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Conserved domains on  [gi|743522156|ref|WP_039039449|]
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MULTISPECIES: UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase [Aeromonas]

Protein Classification

UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase( domain architecture ID 11479317)

UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase catalyzes the N-acylation of UDP-3-O-(hydroxytetradecanoyl)glucosamine using 3-hydroxytetradecanoyl-ACP as the acyl donor

CATH:  3.40.1390.10|2.160.10.10
Gene Ontology:  GO:0103118|GO:0009245
PubMed:  17360522|15500694|11747907
SCOP:  4004951|4002830

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 1-339 0e+00

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


:

Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 550.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156   1 MAFTLAQLAQQLGAEVHGDGTREIRKVATLEKAGEGEIAFLSNKKYRHFLEQSKATAVLITEADLPFCP--TNALVLKDP 78
Cdd:PRK00892   1 MSLTLAELAELLGAELVGDGDIEITGVASLEEAGPGQISFLANPKYRKQLATTKAGAVIVSPDDAEFVPagNALLVVKNP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  79 YVGFARVAQLLD--TTPQPAMDIHPSAVIAADVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVGKDTRLGARSRLWAN 156
Cdd:PRK00892  81 YLAFARLAQLFDppATPSPAAGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHAN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 157 VTLYHNVTLGTDCLVQAGTVIGADGFGYANERGEWIKIPQLGGVTIGNRVEIGACTTIDRGALEDTRIADNVIIDNQCQI 236
Cdd:PRK00892 161 VTIYHAVRIGNRVIIHSGAVIGSDGFGFANDRGGWVKIPQLGRVIIGDDVEIGANTTIDRGALDDTVIGEGVKIDNLVQI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 237 AHNVEIGYGTAVAGSTVMAGSLKVGKYCIIGGASVFNGHMEICDQATVTGMAMVMRPITEPGIYSSGIPLQTNKEWRKTA 316
Cdd:PRK00892 241 AHNVVIGRHTAIAAQVGIAGSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPGEYSSGIPAQPNKEWLRTA 320

                        330       340
                 ....*....|....*....|...
gi 743522156 317 ARVMRIEEMHKRLSKLEKKLDQE 339
Cdd:PRK00892 321 ARLRRLDELRKRLKALEKKVEQL 343
 
Name Accession Description Interval E-value
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 1-339 0e+00

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 550.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156   1 MAFTLAQLAQQLGAEVHGDGTREIRKVATLEKAGEGEIAFLSNKKYRHFLEQSKATAVLITEADLPFCP--TNALVLKDP 78
Cdd:PRK00892   1 MSLTLAELAELLGAELVGDGDIEITGVASLEEAGPGQISFLANPKYRKQLATTKAGAVIVSPDDAEFVPagNALLVVKNP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  79 YVGFARVAQLLD--TTPQPAMDIHPSAVIAADVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVGKDTRLGARSRLWAN 156
Cdd:PRK00892  81 YLAFARLAQLFDppATPSPAAGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHAN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 157 VTLYHNVTLGTDCLVQAGTVIGADGFGYANERGEWIKIPQLGGVTIGNRVEIGACTTIDRGALEDTRIADNVIIDNQCQI 236
Cdd:PRK00892 161 VTIYHAVRIGNRVIIHSGAVIGSDGFGFANDRGGWVKIPQLGRVIIGDDVEIGANTTIDRGALDDTVIGEGVKIDNLVQI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 237 AHNVEIGYGTAVAGSTVMAGSLKVGKYCIIGGASVFNGHMEICDQATVTGMAMVMRPITEPGIYSSGIPLQTNKEWRKTA 316
Cdd:PRK00892 241 AHNVVIGRHTAIAAQVGIAGSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPGEYSSGIPAQPNKEWLRTA 320

                        330       340
                 ....*....|....*....|...
gi 743522156 317 ARVMRIEEMHKRLSKLEKKLDQE 339
Cdd:PRK00892 321 ARLRRLDELRKRLKALEKKVEQL 343
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 2-335 0e+00

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: 512.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156   2 AFTLAQLAQQLGAEVHGDGTREIRKVATLEKAGEGEIAFLSNKKYRHFLEQSKATAVLITEADLPFCP-TNALVLKDPYV 80
Cdd:COG1044    1 SFTLAELAELLGGELVGDGDLEITGVAPLEEAGPGDLSFLANPKYAKQLATTKASAVIVPPDFAAALPgLALIVVDNPYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  81 GFARVAQLLDTTPQPAMDIHPSAVIAADVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVGKDTRLGARSRLWANVTLY 160
Cdd:COG1044   81 AFAKLLQLFYPPPAPAPGIHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 161 HNVTLGTDCLVQAGTVIGADGFGYAN-ERGEWIKIPQLGGVTIGNRVEIGACTTIDRGALEDTRIADNVIIDNQCQIAHN 239
Cdd:COG1044  161 ERCVIGDRVIIHSGAVIGADGFGFAPdEDGGWVKIPQLGRVVIGDDVEIGANTTIDRGALGDTVIGDGTKIDNLVQIAHN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 240 VEIGYGTAVAGSTVMAGSLKVGKYCIIGGASVFNGHMEICDQATVTGMAMVMRPITEPGIYsSGIPLQTNKEWRKTAARV 319
Cdd:COG1044  241 VRIGEHTAIAAQVGIAGSTKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVY-SGSPAQPHREWLRNAAAL 319

                        330
                 ....*....|....*.
gi 743522156 320 MRIEEMHKRLSKLEKK 335
Cdd:COG1044  320 RRLPELAKRLKELEKK 335
lipid_A_lpxD TIGR01853
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, an ...
 7-329 8.79e-139

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


Pssm-ID: 273834 [Multi-domain]  Cd Length: 324  Bit Score: 396.28  E-value: 8.79e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156    7 QLAQQLGAEVHGDGTREIRKVATLEKAGEGEIAFLSNKKYRHFLEQSKATAVLITEADLP-FCPTNALVLKDPYVGFARV 85
Cdd:TIGR01853   1 ELAERLGAELKGNGDIVITGVAPLEKAKANHITFLANPKYLKHLKSSQAGAVIVSPDDQGlPAKCAALVVKDPYLAFAKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156   86 AQLLDTTPQPAMDIHPSAVIAADVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVGKDTRLGARSRLWANVTLYHNVTL 165
Cdd:TIGR01853  81 AELFDPPPKREAGIHPTAVVDPSAKIGDGVTIGPNVVIGAGVEIGENVIIGPGVVIGDDVVIGDGSRIHPNVVIYERVQL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  166 GTDCLVQAGTVIGADGFGYA-NERGEWIKIPQLGGVTIGNRVEIGACTTIDRGALEDTRIADNVIIDNQCQIAHNVEIGY 244
Cdd:TIGR01853 161 GKNVIIHSGAVIGSDGFGYAhTANGGHVKIPQIGRVIIEDDVEIGANTTIDRGAFDDTIIGEGTKIDNLVQIAHNCRIGE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  245 GTAVAGSTVMAGSLKVGKYCIIGGASVFNGHMEICDQATVTGMAMVMRPITEPGIYsSGIPLQTNKEWRKTAARVMRIEE 324
Cdd:TIGR01853 241 NCIIVAQVGIAGSTKIGRNVIIGGQVGVAGHLEIGDNVTIGAKSGVTKSIPPPGVY-GGIPARPNKEWLRIAAKVKRLPE 319


