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Conserved domains on  [gi|2319249963|gb|UYK70432|]
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Gfo/Idh/MocA family oxidoreductase [Coxiella burnetii]

Protein Classification

acyltransferase( domain architecture ID 11430611)

acyltransferase belonging to the transferase hexapeptide repeat family, catalyzes the transfer of an acyl group from an acyl-CoA to a substrate; similar to O-antigen biosynthesis protein WlbB, a bacterial N-acetyltransferase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 362-480 3.52e-71

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: 222.38  E-value: 3.52e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 362 IGENCIIGQNVMIGPDVKIGNYCKIQNNVSLYKGVTLEDGVFCGPSCVFTNVNNPRAEIERKNEFKKTYVERGVTIGANA 441
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYRKWELKGTTVKRGASIGANA 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2319249963 442 TIVCGVHLGAYSFIGAGAVVTKDVKPHALVLGNPARQVG 480
Cdd:cd03358    81 TILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
MviM COG0673
Predicted dehydrogenase [General function prediction only];
6-319 3.35e-56

Predicted dehydrogenase [General function prediction only];


:

Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 189.75  E-value: 3.35e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963   6 KIVVVGGGYWGKNLIRNFAKLGA--LAGICEVSQEVAIKLGEEYKVPV-LSWKETLTNTSYNAVAIATPAKDHAELAWQA 82
Cdd:COG0673     5 RVGIIGAGGIGRAHAPALAALPGveLVAVADRDPERAEAFAEEYGVRVyTDYEELLADPDIDAVVIATPNHLHAELAIAA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963  83 LEANKDVFVEKPLALQMDDAEKVGQLAFARHRILMVGHLLQYHPAFTALKLLAHEGKLGRLQYLYSNRLNLG-------K 155
Cdd:COG0673    85 LEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRpagpadwR 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 156 IRREED---ILWSFAPHDISMILSLVNEKPSVVKAMGGYFLHKSI--ADVTTTHLEFPSGVQAHIFVSWLHPHK--EQKL 228
Cdd:COG0673   165 FDPELAgggALLDLGIHDIDLARWLLGSEPESVSATGGRLVPDRVevDDTAAATLRFANGAVATLEASWVAPGGerDERL 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 229 VVVGSKGMAvfddakpwtqklafyshqihwrdgmpfpdkadatycslteeepltrecqhFIDCVKTREQPITDAKEGLRV 308
Cdd:COG0673   245 EVYGTKGTL--------------------------------------------------FVDAIRGGEPPPVSLEDGLRA 274

                         330
                  ....*....|.
gi 2319249963 309 LEVLNQATKSL 319
Cdd:COG0673   275 LELAEAAYESA 285
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 330-392 1.05e-05

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.


The actual alignment was detected with superfamily member cd00208:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 78  Bit Score: 43.39  E-value: 1.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2319249963 330 FFIHETAVVDNHVALGKNTKVWHFSHILE--------GCKIGENCIIGQNVMIGPDVKIGNYCKIQNNVSL 392
Cdd:cd00208     7 VKIHPKAVIRGPVVIGDNVNIGPGAVIGAatgpneknPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVV 77
 
Name Accession Description Interval E-value
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 362-480 3.52e-71

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: 222.38  E-value: 3.52e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 362 IGENCIIGQNVMIGPDVKIGNYCKIQNNVSLYKGVTLEDGVFCGPSCVFTNVNNPRAEIERKNEFKKTYVERGVTIGANA 441
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYRKWELKGTTVKRGASIGANA 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2319249963 442 TIVCGVHLGAYSFIGAGAVVTKDVKPHALVLGNPARQVG 480
Cdd:cd03358    81 TILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
MviM COG0673
Predicted dehydrogenase [General function prediction only];
6-319 3.35e-56

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 189.75  E-value: 3.35e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963   6 KIVVVGGGYWGKNLIRNFAKLGA--LAGICEVSQEVAIKLGEEYKVPV-LSWKETLTNTSYNAVAIATPAKDHAELAWQA 82
Cdd:COG0673     5 RVGIIGAGGIGRAHAPALAALPGveLVAVADRDPERAEAFAEEYGVRVyTDYEELLADPDIDAVVIATPNHLHAELAIAA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963  83 LEANKDVFVEKPLALQMDDAEKVGQLAFARHRILMVGHLLQYHPAFTALKLLAHEGKLGRLQYLYSNRLNLG-------K 155
Cdd:COG0673    85 LEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRpagpadwR 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 156 IRREED---ILWSFAPHDISMILSLVNEKPSVVKAMGGYFLHKSI--ADVTTTHLEFPSGVQAHIFVSWLHPHK--EQKL 228
Cdd:COG0673   165 FDPELAgggALLDLGIHDIDLARWLLGSEPESVSATGGRLVPDRVevDDTAAATLRFANGAVATLEASWVAPGGerDERL 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 229 VVVGSKGMAvfddakpwtqklafyshqihwrdgmpfpdkadatycslteeepltrecqhFIDCVKTREQPITDAKEGLRV 308
Cdd:COG0673   245 EVYGTKGTL--------------------------------------------------FVDAIRGGEPPPVSLEDGLRA 274

                         330
                  ....*....|.
gi 2319249963 309 LEVLNQATKSL 319
Cdd:COG0673   275 LELAEAAYESA 285
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
356-487 6.14e-40

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 141.16  E-value: 6.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 356 ILEGCKIGENCIIGQNVMI-GPDVKIGNYCKIQNNVSLY--KGVTLEDGVFCGPSCVFTNVNNPRAEIERKNE-FKKTYV 431
Cdd:COG0110     5 LLFGARIGDGVVIGPGVRIyGGNITIGDNVYIGPGVTIDdpGGITIGDNVLIGPGVTILTGNHPIDDPATFPLrTGPVTI 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2319249963 432 ERGVTIGANATIVCGVHLGAYSFIGAGAVVTKDVKPHALVLGNPARQVGWVSHAGE 487
Cdd:COG0110    85 GDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEER 140
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 332-476 2.04e-27

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: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 109.12  E-value: 2.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 332 IHETAVVDNHVALGKNTKVWHFSHILEGCKIGENCIIGQNVMIGPDVKIGNYCKIQNNVSLYKGVTLEDGVFcgpscvft 411
Cdd:TIGR03570  90 IHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGEGVF-------- 161

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2319249963 412 nvnnpraeierknefkktyvergvtIGANATIVCGVHLGAYSFIGAGAVVTKDVKPHALVLGNPA 476
Cdd:TIGR03570 162 -------------------------IGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 6-120 1.15e-19

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 84.57  E-value: 1.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963   6 KIVVVGGGYWGKNLIRNF---AKLGALAGICEVSQEVAIKLGEEYKVPV-LSWKETLTNTSYNAVAIATPAKDHAELAWQ 81
Cdd:pfam01408   2 RVGIIGAGKIGSKHARALnasQPGAELVAILDPNSERAEAVAESFGVEVySDLEELLNDPEIDAVIVATPNGLHYDLAIA 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2319249963  82 ALEANKDVFVEKPLALQMDDAEKVGQLAFARHRILMVGH 120
Cdd:pfam01408  82 ALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 332-443 9.49e-17

