVRLNDgCIIGFNVKI 420
Cdd:COG1208  278 PYT-----------VIGEGVTIGNGVEIKNSIIMDNVVIGHGSYIGDSIIGENCKIGASLIIGD-VVIGINSEI 339
 
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; ...
27-243 4.88e-103

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  Cd Length: 217  Bit Score: 316.86  E-value: 4.88e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  27 LQAVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIENSKWNLP-WSPFKIT 105
Cdd:cd04197    1 LQAVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKSKWSKPkSSLMIVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 106 TIMSPEARCTGDVMRDLDNRGIITGDFILVSGDVLTNIDFSKMLEFHKKMHLQDKDHISTMCLSKASTYPKTR-TIEPAA 184
Cdd:cd04197   81 IIMSEDCRSLGDALRDLDAKGLIRGDFILVSGDVVSNIDLKEILEEHKERRKKDKNAIMTMVLKEASPPHRTRrTGEEFV 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 398366139 185 FVLDKSTSRCIYYQDLPLPSSREKTsiQIDPELLDNVDEFVIRNDLIDCRIDICTSHVP 243
Cdd:cd04197  161 IAVDPKTSRLLHYEELPGSKYRSIT--DLPSELLGSNSEVEIRHDLLDCHIDICSPDVL 217
W2_eIF2B_epsilon cd11558
C-terminal W2 domain of eukaryotic translation initiation factor 2B epsilon; eIF2B is a ...
550-704 1.66e-50

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: 173.98  E-value: 1.66e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 550 IATVERAMENNHDLDTALLELNTLRMSMNVTYHEVRIATITALLRRVYHFIATQTLGPKDAVVKVFNQWGLLFKRQAFDE 629
Cdd:cd11558   11 VESLERALEENHSVDNAILEINSLRMAYNVTDHDVRRAVVKALLELILEVSSTSTAELLEALKKLLSKWGPLLENYVKSQ 90
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366139 630 EEYIDLMNIIMEKIVEqsFDKPDLILFSALVSLYDNDIIEEDVIYKWWDNVST--DPRYDEVKKLTVKWVEWLQNAD 704
Cdd:cd11558   91 DDQVELLLALEEFCLE--SEEGGPLFAKLLHALYDLDILEEEAILEWWEEPDAgaDEEMKKVRELVKKFIEWLEEAE 165
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
344-422 5.85e-37

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: 133.47  E-value: 5.85e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366139 344 AIGSGTKIGEGTKIENSVIGRNCQIGENIRIKNSFIWDDCIIGNNSIIDHSLIASNATLGSNVRLNDGCIIGFNVKIDD 422
Cdd:cd05787    1 VIGRGTSIGEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPGSLISFGVVIGD 79
eIF5C smart00515
Domain at the C-termini of GCD6, eIF-2B epsilon, eIF-4 gamma and eIF-5;
619-703 6.22e-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: 105.45  E-value: 6.22e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139   619 GLLFKRQAFDEEEYIDLMNIIMEKIVEQsfDKPDLILFSALVSLYDNDIIEEDVIYKWWDNVSTDPRYDEVKKLTVKWVE 698
Cdd:smart00515   1 GPLLKFLAKDEEEQLELLYAIEEFCVEL--EKLGKLLPKILKSLYDADILEEEAILKWYEKAVSAEGKKKVRKNAKPFVT 78

                   ....*
gi 398366139   699 WLQNA 703
Cdd:smart00515  79 WLQEA 83
W2 pfam02020
eIF4-gamma/eIF5/eIF2-epsilon; This domain of unknown function is found at the C-terminus of ...
629-703 6.03e-15

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


Pssm-ID: 251043  Cd Length: 77  Bit Score: 71.13  E-value: 6.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  629 EEEYIDLMNIIMEKIVEqsfDKPDLI--LFSALVSLYDNDIIEEDVIYKWWDNVStdPRYDE-----VKKLTVKWVEWLQ 701
Cdd:pfam02020   1 EDAQKDLLGALERFCGK---ENPELIklLPKILKLLYDLDILEEEAILKWYEKVS--KYVAGkgsakVRKQAKPFVTWLE 75

                  ..
gi 398366139  702 NA 703
Cdd:pfam02020  76 EA 77
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
29-154 5.30e-09

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 249894  Cd Length: 247  Bit Score: 56.06  E-value: 5.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139   29 AVVLTDSYETRFMPLTAVKPRCLLPLAN-VPLIEYTLEFLAKAGVHEVFLICSS-HANQINDYI-ENSKWNLpwspfKIT 105
Cdd:pfam00483   2 AIILAGGSGTRLWPLTRTLAKPLVPVLDkYPMIQYTLSRLMNAGIREPIVICTQeHRFLVAEQLgDGSKFGL-----QVT 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 398366139  106 TIMSPEARCTGDVMRdlDNRGIITGD---FILV-SGDVLTNIDFSKMLEFHKK 154
Cdd:pfam00483  77 YALQPEPRGTAPAVA--LAADFLGDDdpeLVLVlGGDHIYRMDFEEAVQKARA 127
COG1213 COG1213
Predicted sugar nucleotidyltransferases [Cell envelope biogenesis, outer membrane]
29-149 3.98e-08

Predicted sugar nucleotidyltransferases [Cell envelope biogenesis, outer membrane]


Pssm-ID: 224134  Cd Length: 239  Bit Score: 53.49  E-value: 3.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  29 AVVLTDSYETRFMPltaVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIENSKwnlpwsPFKITTIM 108
Cdd:COG1213    6 AVILAAGFGSRLGP---DIPKALVEVGGREIIYRTIENLAKAGITEFVVVTNGYRADLVEEFLKKY------PFNAKIVI 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 398366139 109 SPEARCTGDVMRDLDNRGIITGDFILVSGDVLTNIDFSKML 149
Cdd:COG1213   77 NSDYEKTNTGYSLLLAKDYMDGRFILVMSDHVYEPSILERL 117
galU TIGR01099
UTP-glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ...
29-93 2.94e-07

UTP-glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar genes galU and galF [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides].


Pssm-ID: 233272  Cd Length: 260  Bit Score: 51.15  E-value: 2.94e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366139   29 AVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIENS 93
Cdd:TIGR01099   3 AVIPAAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVEAGIEDILIVTGRGKRSIEDHFDTS 67
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase subunit GalU; Provisional
28-93 8.72e-06

UTP--glucose-1-phosphate uridylyltransferase subunit GalU; Provisional


Pssm-ID: 184021  Cd Length: 302  Bit Score: 46.82  E-value: 8.72e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366139  28 QAVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIENS 93
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTS 75
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
348-393 9.01e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 249615  Cd Length: 36  Bit Score: 40.83  E-value: 9.01e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 398366139  348 GTKIGEGTKIE-NSVIGRNCQIGENiriknsfiwddCIIGNNSIIDH 393
Cdd:pfam00132   1 GTVIGENVLIGpNVVIGGGVIIGDN-----------VIIGAGVVIGG 36
GCD1 COG1208
Nucleoside-diphosphate-sugar pyrophosphorylase involved in lipopolysaccharide biosynthesis ...
28-420 1.04e-66

Nucleoside-diphosphate-sugar pyrophosphorylase involved in lipopolysaccharide biosynthesis/translation initiation factor 2B, gamma/epsilon subunits (eIF-2Bgamma/eIF-2Bepsilon) [Cell envelope biogenesis, outer membrane / Translation, ribosomal structure and biogenesis]


Pssm-ID: 224129 [Multi-domain]  Cd Length: 358  Bit Score: 225.68  E-value: 1.04e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  28 QAVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIENSKwnlpWSPFKITTI 107
Cdd:COG1208    3 KAVILAGGYGTRLRPLTDDRPKPLLPIAGKPLIEYVLEALAAAGVEEIVLVVGYLGEQIEEYFGDGE----GLGVRITYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 108 MSPEARCTGDVMRDLDNRgIITGDFILVSGDVLTNIDFSKMLEFHKKmHLQDKDHISTMCLSKasTYPKTRTIEPAAFVL 187
Cdd:COG1208   79 VEKEPLGTAGALKNALDL-LGGDDFLVLNGDVLTDLDLSELLEFHKK-KGALATIALTRVLDP--SEFGVVETDDGDGRV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 188 DKSTSRCIYYQdlPLPSSREKTSIQIDPELLDNVdEFVIRNDLIDcridictSHVPLIFQENFDYQSLRTDfvkgvissd 267
Cdd:COG1208  155 VEFREKPGPEE--PPSNLINAGIYIFDPEVFDYI-EKGERFDFEE-------ELLPALAAKGEDVYGYVFE--------- 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 268 ilgKHIYAYLTDE-YAVRVESWQTYDTISQdfLGRWCYPLVLDsniqddqtysyesRHIYKEKDVVLAQSCKIGKCTAIG 346
Cdd:COG1208  216 ---GYWLDIGTPEdLLEANELLLRGDGKSP--LGPIEEPVVII-------------RSAYIIGPVVIGPGAKIGPGALIG 277
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366139 347 SGTkigegtkiensVIGRNCQIGENIRIKNSFIWDDCIIGNNSIIDHSLIASNATLGSNVRLNDgCIIGFNVKI 420
Cdd:COG1208  278 PYT-----------VIGEGVTIGNGVEIKNSIIMDNVVIGHGSYIGDSIIGENCKIGASLIIGD-VVIGINSEI 339
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
27-449 2.23e-20

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.


Pssm-ID: 234433 [Multi-domain]  Cd Length: 393  Bit Score: 92.66  E-value: 2.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139   27 LQAVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIEN-SKWnlpwsPFKIT 105
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDgSRG-----GVPIE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  106 TIMSPEARCTGDVMRDLdnRGIITGDFILVSGDVLTnidfskmlefhkkmhlqDKDHISTMCLSKASTYPKTRTIEPAAF 185
Cdd:TIGR03992  76 YVVQEEQLGTADALGSA--KEYVDDEFLVLNGDVLL-----------------DSDLLERLIRAEAPAIAVVEVDDPSDY 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  186 ---VLDKSTSRCIYYQDLPLPSSREKTSIQI-DPELLDNVDEfvirndlidcridictshVPLifqenfdyqSLR----- 256
Cdd:TIGR03992 137 gvvETDGGRVTGIVEKPENPPSNLINAGIYLfSPEIFELLEK------------------TKL---------SPRgeyel 189
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  257 TDFVKGVIssdilgkhiyayltDEYAVRVESwqtYDTISQDfLGR-WcypLVLDSNiqddqtySYESRHIYKEKDVVLAQ 335
Cdd:TIGR03992 190 TDALQLLI--------------DEGKVKAVE---LDGFWLD-VGRpW---DLLDAN-------EALLDNLEPRIEGTVEE 241
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  336 SCKIGKCTAIGSGTKIGEGTKIENSV-IGRNCQIGENIRIK-NSFIWDDCIIGN-----NSII------DH------SLI 396
Cdd:TIGR03992 242 NVTIKGPVVIGEGAVIRSGTYIEGPVyIGKNCDIGPNAYIRpYTVIGNNVHIGNaveikNSIImegtkiPHlsyvgdSVI 321
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366139  397 ASNATLG-----SNVRLND-------------------GCIIGFNVKIDDNMDLDRNTKISasplknAGSRMYDNES 449
Cdd:TIGR03992 322 GENCNFGagtkvANLRHDDkpvkvtvkgkrvdtgrrklGAIVGDGVKTGINVSINPGVKIG------SGARIYPGEV 392
glmU PRK14354
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
343-433 1.65e-12

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 68.70  E-value: 1.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 343 TAIGSGTKIGEGTKIE-------NSVIGRNCQIGENIRIKNSFIWDDCIIgNNSIIDHSLIASNATLGSNVRLNDGCIIG 415
Cdd:PRK14354 260 TYIDADVEIGSDTVIEpgvvikgNTVIGEDCVIGPGSRIVDSTIGDGVTI-TNSVIEESKVGDNVTVGPFAHLRPGSVIG 338
                         90       100
                 ....*....|....*....|...
gi 398366139 416 FNVKIDD-----NMDLDRNTKIS 433
Cdd:PRK14354 339 EEVKIGNfveikKSTIGEGTKVS 361
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl]
375-432 1.88e-05

UDP-3-O-[3-hydroxymyristoyl]


Pssm-ID: 223974 [Multi-domain]  Cd Length: 338  Bit Score: 46.14  E-value: 1.88e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 398366139 375 KNSFIWDDCIIGNNSII-DHSLIASNATLGSNVRLNDGCIIGFNVKIDDNMDLDRNTKI 432
Cdd:COG1044  104 PTAVIDPTATIGKNVSIgPNVVIGAGVVIGENVVIGAGAVIGENVKIGDGTVIHPNVTI 162
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
378-434 1.67e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 42.82  E-value: 1.67e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 398366139 378 FIWDDCIIGNNSIIDHsliasNATLGSNVRLNDGCIIGFNVKIDDNMDLDRNTKISA 434
Cdd:PRK00892 108 VIDPSAKIGEGVSIGP-----NAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHA 159
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
351-377 8.89e-03

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 37.53  E-value: 8.89e-03
                         10        20
                 ....*....|....*....|....*..
gi 398366139 351 IGEGTKIENSVIGRNCQIGENIRIKNS 377
Cdd:PLN02241 376 IGENTKIRNAIIDKNARIGKNVVIINK 402
 