                  ....*
gi 743522156  325 MHKRL 329
Cdd:TIGR01853 320 LRKRI 324
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 108-313 1.73e-106

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: 309.72  E-value: 1.73e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 108 DVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVGKDTRLGARSRLWANVTLYHNVTLGTDCLVQAGTVIGADGFGYANE 187
Cdd:cd03352    1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSDGFGFAPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 188 RGEWIKIPQLGGVTIGNRVEIGACTTIDRGALEDTRIADNVIIDNQCQIAHNVEIGYGTAVAGSTVMAGSLKVGKYCIIG 267
Cdd:cd03352   81 GGGWVKIPQLGGVIIGDDVEIGANTTIDRGALGDTVIGDGTKIDNLVQIAHNVRIGENCLIAAQVGIAGSTTIGDNVIIG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 743522156 268 GASVFNGHMEICDQATVTGMAMVMRpITEPGIYSSGIPLQTNKEWR 313
Cdd:cd03352  161 GQVGIAGHLTIGDGVVIGAGSGVTS-IVPPGEYVSGTPAQPHREWL 205
LpxD pfam04613
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, LpxD; UDP-3-O-[3-hydroxymyristoyl] ...
 22-88 2.58e-24

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, LpxD; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase (EC 2.3.1.-) catalyzes an early step in lipid A biosynthesis: UDP-3-O-(3-hydroxytetradecanoyl)glucosamine + (R)-3-hydroxytetradecanoyl- [acyl carrier protein] -> UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + [acyl carrier protein]. Members of this family also contain a hexapeptide repeat (pfam00132). This family constitutes the non-repeating region of LPXD proteins.


Pssm-ID: 461366 [Multi-domain]  Cd Length: 69  Bit Score: 94.10  E-value: 2.58e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743522156   22 REIRKVATLEKAGEGEIAFLSNKKYRHFLEQSKATAVLITEADLPFCPTNA--LVLKDPYVGFARVAQL 88
Cdd:pfam04613   1 LEITGVAPLEEAGPGDLSFLANPKYAKYLATTKASAVIVPPDFAPQAPATAtlLVVDNPYLAFAKLLQL 69
 
Name Accession Description Interval E-value
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 1-339 0e+00

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 550.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156   1 MAFTLAQLAQQLGAEVHGDGTREIRKVATLEKAGEGEIAFLSNKKYRHFLEQSKATAVLITEADLPFCP--TNALVLKDP 78
Cdd:PRK00892   1 MSLTLAELAELLGAELVGDGDIEITGVASLEEAGPGQISFLANPKYRKQLATTKAGAVIVSPDDAEFVPagNALLVVKNP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  79 YVGFARVAQLLD--TTPQPAMDIHPSAVIAADVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVGKDTRLGARSRLWAN 156
Cdd:PRK00892  81 YLAFARLAQLFDppATPSPAAGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHAN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 157 VTLYHNVTLGTDCLVQAGTVIGADGFGYANERGEWIKIPQLGGVTIGNRVEIGACTTIDRGALEDTRIADNVIIDNQCQI 236
Cdd:PRK00892 161 VTIYHAVRIGNRVIIHSGAVIGSDGFGFANDRGGWVKIPQLGRVIIGDDVEIGANTTIDRGALDDTVIGEGVKIDNLVQI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 237 AHNVEIGYGTAVAGSTVMAGSLKVGKYCIIGGASVFNGHMEICDQATVTGMAMVMRPITEPGIYSSGIPLQTNKEWRKTA 316
Cdd:PRK00892 241 AHNVVIGRHTAIAAQVGIAGSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPGEYSSGIPAQPNKEWLRTA 320

                        330       340
                 ....*....|....*....|...
gi 743522156 317 ARVMRIEEMHKRLSKLEKKLDQE 339
Cdd:PRK00892 321 ARLRRLDELRKRLKALEKKVEQL 343
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 2-335 0e+00

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: 512.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156   2 AFTLAQLAQQLGAEVHGDGTREIRKVATLEKAGEGEIAFLSNKKYRHFLEQSKATAVLITEADLPFCP-TNALVLKDPYV 80
Cdd:COG1044    1 SFTLAELAELLGGELVGDGDLEITGVAPLEEAGPGDLSFLANPKYAKQLATTKASAVIVPPDFAAALPgLALIVVDNPYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  81 GFARVAQLLDTTPQPAMDIHPSAVIAADVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVGKDTRLGARSRLWANVTLY 160
Cdd:COG1044   81 AFAKLLQLFYPPPAPAPGIHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 161 HNVTLGTDCLVQAGTVIGADGFGYAN-ERGEWIKIPQLGGVTIGNRVEIGACTTIDRGALEDTRIADNVIIDNQCQIAHN 239
Cdd:COG1044  161 ERCVIGDRVIIHSGAVIGADGFGFAPdEDGGWVKIPQLGRVVIGDDVEIGANTTIDRGALGDTVIGDGTKIDNLVQIAHN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 240 VEIGYGTAVAGSTVMAGSLKVGKYCIIGGASVFNGHMEICDQATVTGMAMVMRPITEPGIYsSGIPLQTNKEWRKTAARV 319
Cdd:COG1044  241 VRIGEHTAIAAQVGIAGSTKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVY-SGSPAQPHREWLRNAAAL 319

                        330
                 ....*....|....*.
gi 743522156 320 MRIEEMHKRLSKLEKK 335
Cdd:COG1044  320 RRLPELAKRLKELEKK 335
lipid_A_lpxD TIGR01853
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, an ...
 7-329 8.79e-139