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 81.34  E-value: 9.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 332 IHETAVVDNHVALGKNTKVWHFSHILEGCKIGENCIIGQNVMIGPDVKIGNYCKIQNNVSLYKGVTLEDGVFCGPSCV-- 409
Cdd:PRK00892  103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVig 182

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2319249963 410 ---FTNVNNpraeierKNEFKKTY------VERGVTIGANATI 443
Cdd:PRK00892  183 sdgFGFAND-------RGGWVKIPqlgrviIGDDVEIGANTTI 218
PRK11579 PRK11579
putative oxidoreductase; Provisional
 1-177 7.94e-13

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 69.75  E-value: 7.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963   1 MQDQPKIVVVGGGYWGKN----LIRNFAKLgALAGiceVSQEVAIKLGEEY-KVPVLSWKETLTNT-SYNAVAIATPAKD 74
Cdd:PRK11579    1 MSDKIRVGLIGYGYASKTfhapLIAGTPGL-ELAA---VSSSDATKVKADWpTVTVVSEPQHLFNDpNIDLIVIPTPNDT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963  75 HAELAWQALEANKDVFVEKPLALQMDDAEKVGQLAFARHRILMVGHLLQYHPAFTALKLLAHEGKLGRLQYLYSN----R 150
Cdd:PRK11579   77 HFPLAKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFLTLKALLAEGVLGEVAYFESHfdrfR 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2319249963 151 LNLGKIRREE-----DILWSFAPHDISMILSL 177
Cdd:PRK11579  157 PQVRQRWREQggpgsGIWYDLAPHLLDQAIQL 188
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
359-388 1.38e-07

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 47.33  E-value: 1.38e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 2319249963 359 GCKIGENCIIGQNVMIGPDVKIGNYCKIQN 388
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 330-392 1.05e-05

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: 43.39  E-value: 1.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2319249963 330 FFIHETAVVDNHVALGKNTKVWHFSHILE--------GCKIGENCIIGQNVMIGPDVKIGNYCKIQNNVSL 392
Cdd:cd00208     7 VKIHPKAVIRGPVVIGDNVNIGPGAVIGAatgpneknPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVV 77
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
341-369 1.45e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 41.94  E-value: 1.45e-05
                          10        20
                  ....*....|....*....|....*....
gi 2319249963 341 HVALGKNTKVWHFSHILEGCKIGENCIIG 369
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 326-381 8.16e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 38.70  E-value: 8.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 326 RVNDFFIHETAVVDNH---------VALGKNTKVWHfSHILEGCKIGENC-----IIGQNVMIGPDVKIG 381
Cdd:PRK05293  290 KVKNSLVVEGCVVYGTvehsvlfqgVQVGEGSVVKD-SVIMPGAKIGENVvieraIIGENAVIGDGVIIG 358
 
Name Accession Description Interval E-value
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 362-480 3.52e-71

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: 222.38  E-value: 3.52e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 362 IGENCIIGQNVMIGPDVKIGNYCKIQNNVSLYKGVTLEDGVFCGPSCVFTNVNNPRAEIERKNEFKKTYVERGVTIGANA 441
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYRKWELKGTTVKRGASIGANA 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2319249963 442 TIVCGVHLGAYSFIGAGAVVTKDVKPHALVLGNPARQVG 480
Cdd:cd03358    81 TILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
MviM COG0673
Predicted dehydrogenase [General function prediction only];
6-319 3.35e-56

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 189.75  E-value: 3.35e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963   6 KIVVVGGGYWGKNLIRNFAKLGA--LAGICEVSQEVAIKLGEEYKVPV-LSWKETLTNTSYNAVAIATPAKDHAELAWQA 82
Cdd:COG0673     5 RVGIIGAGGIGRAHAPALAALPGveLVAVADRDPERAEAFAEEYGVRVyTDYEELLADPDIDAVVIATPNHLHAELAIAA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963  83 LEANKDVFVEKPLALQMDDAEKVGQLAFARHRILMVGHLLQYHPAFTALKLLAHEGKLGRLQYLYSNRLNLG-------K 155
Cdd:COG0673    85 LEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRpagpadwR 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 156 IRREED---ILWSFAPHDISMILSLVNEKPSVVKAMGGYFLHKSI--ADVTTTHLEFPSGVQAHIFVSWLHPHK--EQKL 228
Cdd:COG0673   165 FDPELAgggALLDLGIHDIDLARWLLGSEPESVSATGGRLVPDRVevDDTAAATLRFANGAVATLEASWVAPGGerDERL 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 229 VVVGSKGMAvfddakpwtqklafyshqihwrdgmpfpdkadatycslteeepltrecqhFIDCVKTREQPITDAKEGLRV 308
Cdd:COG0673   245 EVYGTKGTL--------------------------------------------------FVDAIRGGEPPPVSLEDGLRA 274

                         330
                  ....*....|.
gi 2319249963 309 LEVLNQATKSL 319
Cdd:COG0673   275 LELAEAAYESA 285
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
356-487 6.14e-40

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 141.16  E-value: 6.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 356 ILEGCKIGENCIIGQNVMI-GPDVKIGNYCKIQNNVSLY--KGVTLEDGVFCGPSCVFTNVNNPRAEIERKNE-FKKTYV 431
Cdd:COG0110     5 LLFGARIGDGVVIGPGVRIyGGNITIGDNVYIGPGVTIDdpGGITIGDNVLIGPGVTILTGNHPIDDPATFPLrTGPVTI 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2319249963 432 ERGVTIGANATIVCGVHLGAYSFIGAGAVVTKDVKPHALVLGNPARQVGWVSHAGE 487
Cdd:COG0110    85 GDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEER 140
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 332-476 2.04e-27

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: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 109.12  E-value: 2.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 332 IHETAVVDNHVALGKNTKVWHFSHILEGCKIGENCIIGQNVMIGPDVKIGNYCKIQNNVSLYKGVTLEDGVFcgpscvft 411
Cdd:TIGR03570  90 IHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGEGVF-------- 161

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2319249963 412 nvnnpraeierknefkktyvergvtIGANATIVCGVHLGAYSFIGAGAVVTKDVKPHALVLGNPA 476
Cdd:TIGR03570 162 -------------------------IGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 361-479 5.79e-26

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: 101.76  E-value: 5.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 361 KIGENCIIGQNVMI--GPDVKIGNYCKIQNNVSLYkgvtledgvfcgpsCVFTNVNNPRAEIERKNEFKKTYVERGVTIG 438
Cdd:cd04647     3 SIGDNVYIGPGCVIsaGGGITIGDNVLIGPNVTIY--------------DHNHDIDDPERPIEQGVTSAPIVIGDDVWIG 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2319249963 439 ANATIVCGVHLGAYSFIGAGAVVTKDVKPHALVLGNPARQV 479
Cdd:cd04647    69 ANVVILPGVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 331-475 2.68e-25

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: 102.95  E-value: 2.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 331 FIHETAVVDNHVALGKNTKVWHFSHILEGCKIGENCIIGQNVMIGPDVKIGNYCKIQNNVSLYKGVTLEDGVFcgpscvf 410
Cdd:cd03360    86 LIHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEGAF------- 158