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; ...
27-243 4.88e-103

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  Cd Length: 217  Bit Score: 316.86  E-value: 4.88e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  27 LQAVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIENSKWNLP-WSPFKIT 105
Cdd:cd04197    1 LQAVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKSKWSKPkSSLMIVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 106 TIMSPEARCTGDVMRDLDNRGIITGDFILVSGDVLTNIDFSKMLEFHKKMHLQDKDHISTMCLSKASTYPKTR-TIEPAA 184
Cdd:cd04197   81 IIMSEDCRSLGDALRDLDAKGLIRGDFILVSGDVVSNIDLKEILEEHKERRKKDKNAIMTMVLKEASPPHRTRrTGEEFV 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 398366139 185 FVLDKSTSRCIYYQDLPLPSSREKTsiQIDPELLDNVDEFVIRNDLIDCRIDICTSHVP 243
Cdd:cd04197  161 IAVDPKTSRLLHYEELPGSKYRSIT--DLPSELLGSNSEVEIRHDLLDCHIDICSPDVL 217
W2_eIF2B_epsilon cd11558
C-terminal W2 domain of eukaryotic translation initiation factor 2B epsilon; eIF2B is a ...
550-704 1.66e-50

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: 173.98  E-value: 1.66e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 550 IATVERAMENNHDLDTALLELNTLRMSMNVTYHEVRIATITALLRRVYHFIATQTLGPKDAVVKVFNQWGLLFKRQAFDE 629
Cdd:cd11558   11 VESLERALEENHSVDNAILEINSLRMAYNVTDHDVRRAVVKALLELILEVSSTSTAELLEALKKLLSKWGPLLENYVKSQ 90
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366139 630 EEYIDLMNIIMEKIVEqsFDKPDLILFSALVSLYDNDIIEEDVIYKWWDNVST--DPRYDEVKKLTVKWVEWLQNAD 704
Cdd:cd11558   91 DDQVELLLALEEFCLE--SEEGGPLFAKLLHALYDLDILEEEAILEWWEEPDAgaDEEMKKVRELVKKFIEWLEEAE 165
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
344-422 5.85e-37

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: 133.47  E-value: 5.85e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366139 344 AIGSGTKIGEGTKIENSVIGRNCQIGENIRIKNSFIWDDCIIGNNSIIDHSLIASNATLGSNVRLNDGCIIGFNVKIDD 422
Cdd:cd05787    1 VIGRGTSIGEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPGSLISFGVVIGD 79
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
27-243 1.22e-73

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  Cd Length: 216  Bit Score: 239.46  E-value: 1.22e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  27 LQAVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIENSKWNLPWSPFKITT 106
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKWSSLSSKMIVDV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 107 IMSPEARCTGDVMRDLDNRGIITGDFILVSGDVLTNIDFSKMLEFHKKMHlqdKDHISTMCLSKA----STYPKTRTIEP 182
Cdd:cd02507   81 ITSDLCESAGDALRLRDIRGLIRSDFLLLSCDLVSNIPLSELLEERRKKD---KNAIATLTVLLAsppvSTEQSKKTEEE 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366139 183 AAFVLDKSTSR--CIYYQDLPLpssrEKTSIQIDPELLDNVDEFVIRNDLIDCRIDICTSHVP 243
Cdd:cd02507  158 DVIAVDSKTQRllLLHYEEDLD----EDLELIIRKSLLSKHPNVTIRTDLLDCHIYICSPDVL 216
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
29-168 3.56e-27

NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.


Pssm-ID: 133024  Cd Length: 217  Bit Score: 110.36  E-value: 3.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  29 AVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIEN-SKWNLpwspfKITTI 107
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDgSKFGV-----NIEYV 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366139 108 MSPEARCTGDVMRDLDNRgIITGDFILVSGDVLTNIDFSKMLEFHKKmhlqdKDHISTMCL 168
Cdd:cd04181   76 VQEEPLGTAGAVRNAEDF-LGDDDFLVVNGDVLTDLDLSELLRFHRE-----KGADATIAV 130
eIF5C smart00515
Domain at the C-termini of GCD6, eIF-2B epsilon, eIF-4 gamma and eIF-5;
619-703 6.22e-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: 105.45  E-value: 6.22e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139   619 GLLFKRQAFDEEEYIDLMNIIMEKIVEQsfDKPDLILFSALVSLYDNDIIEEDVIYKWWDNVSTDPRYDEVKKLTVKWVE 698
Cdd:smart00515   1 GPLLKFLAKDEEEQLELLYAIEEFCVEL--EKLGKLLPKILKSLYDADILEEEAILKWYEKAVSAEGKKKVRKNAKPFVT 78

                   ....*
gi 398366139   699 WLQNA 703
Cdd:smart00515  79 WLQEA 83
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
345-422 1.79e-25

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: 101.16  E-value: 1.79e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366139 345 IGSGTKIGEGTKIENSVIGRNCQIGENIRIKNSFIWDDCIIGNNSIIDHSLIASNATLGSNVRLNDGCIIGFNVKIDD 422
Cdd:cd03356    2 IGESTVIGENAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNLCIIGDDVVVED 79
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
27-193 1.26e-23

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  Cd Length: 214  Bit Score: 100.04  E-value: 1.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  27 LQAVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICS-SHANQINDYIENSKWNLPWSPFKIt 105
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPeEEQAEISTYLRSFPLNLKQKLDEV- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 106 TIMSPEARCTGDVMRDLDNRgiITGDFILVSGDVLTNIDFSKMLEFHKKmhlqdKDHISTMCL--------SKASTYPKT 177
Cdd:cd04198   80 TIVLDEDMGTADSLRHIRKK--IKKDFLVLSCDLITDLPLIELVDLHRS-----HDASLTVLLypppvsseQKGGKGKSK 152
                        170
                 ....*....|....*.
gi 398366139 178 RTIEPAAFVLDKSTSR 193
Cdd:cd04198  153 KADERDVIGLDEKTQR 168
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
345-423 5.11e-17

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: 77.23  E-value: 5.11e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366139 345 IGSGTKIGEGTKIENSVIGRNCQIGENIRIKNSFIWDDCIIGNNSIIDHSLIASNATLGSNVRLNDgCIIGFNVKIDDN 423
Cdd:cd04652    2 VGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKD-CLVGSGYRVEAG 79
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
38-167 5.51e-16

NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133048  Cd Length: 220  Bit Score: 77.17  E-value: 5.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  38 TRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIEN-SKWNLpwspfKITTIMSPEARCTG 116
Cdd:cd06426   10 TRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDgSKFGV-----NISYVREDKPLGTA 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 398366139 117 DVMRDLDNRgiITGDFILVSGDVLTNIDFSKMLEFHKKmhlqdKDHISTMC 167
Cdd:cd06426   85 GALSLLPEK--PTDPFLVMNGDILTNLNYEHLLDFHKE-----NNADATVC 128
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
29-152 7.32e-16

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  Cd Length: 236  Bit Score: 76.84  E-value: 7.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  29 AVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYI-ENSKWNLpwspfKITTI 107
Cdd:cd04189    3 GLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALgDGSRFGV-----RITYI 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 398366139 108 MSPEARCTGD-VMRDLDNRGiiTGDFILVSGDVLTNIDFSKMLEFH 152
Cdd:cd04189   78 LQEEPLGLAHaVLAARDFLG--DEPFVVYLGDNLIQEGISPLVRDF 121
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
38-223 2.45e-15

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  Cd Length: 221  Bit Score: 75.30  E-value: 2.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  38 TRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIENSKWNLPwspfkITTIMSPEARctgd 117
Cdd:cd06422   11 TRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDSRFGLR-----ITISDEPDEL---- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 118 vmrdLDNRGII--------TGDFILVSGDVLTNIDFSKMLEfhkkmHLQDKDHISTMCLskastyPKTRTIE---PAAFV 186
Cdd:cd06422   82 ----LETGGGIkkalpllgDEPFLVVNGDILWDGDLAPLLL-----LHAWRMDALLLLL------PLVRNPGhngVGDFS 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 398366139 187 LD----------KSTSRCIYyqdlplpssrekTSIQI-DPELLDNVDE 223
Cdd:cd06422  147 LDadgrlrrgggGAVAPFTF------------TGIQIlSPELFAGIPP 182
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
330-432 3.80e-15

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: 74.37  E-value: 3.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 330 DVVLAQSCKIGKCTAIGSGTKIGEGTKIE-NSVIGRNCQIGENIRIK-NSFIWDDCIIGNNSIIDhsliaSNATLGS--- 404
Cdd:cd03352    1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGpGVVIGDGVVIGDDCVIHpNVTIYEGCIIGDRVIIH-----SGAVIGSdgf 75
                         90       100       110
                 ....*....|....*....|....*....|...
gi 398366139 405 -NVRLNDGCI----IGfNVKIDDNMDLDRNTKI 432
Cdd:cd03352   76 gFAPDGGGWVkipqLG-GVIIGDDVEIGANTTI 107
W2 pfam02020
eIF4-gamma/eIF5/eIF2-epsilon; This domain of unknown function is found at the C-terminus of ...
629-703 6.03e-15

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


Pssm-ID: 251043  Cd Length: 77  Bit Score: 71.13  E-value: 6.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  629 EEEYIDLMNIIMEKIVEqsfDKPDLI--LFSALVSLYDNDIIEEDVIYKWWDNVStdPRYDE-----VKKLTVKWVEWLQ 701
Cdd:pfam02020   1 EDAQKDLLGALERFCGK---ENPELIklLPKILKLLYDLDILEEEAILKWYEKVS--KYVAGkgsakVRKQAKPFVTWLE 75

                  ..
gi 398366139  702 NA 703
Cdd:pfam02020  76 EA 77
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
361-433 7.78e-15

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: 70.73  E-value: 7.78e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366139 361 VIGRNCQIGENIRIKNSFIWDDCIIGNNSIIDHSLIASNATLGSNVRLNDGcIIGFNVKIDDNMDLDRNTKIS 433
Cdd:cd03356    1 LIGESTVIGENAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDS-IIGDNAVIGENVRVVNLCIIG 72
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
345-433 4.23e-14

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: 70.91  E-value: 4.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 345 IGSGTKIGEGTKIE-NSVIGRNCQIGENIRIKNSFIWDDCIIGNNSIIDHSLIASNATLGSNVRLNDGCIIGFNVKIDD- 422
Cdd:cd03353   18 IGVDVVIDPGVILEgKTVIGEDCVIGPNCVIKDSTIGDGVVIKASSVIEGAVIGNGATVGPFAHLRPGTVLGEGVHIGNf 97
                         90
                 ....*....|....*
gi 398366139 423 ----NMDLDRNTKIS 433
Cdd:cd03353   98 veikKSTIGEGSKAN 112
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
38-281 4.34e-14

N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133050  Cd Length: 257  Bit Score: 71.52  E-value: 4.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  38 TRFMPLTAVKPRCLLPLANVPLIEYTLEFLAK-AGVHEVFLICSSHANQINDYIENSK--WNLPwspfkITTIMSPEARC 114
Cdd:cd06428   12 TRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIGFYPESVFSDFISDAQqeFNVP-----IRYLQEYKPLG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 115 TGDVM---RDLdnrgIITGD---FILVSGDVLTNIDFSKMLEFHKKmhlqdKDHISTMCLSKAStypKTRTIEPAAFVLD 188
Cdd:cd06428   87 TAGGLyhfRDQ----ILAGNpsaFFVLNADVCCDFPLQELLEFHKK-----HGASGTILGTEAS---REQASNYGCIVED 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 189 KSTSRCIYYQdlplpssrEKtsiqidPElldnvdEFVirNDLIDCRIDICTS----HVPLIFQENFDYQSLRTDFVKGVI 264
Cdd:cd06428  155 PSTGEVLHYV--------EK------PE------TFV--SDLINCGVYLFSPeifdTIKKAFQSRQQEAQLGDDNNREGR 212
                        250       260
                 ....*....|....*....|....*...
gi 398366139 265 S------SDIL-----GKHIYAYLTDEY 281
Cdd:cd06428  213 AevirleQDVLtplagSGKLYVYKTDDF 240
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
27-154 4.46e-13

N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133047  Cd Length: 233  Bit Score: 68.39  E-value: 4.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  27 LQAVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIENSKwnlpwSPFKITT 106
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYE-----KKLGIKI 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 398366139 107 IMSPEARCTG---------DVMRDLDNRgiitgdFILVSGDVLTNIDFSKMLEFHKK 154
Cdd:cd06425   76 TFSIETEPLGtagplalarDLLGDDDEP------FFVLNSDVICDFPLAELLDFHKK 126
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
345-422 5.19e-12

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: 63.25  E-value: 5.19e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366139 345 IGSGTKIgEGTKIENSVIGRNCQIGENIRIKNSFIWDDCIIGNNSIIDhsliasNATLGSNVRLNDGCIIGFNVKIDD 422
Cdd:cd04651   15 VSEGCII-SGGTVENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIR------RAIIDKNVVIPDGVVIGGDPEEDR 85
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
361-426 1.74e-11