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


Pssm-ID: 273834 [Multi-domain]  Cd Length: 324  Bit Score: 396.28  E-value: 8.79e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156    7 QLAQQLGAEVHGDGTREIRKVATLEKAGEGEIAFLSNKKYRHFLEQSKATAVLITEADLP-FCPTNALVLKDPYVGFARV 85
Cdd:TIGR01853   1 ELAERLGAELKGNGDIVITGVAPLEKAKANHITFLANPKYLKHLKSSQAGAVIVSPDDQGlPAKCAALVVKDPYLAFAKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156   86 AQLLDTTPQPAMDIHPSAVIAADVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVGKDTRLGARSRLWANVTLYHNVTL 165
Cdd:TIGR01853  81 AELFDPPPKREAGIHPTAVVDPSAKIGDGVTIGPNVVIGAGVEIGENVIIGPGVVIGDDVVIGDGSRIHPNVVIYERVQL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  166 GTDCLVQAGTVIGADGFGYA-NERGEWIKIPQLGGVTIGNRVEIGACTTIDRGALEDTRIADNVIIDNQCQIAHNVEIGY 244
Cdd:TIGR01853 161 GKNVIIHSGAVIGSDGFGYAhTANGGHVKIPQIGRVIIEDDVEIGANTTIDRGAFDDTIIGEGTKIDNLVQIAHNCRIGE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  245 GTAVAGSTVMAGSLKVGKYCIIGGASVFNGHMEICDQATVTGMAMVMRPITEPGIYsSGIPLQTNKEWRKTAARVMRIEE 324
Cdd:TIGR01853 241 NCIIVAQVGIAGSTKIGRNVIIGGQVGVAGHLEIGDNVTIGAKSGVTKSIPPPGVY-GGIPARPNKEWLRIAAKVKRLPE 319


                  ....*
gi 743522156  325 MHKRL 329
Cdd:TIGR01853 320 LRKRI 324
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 108-313 1.73e-106

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: 309.72  E-value: 1.73e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 108 DVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVGKDTRLGARSRLWANVTLYHNVTLGTDCLVQAGTVIGADGFGYANE 187
Cdd:cd03352    1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSDGFGFAPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 188 RGEWIKIPQLGGVTIGNRVEIGACTTIDRGALEDTRIADNVIIDNQCQIAHNVEIGYGTAVAGSTVMAGSLKVGKYCIIG 267
Cdd:cd03352   81 GGGWVKIPQLGGVIIGDDVEIGANTTIDRGALGDTVIGDGTKIDNLVQIAHNVRIGENCLIAAQVGIAGSTTIGDNVIIG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 743522156 268 GASVFNGHMEICDQATVTGMAMVMRpITEPGIYSSGIPLQTNKEWR 313
Cdd:cd03352  161 GQVGIAGHLTIGDGVVIGAGSGVTS-IVPPGEYVSGTPAQPHREWL 205
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 96-290 6.82e-28

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: 109.34  E-value: 6.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  96 AMDIHPSaviaadvqlgervaiganAVIESGVVLGDDVRIGPGCFVGKDTRLGARSRLWANVTLYHNVTLGTDCLVQAGT 175
Cdd:COG1043    1 MAMIHPT------------------AIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFA 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 176 VIGADG--FGYANERGEwikipqlggVTIGNRVEIGACTTIDRGALED---TRIADNVIIDNQCQIAHNVEIGYGTAVAG 250
Cdd:COG1043   63 SIGEEPqdLKYKGEPTR---------LEIGDNNTIREFVTIHRGTVQGggvTRIGDDNLLMAYVHVAHDCVVGNNVILAN 133

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 743522156 251 STVMAGSLKVGKYCIIGGASVFNGHMEICDQATVTGMAMV 290
Cdd:COG1043  134 NATLAGHVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGV 173
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 99-292 2.02e-27

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: 107.90  E-value: 2.02e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  99 IHPSAVIAADVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVGKDTRLGARSRlwanvtLYHNVTLGTDClvQAgtvig 178
Cdd:cd03351    2 IHPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNR------IFPFASIGEAP--QD----- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 179 adgFGYANERGEwikipqlggVTIGNRVEIGACTTIDRGALED---TRIADNVIIDNQCQIAHNVEIGYGTAVAGSTVMA 255
Cdd:cd03351   69 ---LKYKGEPTR---------LEIGDNNTIREFVTIHRGTAQGggvTRIGNNNLLMAYVHVAHDCVIGNNVILANNATLA 136

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 743522156 256 GSLKVGKYCIIGGASVFNGHMEICDQATVTGMAMVMR 292
Cdd:cd03351  137 GHVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQ 173
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
117-292 3.07e-27

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 107.49  E-value: 3.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 117 IGANAVIESGVVLGDDVRIGPGCFVGKDTRLGARSRLWANVTLYHNVTLGTDCLVQAGTVIGAD--GFGYANERGEwiki 194
Cdd:PRK05289   5 IHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEDpqDLKYKGEPTR---- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 195 pqlggVTIGNRVEIGACTTIDRGALED---TRIADNVIIDNQCQIAHNVEIGYGTAVAGSTVMAGSLKVGKYCIIGGASV 271
Cdd:PRK05289  81 -----LVIGDNNTIREFVTINRGTVQGggvTRIGDNNLLMAYVHVAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLTA 155

                        170       180
                 ....*....|....*....|.
gi 743522156 272 FNGHMEICDQATVTGMAMVMR 292
Cdd:PRK05289 156 VHQFVRIGAHAMVGGMSGVSQ 176
LpxD pfam04613
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, LpxD; UDP-3-O-[3-hydroxymyristoyl] ...
 22-88 2.58e-24

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, LpxD; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase (EC 2.3.1.-) catalyzes an early step in lipid A biosynthesis: UDP-3-O-(3-hydroxytetradecanoyl)glucosamine + (R)-3-hydroxytetradecanoyl- [acyl carrier protein] -> UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + [acyl carrier protein]. Members of this family also contain a hexapeptide repeat (pfam00132). This family constitutes the non-repeating region of LPXD proteins.


Pssm-ID: 461366 [Multi-domain]  Cd Length: 69  Bit Score: 94.10  E-value: 2.58e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743522156   22 REIRKVATLEKAGEGEIAFLSNKKYRHFLEQSKATAVLITEADLPFCPTNA--LVLKDPYVGFARVAQL 88
Cdd:pfam04613   1 LEITGVAPLEEAGPGDLSFLANPKYAKYLATTKASAVIVPPDFAPQAPATAtlLVVDNPYLAFAKLLQL 69
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 99-294 2.26e-23

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


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 96.95  E-value: 2.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156   99 IHPSAVIAADVQLGERVAIGANAVIESGVVLGDDVRIGPgcfvgkdtrlgarsrlwaNVTLYHNVTLGTDCLVQAGTVIG 178
Cdd:TIGR01852   1 IHPTAIIEPGAEIGENVEIGPFCIVGPGVKIGDGVELKS------------------HVVILGHTTIGEGTRIFPGAVIG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  179 AD--GFGYANERGEwikipqlggVTIGNRVEIGACTTIDRGALED---TRIADNVIIDNQCQIAHNVEIGYGTAVAGSTV 253
Cdd:TIGR01852  63 GVpqDLKYKGEKTR---------LIIGDNNTIREFVTINRGTASGggvTRIGNNNLLMAYSHIAHDCVVGNHVILANNAT 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 743522156  254 MAGSLKVGKYCIIGGASVFNGHMEICDQATVTGMAMVMRPI 294
Cdd:TIGR01852 134 LAGHVEVGDYAIIGGLVAVHQFVRIGRYAMIGGLSAVSKDV 174
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 99-271 2.36e-20