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2319249963 411 tnvnnpraeierknefkktyvergvtIGANATIVCGVHLGAYSFIGAGAVVTKDVKPHALVLGNP 475
Cdd:cd03360   159 --------------------------IGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 332-477 9.63e-21

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 93.16  E-value: 9.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 332 IHETAVVDNHVALGKNTKVWHFSHILEGCKIGENCIIGQNVMIGPDVKIGNYCKIQNNVSLYKGVTLEDGVFCGPSCV-- 409
Cdd:COG1044    99 IHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVig 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 410 ---FTNVNNPRAEIERKNEFKKTYVERGVTIGANATIVCG----------------------VHLGAYSFI--------- 455
Cdd:COG1044   179 adgFGFAPDEDGGWVKIPQLGRVVIGDDVEIGANTTIDRGalgdtvigdgtkidnlvqiahnVRIGEHTAIaaqvgiags 258

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2319249963 456 ---------------------------GAGAVVTKDVKPHALVLGNPAR 477
Cdd:COG1044   259 tkigdnvviggqvgiaghltigdgviiGAQSGVTKSIPEGGVYSGSPAQ 307
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 359-480 5.20e-20

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 87.45  E-value: 5.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 359 GCKIGENCII--GQNVMIGPDVKIGNyckiqnNVSLYKGVTLedgvfcGpscvftnvnnpraeiERKNEFKKTY--VERG 434
Cdd:COG1045    71 GATIGRGFFIdhGTGVVIGETAVIGD------NVTIYQGVTL------G---------------GTGKEKGKRHptIGDN 123

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2319249963 435 VTIGANATIVCGVHLGAYSFIGAGAVVTKDVKPHALVLGNPARQVG 480
Cdd:COG1045   124 VVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVK 169
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 355-475 1.02e-19

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: 84.03  E-value: 1.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 355 HILEGCKIGENCII--GQNVMIGPDVKIGNyckiqnNVSLYKGVTLEDGVFCGpscvftnvnNPRAEIerknefkktyVE 432
Cdd:cd03354     4 DIHPGAKIGPGLFIdhGTGIVIGETAVIGD------NCTIYQGVTLGGKGKGG---------GKRHPT----------IG 58

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2319249963 433 RGVTIGANATIVCGVHLGAYSFIGAGAVVTKDVKPHALVLGNP 475
Cdd:cd03354    59 DNVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 6-120 1.15e-19

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 84.57  E-value: 1.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963   6 KIVVVGGGYWGKNLIRNF---AKLGALAGICEVSQEVAIKLGEEYKVPV-LSWKETLTNTSYNAVAIATPAKDHAELAWQ 81
Cdd:pfam01408   2 RVGIIGAGKIGSKHARALnasQPGAELVAILDPNSERAEAVAESFGVEVySDLEELLNDPEIDAVIVATPNGLHYDLAIA 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2319249963  82 ALEANKDVFVEKPLALQMDDAEKVGQLAFARHRILMVGH 120
Cdd:pfam01408  82 ALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 335-477 3.49e-18

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: 82.84  E-value: 3.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 335 TAVVDNHVALGkntkvwHFSHILEGCKIGENCIIGQNVMIGPDVKIGNYCKIQNNVSLYKGVTLEDGVFCGPSCV----- 409
Cdd:cd03352     1 SAKIGENVSIG------PNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVigsdg 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 410 FTNVNNP----------RAEIERKNE-----------FKKTYVERG---------------------------------- 434
Cdd:cd03352    75 FGFAPDGggwvkipqlgGVIIGDDVEiganttidrgaLGDTVIGDGtkidnlvqiahnvrigencliaaqvgiagsttig 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2319249963 435 --VTIGANATIVCGVHLGAYSFIGAGAVVTKDVKPHALVLGNPAR 477
Cdd:cd03352   155 dnVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQ 199
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 334-478 1.61e-17

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: 80.54  E-value: 1.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 334 ETAVVDNHVALGKNTKVWHFSHILEGCKIGENCIIGQNVMIGpDVKIGNYCKIQNNvSLYKGVTLEDGVFCGPscvFTNV 413
Cdd:cd03353     8 ETTYIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIK-DSTIGDGVVIKAS-SVIEGAVIGNGATVGP---FAHL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 414 nNPRAEIERKN------EFKKTYVERGV-----------TIGANATIVCG------------------------------ 446
Cdd:cd03353    83 -RPGTVLGEGVhignfvEIKKSTIGEGSkanhlsylgdaEIGEGVNIGAGtitcnydgvnkhrtvigdnvfigsnsqlva 161

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2319249963 447 -VHLGAYSFIGAGAVVTKDVKPHALVLGNpARQ 478
Cdd:cd03353   162 pVTIGDGATIAAGSTITKDVPPGALAIAR-ARQ 193
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 361-477 1.92e-17

Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100047 [Multi-domain]  Cd Length: 169  Bit Score: 79.77  E-value: 1.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 361 KIGENCII--------GQNVMIGPDVKIgNY-CKIQNNVslykGVTLEDGVFCGPSCVFTNVNNPRAEIERKN--EF-KK 428
Cdd:cd03357    44 SVGENVYIeppfhcdyGYNIHIGDNFYA-NFnCTILDVA----PVTIGDNVLIGPNVQIYTAGHPLDPEERNRglEYaKP 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2319249963 429 TYVERGVTIGANATIVCGVHLGAYSFIGAGAVVTKDVKPHALVLGNPAR 477
Cdd:cd03357   119 ITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPAR 167
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 332-480 3.23e-17

Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane/envelope biogenesis]; Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 81.22  E-value: 3.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 332 IHETAVVDNHVALGKNTKVWHFSHILEGCKIGENCIIGQNVMIGPDVKIGNYCKIQNNVSL--------YKG-------- 395
Cdd:COG1043     4 IHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIgeepqdlkYKGeptrleig 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 396 --------VTL------EDGV--------F---------C--GPSCVFTN-------VnnpraeierknefkktYVERGV 435
Cdd:COG1043    84 dnntirefVTIhrgtvqGGGVtrigddnlLmayvhvahdCvvGNNVILANnatlaghV----------------EVGDHA 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2319249963 436 TIGANATIVCGVHLGAYSFIGAGAVVTKDVKPHALVLGNPARQVG 480
Cdd:COG1043   148 IIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARLRG 192
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 332-443 9.49e-17

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 81.34  E-value: 9.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 332 IHETAVVDNHVALGKNTKVWHFSHILEGCKIGENCIIGQNVMIGPDVKIGNYCKIQNNVSLYKGVTLEDGVFCGPSCV-- 409
Cdd:PRK00892  103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVig 182

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2319249963 410 ---FTNVNNpraeierKNEFKKTY------VERGVTIGANATI 443
Cdd:PRK00892  183 sdgFGFAND-------RGGWVKIPqlgrviIGDDVEIGANTTI 218
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 353-494 1.78e-16