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: 61.05  E-value: 1.74e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366139 361 VIGRNCQIGENIRIKNSFIWDDCIIGNNSIIDHSLIASNATLGSNVRLnDGCIIGFNVKIDDNMDL 426
Cdd:cd04652    1 LVGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTL-ENCIIGNGAVIGEKCKL 65
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
328-434 3.77e-11

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: 62.04  E-value: 3.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 328 EKDVVLAQSCKIGKCTAIGSGTKIGEGTKI-ENSVIGRNCQIGENIRIK------------------------------- 375
Cdd:cd03352   17 GEGVVIGDGVVIGPGVVIGDGVVIGDDCVIhPNVTIYEGCIIGDRVIIHsgavigsdgfgfapdgggwvkipqlggviig 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 376 -------NSFI----WDDCIIGNNSIID-------------HSLIASNATLGSNVRLNDGCIIGFNVKIDDNMDLDRNTK 431
Cdd:cd03352   97 ddveigaNTTIdrgaLGDTVIGDGTKIDnlvqiahnvrigeNCLIAAQVGIAGSTTIGDNVIIGGQVGIAGHLTIGDGVV 176

                 ...
gi 398366139 432 ISA 434
Cdd:cd03352  177 IGA 179
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
345-434 4.99e-11

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: 61.73  E-value: 4.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 345 IGSGTKIGEGTKI-ENSVIGRNCQIGENiriknSFIWDDCIIGNNSII-DHSLIASNATLGSNVRLNDGCIIGFNVKIDD 422
Cdd:cd03360   93 VSPSAVIGEGCVImAGAVINPDARIGDN-----VIINTGAVIGHDCVIgDFVHIAPGVVLSGGVTIGEGAFIGAGATIIQ 167
                         90
                 ....*....|..
gi 398366139 423 NMDLDRNTKISA 434
Cdd:cd03360  168 GVTIGAGAIIGA 179
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
38-140 8.57e-10

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  Cd Length: 229  Bit Score: 58.01  E-value: 8.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  38 TRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIENSkwnlpwspFKITTIMSPEARCTGD 117
Cdd:cd02523   10 SRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKY--------PNIKFVYNPDYAETNN 81
                         90       100
                 ....*....|....*....|...
gi 398366139 118 VMRDLDNRGIITGDFILVSGDVL 140
Cdd:cd02523   82 IYSLYLARDFLDEDFLLLEGDVV 104
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
349-424 1.54e-09

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


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 55.93  E-value: 1.54e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366139 349 TKIGEGTKIENSVIGRNCQIgENIRIKNSFIWDDCIIGNNSIIDHSLIASNATLGSNVRLnDGCIIGFNVKIDDNM 424
Cdd:cd04651    2 PYIGRRGEVKNSLVSEGCII-SGGTVENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVI-RRAIIDKNVVIPDGV 75
W2_eIF5 cd11561
C-terminal W2 domain of eukaryotic translation initiation factor 5; eIF5 functions as a GTPase ...
640-704 4.59e-09

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: 55.31  E-value: 4.59e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366139 640 MEKIVEQsfDKPDLILFSALV--SLYDNDIIEEDVIYKWWDNVS----TDPRYDEVKKLTVKWVEWLQNAD 704
Cdd:cd11561   85 IERFCGK--HSPELLKKVPLIlkALYDNDILEEEVILKWYEKVSkkyvSKEKSKKVRKAAEPFVEWLEEAE 153
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
29-154 5.30e-09

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 249894  Cd Length: 247  Bit Score: 56.06  E-value: 5.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139   29 AVVLTDSYETRFMPLTAVKPRCLLPLAN-VPLIEYTLEFLAKAGVHEVFLICSS-HANQINDYI-ENSKWNLpwspfKIT 105
Cdd:pfam00483   2 AIILAGGSGTRLWPLTRTLAKPLVPVLDkYPMIQYTLSRLMNAGIREPIVICTQeHRFLVAEQLgDGSKFGL-----QVT 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 398366139  106 TIMSPEARCTGDVMRdlDNRGIITGD---FILV-SGDVLTNIDFSKMLEFHKK 154
Cdd:pfam00483  77 YALQPEPRGTAPAVA--LAADFLGDDdpeLVLVlGGDHIYRMDFEEAVQKARA 127
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
328-415 8.76e-09

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: 55.52  E-value: 8.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 328 EKDVVLAQSCKIGKCTAIGSGTKIGEGTKI-----------------ENS--VIGRNCQIGENI-------------RIK 375
Cdd:cd03351   27 GPNVEIGDGTVIGSHVVIDGPTTIGKNNRIfpfasigeapqdlkykgEPTrlEIGDNNTIREFVtihrgtaqgggvtRIG 106
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 398366139 376 N-------SFIWDDCIIGNNSIIdhsliASNATLGSNVRLNDGCIIG 415
Cdd:cd03351  107 NnnllmayVHVAHDCVIGNNVIL-----ANNATLAGHVEIGDYAIIG 148
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
345-415 1.40e-08

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: 53.27  E-value: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 345 IGSGTKIGEGTKIENsvigrNCQIGENIRIK-NSFIWDDCIIGNNSII----------------------------DHSL 395
Cdd:cd03358    1 IGDNCIIGTNVFIEN-----DVKIGDNVKIQsNVSIYEGVTIEDDVFIgpnvvftndlyprskiyrkwelkgttvkRGAS 75
                         90       100
                 ....*....|....*....|
gi 398366139 396 IASNATLGSNVRLNDGCIIG 415
Cdd:cd03358   76 IGANATILPGVTIGEYALVG 95
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
29-152 1.76e-08

WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars.


Pssm-ID: 133065  Cd Length: 223  Bit Score: 54.10  E-value: 1.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  29 AVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIENSKWNLpwspFKITTIM 108
Cdd:cd06915    1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGG----IRIYYVI 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 398366139 109 SPEARCT-GDVMRDLdnRGIITGDFILVSGDVLTNIDFSKMLEFH 152
Cdd:cd06915   77 EPEPLGTgGAIKNAL--PKLPEDQFLVLNGDTYFDVDLLALLAAL 119
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
29-156 2.64e-08

ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2.


Pssm-ID: 133002  Cd Length: 200  Bit Score: 53.32  E-value: 2.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  29 AVVLTDSYETRFMPLTAVKPRCLLPLA-NVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIENSK-WNLPWSpFKITT 106
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFGgRYRLIDFPLSNMVNSGIRNVGVLTQYKSRSLNDHLGSGKeWDLDRK-NGGLF 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 398366139 107 IMSPEARCTGDVMR-DLD----NRGIITG---DFILV-SGDVLTNIDFSKMLEFHKKMH 156
Cdd:cd02508   80 ILPPQQRKGGDWYRgTADaiyqNLDYIERsdpEYVLIlSGDHIYNMDYREMLDFHIESG 138
COG1213 COG1213
Predicted sugar nucleotidyltransferases [Cell envelope biogenesis, outer membrane]
29-149 3.98e-08

Predicted sugar nucleotidyltransferases [Cell envelope biogenesis, outer membrane]


Pssm-ID: 224134  Cd Length: 239  Bit Score: 53.49  E-value: 3.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  29 AVVLTDSYETRFMPltaVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIENSKwnlpwsPFKITTIM 108
Cdd:COG1213    6 AVILAAGFGSRLGP---DIPKALVEVGGREIIYRTIENLAKAGITEFVVVTNGYRADLVEEFLKKY------PFNAKIVI 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 398366139 109 SPEARCTGDVMRDLDNRGIITGDFILVSGDVLTNIDFSKML 149
Cdd:COG1213   77 NSDYEKTNTGYSLLLAKDYMDGRFILVMSDHVYEPSILERL 117
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
324-432 1.12e-07

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: 51.05  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 324 HIYKEKDVVLAQSCKIGKCTAIGSGTKIGEGTKIE-NSVIGRNCQIGENIRIKNSFIWDDCIIGNNSIIDHSLIASNATL 402
Cdd:cd05636   17 PVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRgYTVLGDGCVVGNSVEVKNSIIMDGTKVPHLNYVGDSVLGENVNL 96
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 398366139 403 G-----SNVRLND-------------------GCIIGFNVKIDDNMDLDRNTKI 432
Cdd:cd05636   97 GagtitANLRFDDkpvkvrlkgervdtgrrklGAIIGDGVKTGINVSLNPGVKI 150
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
338-415 1.29e-07

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: 50.15  E-value: 1.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 338 KIGKCTAIGSGTKIGEGTKIEnsvIGRNCQIGENIRI---------KNSFIWDDCIIGNNSIIDHSLIASNATLGSNVRL 408
Cdd:cd04647    3 SIGDNVYIGPGCVISAGGGIT---IGDNVLIGPNVTIydhnhdiddPERPIEQGVTSAPIVIGDDVWIGANVVILPGVTI 79

                 ....*..
gi 398366139 409 NDGCIIG 415
Cdd:cd04647   80 GDGAVVG 86
galU TIGR01099
UTP-glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ...
29-93 2.94e-07

UTP-glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar genes galU and galF [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides].


Pssm-ID: 233272  Cd Length: 260  Bit Score: 51.15  E-value: 2.94e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366139   29 AVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIENS 93
Cdd:TIGR01099   3 AVIPAAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVEAGIEDILIVTGRGKRSIEDHFDTS 67
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
345-420 3.48e-07

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 48.98  E-value: 3.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 345 IGSGTKIGEGTKIENS---VIGRNCQIGENIRiknsfIWDDCIIGNNSII---DHSLIASNATLGSNVRLNDGCIIGFNV 418
Cdd:cd03354    5 IHPGAKIGPGLFIDHGtgiVIGETAVIGDNCT-----IYQGVTLGGKGKGggkRHPTIGDNVVIGAGAKILGNITIGDNV 79

                 ..
gi 398366139 419 KI 420
Cdd:cd03354   80 KI 81
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
350-421 4.32e-07

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: 48.40  E-value: 4.32e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366139 350 KIGEGTKIE-NSVIGRNCQIGeniriKNSFIWDDCIIGNNSIIDHSL---IASNATLGSNVRLNDGCIIGFNVKID 421
Cdd:cd00208    2 FIGEGVKIHpKAVIRGPVVIG-----DNVNIGPGAVIGAATGPNEKNptiIGDNVEIGANAVIHGGVKIGDNAVIG 72
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
327-387 5.01e-07

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: 48.01  E-value: 5.01e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366139 327 KEKDVVLAQSCKIG-----KCTAIGSGTKIGEGTKIENSVIGRNCQIGENIRIKN-SFIWDDCIIGN 387
Cdd:cd03356   13 IIKNSVIGDNVRIGdgvtiTNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNlCIIGDDVVVED 79
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
28-93 5.40e-07

Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity.


Pssm-ID: 133021  Cd Length: 267  Bit Score: 50.22  E-value: 5.40e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366139  28 QAVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIENS 93
Cdd:cd02541    2 KAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRS 67
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
328-420 6.83e-07

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 48.96  E-value: 6.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 328 EKDVVLAQSCKIG-----KCTAIGSGTKIGEGTKIENSVIGRNCQIGENIRIK-NSFIWDDCIIGN-----NSIIDHSLI 396
Cdd:cd03353   31 EGKTVIGEDCVIGpncviKDSTIGDGVVIKASSVIEGAVIGNGATVGPFAHLRpGTVLGEGVHIGNfveikKSTIGEGSK 110
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 398366139 397 AS------NATLGSNVrlNDGC---------------IIGFNVKI 420
Cdd:cd03353  111 ANhlsylgDAEIGEGV--NIGAgtitcnydgvnkhrtVIGDNVFI 153
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
340-434 6.97e-07

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


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 48.36  E-value: 6.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 340 GKCTaIGSGTKI-GEgtkIENSVIGRNCQIGENIRIKNSF-------------IWDDCIIGNNSIIDHSLIASNATLGSN 405
Cdd:cd03359   26 GKTI-IQSDVIIrGD---LATVSIGRYCILSEGCVIRPPFkkfskgvaffplhIGDYVFIGENCVVNAAQIGSYVHIGKN 101
                         90       100
                 ....*....|....*....|....*....
gi 398366139 406 VRLNDGCIIGFNVKIDDNMDLDRNTKISA 434
Cdd:cd03359  102 CVIGRRCIIKDCVKILDGTVVPPDTVIPP 130
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
362-418 1.81e-06

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: 46.73  E-value: 1.81e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 398366139 362 IGRNCQIGeniriKNSFIWDDCIIGNNSIIDhsliaSNATLGSNVRLNDGCIIGFNV 418
Cdd:cd03358    1 IGDNCIIG-----TNVFIENDVKIGDNVKIQ-----SNVSIYEGVTIEDDVFIGPNV 47
GalU COG1210
UDP-glucose pyrophosphorylase [Cell envelope biogenesis, outer membrane]
29-93 2.91e-06

UDP-glucose pyrophosphorylase [Cell envelope biogenesis, outer membrane]


Pssm-ID: 224131  Cd Length: 291  Bit Score: 48.30  E-value: 2.91e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366139  29 AVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIENS 93
Cdd:COG1210    7 AVIPAAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVAAGIEEILIVTGRGKRAIEDHFDTS 71
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
360-423 5.42e-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: 5.42e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366139 360 SVIGRNCQIGENIRI-KNSFIWDDCIIGNNSII---DHSLIASNATLGSNVRLNDGCIIGFNVKIDDN 423
Cdd:cd00208    1 VFIGEGVKIHPKAVIrGPVVIGDNVNIGPGAVIgaaTGPNEKNPTIIGDNVEIGANAVIHGGVKIGDN 68
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase subunit GalU; Provisional
28-93 8.72e-06