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 88.54  E-value: 2.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  99 IHPSAVIAADVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVGKDTRlgarsrlwanvtlyhnvtLGTDCLVQAGTVIG 178
Cdd:PRK12461   2 IHPTAVIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTR------------------IGKNNKIHQGAVVG 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 179 AD--GFGYANERGEwikipqlggVTIGNRVEIGACTTIDRGALED--TRIADNVIIDNQCQIAHNVEIGYGTAVAGSTVM 254
Cdd:PRK12461  64 DEpqDFTYKGEESR---------LEIGDRNVIREGVTIHRGTKGGgvTRIGNDNLLMAYSHVAHDCQIGNNVILVNGALL 134

                        170
                 ....*....|....*..
gi 743522156 255 AGSLKVGKYCIIGGASV 271
Cdd:PRK12461 135 AGHVTVGDRAIISGNCL 151
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 99-210 3.27e-15

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: 73.30  E-value: 3.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156   99 IHPSAVIAADVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVGKDTRLGARSRLWANVTLYHNVTLGTDCLVQAGTVIg 178
Cdd:TIGR03570  90 IHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGEGVFIGAGATI- 168

                          90       100       110
                  ....*....|....*....|....*....|..
gi 743522156  179 adgfgyanergewikipqLGGVTIGNRVEIGA 210
Cdd:TIGR03570 169 ------------------IQGVTIGAGAIVGA 182
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 99-216 3.06e-14

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: 70.21  E-value: 3.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  99 IHPSAVIAADVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVGKDTRLGARSRLWANVTLYHNVTLGTDCLVQAGTVIg 178
Cdd:cd03360   87 IHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEGAFIGAGATI- 165

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 743522156 179 adgfgyanergewikipqLGGVTIGNRVEIGACTTIDR 216
Cdd:cd03360  166 ------------------IQGVTIGAGAIIGAGAVVTK 185
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 200-305 2.58e-10

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


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 59.04  E-value: 2.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  200 VTIGNRVEIGACTTIDRGAL--EDTRIADNVIIDNQCQIAHNVEIGYGTAVAGSTVMAGSLKVGKYCIIGGASVFNGHME 277
Cdd:TIGR03570  94 AIVSPSASIGEGTVIMAGAVinPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGEGVFIGAGATIIQGVT 173

                          90       100
                  ....*....|....*....|....*....
gi 743522156  278 ICDQATVtGM-AMVMRPITEPGIYsSGIP 305
Cdd:TIGR03570 174 IGAGAIV-GAgAVVTKDIPDGGVV-VGVP 200
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 200-305 2.99e-10

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: 59.04  E-value: 2.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 200 VTIGNRVEIGACTTIDRGAL--EDTRIADNVIIDNQCQIAHNVEIGYGTAVAGSTVMAGSLKVGKYCIIG-GASVFNGhM 276
Cdd:cd03360   91 AVVSPSAVIGEGCVIMAGAVinPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEGAFIGaGATIIQG-V 169

                         90       100       110
                 ....*....|....*....|....*....|
gi 743522156 277 EICDQATVtGM-AMVMRPITEPGIYsSGIP 305
Cdd:cd03360  170 TIGAGAII-GAgAVVTKDVPDGSVV-VGNP 197
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 105-261 7.52e-10

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 57.82  E-value: 7.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 105 IAADVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVgKDTRLGARSRLWANVTLyHNVTLGTDCLV------QAGTVIG 178
Cdd:cd03353   12 IDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVI-KDSTIGDGVVIKASSVI-EGAVIGNGATVgpfahlRPGTVLG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 179 AD---GfgyaN-------ERGEWIKIPQL---GGVTIGNRVEIGaCTTI----DRGALEDTRIADNVIIDNQCQIAHNVE 241
Cdd:cd03353   90 EGvhiG----NfveikksTIGEGSKANHLsylGDAEIGEGVNIG-AGTItcnyDGVNKHRTVIGDNVFIGSNSQLVAPVT 164

                        170       180
                 ....*....|....*....|....*
gi 743522156 242 IGYGTAV-AGSTVM----AGSLKVG 261
Cdd:cd03353  165 IGDGATIaAGSTITkdvpPGALAIA 189
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 129-214 8.06e-10

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: 55.97  E-value: 8.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 129 LGDDVRIGPGCFVGKDTRLGARSRLWANVTLYHNVTLGTDCLVQAGTVIGADGFGYANERGEWikipQLGGVTIGNRVEI 208
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYRKW----ELKGTTVKRGASI 76


                 ....*.
gi 743522156 209 GACTTI 214
Cdd:cd03358   77 GANATI 82
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 99-296 4.50e-09

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 55.03  E-value: 4.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  99 IHPSAVIAADVQLGERVAIGANAVIEsgvvlGDDVRIgpgcfvgkdtRLGARSrlwaNvtlyhnvtlgtdclVQAGTVIG 178
Cdd:COG0663   19 VAPTAVVIGDVTIGEDVSVWPGAVLR-----GDVGPI----------RIGEGS----N--------------IQDGVVLH 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 179 ADGfGYAnergewikipqlggVTIGNRVEIG------ACTtidrgaledtrIADNVIIdnqcqiahnveigyGTavaGST 252
Cdd:COG0663   66 VDP-GYP--------------LTIGDDVTIGhgailhGCT-----------IGDNVLI--------------GM---GAI 102

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 743522156 253 VMAGSlKVGKYCIIGGASVFNGHMEICDQATVTGM-AMVMRPITE 296
Cdd:COG0663  103 VLDGA-VIGDGSIVGAGALVTEGKVVPPGSLVVGSpAKVVRELTE 146
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 99-253 9.20e-08

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 53.21  E-value: 9.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  99 IHPSAVIAADVQLGERVAIGANAVIeSGVVLGDDVRIGPGCF-----VGKDTRLGARSRLWANVTLYHNVTLGTdcLVQA 173
Cdd:PRK14355 277 IYPGVCISGDTRIGEGCTIEQGVVI-KGCRIGDDVTVKAGSVledsvVGDDVAIGPMAHLRPGTELSAHVKIGN--FVET 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 174 GTVIGADGFGYANergewikIPQLGGVTIGNRVEIGaCTTI----DRGALEDTRIADNVIIDNQCQIAHNVEIGYGTAV- 248
Cdd:PRK14355 354 KKIVMGEGSKASH-------LTYLGDATIGRNVNIG-CGTItcnyDGVKKHRTVIEDDVFVGSDVQFVAPVTVGRNSLIa 425


                 ....*
gi 743522156 249 AGSTV 253
Cdd:PRK14355 426 AGTTV 430
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
120-271 9.57e-08

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 50.64  E-value: 9.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 120 NAVIESGVVLGDDVRIGPGCFVGKdtrlgarsrlwanvtlyHNVTLGTDCLVQAGTVIGAdgfgyanergewikipqLGG 199
Cdd:COG0110    2 KLLLLFGARIGDGVVIGPGVRIYG-----------------GNITIGDNVYIGPGVTIDD-----------------PGG 47