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: 76.43  E-value: 1.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 353 FSHILEGCKI--GENCIIGQNVMIGPDVKIGNYckiQN----NVSLYkgvtledgvfcgPSCVFTNVNNPRAEIERKNEF 426
Cdd:cd03349     7 YSYGSGPDCDvgGDKLSIGKFCSIAPGVKIGLG---GNhptdWVSTY------------PFYIFGGEWEDDAKFDDWPSK 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2319249963 427 KKTYVERGVTIGANATIVCGVHLGAYSFIGAGAVVTKDVKPHALVLGNPARQVGWvshageRLDDRLI 494
Cdd:cd03349    72 GDVIIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRY------RFDEETI 133
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
332-480 3.83e-16

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 78.22  E-value: 3.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 332 IHETAVVDNHVALGKNTKVWHFSHILEGCKIGENCIIGQNVMIGPDVKIGNYCKIQNNVSL--------YKG-------- 395
Cdd:PRK05289    5 IHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIgedpqdlkYKGeptrlvig 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 396 --------VTL------EDGV--------F---------C--GPSCVFTNvnnpraeierknefkktYVERG--VTIGAN 440
Cdd:PRK05289   85 dnntirefVTInrgtvqGGGVtrigdnnlLmayvhvahdCvvGNHVILAN-----------------NATLAghVEVGDY 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2319249963 441 ATI--VCGVH----LGAYSFIGAGAVVTKDVKPHALVLGNPARQVG 480
Cdd:PRK05289  148 AIIggLTAVHqfvrIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRG 193
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 332-480 6.00e-16

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: 77.47  E-value: 6.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 332 IHETAVVDNHVALGKNTKVWHFSHILEGCKIGENCIIGQNVMIGPDVKIGNYCKIQNNVSL--------YKGvtlED-GV 402
Cdd:cd03351     2 IHPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIgeapqdlkYKG---EPtRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 403 FCGPSCV---FTNVNnpRAEIERKNefkKTYVerG--------------------------------VTIGANATI--VC 445
Cdd:cd03351    79 EIGDNNTireFVTIH--RGTAQGGG---VTRI--GnnnllmayvhvahdcvignnvilannatlaghVEIGDYAIIggLS 151

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2319249963 446 GVH----LGAYSFIGAGAVVTKDVKPHALVLGNPARQVG 480
Cdd:cd03351   152 AVHqfcrIGRHAMVGGGSGVVQDVPPYVIAAGNRARLRG 190
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 324-485 6.42e-16

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 75.45  E-value: 6.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 324 SPRV-NDFFIHETAVVDNHVALGKNTKVWH-------FSHIlegcKIGENCIIGQNVMI----GPDVKIGNYCKIQNNVS 391
Cdd:COG0663    10 TPQIhPSAFVAPTAVVIGDVTIGEDVSVWPgavlrgdVGPI----RIGEGSNIQDGVVLhvdpGYPLTIGDDVTIGHGAI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 392 LyKGVTLEDGVFcgpscvftnvnnpraeierknefkktyvergvtIGANATIVCGVHLGAYSFIGAGAVVT--KDVKPHA 469
Cdd:COG0663    86 L-HGCTIGDNVL---------------------------------IGMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGS 131

                         170
                  ....*....|....*.
gi 2319249963 470 LVLGNPARQVGWVSHA 485
Cdd:COG0663   132 LVVGSPAKVVRELTEE 147
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 331-479 7.00e-16

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: 74.76  E-value: 7.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 331 FIHETAVVDNHVALGKNTKVWH-------FSHIlegcKIGENCIIGQNVMI----GPDVKIGNYCKIQNNVSLYkGVTLE 399
Cdd:cd04645     7 FIAPNATVIGDVTLGEGSSVWFgavlrgdVNPI----RIGERTNIQDGSVLhvdpGYPTIIGDNVTVGHGAVLH-GCTIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 400 DGVFcgpscvftnvnnpraeierknefkktyvergvtIGANATIVCGVHLGAYSFIGAGAVVT--KDVKPHALVLGNPAR 477
Cdd:cd04645    82 DNCL---------------------------------IGMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAK 128


                  ..
gi 2319249963 478 QV 479
Cdd:cd04645   129 VV 130
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 334-482 7.43e-16

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 79.81  E-value: 7.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 334 ETAVVDNHVALGKNTKVWHFSHILEGCKIGENCIIGQNVMIgPDVKIGNYCK----------IQNNVS------LYKGVT 397
Cdd:PRK14357  248 NTTYIHYDVEIGMDTIIYPMTFIEGKTRIGEDCEIGPMTRI-VDCEIGNNVKiirseceksvIEDDVSvgpfsrLREGTV 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 398 LEDGV-----------------------FCGPSCVFTNVNNPRAEI------ERKNefkKTYVERGVTIGANATIVCGVH 448
Cdd:PRK14357  327 LKKSVkignfveikkstigentkaqhltYLGDATVGKNVNIGAGTItcnydgKKKN---PTFIEDGAFIGSNSSLVAPVR 403

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2319249963 449 LGAYSFIGAGAVVTKDVKPHALVLGNpARQV---GWV 482
Cdd:PRK14357  404 IGKGALIGAGSVITEDVPPYSLALGR-ARQIvkeGWV 439
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 338-482 9.20e-15

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 76.60  E-value: 9.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 338 VDNHVALGKNTKVWHFSHILEGCKIGENCIIGQNVMIgPDVKIGNYCKIQNnvSLYKGVTLEDGVFCGPscvFTNVnNPR 417
Cdd:COG1207   263 IDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTL-KDSTIGDGVVIKY--SVIEDAVVGAGATVGP---FARL-RPG 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 418 AEIERKN------EFKKTYVERGV-----------TIGANA-----TIVC---GVH-----------------------L 449
Cdd:COG1207   336 TVLGEGVkignfvEVKNSTIGEGSkvnhlsyigdaEIGEGVnigagTITCnydGVNkhrtvigdgafigsntnlvapvtI 415

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2319249963 450 GAYSFIGAGAVVTKDVKPHALVLGNpARQV---GWV 482
Cdd:COG1207   416 GDGATIGAGSTITKDVPAGALAIAR-ARQRnieGWV 450
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 326-482 2.64e-13

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 71.79  E-value: 2.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 326 RVNDFFIHETAVVDNHVAL----GKNTKVWHFSHILEGCKIGENciigqnvmigpdVKIGNYCKIqnnvslyKGVTLEDG 401
Cdd:PRK14354  297 RIVDSTIGDGVTITNSVIEeskvGDNVTVGPFAHLRPGSVIGEE------------VKIGNFVEI-------KKSTIGEG 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 402 V------FCGPSCVFTNVNNPRAEI----ERKNEFKkTYVERGVTIGANATIVCGVHLGAYSFIGAGAVVTKDVKPHALV 471
Cdd:PRK14354  358 TkvshltYIGDAEVGENVNIGCGTItvnyDGKNKFK-TIIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALA 436

                         170
                  ....*....|....
gi 2319249963 472 LGNpARQV---GWV 482
Cdd:PRK14354  437 IAR-ARQVnkeGYV 449
PRK11579 PRK11579
putative oxidoreductase; Provisional
 1-177 7.94e-13