UTP--glucose-1-phosphate uridylyltransferase subunit GalU; Provisional


Pssm-ID: 184021  Cd Length: 302  Bit Score: 46.82  E-value: 8.72e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366139  28 QAVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIENS 93
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTS 75
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
359-434 1.08e-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: 45.48  E-value: 1.08e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366139 359 NSVIGRNCQIGENiriknSFIWDDCIIGNNSIIdhsliASNATLGSNVRLNDGCIIGFNVKIDDNMDLDRNTKISA 434
Cdd:cd03352    1 SAKIGENVSIGPN-----AVIGEGVVIGDGVVI-----GPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHS 66
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
350-432 1.73e-05

Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p27 is part of the pointed-end subcomplex in dynactin that also includes p25, p26, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain the imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100052 [Multi-domain]  Cd Length: 164  Bit Score: 44.24  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 350 KIGEGTKIENS----------VIGRNCQIGENIRIKNSFIWDDC-----IIGNN------------SIIDHSLIASNATL 402
Cdd:cd04646   19 TIGPGTVVHPRatiiaeagpiIIGENNIIEEQVTIVNKKPKDPAepkpmIIGSNnvfevgckcealKIGNNNVFESKSFV 98
                         90       100       110
                 ....*....|....*....|....*....|
gi 398366139 403 GSNVRLNDGCIIGFNVKIDDNMDLDRNTKI 432
Cdd:cd04646   99 GKNVIITDGCIIGAGCKLPSSEILPENTVI 128
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
345-422 2.11e-05

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: 43.30  E-value: 2.11e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366139 345 IGSGTKIGEgtkieNSVIGRNCQIGENIRIKNSFIWDDCIIGNNSIIDHSLIASNATLGSNVRLNDGCIIGFNVKIDD 422
Cdd:cd05824    8 IGKTAKIGP-----NVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLENVTVLGDDVTIKD 80
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
350-415 4.51e-05

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: 4.51e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366139 350 KIGEGTKI-ENSVI----GRNCQIGeniriknsfiwDDCIIGNNSII------DHSLIASNATLGSNVRLNDGCIIG 415
Cdd:cd04645   40 RIGERTNIqDGSVLhvdpGYPTIIG-----------DNVTVGHGAVLhgctigDNCLIGMGAIILDGAVIGKGSIVA 105
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
368-432 5.90e-05

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: 42.07  E-value: 5.90e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 368 IGENIRIKNSFIWDDCIIgNNSIIDHSLIASNATLGSNVRLND-----GCIIGFNVKIdDNMDLDRNTKI 432
Cdd:cd04651    4 IGRRGEVKNSLVSEGCII-SGGTVENSVLFRGVRVGSGSVVEDsvimpNVGIGRNAVI-RRAIIDKNVVI 71
galF TIGR01105
UTP-glucose-1-phosphate uridylyltransferase, non-catalytic GalF subunit; GalF is a ...
27-93 8.80e-05

UTP-glucose-1-phosphate uridylyltransferase, non-catalytic GalF subunit; GalF is a non-catalytic subunit of the UTP-glucose pyrophosphorylase modulating the enzyme activity to increase the formation of UDP-glucose [Regulatory functions, Protein interactions].


Pssm-ID: 130175  Cd Length: 297  Bit Score: 43.87  E-value: 8.80e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366139   27 LQAVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIENS 93
Cdd:TIGR01105   4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTS 70
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
348-393 9.01e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 249615  Cd Length: 36  Bit Score: 40.83  E-value: 9.01e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 398366139  348 GTKIGEGTKIE-NSVIGRNCQIGENiriknsfiwddCIIGNNSIIDH 393
Cdd:pfam00132   1 GTVIGENVLIGpNVVIGGGVIIGDN-----------VIIGAGVVIGG 36
G1P_cyt_trans TIGR02623
glucose-1-phosphate cytidylyltransferase; Members of this family are the enzyme ...
28-154 1.24e-04

glucose-1-phosphate cytidylyltransferase; Members of this family are the enzyme glucose-1-phosphate cytidylyltransferase, also called CDP-glucose pyrophosphorylase, the product of the rfbF gene [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides].


Pssm-ID: 131672  Cd Length: 254  Bit Score: 42.82  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139   28 QAVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEvFLICSSHANQ-INDYIENskWNLPWS------ 100
Cdd:TIGR02623   1 KAVILAGGLGTRISEETHLRPKPMVEIGGKPILWHIMKIYSHHGIND-FIICCGYKGYvIKEYFAN--YFLHMSdvtfhm 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366139  101 -------------PFKITTIMSPEARCTGDVMRDLDNRgIITGDFILVSGDVLTNIDFSKMLEFHKK 154
Cdd:TIGR02623  78 adntmevhhkrvePWRVTLVDTGESTQTGGRLKRVREY-LDDEAFCFTYGDGVADIDIKALIAFHRK 143
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
359-403 1.33e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 249615  Cd Length: 36  Bit Score: 40.45  E-value: 1.33e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 398366139  359 NSVIGRNCQIGeniriKNSFIWDDCIIGNNSIidhslIASNATLG 403
Cdd:pfam00132   1 GTVIGENVLIG-----PNVVIGGGVIIGDNVI-----IGAGVVIG 35
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
382-420 1.94e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 249615  Cd Length: 36  Bit Score: 39.68  E-value: 1.94e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 398366139  382 DCIIGNNSIIDHsliasNATLGSNVRLNDGCIIGFNVKI 420
Cdd:pfam00132   1 GTVIGENVLIGP-----NVVIGGGVIIGDNVIIGAGVVI 34
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
329-432 2.31e-04

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP succinyltransferase): THDP N-succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA. It is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The enzyme is homotrimeric and each subunit contains an N-terminal region with alpha helices and hairpin loops, as well as a C-terminal region with a left-handed parallel alpha-helix (LbH) structural motif encoded by hexapeptide repeat motifs.


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 40.44  E-value: 2.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 329 KDVVLAQSCKIGKCTAIGSGTKIGEGTKIE-NSVIGRNCQIGENiriknsfiwddCIIGNNSIIDHSL---------IAS 398
Cdd:cd03350   12 DGAFIGPGAVLMMPSYVNIGAYVDEGTMVDsWATVGSCAQIGKN-----------VHLSAGAVIGGVLeplqatpviIED 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 398366139 399 NATLGSNVRLNDGCIIGFNVKIDDNMDLDRNTKI 432
Cdd:cd03350   81 DVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTPI 114
W2 cd11473
C-terminal domain of eIF4-gamma/eIF5/eIF2b-epsilon; This domain is found at the C-terminus of ...
608-676 2.39e-04

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: 40.54  E-value: 2.39e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398366139 608 KDAVVKVFNQWGLLFKRQAFDEEEyiDLMNII--MEKIVEQSFDKPDLILFSA-LVSLYDNDIIEEDVIYKW 676
Cdd:cd11473   65 KEQLVLVLKKYGPVLRELLKLIKK--DQLYLLlkIEKLCLQLKLSELISLLEKiLDLLYDADVLSEEAILSW 134
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
331-391 3.21e-04

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: 39.54  E-value: 3.21e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366139 331 VVLAQSCKIGKCTAIGSGTKIGEGTKIENSV---------------IGRNCQIGENIRI-KNSFIWDDCIIGNNSII 391
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAvigaatgpneknptiIGDNVEIGANAVIhGGVKIGDNAVIGAGAVV 77
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
353-432 4.36e-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: 40.26  E-value: 4.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 353 EGTKIENSVIGRNCQIGENIRIK-NSFIWDDCIIGNNSIIDHsliasNATLGSNVRLNDGCIIGFNVKIDDNMDLDrNTK 431
Cdd:cd05636    5 EGTVEEGVTIKGPVWIGEGAIVRsGAYIEGPVIIGKGCEIGP-----NAYIRGYTVLGDGCVVGNSVEVKNSIIMD-GTK 78

                 .
gi 398366139 432 I 432
Cdd:cd05636   79 V 79
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
310-406 7.01e-04

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


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 39.27  E-value: 7.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 310 SNIQDDQTYsyesrHIYKEKDVVLaqsckigkctaiGSGTKIGEGTKIENSVIGRNCQIGeniriKNSFIWDDCIIGNNS 389
Cdd:cd04745   46 ANVQDNCVI-----HGFPGQDTVL------------EENGHIGHGAILHGCTIGRNALVG-----MNAVVMDGAVIGEES 103
                         90
                 ....*....|....*...
gi 398366139 390 IID-HSLIASNATLGSNV 406
Cdd:cd04745  104 IVGaMAFVKAGTVIPPRS 121
PRK10122 PRK10122
GalU regulator GalF; Provisional
26-93 7.57e-04

GalU regulator GalF; Provisional


Pssm-ID: 182252  Cd Length: 297  Bit Score: 40.64  E-value: 7.57e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366139  26 RLQAVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIENS 93
Cdd:PRK10122   3 NLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTS 70
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
337-401 8.22e-04

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


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 39.78  E-value: 8.22e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366139 337 CKIGKCTAIGSGTKIGEGTKI-ENSVIGRNCQIGENIRIKnsfiwDDCIIGNNSIIDHSlIASNAT 401
Cdd:cd03360  133 CVIGDFVHIAPGVVLSGGVTIgEGAFIGAGATIIQGVTIG-----AGAIIGAGAVVTKD-VPDGSV 192
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
379-423 1.13e-03

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


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 38.25  E-value: 1.13e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 398366139 379 IWDDCIIGNNSIIDHsliasNATLGSNVRLNDGCIIGFNVKIDDN 423
Cdd:cd03358    1 IGDNCIIGTNVFIEN-----DVKIGDNVKIQSNVSIYEGVTIEDD 40
W2_eIF5C_like cd11560
C-terminal W2 domain of the eukaryotic translation initiation factor 5C and similar proteins; ...
609-704 1.24e-03

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  Cd Length: 194  Bit Score: 39.50  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 609 DAVVKVFNQWGLLFKrqAFDEEEYIDLMniIMEKIVEQSFDKPDLI-LFSA-LVSLYDNDIIEEDVIYKWW-DNVSTDPR 685
Cdd:cd11560   99 EQALRHLKKYAPLLA--AFCTTARAELA--LLNKIQEYCYENMKFMkVFQKiVKLLYKADVLSEDAILKWYkKGHSPKGK 174
                         90       100
                 ....*....|....*....|..
gi 398366139 686 ---YDEVKKLtvkwVEWLQNAD 704
Cdd:cd11560  175 qvfLKQMEPF----VEWLQEAE 192
LicC COG4750
CTP:phosphocholine cytidylyltransferase involved in choline phosphorylation for cell surface ...
27-78 1.32e-03

CTP:phosphocholine cytidylyltransferase involved in choline phosphorylation for cell surface LPS epitopes [Cell envelope biogenesis, outer membrane]


Pssm-ID: 227093  Cd Length: 231  Bit Score: 39.73  E-value: 1.32e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 398366139  27 LQAVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLI 78
Cdd:COG4750    1 MNAIILAAGLGSRFVPLTQSTPKSLLKVNGEPLIERQIEQLREAGIDDITIV 52
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
318-415 2.30e-03

Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of a large number of microbial enzymes that catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. Members of this class of enzymes include Enterococcus faecium streptogramin A acetyltransferase and Pseudomonas aeruginosa chloramphenicol acetyltransferase. They contain repeated copies of a six-residue hexapeptide repeat sequence motif (X-[STAV]-X-[LIV]-[GAED]-X) and adopt a left-handed parallel beta helix (LbH) structure. The active enzyme is a trimer with CoA and substrate binding sites at the interface of two separate LbH subunits. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients.