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743522156 200 VTIGNRVEIGACTTIDRGALEDTRIADNVIIDNQCQIAHNVEIGygtavAGSTVMAGSlKVGKYCIIGGASV 271
Cdd:COG0110   48 ITIGDNVLIGPGVTILTGNHPIDDPATFPLRTGPVTIGDDVWIG-----AGATILPGV-TIGDGAVVGAGSV 113
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 99-296 9.82e-08

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: 50.87  E-value: 9.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  99 IHPSAVIAADVQLGERVAIGANAVIEsgvvlGDdvrigpgcfvgkdtrlgarsrlwanvtlYHNVTLGTDCLVQAGTVIG 178
Cdd:cd04645    8 IAPNATVIGDVTLGEGSSVWFGAVLR-----GD----------------------------VNPIRIGERTNIQDGSVLH 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 179 ADGfGYANERGEWikipqlggVTIGNRVEIGACtTIDRGALedtriadnviidnqcqiahnveIGYgtavaGSTVMAGSl 258
Cdd:cd04645   55 VDP-GYPTIIGDN--------VTVGHGAVLHGC-TIGDNCL----------------------IGM-----GAIILDGA- 96

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 743522156 259 KVGKYCIIGGASVFNGHMEICDQATVTG-MAMVMRPITE 296
Cdd:cd04645   97 VIGKGSIVAAGSLVPPGKVIPPGSLVAGsPAKVVRELTD 135
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 105-253 1.08e-07

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: 53.11  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 105 IAADVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVgKDTRLGarsrlwANVTLYHnvTLGTDCLVQAGTVIGAdgfgY 184
Cdd:COG1207  263 IDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTL-KDSTIG------DGVVIKY--SVIEDAVVGAGATVGP----F 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 185 ANER----------------------GEWIKIPQL---GGVTIGNRVEIGaCTTI----D-----RgaledTRIADNVII 230
Cdd:COG1207  330 ARLRpgtvlgegvkignfvevknstiGEGSKVNHLsyiGDAEIGEGVNIG-AGTItcnyDgvnkhR-----TVIGDGAFI 403

                        170       180
                 ....*....|....*....|....
gi 743522156 231 DNQCQIAHNVEIGYGTAV-AGSTV 253
Cdd:COG1207  404 GSNTNLVAPVTIGDGATIgAGSTI 427
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 101-145 1.39e-07

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: 50.95  E-value: 1.39e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 743522156 101 PSAVIAADVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVGKDT 145
Cdd:cd03360  143 PGVVLSGGVTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDV 187
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 97-210 2.24e-07

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: 50.08  E-value: 2.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  97 MDIHPSAVIaadvqlGERVAI--GanavieSGVVLGDDVRIGpgcfvgkdtrlgarsrlwANVTLYHNVTLGT------- 167
Cdd:COG1045   66 IDIHPGATI------GRGFFIdhG------TGVVIGETAVIG------------------DNVTIYQGVTLGGtgkekgk 115

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 743522156 168 -------DCLVQAGTVIgadgfgyanergewikipqLGGVTIGNRVEIGA 210
Cdd:COG1045  116 rhptigdNVVIGAGAKI-------------------LGPITIGDNAKIGA 146
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 99-177 3.09e-07

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: 48.65  E-value: 3.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  99 IHPSAVIAADVQLGERVAIGANAVIESGVVLGDDVRIGPGC-FVG--------------KDTRLGARSRLWANVTLYHNV 163
Cdd:cd03358    7 IGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVvFTNdlyprskiyrkwelKGTTVKRGASIGANATILPGV 86

                         90
                 ....*....|....
gi 743522156 164 TLGTDCLVQAGTVI 177
Cdd:cd03358   87 TIGEYALVGAGAVV 100
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 108-211 3.73e-07

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


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 47.84  E-value: 3.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 108 DVQLGERVAIGANAVI--ESGVVLGDDVRIGPGC-FVGKDTRLGARSRLWANVTLYHNVTLGTDCLVQAGTVIgadgfgy 184
Cdd:cd04647    1 NISIGDNVYIGPGCVIsaGGGITIGDNVLIGPNVtIYDHNHDIDDPERPIEQGVTSAPIVIGDDVWIGANVVI------- 73

                         90       100
                 ....*....|....*....|....*..
gi 743522156 185 anergewikipqLGGVTIGNRVEIGAC 211
Cdd:cd04647   74 ------------LPGVTIGDGAVVGAG 88
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 99-223 5.11e-07

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: 48.90  E-value: 5.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  99 IHPSAVIAADVQLGERVAIGANAVIE---SGVVLGDDVRIGPGC----FVGKDTRLGARSRLWANVTLyHNVTLGTDCLV 171
Cdd:cd04745    9 VHPTAVLIGDVIIGKNCYIGPHASLRgdfGRIVIRDGANVQDNCvihgFPGQDTVLEENGHIGHGAIL-HGCTIGRNALV 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 743522156 172 QAGTVIgadgfgyanergewikipqLGGVTIGNRVEIGACTTIDRGALEDTR 223
Cdd:cd04745   88 GMNAVV-------------------MDGAVIGEESIVGAMAFVKAGTVIPPR 120
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 109-178 1.04e-06

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 45.70  E-value: 1.04e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743522156 109 VQLGERVAIGANAVIESGVVLGDDVRIGPGCFVG--------KDTRLGARSRLWANVTLYHNVTLGTDCLVQAGTVIG 178
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGaatgpnekNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 97-212 1.74e-06

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: 45.89  E-value: 1.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  97 MDIHPSAVIaadvqlGERVAIGaNAvieSGVVLGDDVRIGpgcfvgkdtrlgarsrlwANVTLYHNVTLGTDCLVQAGT- 175
Cdd:cd03354    3 IDIHPGAKI------GPGLFID-HG---TGIVIGETAVIG------------------DNCTIYQGVTLGGKGKGGGKRh 54

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 743522156 176 -VIGADGFGYANErgewiKIpqLGGVTIGNRVEIGACT 212
Cdd:cd03354   55 pTIGDNVVIGAGA-----KI--LGNITIGDNVKIGANA 85
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 109-254 3.59e-06

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 48.48  E-value: 3.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 109 VQLGERVAIGANAVIESGVVLGDDVRIGPGCfVGKDTRLGARSRLwANVTLYHNVTLGTDCLV------QAGTVIGADGf 182
Cdd:PRK09451 266 LTHGRDVEIDTNVIIEGNVTLGNRVKIGAGC-VLKNCVIGDDCEI-SPYSVVEDANLGAACTIgpfarlRPGAELAEGA- 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 183 gyanERGEWIKIPQ--------------LGGVTIGNRVEIGACT---TIDRGALEDTRIADNVIIDNQCQIAHNVEIGYG 245
Cdd:PRK09451 343 ----HVGNFVEMKKarlgkgskaghltyLGDAEIGDNVNIGAGTitcNYDGANKFKTIIGDDVFVGSDTQLVAPVTVGKG 418