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 69.75  E-value: 7.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963   1 MQDQPKIVVVGGGYWGKN----LIRNFAKLgALAGiceVSQEVAIKLGEEY-KVPVLSWKETLTNT-SYNAVAIATPAKD 74
Cdd:PRK11579    1 MSDKIRVGLIGYGYASKTfhapLIAGTPGL-ELAA---VSSSDATKVKADWpTVTVVSEPQHLFNDpNIDLIVIPTPNDT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963  75 HAELAWQALEANKDVFVEKPLALQMDDAEKVGQLAFARHRILMVGHLLQYHPAFTALKLLAHEGKLGRLQYLYSN----R 150
Cdd:PRK11579   77 HFPLAKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFLTLKALLAEGVLGEVAYFESHfdrfR 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2319249963 151 LNLGKIRREE-----DILWSFAPHDISMILSL 177
Cdd:PRK11579  157 PQVRQRWREQggpgsGIWYDLAPHLLDQAIQL 188
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 365-479 5.17e-12

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


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 62.24  E-value: 5.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 365 NCIIGQNVMIGPDVKIGNYCKIQ--NNVSLYKGVTLedgvfCGPSCVFTNVNNP--RAEIErknefkktyVERGVTIGAN 440
Cdd:cd05825     3 NLTIGDNSWIGEGVWIYNLAPVTigSDACISQGAYL-----CTGSHDYRSPAFPliTAPIV---------IGDGAWVAAE 68

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2319249963 441 ATIVCGVHLGAYSFIGAGAVVTKDVKPHALVLGNPARQV 479
Cdd:cd05825    69 AFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 332-476 8.77e-12

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 65.43  E-value: 8.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 332 IHETAVVDNHVALGKNTKVWHFSHILEGCKIGENCIIGQNVMIGPDVKIGNYCKIQNNVSL--------YKGVtlEDGVF 403
Cdd:PRK12461    2 IHPTAVIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVgdepqdftYKGE--ESRLE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 404 CGPSCVF-TNVNNPRA-------EIERKNEF-KKTYVERGVTIGANATIV--------------------CGVH----LG 450
Cdd:PRK12461   80 IGDRNVIrEGVTIHRGtkgggvtRIGNDNLLmAYSHVAHDCQIGNNVILVngallaghvtvgdraiisgnCLVHqfcrIG 159

                         170       180
                  ....*....|....*....|....*.
gi 2319249963 451 AYSFIGAGAVVTKDVKPHALVLGNPA 476
Cdd:PRK12461  160 ALAMMAGGSRISKDVPPYCMMAGHPT 185
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 331-479 1.04e-11

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 67.06  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 331 FIHETAVVDNHVALgKNTKVWH------FSHiLEGCKIGENCIIGQNVMIGP------DVKIGNYCKIQNNVsLYKGVTL 398
Cdd:PRK14356  289 RIARGAVIHSHCWL-RDAVVSSgatihsFSH-LEGAEVGDGCSVGPYARLRPgavleeGARVGNFVEMKKAV-LGKGAKA 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 399 EDGVFCGPSCVFTNVNNPRAEI----ERKNEfKKTYVERGVTIGANATIVCGVHLGAYSFIGAGAVVTKDVKPHALVLGN 474
Cdd:PRK14356  366 NHLTYLGDAEIGAGANIGAGTItcnyDGVNK-HRTVIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLAIAR 444


                  ....*
gi 2319249963 475 pARQV 479
Cdd:PRK14356  445 -GRQK 448
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 344-481 1.47e-11

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 66.49  E-value: 1.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 344 LGKNTKVwHFSHILEgCKIGENCIIGQNVMIGPDVKIGNYCKIQNNVSLyKGVTLEDGV------FCGPSCVFTNVNNPR 417
Cdd:PRK14360  300 IGENVTV-LYSVVSD-SQIGDGVKIGPYAHLRPEAQIGSNCRIGNFVEI-KKSQLGEGSkvnhlsYIGDATLGEQVNIGA 376

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2319249963 418 AEI------ERKNefkKTYVERGVTIGANATIVCGVHLGAYSFIGAGAVVTKDVKPHALVLGNpARQV---GW 481
Cdd:PRK14360  377 GTItanydgVKKH---RTVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIAR-SRQVikeNW 445
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 378-462 1.57e-11

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: 59.96  E-value: 1.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 378 VKIGNYCKIQNNVSLYKGVTLEDGVFCGPSCVFTNVNNPraeierkNEFKKTYVERGVTIGANATIVCGVHLGAYSFIGA 457
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGP-------NEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGA 73


                  ....*
gi 2319249963 458 GAVVT 462
Cdd:cd00208    74 GAVVT 78
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 325-479 2.73e-11

Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in iron acquisition. It binds iron when it is complexed with pyochelin. It adopts the left-handed parallel beta-helix (LbH) structure, and contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Acyltransferase activity has not been observed in this group.


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 61.82  E-value: 2.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 325 PRVN-DFFIHETAVVDNHVALGKNTKVWHFShilegckigenCIIGQNVMIgpdvKIGNYCKIQNNVSLY--KGVTLEDG 401
Cdd:cd04650     1 PRISpKAYVHPTSYVIGDVVIGELTSVWHYA-----------VIRGDNDSI----YIGKYSNVQENVSIHtdHGYPTEIG 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 402 --VFCGPSCVftnVNNPRaeierknefkktyVERGVTIGANATIVCGVHLGAYSFIGAGAVVT--KDVKPHALVLGNPAR 477
Cdd:cd04650    66 dyVTIGHNAV---VHGAK-------------VGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAK 129


                  ..
gi 2319249963 478 QV 479
Cdd:cd04650   130 VV 131
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 334-481 4.20e-11

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 65.15  E-value: 4.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 334 ETAVVDNHVALGKNTKVWHFSHILEGCKIGENCIIGQNVMIgpdvkigNYCKIQNNVSLYKGVTLEDGVF-----CGPSC 408
Cdd:PRK14355  261 ETTYIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVI-------KGCRIGDDVTVKAGSVLEDSVVgddvaIGPMA 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 409 VFTNVNNPRAEIERKN--EFKKTYVERG-----------VTIGANATIVCG----------------------------- 446
Cdd:PRK14355  334 HLRPGTELSAHVKIGNfvETKKIVMGEGskashltylgdATIGRNVNIGCGtitcnydgvkkhrtvieddvfvgsdvqfv 413

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2319249963 447 --VHLGAYSFIGAGAVVTKDVKPHALVLGNpARQV---GW 481
Cdd:PRK14355  414 apVTVGRNSLIAAGTTVTKDVPPDSLAIAR-SPQVnkeGW 452
PLN02694 PLN02694
serine O-acetyltransferase
 313-480 1.06e-10

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 62.74  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 313 NQATKSLNLESSPRVNDFFihetaVVDNHVA--LGKNTKVWHFShileGCKIGENCIIGqnvmigpdvkignyckiqNNV 390
Cdd:PLN02694  141 TQSRRPLALALHSRISDVF-----AVDIHPAakIGKGILFDHAT----GVVIGETAVIG------------------NNV 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 391 SLYKGVTLE-DGVFCGPscvftnvNNPRaeierknefkktyVERGVTIGANATIVCGVHLGAYSFIGAGAVVTKDVKPHA 469
Cdd:PLN02694  194 SILHHVTLGgTGKACGD-------RHPK-------------IGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRT 253