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 37.52  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 318 YSYesrhIYKEKDVVLAQSCKIGKCTAIGSGTKIGEGT-----KIENSVIGRNCQIGENIRIKNSFIWDDC-IIGNNSII 391
Cdd:cd03349    7 YSY----GSGPDCDVGGDKLSIGKFCSIAPGVKIGLGGnhptdWVSTYPFYIFGGEWEDDAKFDDWPSKGDvIIGNDVWI 82
                         90       100
                 ....*....|....*....|....
gi 398366139 392 DHsliasNATLGSNVRLNDGCIIG 415
Cdd:cd03349   83 GH-----GATILPGVTIGDGAVIA 101
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
309-405 2.37e-03

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


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 37.78  E-value: 2.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 309 DSNIQDDQTYsyesrHIYKEKDVVlaqsckigkctaIGSGTKIGEGTKIENSVIGRNCQIGEnirikNSFIWDDCIIGNN 388
Cdd:cd04645   44 RTNIQDGSVL-----HVDPGYPTI------------IGDNVTVGHGAVLHGCTIGDNCLIGM-----GAIILDGAVIGKG 101
                         90
                 ....*....|....*...
gi 398366139 389 SIID-HSLIASNATLGSN 405
Cdd:cd04645  102 SIVAaGSLVPPGKVIPPG 119
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
330-422 3.09e-03

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: 37.61  E-value: 3.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 330 DVVLAQSCKIGKCTAIgsgtKIGEGTKIensVIGRNCQIGENIRI---KNSFIWddciIGNNSIIDH-SLIASNATLGSN 405
Cdd:cd00710   20 DVIIGDNVFVGPGASI----RADEGTPI---IIGANVNIQDGVVIhalEGYSVW----IGKNVSIAHgAIVHGPAYIGDN 88
                         90       100
                 ....*....|....*....|....*...
gi 398366139 406 V-----------RLNDGCIIGFNVKIDD 422
Cdd:cd00710   89 CfigfrsvvfnaKVGDNCVIGHNAVVDG 116
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
357-447 4.80e-03

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


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 36.96  E-value: 4.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 357 IENSVIGRNCQIGEN---------IRIK-----------NSFIWDDCIIGNNSIIDHSLIASNATLGSNvrlndgCIIGF 416
Cdd:cd04745   16 IGDVIIGKNCYIGPHaslrgdfgrIVIRdganvqdncviHGFPGQDTVLEENGHIGHGAILHGCTIGRN------ALVGM 89
                         90       100       110
                 ....*....|....*....|....*....|.
gi 398366139 417 NVKIDDNMDLDRNTKISASPLKNAGSRMYDN 447
Cdd:cd04745   90 NAVVMDGAVIGEESIVGAMAFVKAGTVIPPR 120
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
48-92 6.33e-03

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025  Cd Length: 186  Bit Score: 37.15  E-value: 6.33e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 398366139  48 PRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIEN 92
Cdd:cd04182   17 NKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAG 61
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
38-78 6.83e-03

G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short form of glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.


Pssm-ID: 133019  Cd Length: 240  Bit Score: 37.55  E-value: 6.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 398366139  38 TRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLI 78
Cdd:cd02538   12 TRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILII 52
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
345-376 7.16e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 249615  Cd Length: 36  Bit Score: 35.06  E-value: 7.16e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 398366139  345 IGSGTKIGEGTKI-ENSVIGRNCQIGENIRIKN 376
Cdd:pfam00132   4 IGENVLIGPNVVIgGGVIIGDNVIIGAGVVIGG 36
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
330-364 7.64e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 249615  Cd Length: 36  Bit Score: 35.06  E-value: 7.64e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 398366139  330 DVVLAQSCKIGKCTAIGSGTKIGEGTKI-ENSVIGR 364
Cdd:pfam00132   1 GTVIGENVLIGPNVVIGGGVIIGDNVIIgAGVVIGG 36
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
331-369 9.27e-03

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


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 36.69  E-value: 9.27e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 398366139 331 VVLAQSCKIGKCTAIGSGTKIgegtkIENSVIGRNCQIG 369
Cdd:cd03360  145 VVLSGGVTIGEGAFIGAGATI-----IQGVTIGAGAIIG 178
GCD1 COG1208
Nucleoside-diphosphate-sugar pyrophosphorylase involved in lipopolysaccharide biosynthesis ...
28-420 1.04e-66

Nucleoside-diphosphate-sugar pyrophosphorylase involved in lipopolysaccharide biosynthesis/translation initiation factor 2B, gamma/epsilon subunits (eIF-2Bgamma/eIF-2Bepsilon) [Cell envelope biogenesis, outer membrane / Translation, ribosomal structure and biogenesis]


Pssm-ID: 224129 [Multi-domain]  Cd Length: 358  Bit Score: 225.68  E-value: 1.04e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  28 QAVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIENSKwnlpWSPFKITTI 107
Cdd:COG1208    3 KAVILAGGYGTRLRPLTDDRPKPLLPIAGKPLIEYVLEALAAAGVEEIVLVVGYLGEQIEEYFGDGE----GLGVRITYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 108 MSPEARCTGDVMRDLDNRgIITGDFILVSGDVLTNIDFSKMLEFHKKmHLQDKDHISTMCLSKasTYPKTRTIEPAAFVL 187
Cdd:COG1208   79 VEKEPLGTAGALKNALDL-LGGDDFLVLNGDVLTDLDLSELLEFHKK-KGALATIALTRVLDP--SEFGVVETDDGDGRV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 188 DKSTSRCIYYQdlPLPSSREKTSIQIDPELLDNVdEFVIRNDLIDcridictSHVPLIFQENFDYQSLRTDfvkgvissd 267
Cdd:COG1208  155 VEFREKPGPEE--PPSNLINAGIYIFDPEVFDYI-EKGERFDFEE-------ELLPALAAKGEDVYGYVFE--------- 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 268 ilgKHIYAYLTDE-YAVRVESWQTYDTISQdfLGRWCYPLVLDsniqddqtysyesRHIYKEKDVVLAQSCKIGKCTAIG 346
Cdd:COG1208  216 ---GYWLDIGTPEdLLEANELLLRGDGKSP--LGPIEEPVVII-------------RSAYIIGPVVIGPGAKIGPGALIG 277
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366139 347 SGTkigegtkiensVIGRNCQIGENIRIKNSFIWDDCIIGNNSIIDHSLIASNATLGSNVRLNDgCIIGFNVKI 420
Cdd:COG1208  278 PYT-----------VIGEGVTIGNGVEIKNSIIMDNVVIGHGSYIGDSIIGENCKIGASLIIGD-VVIGINSEI 339
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
27-449 2.23e-20

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.


Pssm-ID: 234433 [Multi-domain]  Cd Length: 393  Bit Score: 92.66  E-value: 2.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139   27 LQAVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIEN-SKWnlpwsPFKIT 105
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDgSRG-----GVPIE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  106 TIMSPEARCTGDVMRDLdnRGIITGDFILVSGDVLTnidfskmlefhkkmhlqDKDHISTMCLSKASTYPKTRTIEPAAF 185
Cdd:TIGR03992  76 YVVQEEQLGTADALGSA--KEYVDDEFLVLNGDVLL-----------------DSDLLERLIRAEAPAIAVVEVDDPSDY 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  186 ---VLDKSTSRCIYYQDLPLPSSREKTSIQI-DPELLDNVDEfvirndlidcridictshVPLifqenfdyqSLR----- 256
Cdd:TIGR03992 137 gvvETDGGRVTGIVEKPENPPSNLINAGIYLfSPEIFELLEK------------------TKL---------SPRgeyel 189
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  257 TDFVKGVIssdilgkhiyayltDEYAVRVESwqtYDTISQDfLGR-WcypLVLDSNiqddqtySYESRHIYKEKDVVLAQ 335
Cdd:TIGR03992 190 TDALQLLI--------------DEGKVKAVE---LDGFWLD-VGRpW---DLLDAN-------EALLDNLEPRIEGTVEE 241
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  336 SCKIGKCTAIGSGTKIGEGTKIENSV-IGRNCQIGENIRIK-NSFIWDDCIIGN-----NSII------DH------SLI 396
Cdd:TIGR03992 242 NVTIKGPVVIGEGAVIRSGTYIEGPVyIGKNCDIGPNAYIRpYTVIGNNVHIGNaveikNSIImegtkiPHlsyvgdSVI 321
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366139  397 ASNATLG-----SNVRLND-------------------GCIIGFNVKIDDNMDLDRNTKISasplknAGSRMYDNES 449
Cdd:TIGR03992 322 GENCNFGagtkvANLRHDDkpvkvtvkgkrvdtgrrklGAIVGDGVKTGINVSINPGVKIG------SGARIYPGEV 392
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl]
328-435 3.53e-14

UDP-3-O-[3-hydroxymyristoyl]


Pssm-ID: 223974 [Multi-domain]  Cd Length: 338  Bit Score: 73.10  E-value: 3.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 328 EKDVVLAQSCKIGKCTAIGSGTKIGEGTKIE-NSVIGRNCQIGENIRI-------KNSFIW------------------- 380
Cdd:COG1044  127 GAGVVIGENVVIGAGAVIGENVKIGDGTVIHpNVTIYHNVVIGNNVIIhsgavigADGFGYagtaigwvkipqigrviig 206
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 398366139 381 DDCIIGNNSIIDHSLIaSNATLGSNVRLNDGCIIGFNVKIDDNMDLDRNTKISAS 435
Cdd:COG1044  207 DDVEIGANTTIDRGAL-DDTVIGEGVKIDNLVQIGHNVRIGEHCIIAGQVGIAGS 260
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
28-420 4.78e-14

glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, 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. Alternate name: dTDP-D-glucose synthase


Pssm-ID: 233311 [Multi-domain]  Cd Length: 353  Bit Score: 72.82  E-value: 4.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139   28 QAVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSH-ANQINDYI-ENSKWNLpwspfKIT 105
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVtGEEIKEIVgEGERFGA-----KIT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  106 TIMSPEARCTGD---VMRDLdnrgIITGDFILVSGDvltNIdFSKMLEFHKKmHLQDKDHISTMCLSKAStypktrtiEP 182
Cdd:TIGR01208  76 YIVQGEPLGLAHavyTARDF----LGDDDFVVYLGD---NL-IQDGISRFVK-SFEEKDYDALILLTKVR--------DP 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  183 AAF---VLD--KSTSRCIyyqdlplpssrEKTsiQIDPELLDNVDEFVIRndlidcridictshvPLIFQENFDYQ-SLR 256
Cdd:TIGR01208 139 TAFgvaVLEdgKRILKLV-----------EKP--KEPPSNLAVVGLYMFR---------------PLIFEAIKNIKpSWR 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  257 -----TDFVKGVISSDilgkhiyayltdeYAV---RVESWQtYDTisqdflGRwcYPLVLDSN--IQDDQTysyesRHIY 326
Cdd:TIGR01208 191 geleiTDAIQWLIEKG-------------YKVggsKVTGWW-KDT------GK--PEDLLDANrlILDEVE-----REVQ 243
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  327 KEKDvvlaQSCKIGKctaigsgTKIGEGTKIENSVIGRNCQIGENIRIKNSFIWDDCIIGNNSII-----DHSLIASNAT 401
Cdd:TIGR01208 244 GVDD----ESKIRGR-------VVVGEGAKIVNSVIRGPAVIGEDCIIENSYIGPYTSIGEGVVIrdaevEHSIVLDESV 312
                         410       420
                  ....*....|....*....|
gi 398366139  402 L-GSNVRLNDgCIIGFNVKI 420
Cdd:TIGR01208 313 IeGVQARIVD-SVIGKKVRI 331
GlgC COG0448
ADP-glucose pyrophosphorylase [Carbohydrate transport and metabolism]
29-408 1.03e-13

ADP-glucose pyrophosphorylase [Carbohydrate transport and metabolism]


Pssm-ID: 223525 [Multi-domain]  Cd Length: 393  Bit Score: 72.29  E-value: 1.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  29 AVVLTDSYETRFMPLTAVKPrcllpLANVP------LIEYTLEFLAKAGVHEVFLICSSHANQINDYIENSKwnlPWSPF 102
Cdd:COG0448    8 AIILAGGRGSRLSPLTKDRA-----KPAVPfggkyrIIDFALSNCVNSGIRRIGVLTQYKSHSLNDHIGRGW---PWDLD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 103 KIT---TIMSPEARCTGDV------------MRDLDNRGIitgDFILV-SGDVLTNIDFSKMLEFHKKMHlqdKDhISTM 166
Cdd:COG0448   80 RKNggvFILPAQQREGGERwyegtadaiyqnLLIIRRSDP---EYVLIlSGDHIYKMDYSDMLDFHIESG---AD-VTVA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 167 CL----SKASTYPKTRtiepaafVLDKSTSRCIYYQDLPLPSSREKTSIQIdpelldnvdeFVIRND-LIDcridictsh 241
Cdd:COG0448  153 VKevprEEASRFGVMN-------VDENGRIIEFVEKPADGPPSNSLASMGI----------YIFNTDlLKE--------- 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 242 vpLIFQENFDYQSLRtDFVKGVISSDILGKHIYAYLTDEYAVRVESWQTYDTISQDFLgrwcyplvldsNIQDDQTYSYE 321
Cdd:COG0448  207 --LLEEDAKDPNSSH-DFGKDIIPKLLERGKVYAYEFSGYWRDVGTIDSYYEANMDLL-----------SPQPELNLYDR 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 322 SRHIY-KEKDVVLAQ--SCKIGKCTAIGSGTKIgEGTkIENSVIGRNCQIGENIRIKNSFIWDDCIIGNNSIIDHSLIAS 398
Cdd:COG0448  273 NWPIYtKNKNLPPAKfvNDSEVSNSLVAGGCII-SGT-VENSVLFRGVRIGKGSVIENSVIMPDVEIGEGAVLRRAIIDK 350
                        410
                 ....*....|
gi 398366139 399 NATLGSNVRL 408
Cdd:COG0448  351 NVVIGEGVVI 360
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl]
328-432 5.10e-13

UDP-3-O-[3-hydroxymyristoyl]