                        170
                 ....*....|
gi 743522156 246 -TAVAGSTVM 254
Cdd:PRK09451 419 aTIGAGTTVT 428
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 102-262 3.87e-06

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 48.29  E-value: 3.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 102 SAVIAADVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVgKDTRLGARSRLWANV----TLYHNVTLGTDCLVQAGTVI 177
Cdd:PRK14354 259 STYIDADVEIGSDTVIEPGVVIKGNTVIGEDCVIGPGSRI-VDSTIGDGVTITNSVieesKVGDNVTVGPFAHLRPGSVI 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 178 GaDGFGYAN-------ERGEWIKIPQL---GGVTIGNRVEIGaCTTI----DRGALEDTRIADNVIIDNQCQIAHNVEIG 243
Cdd:PRK14354 338 G-EEVKIGNfveikksTIGEGTKVSHLtyiGDAEVGENVNIG-CGTItvnyDGKNKFKTIIGDNAFIGCNSNLVAPVTVG 415

                        170       180
                 ....*....|....*....|....
gi 743522156 244 YGTAV-AGST----VMAGSLKVGK 262
Cdd:PRK14354 416 DNAYIaAGSTitkdVPEDALAIAR 439
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 99-271 4.14e-06

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 48.00  E-value: 4.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  99 IHP-SAVIAADVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVgKDTRLGarsrlwANVTLYHNVTlgTDCLVQAGTVI 177
Cdd:PRK14360 252 IDPaSCTISETVELGPDVIIEPQTHLRGNTVIGSGCRIGPGSLI-ENSQIG------ENVTVLYSVV--SDSQIGDGVKI 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 178 GAdgfgYANERGEwIKIPQlgGVTIGNRVEIGAcTTIDRGA-------LEDTRIADNVIIDNQCQIA-------HNVEIG 243
Cdd:PRK14360 323 GP----YAHLRPE-AQIGS--NCRIGNFVEIKK-SQLGEGSkvnhlsyIGDATLGEQVNIGAGTITAnydgvkkHRTVIG 394

                        170       180
                 ....*....|....*....|....*...
gi 743522156 244 YGTAVAGSTVMAGSLKVGKYCIIGGASV 271
Cdd:PRK14360 395 DRSKTGANSVLVAPITLGEDVTVAAGST 422
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
95-144 5.74e-06

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 45.25  E-value: 5.74e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 743522156  95 PAMDIHPSAVIAADVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVGKD 144
Cdd:COG0110   68 PIDDPATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKD 117
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 146-249 2.02e-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: 42.24  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 146 RLGARSRLWANVTLYHNVTLGTDCLVQAGTVIGADGFGYanergewikipQLGGVTIGNRVEIGActtidrgaledtria 225
Cdd:cd00208    2 FIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPN-----------EKNPTIIGDNVEIGA--------------- 55

                         90       100
                 ....*....|....*....|....
gi 743522156 226 dNVIIDNQCQIAHNVEIGYGTAVA 249
Cdd:cd00208   56 -NAVIHGGVKIGDNAVIGAGAVVT 78
PLN02739 PLN02739
serine acetyltransferase
 96-180 2.63e-05

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 45.41  E-value: 2.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  96 AMDIHPSAVIAADVQL--GERVAIGANAVIESGVVLGDDVRIGPgcfVGKDT-----RLGARSRLWANVTLYHNVTLGTD 168
Cdd:PLN02739 205 GIDIHPAARIGKGILLdhGTGVVIGETAVIGDRVSILHGVTLGG---TGKETgdrhpKIGDGALLGACVTILGNISIGAG 281

                         90
                 ....*....|..
gi 743522156 169 CLVQAGTVIGAD 180
Cdd:PLN02739 282 AMVAAGSLVLKD 293
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 199-305 2.99e-05

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


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 42.44  E-value: 2.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 199 GVTIGNRVEIGACTTIDrgALEDTRIADNVIIDNQCQI-AHNVEIGYGTAVAGSTVMAGSLKVGKYCIIGGASVFNGHME 277
Cdd:cd04647    1 NISIGDNVYIGPGCVIS--AGGGITIGDNVLIGPNVTIyDHNHDIDDPERPIEQGVTSAPIVIGDDVWIGANVVILPGVT 78

                         90       100
                 ....*....|....*....|....*...
gi 743522156 278 ICDQATVTGMAMVMRPITEPGIYsSGIP 305
Cdd:cd04647   79 IGDGAVVGAGSVVTKDVPPNSIV-AGNP 105
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 126-230 3.05e-05

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


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 42.44  E-value: 3.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 126 GVVLGDDVRIGPGCFvgkdtrlgarsrLWAnvtlYHNVTLGTDCLVQAGTVIGADGFGYANERGEWIKIPQLGGVTIGNR 205
Cdd:cd04647    1 NISIGDNVYIGPGCV------------ISA----GGGITIGDNVLIGPNVTIYDHNHDIDDPERPIEQGVTSAPIVIGDD 64

                         90       100
                 ....*....|....*....|....*
gi 743522156 206 VEIGACTTIdrgaLEDTRIADNVII 230
Cdd:cd04647   65 VWIGANVVI----LPGVTIGDGAVV 85
LbH_unknown cd05635
Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group ...
 127-213 4.55e-05

Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group are uncharacterized bacterial proteins containing a LbH domain with 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: 100059 [Multi-domain]  Cd Length: 101  Bit Score: 41.88  E-value: 4.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 127 VVLGDDVRIGPGCFVGKDTRLGARSRLWANVTLYHNVTLGTDCLVqAGTVIGADGFGYANERGEWIkipqLGGVTIGNRV 206
Cdd:cd05635   12 IYIGKDAVIEPFAVIEGPVYIGPGSRVKMGARIYGNTTIGPTCKI-GGEVEDSIIEGYSNKQHDGF----LGHSYLGSWC 86


                 ....*..
gi 743522156 207 EIGACTT 213
Cdd:cd05635   87 NLGAGTN 93
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 104-144 4.96e-05

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


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 42.06  E-value: 4.96e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 743522156 104 VIAADVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVGKD 144
Cdd:cd04647   54 VTSAPIVIGDDVWIGANVVILPGVTIGDGAVVGAGSVVTKD 94
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 95-299 7.51e-05

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: 42.56  E-value: 7.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  95 PAMDIHPSAVIAADVQLGERVAIGANAVIEsgvvlGDDVRIgpgcfvgkdtRLGARSRLWANVTLYhnvtlgTDclvqag 174
Cdd:cd04650    5 PKAYVHPTSYVIGDVVIGELTSVWHYAVIR-----GDNDSI----------YIGKYSNVQENVSIH------TD------ 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 175 tvigadgFGYANERGEWikipqlggVTIG-NRVEIGActtidrgaledtRIADNVIIDnqcqiahnveigygtavAGSTV 253
Cdd:cd04650   58 -------HGYPTEIGDY--------VTIGhNAVVHGA------------KVGNYVIVG-----------------MGAIL 93