                         170
                  ....*....|.
gi 2319249963 470 LVLGNPARQVG 480
Cdd:PLN02694  254 TAVGNPARLVG 264
cysE PRK11132
serine acetyltransferase; Provisional
 368-480 1.32e-09

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 58.94  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 368 IGQNVMI--GPDVKIGNYCKIQNNVSLYKGVTLE-DGVFCGPscvftnvNNPRaeierknefkktyVERGVTIGANATIV 444
Cdd:PRK11132  150 IGRGIMLdhATGIVIGETAVIENDVSILQSVTLGgTGKTSGD-------RHPK-------------IREGVMIGAGAKIL 209

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2319249963 445 CGVHLGAYSFIGAGAVVTKDVKPHALVLGNPARQVG 480
Cdd:PRK11132  210 GNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVG 245
PLN02739 PLN02739
serine acetyltransferase
 302-482 7.80e-09

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 57.35  E-value: 7.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 302 AKEGLRVLEVL-NQATKSLNLESSPRVNDFF---IHETAVVDNHVALGKNTkvwhfshileGCKIGENCIIGqnvmigpd 377
Cdd:PLN02739  174 ALQAYRVAHKLwKQGRKLLALALQSRVSEVFgidIHPAARIGKGILLDHGT----------GVVIGETAVIG-------- 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 378 vkignyckiqNNVSLYKGVTLedgvfcGPSCVFTNVNNPRaeierknefkktyVERGVTIGANATIVCGVHLGAYSFIGA 457
Cdd:PLN02739  236 ----------DRVSILHGVTL------GGTGKETGDRHPK-------------IGDGALLGACVTILGNISIGAGAMVAA 286

                         170       180
                  ....*....|....*....|....*
gi 2319249963 458 GAVVTKDVKPHALVLGNPARQVGWV 482
Cdd:PLN02739  287 GSLVLKDVPSHSMVAGNPAKLIGFV 311
PRK10502 PRK10502
putative acyl transferase; Provisional
 368-479 2.23e-08

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 53.80  E-value: 2.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 368 IGQNVMIGPDVK--------IGNYCKIQNNVSLYkgvTLEDgVFCGPSCVF-------TNVNNPRaeierKNEF----KK 428
Cdd:PRK10502   54 IGKGVVIRPSVRitypwkltIGDYAWIGDDVWLY---NLGE-ITIGAHCVIsqksylcTGSHDYS-----DPHFdlntAP 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2319249963 429 TYVERGVTIGANATIVCGVHLGAYSFIGAGAVVTKDVKPHALVLGNPARQV 479
Cdd:PRK10502  125 IVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPI 175
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 331-462 3.10e-08

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: 52.98  E-value: 3.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 331 FIHETAVVDNHVALGKNtkVWhfshILEGCKIGENCIIGQNVMIGPDVKIGNYCKIQNNVsLYKGVTLEDGVFCGPSCVF 410
Cdd:cd05636    19 WIGEGAIVRSGAYIEGP--VI----IGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSI-IMDGTKVPHLNYVGDSVLG 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2319249963 411 TNVN--------NPRA-EIERKNEFKKTYVERG-----------VTIGANATIVCGVHLGAYSFIGAGAVVT 462
Cdd:cd05636    92 ENVNlgagtitaNLRFdDKPVKVRLKGERVDTGrrklgaiigdgVKTGINVSLNPGVKIGPGSWVYPGCVVR 163
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 361-477 8.45e-08

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 52.70  E-value: 8.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 361 KIGENCIIGQNVMI--GPDVKIGNYCKIQNNVSLYKG--VTLEDGVFCGPSCVFTNVNNPRAEIERKN----EFKKTyVE 432
Cdd:PRK09527   57 TVGENAWVEPPVYFsyGSNIHIGRNFYANFNLTIVDDytVTIGDNVLIAPNVTLSVTGHPVHHELRKNgemySFPIT-IG 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2319249963 433 RGVTIGANATIVCGVHLGAYSFIGAGAVVTKDVKPHALVLGNPAR 477
Cdd:PRK09527  136 NNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCR 180
GFO_IDH_MocA_C pfam02894
Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or ...
 167-318 1.15e-07

Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 427044  Cd Length: 203  Bit Score: 52.42  E-value: 1.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 167 APHDISMILSLVNEKPSVVKAMGGyflhksiADVTTTHLEFPSGVQAHIFVSWLH--PHKEQKLVVVGSKGMAVFDDAKP 244
Cdd:pfam02894  47 GIHTIDLLIYLFGEPPSVVAVYAS-------EDTAFATLEFKNGAVGTLETSGGSivEANGHRISIHGTKGSIELDGIDD 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 245 WTQKLAFySHQIHWRDGMPFPDKADATycslTEEEPL------TRECQHFIDCVKTREQPITDAKEGLRVLEVLNQATKS 318
Cdd:pfam02894 120 GLLSVTV-VGEPGWATDDPMVRKGGDE----VPEFLGsfaggyLLEYDAFLEAVRGGKVVLVDAEDGLYALAVIEAAYES 194
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 352-481 1.15e-07

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 54.10  E-value: 1.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 352 HFSHILEgckIGENCIIGQNVMIGPDVKIGNYCKIQnNVSLYKGVTLEDGVFCGPscvFTNVnNPRAEIERK----N--E 425
Cdd:PRK14353  264 FFSYDTV---IGRDVVIEPNVVFGPGVTVASGAVIH-AFSHLEGAHVGEGAEVGP---YARL-RPGAELGEGakvgNfvE 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 426 FKKTYVERGV-----------TIGANA-----TIVC---GV-----HLGAYSFIG------------------AGAVVTK 463
Cdd:PRK14353  336 VKNAKLGEGAkvnhltyigdaTIGAGAnigagTITCnydGFnkhrtEIGAGAFIGsnsalvapvtigdgayiaSGSVITE 415

                         170       180
                  ....*....|....*....|.
gi 2319249963 464 DVKPHALVLGNpARQV---GW 481
Cdd:PRK14353  416 DVPDDALALGR-ARQEtkpGW 435
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
359-388 1.38e-07

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 47.33  E-value: 1.38e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 2319249963 359 GCKIGENCIIGQNVMIGPDVKIGNYCKIQN 388
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 360-477 1.40e-07

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 51.74  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 360 CKIGENCIIGQNVMIGPDVKIGNYCKIQ--NNVSLYKGVTledgvfcgpscVFTnVNNPRAEIERKN--EF-KKTYVERG 434
Cdd:PRK10092   68 CDYGYNIFLGNNFYANFDCVMLDVCPIRigDNCMLAPGVH-----------IYT-ATHPLDPVARNSgaELgKPVTIGNN 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2319249963 435 VTIGANATIVCGVHLGAYSFIGAGAVVTKDVKPHALVLGNPAR 477
Cdd:PRK10092  136 VWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPAR 178
PLN02357 PLN02357
serine acetyltransferase
 368-480 3.50e-07