Pssm-ID: 223974 [Multi-domain]  Cd Length: 338  Bit Score: 69.63  E-value: 5.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 328 EKDVVLAQSCKIGKCTAIGSGTKIGEGTKIE-NSVIGRNCQIGENIRI-KNSFIWDDCIIGNNSIidhslIASNATLGSN 405
Cdd:COG1044  109 DPTATIGKNVSIGPNVVIGAGVVIGENVVIGaGAVIGENVKIGDGTVIhPNVTIYHNVVIGNNVI-----IHSGAVIGAD 183
                         90       100       110
                 ....*....|....*....|....*....|....
gi 398366139 406 VRLNDGCIIGF-------NVKIDDNMDLDRNTKI 432
Cdd:COG1044  184 GFGYAGTAIGWvkipqigRVIIGDDVEIGANTTI 217
glmU PRK14354
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
343-433 1.65e-12

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 68.70  E-value: 1.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 343 TAIGSGTKIGEGTKIE-------NSVIGRNCQIGENIRIKNSFIWDDCIIgNNSIIDHSLIASNATLGSNVRLNDGCIIG 415
Cdd:PRK14354 260 TYIDADVEIGSDTVIEpgvvikgNTVIGEDCVIGPGSRIVDSTIGDGVTI-TNSVIEESKVGDNVTVGPFAHLRPGSVIG 338
                         90       100
                 ....*....|....*....|...
gi 398366139 416 FNVKIDD-----NMDLDRNTKIS 433
Cdd:PRK14354 339 EEVKIGNfveikKSTIGEGTKVS 361
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl]
323-434 6.35e-12

UDP-3-O-[3-hydroxymyristoyl]


Pssm-ID: 223974 [Multi-domain]  Cd Length: 338  Bit Score: 66.17  E-value: 6.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 323 RHIYKEKDVVLAQSCKIGKCTAIGSGTKIGEG-----------TKIE---NSVIGRNCQIGENIRIKNSFIwDDCIIGNN 388
Cdd:COG1044  152 DGTVIHPNVTIYHNVVIGNNVIIHSGAVIGADgfgyagtaigwVKIPqigRVIIGDDVEIGANTTIDRGAL-DDTVIGEG 230
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 398366139 389 SIID-------------HSLIASNATLGSNVRLNDGCIIGFNVKIDDNMDLDRNTKISA 434
Cdd:COG1044  231 VKIDnlvqighnvrigeHCIIAGQVGIAGSVKIGKYVIIGGQVGIAGHLEIGDGVTIGA 289
lipid_A_lpxD TIGR01853
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; This model describes LpxD, an ...
328-432 9.93e-12

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; This model describes LpxD, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species. This protein represents the third step from UDP-N-acetyl-D-glucosamine. The group added at this step generally is 14:0(3-OH) (myristate) but may vary; in Aquifex it appears to be 16:0(3-OH) (palmitate) [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides].


Pssm-ID: 233599 [Multi-domain]  Cd Length: 324  Bit Score: 65.39  E-value: 9.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  328 EKDVVLAQSCKIGKCTAIGSGTKIGEGTKI-ENSVIGRNCQIGENIRI-KNSFIWDDCIIGNNSIIDhsliaSNATLGS- 404
Cdd:TIGR01853 101 DPSAKIGDGVTIGPNVVIGAGVEIGENVIIgPGVVIGDDVVIGDGSRIhPNVVIYERVQLGKNVIIH-----SGAVIGSd 175
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 398366139  405 -------------------NVRLNDGCIIGFNVKID----DNMDLDRNTKI 432
Cdd:TIGR01853 176 gfgyahtangghvkipqigRVIIEDDVEIGANTTIDrgafDDTIIGEGTKI 226
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
332-432 1.21e-11

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 65.55  E-value: 1.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 332 VLAQSCKIGKCTAIGSGTKIGEGTKIE-------NSVIGRNCQIGENIRIK-NSFIWDDCIIGNNSIIdHsliaSNATLG 403
Cdd:PRK00892 108 VIDPSAKIGEGVSIGPNAVIGAGVVIGdgvvigaGAVIGDGVKIGADCRLHaNVTIYHAVRIGNRVII-H----SGAVIG 182
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 398366139 404 S-------------------NVRLNDGCIIGFNVKID----DNMDLDRNTKI 432
Cdd:PRK00892 183 SdgfgfandrggwvkipqlgRVIIGDDVEIGANTTIDrgalDDTVIGEGVKI 234
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
341-427 1.33e-11

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 65.66  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 341 KCTAIGSGTKIgEGTkIENSVIGRNCQIGENIRIKNSFIWDDCIIGNNSIIDHSLIASNATLGSNVRLNDG----CIIGF 416
Cdd:PRK05293 292 KNSLVVEGCVV-YGT-VEHSVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIGGGkeviTVIGE 369
                         90
                 ....*....|.
gi 398366139 417 NVKIDDNMDLD 427
Cdd:PRK05293 370 NEVIGVGTVIG 380
glmU TIGR01173
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; This ...
331-420 4.09e-11

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; This protein is a bifunctional enzyme, GlmU, which catalyzes last two reactions in the four-step pathway of UDP-N-acetylglucosamine biosynthesis from fructose-6-phosphate. Its reaction product is required from peptidoglycan biosynthesis, LPS biosynthesis in species with LPS, and certain other processes [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Central intermediary metabolism, Amino sugars].


Pssm-ID: 233299 [Multi-domain]  Cd Length: 451  Bit Score: 64.22  E-value: 4.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  331 VVLAQSCKIGKCTAIGSGTKIGEGTKIE-NSVIGRNCQIGENIRIKNSFIWDDCIIGNNSIIDHSLIASNATLGSNVRLN 409
Cdd:TIGR01173 250 LRDPARFDIRGTVEIGRDVEIDPNVILEgKVKIGDDVVIGPGCVIKNSVIGSNVVIKAYSVLEGSEIGEGCDVGPFARLR 329
                          90
                  ....*....|.
gi 398366139  410 DGCIIGFNVKI 420
Cdd:TIGR01173 330 PGSVLGAGVHI 340
lipid_A_lpxD TIGR01853
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; This model describes LpxD, an ...
326-435 4.92e-11

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; This model describes LpxD, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species. This protein represents the third step from UDP-N-acetyl-D-glucosamine. The group added at this step generally is 14:0(3-OH) (myristate) but may vary; in Aquifex it appears to be 16:0(3-OH) (palmitate) [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides].


Pssm-ID: 233599 [Multi-domain]  Cd Length: 324  Bit Score: 63.46  E-value: 4.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  326 YKEKDVVLAQSCKIGKCTAIGSGTKIGEGTKI-ENSVIGRNCQIGENIRIKNS-------F------------------- 378
Cdd:TIGR01853 117 VIGAGVEIGENVIIGPGVVIGDDVVIGDGSRIhPNVVIYERVQLGKNVIIHSGavigsdgFgyahtangghvkipqigrv 196
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 398366139  379 -IWDDCIIGNNSIIDHSLIaSNATLGSNVRLNDGCIIGFNVKIDDNMDLDRNTKISAS 435
Cdd:TIGR01853 197 iIEDDVEIGANTTIDRGAF-DDTIIGEGTKIDNLVQIAHNCRIGENCIIVAQVGIAGS 253
glgD TIGR02092
glucose-1-phosphate adenylyltransferase, GlgD subunit; This family is GlgD, an apparent ...
25-408 5.92e-11

glucose-1-phosphate adenylyltransferase, GlgD subunit; This family is GlgD, an apparent regulatory protein that appears in an alpha2/beta2 heterotetramer with GlgC (glucose-1-phosphate adenylyltransferase, TIGR02091) in a subset of bacteria that use GlgC for glycogen biosynthesis [Energy metabolism, Biosynthesis and degradation of polysaccharides].


Pssm-ID: 233721 [Multi-domain]  Cd Length: 369  Bit Score: 63.56  E-value: 5.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139   25 DRLQAVVLTDSYETRFMPLTAVKPRCLLPLA-NVPLIEYTLEFLAKAGVHEVFLIC-SSHANQINDYIENSK-WNLP--- 98
Cdd:TIGR02092   1 NKMSAIINLTESSKNLSPLTKVRPLASLPFGgRYRLIDFPLSNMVNAGIRNVFIFFkNKERQSLFDHLGSGReWDLHrkr 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139   99 ----WSPFKITTIMSPEARCTGDVMRDLDNRGiiTGDFILVSG-DVLTNIDFSKMLEFHKKmhlQDKDhiSTMCLSKASt 173
Cdd:TIGR02092  81 dglfVFPYNDRDDLSEGGKRYFSQNLEFLKRS--TSEYTVVLNsHMVCNIDLKAVLKYHEE---TGKD--ITVVYKKVK- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  174 ypKTRTIEPAAFVLDKSTSRCIYYQDLPLPSSREKTSIQIdpelldnvdeFVIRNDLIdcrIDICTSHvplifQENFDYQ 253
Cdd:TIGR02092 153 --PADASEYDTILRFDESGKVKSIGQNLNPEEEENISLDI----------YIVSTDLL---IELLYEC-----IQRGKLT 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  254 SLRTdfvkgVISSDILGKHIYAYLTDEYAVRVESWQTYDTISQDflgrwcyplVLDSNIQDDQTYSYESRhIY-KEKDVV 332
Cdd:TIGR02092 213 SLEE-----LIRENLKELNINAYEYTGYLANINSVKSYYKANMD---------LLDPQNFQSLFYSSQGP-IYtKVKDEP 277
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366139  333 LAQSCKIGKCT--AIGSGTKIgEGtKIENSVIGRNCQIGENIRIKNSFIWDDCIIGNNSIIDHSLIASNATLGSNVRL 408
Cdd:TIGR02092 278 PTYYAENSKVEnsLVANGCII-EG-KVENSILSRGVHVGKDALIKNCIIMQRTVIGEGAHLENVIIDKDVVIEPNVKI 353
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
345-434 3.24e-10

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 234265 [Multi-domain]  Cd Length: 193  Bit Score: 59.06  E-value: 3.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  345 IGSGTKIGEGTKI-ENSVIGRNCQIGENIRI-KNSFIWDDCIIGnnsiiDHSLIASNATLGSNVRLNDGCIIGFNVKIDD 422
Cdd:TIGR03570  87 VSPSASIGEGTVImAGAVINPDVRIGDNVIInTGAIVEHDCVIG-----DYVHIAPGVTLSGGVVIGEGVFIGAGATIIQ 161
                          90
                  ....*....|..
gi 398366139  423 NMDLDRNTKISA 434
Cdd:TIGR03570 162 GVTIGAGAVVGA 173
GlmU COG1207
N-acetylglucosamine-1-phosphate uridyltransferase (contains nucleotidyltransferase and I-patch ...
339-420 3.38e-10

N-acetylglucosamine-1-phosphate uridyltransferase (contains nucleotidyltransferase and I-patch acetyltransferase domains) [Cell envelope biogenesis, outer membrane]


Pssm-ID: 224128 [Multi-domain]  Cd Length: 460  Bit Score: 61.43  E-value: 3.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 339 IGKCTAIGSGTKIGEGTKIE-NSVIGRNCQIGENIRIKNSFIWDDCIIGNNSIIDHSLIASNATLGSNVRLNDGCIIGFN 417
Cdd:COG1207  265 IRGDVEIGRDVVIEPNVILEgNTVIGDNVVIGPGSVIKDSVIGDNAVIKAYSVIEGSTVGEGATVGPFARLRPGAVLGAD 344

                 ...
gi 398366139 418 VKI 420
Cdd:COG1207  345 VHI 347
lipid_A_lpxD TIGR01853
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; This model describes LpxD, an ...
324-434 1.61e-09

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; This model describes LpxD, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species. This protein represents the third step from UDP-N-acetyl-D-glucosamine. The group added at this step generally is 14:0(3-OH) (myristate) but may vary; in Aquifex it appears to be 16:0(3-OH) (palmitate) [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides].


Pssm-ID: 233599 [Multi-domain]  Cd Length: 324  Bit Score: 58.84  E-value: 1.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  324 HIYKEKDVVLAQSCKIGKCTAIGSG----TKIGEGTKIENSV-IGRNCQIGEniriknsfiwddciignnsiidHSLIAS 398
Cdd:TIGR01853 189 KIPQIGRVIIEDDVEIGANTTIDRGafddTIIGEGTKIDNLVqIAHNCRIGE----------------------NCIIVA 246
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 398366139  399 NATLGSNVRLNDGCIIGFNVKIDDNMDLDRNTKISA 434
Cdd:TIGR01853 247 QVGIAGSTKIGRNVIIGGQVGVAGHLEIGDNVTIGA 282
glmU PRK14360
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
328-434 3.75e-09

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 58.02  E-value: 3.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 328 EKDVVLAQSCKIGKCTAIGSGTKIGEGTKIENSVIGRNC----------QIGENIRI-------KNSFIWDDCIIGN--- 387
Cdd:PRK14360 266 GPDVIIEPQTHLRGNTVIGSGCRIGPGSLIENSQIGENVtvlysvvsdsQIGDGVKIgpyahlrPEAQIGSNCRIGNfve 345
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398366139 388 --NSII-DHSLIA-----SNATLGSNVRLNDGCII----GFN---VKIDDnmdldrNTKISA 434
Cdd:PRK14360 346 ikKSQLgEGSKVNhlsyiGDATLGEQVNIGAGTITanydGVKkhrTVIGD------RSKTGA 401
glgC TIGR02091
glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, ...
29-392 2.29e-08

glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, is also called ADP-glucose pyrophosphorylase. The plant form is an alpha2,beta2 heterodimer, allosterically regulated in plants. Both subunits are homologous and included in this model. In bacteria, both homomeric forms of GlgC and more active heterodimers of GlgC and GlgD have been described. This model describes the GlgC subunit only. This enzyme appears in variants of glycogen synthesis pathways that use ADP-glucose, rather than UDP-glucose as in animals [Energy metabolism, Biosynthesis and degradation of polysaccharides].