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 743522156 254 MAGSlKVGKYCIIGGASVFNGHMEICDQATVTGM-AMVMRPITEPGI 299
Cdd:cd04650   94 LNGA-KIGDHVIIGAGAVVTPGKEIPDYSLVLGVpAKVVRKLTEEEI 139
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 99-152 8.44e-05

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


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 42.20  E-value: 8.44e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 743522156  99 IHPSAVIAAdVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVGKDTRLGARSR 152
Cdd:cd03359   81 IGENCVVNA-AQIGSYVHIGKNCVIGRRCIIKDCVKILDGTVVPPDTVIPPYSV 133
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 105-258 8.49e-05

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


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 42.58  E-value: 8.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 105 IAADVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVGKdtrlGARSRlwANVTLYHNVTLGTDCLVQAgTVIGADgfgy 184
Cdd:cd05636    8 VEEGVTIKGPVWIGEGAIVRSGAYIEGPVIIGKGCEIGP----NAYIR--GYTVLGDGCVVGNSVEVKN-SIIMDG---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 185 anergewIKIPQL---GGVTIGNRVEIGACTTID-------------RGALEDT-RIADNVIIDNQCQIAHNVEIGYGTA 247
Cdd:cd05636   77 -------TKVPHLnyvGDSVLGENVNLGAGTITAnlrfddkpvkvrlKGERVDTgRRKLGAIIGDGVKTGINVSLNPGVK 149

                        170
                 ....*....|..
gi 743522156 248 V-AGSTVMAGSL 258
Cdd:cd05636  150 IgPGSWVYPGCV 161
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
108-137 9.53e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 38.86  E-value: 9.53e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 743522156  108 DVQLGERVAIGANAVIESGVVLGDDVRIGP 137
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 98-142 1.59e-04

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 39.54  E-value: 1.59e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 743522156  98 DIHPSAVIAA--------DVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVG 142
Cdd:cd00208   26 NIGPGAVIGAatgpneknPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 197-296 1.79e-04

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


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 41.20  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 197 LGGVTIGNRVEIGACTTIdRGALEDTRIADNVIIDNQCQIaH-----------NVEIGYGTAVAGSTVMAGSL------- 258
Cdd:cd04745   16 IGDVIIGKNCYIGPHASL-RGDFGRIVIRDGANVQDNCVI-HgfpgqdtvleeNGHIGHGAILHGCTIGRNALvgmnavv 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 743522156 259 ----KVGKYCIIGGASVFNGHMEICDQATVTGM-AMVMRPITE 296
Cdd:cd04745   94 mdgaVIGEESIVGAMAFVKAGTVIPPRSLIAGSpAKVIRELSD 136
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 99-177 2.08e-04

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


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 41.46  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  99 IHPSAVIAADVQLGERVAIGANAVIES----------------GVVL----GDDVRIGPG------------CFVGKDTR 146
Cdd:cd00710   11 VHPTAVVIGDVIIGDNVFVGPGASIRAdegtpiiiganvniqdGVVIhaleGYSVWIGKNvsiahgaivhgpAYIGDNCF 90

                         90       100       110
                 ....*....|....*....|....*....|.
gi 743522156 147 LGARSrlwanvtLYHNVTLGTDCLVQAGTVI 177
Cdd:cd00710   91 IGFRS-------VVFNAKVGDNCVIGHNAVV 114
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 111-144 2.12e-04

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: 39.73  E-value: 2.12e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 743522156 111 LGERVAIGANAVIESGVVLGDDVRIGPGCFVGKD 144
Cdd:cd03354   57 IGDNVVIGAGAKILGNITIGDNVKIGANAVVTKD 90
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
198-294 3.65e-04

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 40.24  E-value: 3.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 198 GGVTIGNRVEIGACTTIDrgaledtrIADNVIIDNQCQIAHNVEIGYGT----AVAGSTVMAGSLKVGKYCIIGGASVFN 273
Cdd:COG0110   26 GNITIGDNVYIGPGVTID--------DPGGITIGDNVLIGPGVTILTGNhpidDPATFPLRTGPVTIGDDVWIGAGATIL 97

                         90       100
                 ....*....|....*....|.
gi 743522156 274 GHMEICDQATVTGMAMVMRPI 294
Cdd:COG0110   98 PGVTIGDGAVVGAGSVVTKDV 118
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 104-179 4.90e-04

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: 38.33  E-value: 4.90e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743522156 104 VIAADVQLGERVAIgANAVIESGVVLGDDVRIgPGCFVGKDTRLGARSRLwanvtlyhnvtlgTDCLVQAGTVIGA 179
Cdd:cd04652   18 VIGANCKIGKRVKI-TNCVIMDNVTIEDGCTL-ENCIIGNGAVIGEKCKL-------------KDCLVGSGYRVEA 78
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 110-144 6.26e-04

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: 40.07  E-value: 6.26e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 743522156 110 QLGERVAIGANAVIESGVVLGDDVRIGPGCFVGKD 144
Cdd:COG1045  119 TIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKD 153
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 199-267 8.17e-04

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: 41.17  E-value: 8.17e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743522156 199 GVT--------IGNRVEIGACTTIDRGA-LE-DTRIADNVIIDNQCQIaHNVEIGYGTAVAgSTVMAGSlKVGKYCIIG 267
Cdd:COG1207  252 GVTiidpattyIDGDVEIGRDVVIDPNViLEgKTVIGEGVVIGPNCTL-KDSTIGDGVVIK-YSVIEDA-VVGAGATVG 327
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 111-210 8.75e-04

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: 39.33  E-value: 8.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 111 LGERVAIGANAVI--ESGVVLGDDVRIGPgcfvgkdtrlgarsrlwaNVTLY------------------HNVTLGTDCL 170
Cdd:cd03357   65 IGDNFYANFNCTIldVAPVTIGDNVLIGP------------------NVQIYtaghpldpeernrgleyaKPITIGDNVW 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 743522156 171 VQAGTVIgadgfgyanergewikipqLGGVTIGNRVEIGA 210
Cdd:cd03357  127 IGGGVII-------------------LPGVTIGDNSVIGA 147
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
99-177 9.32e-04

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 39.08  E-value: 9.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  99 IHPSAVI--AADVQLGERVAIGANAVI----------------ESGVVLGDDVRIGPGCFVGKdtrlgarsrlwanvtly 160
Cdd:COG0110   36 IGPGVTIddPGGITIGDNVLIGPGVTIltgnhpiddpatfplrTGPVTIGDDVWIGAGATILP----------------- 98