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 52.19  E-value: 3.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 368 IGQNVMI--GPDVKIGNYCKIQNNVSLYKGVTLE-DGVFCGPscvftnvNNPRaeierknefkktyVERGVTIGANATIV 444
Cdd:PLN02357  235 IGQGILLdhATGVVIGETAVVGNNVSILHNVTLGgTGKQSGD-------RHPK-------------IGDGVLIGAGTCIL 294

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2319249963 445 CGVHLGAYSFIGAGAVVTKDVKPHALVLGNPARQVG 480
Cdd:PLN02357  295 GNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLIG 330
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 358-442 5.52e-07

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: 47.19  E-value: 5.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 358 EGCKIGE-----NCIIGQNVMIGPDVKIGNyCKIQNNVSLYKGVTLEDGVFCgpscvftnvnnPRAEIERKNEFKKTYVE 432
Cdd:cd04652     4 ENTQVGEktsikRSVIGANCKIGKRVKITN-CVIMDNVTIEDGCTLENCIIG-----------NGAVIGEKCKLKDCLVG 71

                          90
                  ....*....|
gi 2319249963 433 RGVTIGANAT 442
Cdd:cd04652    72 SGYRVEAGTE 81
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 329-481 2.21e-06

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 50.03  E-value: 2.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 329 DFFIHETAVVDNHVALGKNTKVWHFShILEGCKIGENCII-----------GQNVMIGP------------DVKIGNYCK 385
Cdd:PRK09451  271 DVEIDTNVIIEGNVTLGNRVKIGAGC-VLKNCVIGDDCEIspysvvedanlGAACTIGPfarlrpgaelaeGAHVGNFVE 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 386 IQNnVSLYKGVTLEDGVFCGPSCVFTNVNNPRAEI----ERKNEFKkTYVERGVTIGANATIVCGVHLGAYSFIGAGAVV 461
Cdd:PRK09451  350 MKK-ARLGKGSKAGHLTYLGDAEIGDNVNIGAGTItcnyDGANKFK-TIIGDDVFVGSDTQLVAPVTVGKGATIGAGTTV 427

                         170       180
                  ....*....|....*....|..
gi 2319249963 462 TKDVKPHALVLGN-PARQV-GW 481
Cdd:PRK09451  428 TRDVAENELVISRvPQRHIqGW 449
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 356-414 2.40e-06

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: 45.31  E-value: 2.40e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2319249963 356 ILEGCKIGENCIIGqNVMIGPDVKIGNYCKIQNNVsLYKGVTLEDGVFCGPSCVFTNVN 414
Cdd:cd03356     2 IGESTVIGENAIIK-NSVIGDNVRIGDGVTITNSI-LMDNVTIGANSVIVDSIIGDNAV 58
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 336-466 2.40e-06

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: 46.99  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 336 AVVDNHVALGKNTKVWHFSHILEGCKIGENCIIGQNVMIGPDVKIGNYCKIQNNVSLykGVTLEdgvfcgPScvftnvnn 415
Cdd:cd03350     8 AIIRDGAFIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVI--GGVLE------PL-------- 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2319249963 416 praeierknEFKKTYVERGVTIGANATIVCGVHLGAYSFIGAGAVVTKDVK 466
Cdd:cd03350    72 ---------QATPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTP 113
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 343-402 4.98e-06

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: 44.49  E-value: 4.98e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 343 ALGKNTKVWHFSHIlEGCKIGENCIIGQNVMIG-----PDVKIGNYCKIQ-----NNVSLYKGVTLEDGV 402
Cdd:cd05787     1 VIGRGTSIGEGTTI-KNSVIGRNCKIGKNVVIDnsyiwDDVTIEDGCTIHhsivaDGAVIGKGCTIPPGS 69
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 332-477 5.34e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 48.60  E-value: 5.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 332 IHETAVVDNHVALGKNTKVWHFSHILEGCKIGENCIIGQNVMIGPD-----VKIGNYCKI-QNNvslykGVTLEDGVFCG 405
Cdd:PRK00892  139 IGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVIGSDgfgfaNDRGGWVKIpQLG-----RVIIGDDVEIG 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 406 PSCVftnvnnpraeIERkNEFKKTYVERG------------VTIGANATIV--CGV--------------------HL-- 449
Cdd:PRK00892  214 ANTT----------IDR-GALDDTVIGEGvkidnlvqiahnVVIGRHTAIAaqVGIagstkigrycmiggqvgiagHLei 282

                         170       180
                  ....*....|....*....|....*....
gi 2319249963 450 GAYSFIGAGAVVTKDVKPHALVLGN-PAR 477
Cdd:PRK00892  283 GDGVTITAMSGVTKSIPEPGEYSSGiPAQ 311
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 362-477 5.63e-06

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 47.18  E-value: 5.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 362 IGENCIIGQNVMIG--PDVKIGNYCKIQNNVSLykgvTLEDGVFCGPSCVFTNVNNPraEIERKNEFKKTYVERGVTIGA 439
Cdd:PRK09677   68 FGDNVQVNDYVHIAciESITIGRDTLIASKVFI----TDHNHGSFKHSDDFSSPNLP--PDMRTLESSAVVIGQRVWIGE 141

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2319249963 440 NATIVCGVHLGAYSFIGAGAVVTKDVKPHALVLGNPAR 477
Cdd:PRK09677  142 NVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAK 179
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 331-483 8.41e-06

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: 45.82  E-value: 8.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 331 FIHETAVVDNHVALGKntkvwhfshilegckigeNCIIGQNVMIGPD---VKIGNYCKIQNNVSLY----KGVTLEDGVF 403
Cdd:cd04745     8 FVHPTAVLIGDVIIGK------------------NCYIGPHASLRGDfgrIVIRDGANVQDNCVIHgfpgQDTVLEENGH 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 404 CGPSCVFTNVNnpraeierknefkktyVERGVTIGANATIVCGVHLGAYSFIGAGAVVTK--DVKPHALVLGNPARQVGW 481
Cdd:cd04745    70 IGHGAILHGCT----------------IGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVIRE 133


                  ..
gi 2319249963 482 VS 483
Cdd:cd04745   134 LS 135
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 330-392 1.05e-05

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: 43.39  E-value: 1.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2319249963 330 FFIHETAVVDNHVALGKNTKVWHFSHILE--------GCKIGENCIIGQNVMIGPDVKIGNYCKIQNNVSL 392
Cdd:cd00208     7 VKIHPKAVIRGPVVIGDNVNIGPGAVIGAatgpneknPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVV 77
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 329-484 1.20e-05

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 47.62  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 329 DFFIHETAVVDNHVA----LGKNTKVWHFSHILEGCKIGENCIIG-----QNVMIG-----P------DVKIGNYCKIqn 388
Cdd:PRK14352  306 DVTVGEGASVVRTHGseseIGAGATVGPFTYLRPGTVLGEEGKLGafvetKNATIGrgtkvPhltyvgDADIGEHSNI-- 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 389 nvslykgvtledgvfcGPSCVFTNVNNpraeiERKNefkKTYVERGVTIGANATIVCGVHLG--AYSfiGAGAVVTKDVK 466
Cdd:PRK14352  384 ----------------GASSVFVNYDG-----VNKH---RTTIGSHVRTGSDTMFVAPVTVGdgAYT--GAGTVIREDVP 437