Pssm-ID: 233720 [Multi-domain]  Cd Length: 361  Bit Score: 55.34  E-value: 2.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139   29 AVVLTDSYETRFMPLTAVKPRCLLPLA-NVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIENskwnlPWSPFKIT-- 105
Cdd:TIGR02091   1 AMVLAGGRGSRLSPLTKRRAKPAVPFGgKYRIIDFPLSNCINSGIRRIGVLTQYKSHSLNRHIQR-----GWDFDGFIdg 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  106 --TIMSPEARCTGDV------------MRDLDNRGIitgDFILV-SGDVLTNIDFSKMLEFHKKMHlqdkdhistmclsk 170
Cdd:TIGR02091  76 fvTLLPAQQRESGTDwyqgtadavyqnLDLIEDYDP---EYVLIlSGDHIYKMDYEKMLDYHIESG-------------- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  171 astypktrtiepaafvlDKSTSRCIyyqdlPLPssREKTS----IQIDPEllDNVDEFVIR----NDLIDCRIDICTSHV 242
Cdd:TIGR02091 139 -----------------ADVTIACI-----PVP--RKEASrfgvMQVDED--GRIVDFEEKpanpPSIPGMPDFALASMG 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  243 PLIFQENFDYQSLR---------TDFVKGVISSDILGKHIYAYLTDEYavrvesWQTYDTIsQDFlgrWCYPLVLDS--- 310
Cdd:TIGR02091 193 IYIFDKDVLKELLEedaddpessHDFGKDIIPRALEEGSVQAYLFSGY------WRDVGTI-DSF---WEANMDLVSvvp 262
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  311 --NIQDDQT--YSYeSRHIYKEK---------DVVLAQSCKIGKCTA----IGSGTKIGEGTKIENSVIGRNCQIGENIR 373
Cdd:TIGR02091 263 pfDLYDRKWpiYTY-NEFLPPAKfvdsdaqvvDSLVSEGCIISGATVshsvLGIRVRIGSGSTVEDSVIMGDVGIGRGAV 341
                         410
                  ....*....|....*....
gi 398366139  374 IKNSFIWDDCIIGNNSIID 392
Cdd:TIGR02091 342 IRNAIIDKNVRIGEGVVIG 360
RfbA COG1209
dTDP-glucose pyrophosphorylase [Cell envelope biogenesis, outer membrane]
27-154 7.26e-08

dTDP-glucose pyrophosphorylase [Cell envelope biogenesis, outer membrane]


Pssm-ID: 224130 [Multi-domain]  Cd Length: 286  Bit Score: 53.35  E-value: 7.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  27 LQAVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSS-HANQINDYIEN-SKWNLpwspfKI 104
Cdd:COG1209    1 MKGVILAGGSGTRLRPLTRVVPKQLLPVYDKPMIYYPLETLMLAGIRDILIVVGPeDKPTFKELLGDgSDFGV-----DI 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 398366139 105 TTIMSPEARCTGD---VMRD-LDNrgiitGDFILVSGDvltNI---DFSKMLE-FHKK 154
Cdd:COG1209   76 TYAVQPEPDGLAHavlIAEDfVGD-----DDFVLYLGD---NIfqdGLSELLEhFAEE 125
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
331-434 8.10e-08

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 53.60  E-value: 8.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 331 VVLAQSCKIGKCTAIGSG----TKIGEGTKIENSV-IGRNCQIGEniriknsfiwddciignnsiidHSLIASNATL-GS 404
Cdd:PRK00892 204 VIIGDDVEIGANTTIDRGalddTVIGEGVKIDNLVqIAHNVVIGR----------------------HTAIAAQVGIaGS 261
                         90       100       110
                 ....*....|....*....|....*....|
gi 398366139 405 nVRLNDGCIIGFNVKIDDNMDLDRNTKISA 434
Cdd:PRK00892 262 -TKIGRYCMIGGQVGIAGHLEIGDGVTITA 290
PRK05289 PRK05289
UDP-N-acetylglucosamine acyltransferase; Provisional
328-415 1.17e-07

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 52.41  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 328 EKDVVLAQSCKIGKCTAIGSGTKIGEGTKIENSV-------IGRNCQ------------------------IGENIRIK- 375
Cdd:PRK05289  12 EPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVvidghttIGKNNRifpfasigedpqdlkykgeptrlvIGDNNTIRe 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366139 376 -------------------------NSFIWDDCIIGNNSIidhslIASNATLGSNVRLNDGCIIG 415
Cdd:PRK05289  92 fvtinrgtvqgggvtrigdnnllmaYVHVAHDCVVGNHVI-----LANNATLAGHVEVGDYAIIG 151
glgC TIGR02091
glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, ...
351-424 1.38e-07

glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, is also called ADP-glucose pyrophosphorylase. The plant form is an alpha2,beta2 heterodimer, allosterically regulated in plants. Both subunits are homologous and included in this model. In bacteria, both homomeric forms of GlgC and more active heterodimers of GlgC and GlgD have been described. This model describes the GlgC subunit only. This enzyme appears in variants of glycogen synthesis pathways that use ADP-glucose, rather than UDP-glucose as in animals [Energy metabolism, Biosynthesis and degradation of polysaccharides].


Pssm-ID: 233720 [Multi-domain]  Cd Length: 361  Bit Score: 52.65  E-value: 1.38e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366139  351 IGEGTKIENSVIGRNCQIGENiRIKNSFIWDDCIIGNNSIIDHSLIASNATLGSNVRLNdGCIIGFNVKIDDNM 424
Cdd:TIGR02091 286 VDSDAQVVDSLVSEGCIISGA-TVSHSVLGIRVRIGSGSTVEDSVIMGDVGIGRGAVIR-NAIIDKNVRIGEGV 357
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
328-420 5.96e-07

acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes LpxA, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species, but this protein represents the first step (from UDP-N-acetyl-D-glucosamine) and appears to be conserved in function. Proteins from this family contain many copies of the bacterial transferase hexapeptide repeat (pfam00132) [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides].


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 49.95  E-value: 5.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  328 EKDVVLAQSCKIGKCTAIGSGTKIGEGTKI-----------------ENS--VIGRNCQIGENIRIK------------- 375
Cdd:TIGR01852  26 GPGVKIGDGVELKSHVVILGHTTIGEGTRIfpgaviggvpqdlkykgERTrlIIGDNNTIREFVTINrgtasgggvtrig 105
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 398366139  376 -------NSFIWDDCIIGNNSIIdhsliASNATLGSNVRLNDGCIIGFNVKI 420
Cdd:TIGR01852 106 nnnllmaYSHIAHDCVVGNHVIL-----ANNATLAGHVEVGDYAIIGGLVAV 152
glmU PRK14355
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
326-420 1.72e-06

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 49.74  E-value: 1.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 326 YKEKDVVLAQSCKIGKCTAIGSGTKIGEGTKIENSVIGRNCQIGENIRIKNSfiwddciignnSIIDHSLIASNATLGSN 405
Cdd:PRK14355 264 YIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKGCRIGDDVTVKAG-----------SVLEDSVVGDDVAIGPM 332
                         90
                 ....*....|....*
gi 398366139 406 VRLNDGCIIGFNVKI 420
Cdd:PRK14355 333 AHLRPGTELSAHVKI 347
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
368-427 1.90e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 49.10  E-value: 1.90e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366139 368 IGENIRIKNSFIWDDCI---------------IGNNSIIDHSLIASNATLGSNVRLNDgCIIGFNVKIDDNMDLD 427
Cdd:PRK05293 285 IAENAKVKNSLVVEGCVvygtvehsvlfqgvqVGEGSVVKDSVIMPGAKIGENVVIER-AIIGENAVIGDGVIIG 358
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
326-418 2.66e-06

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 48.09  E-value: 2.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 326 YKEKDVVLAQSCKIGKCTAIGSGTKIGEGTKI-----------------ENS--VIGRNCQIGENIRIK----------- 375
Cdd:PRK12461  25 VIGANVEIGDGTWIGPHAVILGPTRIGKNNKIhqgavvgdepqdftykgEESrlEIGDRNVIREGVTIHrgtkgggvtri 104
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 398366139 376 --------NSFIWDDCIIGNNSIIdhsliASNATLGSNVRLNDGCIIGFNV 418
Cdd:PRK12461 105 gndnllmaYSHVAHDCQIGNNVIL-----VNGALLAGHVTVGDRAIISGNC 150
LpxA COG1043
Acyl-[acyl carrier protein]
329-415 3.02e-06

Acyl-[acyl carrier protein]


Pssm-ID: 223973 [Multi-domain]  Cd Length: 260  Bit Score: 47.99  E-value: 3.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 329 KDVVLAQSCKIGKCTAIGSGTKIGEGTKI-----------------ENS--VIGRNCQIGENIRI--------------- 374
Cdd:COG1043   32 PNVEIGDGTVLKSHVVVEGHTTIGRNNRIfpfasigedpqdlkykgEPTrlIIGDNNTIREFVTIhrgtvqgggvtrigd 111
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 398366139 375 KNSF-----IWDDCIIGNNSIIdhsliASNATLGSNVRLNDGCIIG 415
Cdd:COG1043  112 NNLImayahVAHDCVIGNNCIL-----ANNATLAGHVEVGDYAIIG 152
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
256-408 3.17e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 48.73  E-value: 3.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 256 RTDFVKGVISSDILGKHIYAYLTDEYavrvesWQTYDTIsQDFlgrwcYPLVLDSNIQDDQTYSY--ESRHIYKeKDVVL 333
Cdd:PRK02862 230 YTDFGKEIIPEAIRDYKVQSYLFDGY------WEDIGTI-EAF-----YEANLALTQQPNPPFSFydEKAPIYT-RARYL 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 334 AQScKIGKCTAIGSgtKIGEG-----TKIENSVIGRNCQIGENIRIKNSFI-------WDDCI------------IGNNS 389
Cdd:PRK02862 297 PPS-KLLDATITES--IIAEGciiknCSIHHSVLGIRSRIESGCTIEDTLVmgadfyeSSEEReelrkegkpplgIGEGT 373
                        170
                 ....*....|....*....
gi 398366139 390 IIDHSLIASNATLGSNVRL 408
Cdd:PRK02862 374 TIKRAIIDKNARIGNNVRI 392
PaaY COG0663
Carbonic anhydrases/acetyltransferases, isoleucine patch superfamily [General function ...
330-439 6.16e-06

Carbonic anhydrases/acetyltransferases, isoleucine patch superfamily [General function prediction only]


Pssm-ID: 223735 [Multi-domain]  Cd Length: 176  Bit Score: 45.66  E-value: 6.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 330 DVVLAQSCKIGKCTAIG---SGTKIGEGTKI-ENSVI----GRNCQIGENIRIKNSFIWDDCIIGNNSiidhsLIASNAT 401
Cdd:COG0663   29 DVRIGAGVSIWPGAVLRgdvEPIRIGARTNIqDGVVIhadpGYPVTIGDDVTIGHGAVVHGCTIGDNV-----LIGMGAT 103
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 398366139 402 LGSNVRLNDGCIIGFNVKIDDNMDLDRNTKISASPLKN 439
Cdd:COG0663  104 VLDGAVIGDGSIVGAGALVTPGKEIPGGSLVVGSPAKV 141
lipid_A_lpxD TIGR01853
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; This model describes LpxD, an ...
350-435 8.34e-06

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; This model describes LpxD, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species. This protein represents the third step from UDP-N-acetyl-D-glucosamine. The group added at this step generally is 14:0(3-OH) (myristate) but may vary; in Aquifex it appears to be 16:0(3-OH) (palmitate) [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides].