                         90
                 ....*....|....*..
gi 743522156 161 hNVTLGTDCLVQAGTVI 177
Cdd:COG0110   99 -GVTIGDGAVVGAGSVV 114
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 99-231 9.38e-04

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


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 39.49  E-value: 9.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  99 IHPSAVIAADVQLGERVAIGANAVIESGVVLGDDVRIGPGC-----FVGKDTRLGARSRLWANVtlyhnvtLGTDCLVQA 173
Cdd:cd05636   26 VRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVevknsIIMDGTKVPHLNYVGDSV-------LGENVNLGA 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743522156 174 GTVIgadgfgyANER--GEWIKIPQLG----------GVTIGNRVEIGACTTIDRGAL--EDTRIADNVIID 231
Cdd:cd05636   99 GTIT-------ANLRfdDKPVKVRLKGervdtgrrklGAIIGDGVKTGINVSLNPGVKigPGSWVYPGCVVR 163
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 135-232 1.05e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 40.64  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 135 IGPGCFVgKDTR-----LGARSRLWANVTLyhnvtlgTDCLVqagtvIGADGFGYANERgewIKIPQLGGVTIGnrveIG 209
Cdd:PRK02862 311 IAEGCII-KNCSihhsvLGIRSRIESGCTI-------EDTLV-----MGADFYESSEER---EELRKEGKPPLG----IG 370

                         90       100
                 ....*....|....*....|....*
gi 743522156 210 ACTTIdRGALED--TRIADNVIIDN 232
Cdd:PRK02862 371 EGTTI-KRAIIDknARIGNNVRIVN 394
PLN02694 PLN02694
serine O-acetyltransferase
 96-180 1.10e-03

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 40.40  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  96 AMDIHPSAVI--------AADVQLGERVAIGANAVIESGVVLGDD--------VRIGPGCFVGkdtrlgarsrlwANVTL 159
Cdd:PLN02694 160 AVDIHPAAKIgkgilfdhATGVVIGETAVIGNNVSILHHVTLGGTgkacgdrhPKIGDGVLIG------------AGATI 227

                         90       100
                 ....*....|....*....|.
gi 743522156 160 YHNVTLGTDCLVQAGTVIGAD 180
Cdd:PLN02694 228 LGNVKIGEGAKIGAGSVVLID 248
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 91-144 1.20e-03

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 39.41  E-value: 1.20e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 743522156  91 TTPQPAMDIHPSAVIAADVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVGKD 144
Cdd:PRK10092 112 THPLDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKD 165
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
117-142 1.66e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.39  E-value: 1.66e-03
                          10        20
                  ....*....|....*....|....*.
gi 743522156  117 IGANAVIESGVVLGDDVRIGPGCFVG 142
Cdd:pfam00132   4 IGDNVLIGPNAVIGGGVIIGDNVIIG 29
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 105-157 2.98e-03

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 38.16  E-value: 2.98e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 743522156 105 IAADVQLGERVAIGANAVIESGVVLGDDVRIGPGC------FVGKDTRLGARSRLWANV 157
Cdd:cd03352  129 IAHNVRIGENCLIAAQVGIAGSTTIGDNVIIGGQVgiaghlTIGDGVVIGAGSGVTSIV 187
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 99-232 3.16e-03

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 39.14  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  99 IHPSAVIAaDVQLGERVAIGANAVIESGVvlGDDVRIGP------------GCFVG-----KDTRLGARSRLwANVTLYH 161
Cdd:PRK14360 289 IGPGSLIE-NSQIGENVTVLYSVVSDSQI--GDGVKIGPyahlrpeaqigsNCRIGnfveiKKSQLGEGSKV-NHLSYIG 364

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 162 NVTLGTDCLVQAGTvIGA--DGFG-YANERGEWIKI--------PqlggVTIGNRVEIGACTTIDR----GALEDTRiAD 226
Cdd:PRK14360 365 DATLGEQVNIGAGT-ITAnyDGVKkHRTVIGDRSKTgansvlvaP----ITLGEDVTVAAGSTITKdvpdNSLAIAR-SR 438


                 ....*.
gi 743522156 227 NVIIDN 232
Cdd:PRK14360 439 QVIKEN 444
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 106-146 3.44e-03

Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; Tetrahydrodipicolinate N-succinyltransferase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 38.56  E-value: 3.44e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 743522156 106 AADVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVGKDTR 146
Cdd:COG2171  168 AAPVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTASTK 208
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 199-294 4.59e-03

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: 36.26  E-value: 4.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 199 GVTIGNRVEIGACTTIDRGAleDTRIADNVIIDNQCQIAHNVEIGYGTAVAGstvmAGSLKVGKYCIIG-GASVFnGHME 277
Cdd:cd03354    2 GIDIHPGAKIGPGLFIDHGT--GIVIGETAVIGDNCTIYQGVTLGGKGKGGG----KRHPTIGDNVVIGaGAKIL-GNIT 74

                         90
                 ....*....|....*..
gi 743522156 278 ICDQATVTGMAMVMRPI 294
Cdd:cd03354   75 IGDNVKIGANAVVTKDV 91
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 111-180 5.82e-03

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: 35.90  E-value: 5.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156 111 LGERVAIGANAVIESGVVLGdDVRIGPGCFVgkdtrlgarsrlwanvtlyHNVTLGTDCLVQAGTVIGAD 180
Cdd:cd04651   31 LFRGVRVGSGSVVEDSVIMP-NVGIGRNAVI-------------------RRAIIDKNVVIPDGVVIGGD 80
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 111-178 6.17e-03

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: 35.25  E-value: 6.17e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743522156 111 LGERVAIGANAVIESGVVLgDDVRIGPGCFVGkdtrlgaRSRLWANVTLYHNVTLGTDCLVQAGTVIG 178
Cdd:cd05787   19 IGRNCKIGKNVVIDNSYIW-DDVTIEDGCTIH-------HSIVADGAVIGKGCTIPPGSLISFGVVIG 78
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 105-144 6.59e-03

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: 37.02  E-value: 6.59e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 743522156 105 IAADVQLGERVAIGANAVIESGVVLGDDVRIGPGCFVGKD 144
Cdd:cd03357  115 YAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKD 154
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 147-251 7.08e-03

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 38.19  E-value: 7.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522156  147 LGARsrLWANVTLYHNVTLGTDCL-VQAGTVIGADGF--GYANERGewikIPQLGGVTIGNRVEIGACTTIDRgaleDTR 223
Cdd:TIGR02353 111 LGAK--IGKGVDIGSLPPVCTDLLtIGAGTIVRKEVMllGYRAERG----RLHTGPVTLGRDAFIGTRSTLDI----DTS 180

                          90       100
                  ....*....|....*....|....*...
gi 743522156  224 IADNVIIDNQCQIAHNVEIGYGTAVAGS 251
Cdd:TIGR02353 181 IGDGAQLGHGSALQGGQSIPDGERWHGS 208
 
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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