                         170       180
                  ....*....|....*....|
gi 2319249963 467 PHALVL-GNPARQV-GWVSH 484
Cdd:PRK14352  438 PGALAVsEGPQRNIeGWVQR 457
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
341-369 1.45e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 41.94  E-value: 1.45e-05
                          10        20
                  ....*....|....*....|....*....
gi 2319249963 341 HVALGKNTKVWHFSHILEGCKIGENCIIG 369
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 324-382 3.68e-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: 42.84  E-value: 3.68e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2319249963 324 SPRVndfFIHETAVVDNHVALGKntkvwhfSHILEGCKIgENCIIGQNVMIGPDVKIGN 382
Cdd:cd04651    32 FRGV---RVGSGSVVEDSVIMPN-------VGIGRNAVI-RRAIIDKNVVIPDGVVIGG 79
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 320-400 5.31e-05

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: 41.46  E-value: 5.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 320 NLESSPRVNDFFIHETAVVDNHVALGKNTKVWHfSHILEGCKIGENCIIgQNVMIGPDVKIGNYCKIQNNVSLYKGVTLE 399
Cdd:cd03356     1 LIGESTVIGENAIIKNSVIGDNVRIGDGVTITN-SILMDNVTIGANSVI-VDSIIGDNAVIGENVRVVNLCIIGDDVVVE 78


                  .
gi 2319249963 400 D 400
Cdd:cd03356    79 D 79
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 361-400 7.16e-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: 41.37  E-value: 7.16e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2319249963 361 KIGENCIIGQNVMIGPDVKIGNYCKIQNNVSLyKGVTLED 400
Cdd:cd05824     7 KIGKTAKIGPNVVIGPNVTIGDGVRLQRCVIL-SNSTVRD 45
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 359-466 1.81e-04

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: 40.25  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 359 GCKIGENCIIGQNVmIGPDVKIGNYCKIQNnvslykgvtledgvfcgpscvftnvnnpraeierknefkkTYVERGVTIG 438
Cdd:cd05787     5 GTSIGEGTTIKNSV-IGRNCKIGKNVVIDN----------------------------------------SYIWDDVTIE 43

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2319249963 439 ANATI----VC-GVHLGAYSFIGAGAVVTKDVK 466
Cdd:cd05787    44 DGCTIhhsiVAdGAVIGKGCTIPPGSLISFGVV 76
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 327-481 1.95e-04

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 43.81  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 327 VNDFFIHETAVVDNHVAL-----GKNTKVWHFSHILEGCKIGENciigqnvmigpdVKIGNYCKIQNnVSLYKGVTLEDG 401
Cdd:PRK14358  303 VTDSVLHEGAVIKPHSVLegaevGAGSDVGPFARLRPGTVLGEG------------VHIGNFVETKN-ARLDAGVKAGHL 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 402 VFCGPSCVF--TNVNNPR--AEIERKNEFKKTyVERGVTIGANATIVCGVHLGAYSFIGAGAVVTKDVKPHALVL--GNP 475
Cdd:PRK14358  370 AYLGDVTIGaeTNVGAGTivANFDGVNKHQSK-VGAGVFIGSNTTLIAPRVVGDAAFIAAGSAVHDDVPEGAMAVarGKQ 448


                  ....*.
gi 2319249963 476 ARQVGW 481
Cdd:PRK14358  449 RNLEGW 454
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 431-474 2.47e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 43.20  E-value: 2.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2319249963 431 VERGVTIGANATIVCGVHLGAYSFIGAGAVVTKDVK--------P-----HALVLGN 474
Cdd:PRK00892  115 IGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKigadcrlhAnvtiyHAVRIGN 171
PRK10206 PRK10206
putative oxidoreductase; Provisional
 56-143 3.25e-04

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 42.89  E-value: 3.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963  56 ETLTNTSYNAVAIATPAKDHAELAWQALEANKDVFVEKPLALQMDDAEKVgqLAFARHRILMVGHLL--QYHPAFTALKL 133
Cdd:PRK10206   58 EVLNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTLAEAKEL--FALAKSKGLTVTPYQnrRFDSCFLTAKK 135

                          90
                  ....*....|
gi 2319249963 134 LAHEGKLGRL 143
Cdd:PRK10206  136 AIESGKLGEI 145
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 337-400 4.65e-04

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: 39.10  E-value: 4.65e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2319249963 337 VVDNHVALGKNTKVwHFSHILEGCKIGENCIIGQNVmIGPDVKIGNYCKIQNNVSLYKGVTLED 400
Cdd:cd05787    18 VIGRNCKIGKNVVI-DNSYIWDDVTIEDGCTIHHSI-VADGAVIGKGCTIPPGSLISFGVVIGD 79
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
354-382 5.42e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 37.32  E-value: 5.42e-04
                          10        20
                  ....*....|....*....|....*....
gi 2319249963 354 SHILEGCKIGENCIIGQNVMIGPDVKIGN 382
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
361-394 9.41e-04

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 36.65  E-value: 9.41e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2319249963 361 KIGENCIIGQNVMIGpdVKIGNYCKIQNNVSLYK 394
Cdd:pfam14602   2 IIGDNCLIGANSGIG--VSLGDNCVVGAGVVITA 33
PRK10191 PRK10191
putative acyl transferase; Provisional
 434-477 1.83e-03

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 38.72  E-value: 1.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2319249963 434 GVTIGANATIVCGVHLGAYSFIGAGAVVTKDVKPHALVLGNPAR 477
Cdd:PRK10191   98 GVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKAR 141
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
365-392 2.12e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.78  E-value: 2.12e-03
                          10        20
                  ....*....|....*....|....*...
gi 2319249963 365 NCIIGQNVMIGPDVKIGNYCKIQNNVSL 392
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVII 28
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 362-489 3.75e-03

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


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 38.35  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 362 IGENCIIGQNVMIGPD---VKIGNYCKIQNNV------SLYKG------VTLEDGVFCGPSCVftnvnnpraeierkneF 426
Cdd:cd03359    24 LNGKTIIQSDVIIRGDlatVSIGRYCILSEGCvirppfKKFSKgvaffpLHIGDYVFIGENCV----------------V 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2319249963 427 KKTYVERGVTIGANATIVCGVHLGAYSFIGAGAVVTKD--VKPHALVLGNPARQVGWVSHAGERL 489
Cdd:cd03359    88 NAAQIGSYVHIGKNCVIGRRCIIKDCVKILDGTVVPPDtvIPPYSVVSGRPARFIGELPECTQEL 152
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
428-457 6.45e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 34.23  E-value: 6.45e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2319249963 428 KTYVERGVTIGANATIVCGVHLGAYSFIGA 457
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 326-381 8.16e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 38.70  E-value: 8.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319249963 326 RVNDFFIHETAVVDNH---------VALGKNTKVWHfSHILEGCKIGENC-----IIGQNVMIGPDVKIG 381
Cdd:PRK05293  290 KVKNSLVVEGCVVYGTvehsvlfqgVQVGEGSVVKD-SVIMPGAKIGENVvieraIIGENAVIGDGVIIG 358
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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