Pssm-ID: 233599 [Multi-domain]  Cd Length: 324  Bit Score: 46.90  E-value: 8.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  350 KIGEGTKIE-NSVIGRNCQIGENiriknsfiwddCIIGnnsiidhsliaSNATLGSNVRLNDGCIIGFNVKIDDNMDLDR 428
Cdd:TIGR01853 105 KIGDGVTIGpNVVIGAGVEIGEN-----------VIIG-----------PGVVIGDDVVIGDGSRIHPNVVIYERVQLGK 162

                  ....*..
gi 398366139  429 NTKISAS 435
Cdd:TIGR01853 163 NVIIHSG 169
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
377-422 9.41e-06

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 234265 [Multi-domain]  Cd Length: 193  Bit Score: 45.58  E-value: 9.41e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 398366139  377 SFIWDDCIIGNNSII-DHSLIASNATLGSNVRLNDGCIIGFNVKIDD 422
Cdd:TIGR03570  85 AIVSPSASIGEGTVImAGAVINPDVRIGDNVIINTGAIVEHDCVIGD 131
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
333-422 1.15e-05

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 46.17  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 333 LAQSCKIGKCTAIGSGTKIGEGTKI-ENSVIGRNCQIGENIRI-KNSFIWDD------------CIIGNNSII------- 391
Cdd:PRK12461  14 LGSGVEIGPFAVIGANVEIGDGTWIgPHAVILGPTRIGKNNKIhQGAVVGDEpqdftykgeesrLEIGDRNVIregvtih 93
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 398366139 392 ------------------DHSLIASNATLGSNVRLNDGCIIGFNVKIDD 422
Cdd:PRK12461  94 rgtkgggvtrigndnllmAYSHVAHDCQIGNNVILVNGALLAGHVTVGD 142
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl]
375-432 1.88e-05

UDP-3-O-[3-hydroxymyristoyl]


Pssm-ID: 223974 [Multi-domain]  Cd Length: 338  Bit Score: 46.14  E-value: 1.88e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 398366139 375 KNSFIWDDCIIGNNSII-DHSLIASNATLGSNVRLNDGCIIGFNVKIDDNMDLDRNTKI 432
Cdd:COG1044  104 PTAVIDPTATIGKNVSIgPNVVIGAGVVIGENVVIGAGAVIGENVKIGDGTVIHPNVTI 162
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
345-417 2.32e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 45.97  E-value: 2.32e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366139 345 IGSGTKIgEGTKIENSVIGRNCQIGENIRIKNSFIWDDCIIGNNSIIDHsliasnATLGSNVRLNDGCIIGFN 417
Cdd:PRK00844 318 VSAGSII-SGATVRNSVLSPNVVVESGAEVEDSVLMDGVRIGRGAVVRR------AILDKNVVVPPGATIGVD 383
glmU PRK14357
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
336-431 3.58e-05

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 45.52  E-value: 3.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 336 SCKIGKCTAIGSGTKIGEGTKIensviGRNCQIGENIRIKnsfiwdDCIIGNN-----SIIDHSLIASNATLGSNVRLND 410
Cdd:PRK14357 255 DVEIGMDTIIYPMTFIEGKTRI-----GEDCEIGPMTRIV------DCEIGNNvkiirSECEKSVIEDDVSVGPFSRLRE 323
                         90       100
                 ....*....|....*....|....*.
gi 398366139 411 GCIIGFNVKIDD-----NMDLDRNTK 431
Cdd:PRK14357 324 GTVLKKSVKIGNfveikKSTIGENTK 349
WbbJ COG0110
Acetyltransferase (isoleucine patch superfamily) [General function prediction only]
267-415 8.07e-05

Acetyltransferase (isoleucine patch superfamily) [General function prediction only]


Pssm-ID: 223188 [Multi-domain]  Cd Length: 190  Bit Score: 42.95  E-value: 8.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 267 DILGKHIYAYLTDEYAVRVESWQTYDTISQDFLGRWcyplvldSNIQDDQTYSYESRHIYKEKDV---VLAQSCKIGKCT 343
Cdd:COG0110    2 LYTDEIDRELLADRARVRIDDGAFNVAGKPVKLGRY-------AEILGRLVGIKIGEVAVIRPPVridLGEKNLTIGDLC 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 344 AIGSGTKI--GEGTKI-ENSVIGRNCQIG-----ENIRIKNSFIWD---DCIIGNNSIIdhsliASNATLGSNVRLNDGC 412
Cdd:COG0110   75 FIGVNVVIlvGEGITIgDNVVVGPNVTIYtnshpGDFVTANIGALVgagPVTIGEDVWI-----GAGAVILPGVTIGEGA 149

                 ...
gi 398366139 413 IIG 415
Cdd:COG0110  150 VIG 152
glmU PRK09451
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
357-411 8.21e-05

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 44.25  E-value: 8.21e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 398366139 357 IENSV-IGRNCQIGENIRIKNSFIWDDCIIGNNSIIDHSLIASNATLGSNVRLNDG 411
Cdd:PRK09451 280 IEGNVtLGNRVKIGAGCVLKNCVIGDDCEISPYSVVEDANLGAACTIGPFARLRPG 335
glmU TIGR01173
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; This ...
328-442 9.02e-05

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; This protein is a bifunctional enzyme, GlmU, which catalyzes last two reactions in the four-step pathway of UDP-N-acetylglucosamine biosynthesis from fructose-6-phosphate. Its reaction product is required from peptidoglycan biosynthesis, LPS biosynthesis in species with LPS, and certain other processes [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Central intermediary metabolism, Amino sugars].


Pssm-ID: 233299 [Multi-domain]  Cd Length: 451  Bit Score: 44.19  E-value: 9.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139  328 EKDVVLAQSCKIGKCTAIGSGT-----KIGEGTKI------ENSVIGRNCQIGENIRIK-NSFIWDDCIIGN-----NSI 390
Cdd:TIGR01173 271 DPNVILEGKVKIGDDVVIGPGCviknsVIGSNVVIkaysvlEGSEIGEGCDVGPFARLRpGSVLGAGVHIGNfvetkNAR 350
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366139  391 ID------HSLIASNATLGSNVrlNDGC---------------IIGFNVKIDDNMDLDRNTKISASPLKNAGS 442
Cdd:TIGR01173 351 IGkgskagHLSYLGDAEIGSNV--NIGAgtitcnydgankhktIIGDGVFIGSNTQLVAPVKVGDGATIAAGS 421
GlmU COG1207
N-acetylglucosamine-1-phosphate uridyltransferase (contains nucleotidyltransferase and I-patch ...
328-423 9.83e-05

N-acetylglucosamine-1-phosphate uridyltransferase (contains nucleotidyltransferase and I-patch acetyltransferase domains) [Cell envelope biogenesis, outer membrane]


Pssm-ID: 224128 [Multi-domain]  Cd Length: 460  Bit Score: 44.09  E-value: 9.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 328 EKDVVLAQSCKIGKCTAIGSGT-----KIGEGTKI------ENSVIGRNCQIGENIRIK-NSFIWDDCIIGN-----NSI 390
Cdd:COG1207  278 EPNVILEGNTVIGDNVVIGPGSvikdsVIGDNAVIkaysviEGSTVGEGATVGPFARLRpGAVLGADVHIGNfvevkKAT 357
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 398366139 391 IDHSLIAS------NATLGSNVrlNDGC---------------IIGFNVKIDDN 423
Cdd:COG1207  358 IGKGSKAGhltylgDAEIGENV--NIGAgtitcnydgknkfktIIGDNVFIGSN 409
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl]
379-434 1.25e-04

UDP-3-O-[3-hydroxymyristoyl]


Pssm-ID: 223974 [Multi-domain]  Cd Length: 338  Bit Score: 43.44  E-value: 1.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366139 379 IWDDCIIGNNSII-------DHSLIASNATLGSNVRLNDGCIIGFNVKIDDNMDLDRNTKISA 434
Cdd:COG1044  114 IGKNVSIGPNVVIgagvvigENVVIGAGAVIGENVKIGDGTVIHPNVTIYHNVVIGNNVIIHS 176
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
378-434 1.67e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 42.82  E-value: 1.67e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 398366139 378 FIWDDCIIGNNSIIDHsliasNATLGSNVRLNDGCIIGFNVKIDDNMDLDRNTKISA 434
Cdd:PRK00892 108 VIDPSAKIGEGVSIGP-----NAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHA 159
WbbJ COG0110
Acetyltransferase (isoleucine patch superfamily) [General function prediction only]
337-423 6.84e-04

Acetyltransferase (isoleucine patch superfamily) [General function prediction only]


Pssm-ID: 223188 [Multi-domain]  Cd Length: 190  Bit Score: 40.25  E-value: 6.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 337 CKIGKCTAIGS---GTKIGEGTKIENSV----------IGRNCQIGEN---IRIKNSFIWDDCIIGNNSII---DHSLIA 397
Cdd:COG0110   32 VKLGRYAEILGrlvGIKIGEVAVIRPPVridlgeknltIGDLCFIGVNvviLVGEGITIGDNVVVGPNVTIytnSHPGDF 111
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 398366139 398 SNA-----------TLGSNVRLNDGCIIGFNVKIDDN 423
Cdd:COG0110  112 VTAnigalvgagpvTIGEDVWIGAGAVILPGVTIGEG 148
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
351-376 8.08e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 41.02  E-value: 8.08e-04
                         10        20
                 ....*....|....*....|....*.
gi 398366139 351 IGEGTKIENSVIGRNCQIGENIRIKN 376
Cdd:PRK02862 369 IGEGTTIKRAIIDKNARIGNNVRIVN 394
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]
345-421 9.01e-04

Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]


Pssm-ID: 225082 [Multi-domain]  Cd Length: 271  Bit Score: 40.37  E-value: 9.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 345 IGSGtkIGEGTKIE-NSVIGRNCQIGeniriKNSFIWDDCIIG-------NNSII--DHSLIASNATLGSNVRLNDGCII 414
Cdd:COG2171  137 IGAG--TGEGTMVDgRASVGSCAQVG-----KNSHIGGGASIGgvleplqANPVIigDNCLIGANSEVVEGVIVGDGCVV 209

                 ....*..
gi 398366139 415 GFNVKID 421
Cdd:COG2171  210 AAGVFIT 216
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]
337-423 9.43e-04

Serine acetyltransferase [Amino acid transport and metabolism]


Pssm-ID: 223975 [Multi-domain]  Cd Length: 194  Bit Score: 39.60  E-value: 9.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 337 CKIGKCTAIGSGTKIGEGTKIensVIGRNCQIGENIRiknsfIWDDCIIGNNSI---IDHSLIASNATLGSNVrlndgCI 413
Cdd:COG1045   68 IEIHPGAKIGRGLFIDHGTGV---VIGETAVIGDDVT-----IYHGVTLGGTGKesgKRHPTIGNGVYIGAGA-----KI 134
                         90
                 ....*....|
gi 398366139 414 IGfNVKIDDN 423
Cdd:COG1045  135 LG-NIEIGDN 143
glmU PRK14354
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
307-406 1.05e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 40.59  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 307 VLDSNIQDDQT---YSY---ESrhiykekdvVLAQSCKIG-----KCTAIGSGTKIGEGTKIENSVIGRNCQIG-----E 370
Cdd:PRK14354 314 IEESKVGDNVTvgpFAHlrpGS---------VIGEEVKIGnfveiKKSTIGEGTKVSHLTYIGDAEVGENVNIGcgtitV 384
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 398366139 371 NIRIKNSF---IWDDCIIGNNS-------IIDHSLIASNATLGSNV 406
Cdd:PRK14354 385 NYDGKNKFktiIGDNAFIGCNSnlvapvtVGDNAYIAAGSTITKDV 430
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl]
331-403 1.36e-03

UDP-3-O-[3-hydroxymyristoyl]


Pssm-ID: 223974 [Multi-domain]  Cd Length: 338  Bit Score: 39.97  E-value: 1.36e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366139 331 VVLAQSCKIGKCTAIGSGTKIGEGTKiensvIGRNCQIGENIRIKnsfiwDDCIIGNNSIIDH-SLIASNATLG 403
Cdd:COG1044  237 VQIGHNVRIGEHCIIAGQVGIAGSVK-----IGKYVIIGGQVGIA-----GHLEIGDGVTIGArSGVMASITEP 300
GlmU COG1207
N-acetylglucosamine-1-phosphate uridyltransferase (contains nucleotidyltransferase and I-patch ...
332-415 1.70e-03

N-acetylglucosamine-1-phosphate uridyltransferase (contains nucleotidyltransferase and I-patch acetyltransferase domains) [Cell envelope biogenesis, outer membrane]


Pssm-ID: 224128 [Multi-domain]  Cd Length: 460  Bit Score: 39.86  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366139 332 VLAQSCKIG-----KCTAIGSGTKIGEGTKIENSVIGRNCQIGE-----NIRIKNSFIwddCIIGnnsiiDHSLIASNAT 401
Cdd:COG1207  340 VLGADVHIGnfvevKKATIGKGSKAGHLTYLGDAEIGENVNIGAgtitcNYDGKNKFK---TIIG-----DNVFIGSNSQ 411
                         90
                 ....*....|....
gi 398366139 402 LGSNVRLNDGCIIG 415
Cdd:COG1207  412 LVAPVTIGDGATIA 425
phn_thr-fam TIGR03308
phosphonate metabolim protein, transferase hexapeptide repeat family; This family of proteins ...
351-411 2.89e-03

phosphonate metabolim protein, transferase hexapeptide repeat family; This family of proteins contains copies of the Bacterial transferase hexapeptide repeat family (pfam00132) and is only found in operons encoding the phosphonate C-P lyase system (GenProp0232). Many C-P lyase operons, however, lack a homolog of this protein.


Pssm-ID: 132351 [Multi-domain]  Cd Length: 204  Bit Score: 38.22  E-value: 2.89e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366139  351 IGEGTKIENSVIGRNCQIGENIRIKNSFIWDDCIIGNNSIIDHSLIASNATLGSNVRLNDG 411
Cdd:TIGR03308  11 LHPTAELTESKLGRYTEIGERTRLREVALGDYSYVMRDCDIIYTTIGKFCSIAAMVRINAT 71
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
351-377 8.89e-03

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 37.53  E-value: 8.89e-03
                         10        20
                 ....*....|....*....|....*..
gi 398366139 351 IGEGTKIENSVIGRNCQIGENIRIKNS 377
Cdd:PLN02241 376 IGENTKIRNAIIDKNARIGKNVVIINK 402
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.12
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH