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Conserved domains on  [gi|2076014242|pdb|7RA4|C]
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Chain C, Serine acetyltransferase

Protein Classification

LbetaH domain-containing protein( domain architecture ID 372)

LbetaH (left-handed parallel beta-helix) domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 34-282 2.30e-128

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


The actual alignment was detected with superfamily member PRK11132:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 273  Bit Score: 365.94  E-value: 2.30e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C        34 LWHTIREETAAAAAAEPMLASFLHQTVLRHESLGSVLAYHLSSKLGSPIMDVRALFEIYQQALGSDTQISKCVEADLKAI 113
Cdd:PRK11132   9 VWNNIKAEARALADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYAADPEMIASAACDIQAV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C       114 YERDPACDEYSLPLLYFKGFHAIQAHRINHRLYLDGRKTLAYFLQNRMSEVFGVDIHPAARLGYGLMLDHATGFVAGETA 193
Cdd:PRK11132  89 RTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIYLQNQISVAFQVDIHPAAKIGRGIMLDHATGIVIGETA 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C       194 VLGNNISILHGVTLGGSGKEGGDRHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPSITVVGVPAKPVAR-S 272
Cdd:PRK11132 169 VIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVGKpE 248

                        250
                 ....*....|
7RA4_C       273 LKTPSADMDQ 282
Cdd:PRK11132 249 SDKPSMDMDQ 258
 
Name Accession Description Interval E-value
cysE PRK11132
serine acetyltransferase; Provisional
 34-282 2.30e-128

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 365.94  E-value: 2.30e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C        34 LWHTIREETAAAAAAEPMLASFLHQTVLRHESLGSVLAYHLSSKLGSPIMDVRALFEIYQQALGSDTQISKCVEADLKAI 113
Cdd:PRK11132   9 VWNNIKAEARALADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYAADPEMIASAACDIQAV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C       114 YERDPACDEYSLPLLYFKGFHAIQAHRINHRLYLDGRKTLAYFLQNRMSEVFGVDIHPAARLGYGLMLDHATGFVAGETA 193
Cdd:PRK11132  89 RTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIYLQNQISVAFQVDIHPAAKIGRGIMLDHATGIVIGETA 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C       194 VLGNNISILHGVTLGGSGKEGGDRHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPSITVVGVPAKPVAR-S 272
Cdd:PRK11132 169 VIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVGKpE 248

                        250
                 ....*....|
7RA4_C       273 LKTPSADMDQ 282
Cdd:PRK11132 249 SDKPSMDMDQ 258
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 106-267 5.07e-97

serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 282.26  E-value: 5.07e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C        106 VEADLKAIYERDPACDEYSLPLLYFKGFHAIQAHRINHRLYLDGRKTLAYFLQNRMSEVFGVDIHPAARLGYGLMLDHAT 185
Cdd:TIGR01172   1 IREDIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C        186 GFVAGETAVLGNNISILHGVTLGGSGKEGGDRHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPSITVVGVP 265
Cdd:TIGR01172  81 GVVIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVP 160


                  ..
7RA4_C        266 AK 267
Cdd:TIGR01172 161 AR 162
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 102-272 6.08e-95

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: 277.35  E-value: 6.08e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C      102 ISKCVEADLKAIYERDPACDEYSLPLLYFKGFHAIQAHRINHRLYLDGRKTLAYFLQNRMSEVFGVDIHPAARLGYGLML 181
Cdd:COG1045   1 MLKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C      182 DHATGFVAGETAVLGNNISILHGVTLGGSGKEGGDRHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPSITV 261
Cdd:COG1045  81 DHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTV 160

                       170
                ....*....|.
7RA4_C      262 VGVPAKPVARS 272
Cdd:COG1045 161 VGVPARIVKRK 171
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 165-265 2.22e-52

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: 166.46  E-value: 2.22e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C      165 FGVDIHPAARLGYGLMLDHATGFVAGETAVLGNNISILHGVTLGGSGKEGGDRHPKIGDGVMIGANASILGNIRIGSNAK 244
Cdd:cd03354   1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                        90       100
                ....*....|....*....|.
7RA4_C      245 IGAGSVVVSDVPPSITVVGVP 265
Cdd:cd03354  81 IGANAVVTKDVPANSTVVGVP 101
SATase_N pfam06426
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 34-137 5.88e-51

Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a sequence that is conserved in plants and bacteria.


Pssm-ID: 461909 [Multi-domain]  Cd Length: 104  Bit Score: 163.02  E-value: 5.88e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C         34 LWHTIREETAAAAAAEPMLASFLHQTVLRHESLGSVLAYHLSSKLGSPIMDVRALFEIYQQALGSDTQISKCVEADLKAI 113
Cdd:pfam06426   1 VWARLRAEAEEAAEREPLLASFLYATILSHDSLESALAFRLANKLANSTLPATLLRELFEDALEADPEIVEAARADLQAV 80

                          90       100
                  ....*....|....*....|....
7RA4_C        114 YERDPACDEYSLPLLYFKGFHAIQ 137
Cdd:pfam06426  81 YERDPACDRYLTPLLYFKGFHALQ 104
SATase_N smart00971
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 34-138 2.62e-50

Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a sequence that is conserved in plants.and bacteria.


Pssm-ID: 198039 [Multi-domain]  Cd Length: 105  Bit Score: 161.55  E-value: 2.62e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C          34 LWHTIREETAAAAAAEPMLASFLHQTVLRHESLGSVLAYHLSSKLGSPIMDVRALFEIYQQALGSDTQISKCVEADLKAI 113
Cdd:smart00971   1 VWQRIRAEAREAAEREPILASFLYATILNHDSLEAALAYRLANKLGNADMSADLLRELFEDAYAADPEIVEAAAADIQAV 80

                           90       100
                   ....*....|....*....|....*
7RA4_C         114 YERDPACDEYSLPLLYFKGFHAIQA 138
Cdd:smart00971  81 YDRDPACDRYLTPLLYFKGFHALQA 105
 
Name Accession Description Interval E-value
cysE PRK11132
serine acetyltransferase; Provisional
 34-282 2.30e-128

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 365.94  E-value: 2.30e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C        34 LWHTIREETAAAAAAEPMLASFLHQTVLRHESLGSVLAYHLSSKLGSPIMDVRALFEIYQQALGSDTQISKCVEADLKAI 113
Cdd:PRK11132   9 VWNNIKAEARALADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYAADPEMIASAACDIQAV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C       114 YERDPACDEYSLPLLYFKGFHAIQAHRINHRLYLDGRKTLAYFLQNRMSEVFGVDIHPAARLGYGLMLDHATGFVAGETA 193
Cdd:PRK11132  89 RTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIYLQNQISVAFQVDIHPAAKIGRGIMLDHATGIVIGETA 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C       194 VLGNNISILHGVTLGGSGKEGGDRHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPSITVVGVPAKPVAR-S 272
Cdd:PRK11132 169 VIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVGKpE 248

                        250
                 ....*....|
7RA4_C       273 LKTPSADMDQ 282
Cdd:PRK11132 249 SDKPSMDMDQ 258
PLN02357 PLN02357
serine acetyltransferase
 33-293 1.18e-99

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 296.41  E-value: 1.18e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C        33 DLWHTIREETAAAAAAEPMLASFLHQTVLRHESLGSVLAYHLSSKLGSPIMDVRALFEIYQQALGSDTQISKCVEADLKA 112
Cdd:PLN02357  93 DVWLKIQEEAKSDVEQEPILSSYYYASILSHRSLESALANHLSVKLSNLNLPSNTLFDLFIGVLEESPEIIESVKQDLRA 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C       113 IYERDPACDEYSLPLLYFKGFHAIQAHRINHRLYLDGRKTLAYFLQNRMSEVFGVDIHPAARLGYGLMLDHATGFVAGET 192
Cdd:PLN02357 173 VKERDPACISYVHCFLNFKGFLACQAHRIAHKLWTQGRKILALLIQNRVSEAFAVDIHPGAKIGQGILLDHATGVVIGET 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C       193 AVLGNNISILHGVTLGGSGKEGGDRHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPSITVVGVPAKPVA-- 270
Cdd:PLN02357 253 AVVGNNVSILHNVTLGGTGKQSGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLIGgk 332

                        250       260
                 ....*....|....*....|....*...
7RA4_C       271 ----RSLKTPSADMDQNIQFAE-IDFMI 293
Cdd:PLN02357 333 enpiKHDKIPSLTMDQTSHISEwSDYVI 360
PLN02694 PLN02694
serine O-acetyltransferase
 34-282 3.59e-98

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 290.39  E-value: 3.59e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C        34 LWHTIREETAAAAAAEPMLASFLHQTVLRHESLGSVLAYHLSSKLGSPIMDVRALFEIYQQALGSDTQISKCVEADLKAI 113
Cdd:PLN02694  28 LWTQIKAEARRDAESEPALASYLYSTILSHSSLERSLSFHLGNKLCSSTLLSTLLYDLFLNTFSSDPSLRAATVADLRAA 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C       114 YERDPACDEYSLPLLYFKGFHAIQAHRINHRLYLDGRKTLAYFLQNRMSEVFGVDIHPAARLGYGLMLDHATGFVAGETA 193
Cdd:PLN02694 108 RVRDPACVSFSHCLLNYKGFLACQAHRVAHKLWTQSRRPLALALHSRISDVFAVDIHPAAKIGKGILFDHATGVVIGETA 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C       194 VLGNNISILHGVTLGGSGKEGGDRHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPSITVVGVPAKPV---- 269
Cdd:PLN02694 188 VIGNNVSILHHVTLGGTGKACGDRHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLVggke 267

                        250
                 ....*....|....*
7RA4_C       270 --ARSLKTPSADMDQ 282
Cdd:PLN02694 268 kpAKHEECPGESMDH 282
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 106-267 5.07e-97

serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 282.26  E-value: 5.07e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C        106 VEADLKAIYERDPACDEYSLPLLYFKGFHAIQAHRINHRLYLDGRKTLAYFLQNRMSEVFGVDIHPAARLGYGLMLDHAT 185
Cdd:TIGR01172   1 IREDIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C        186 GFVAGETAVLGNNISILHGVTLGGSGKEGGDRHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPSITVVGVP 265
Cdd:TIGR01172  81 GVVIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVP 160


                  ..
7RA4_C        266 AK 267
Cdd:TIGR01172 161 AR 162
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 102-272 6.08e-95

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: 277.35  E-value: 6.08e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C      102 ISKCVEADLKAIYERDPACDEYSLPLLYFKGFHAIQAHRINHRLYLDGRKTLAYFLQNRMSEVFGVDIHPAARLGYGLML 181
Cdd:COG1045   1 MLKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C      182 DHATGFVAGETAVLGNNISILHGVTLGGSGKEGGDRHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPSITV 261
Cdd:COG1045  81 DHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTV 160

                       170
                ....*....|.
7RA4_C      262 VGVPAKPVARS 272
Cdd:COG1045 161 VGVPARIVKRK 171
PLN02739 PLN02739
serine acetyltransferase
 30-267 4.66e-93

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 279.61  E-value: 4.66e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C        30 TGFD-LWHTIREETAAAAAAEPMLASFLHQTVLRHESLGSVLAYHLSSKLGSPIMDVRALFEIYQQALGSDTQISKCVEA 108
Cdd:PLN02739  68 SRYDpIWDSIREEAKLEAEEEPVLSSFLYASILSHDCLEQALSFVLANRLQNPTLLATQLMDIFCNVMVHDRGIQSSIRL 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C       109 DLKAIYERDPACDEYSLPLLYFKGFHAIQAHRINHRLYLDGRKTLAYFLQNRMSEVFGVDIHPAARLGYGLMLDHATGFV 188
Cdd:PLN02739 148 DVQAFKDRDPACLSYSSAILHLKGYLALQAYRVAHKLWKQGRKLLALALQSRVSEVFGIDIHPAARIGKGILLDHGTGVV 227

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
7RA4_C       189 AGETAVLGNNISILHGVTLGGSGKEGGDRHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPSITVVGVPAK 267
Cdd:PLN02739 228 IGETAVIGDRVSILHGVTLGGTGKETGDRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAK 306
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 165-265 2.22e-52

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: 166.46  E-value: 2.22e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C      165 FGVDIHPAARLGYGLMLDHATGFVAGETAVLGNNISILHGVTLGGSGKEGGDRHPKIGDGVMIGANASILGNIRIGSNAK 244
Cdd:cd03354   1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                        90       100
                ....*....|....*....|.
7RA4_C      245 IGAGSVVVSDVPPSITVVGVP 265
Cdd:cd03354  81 IGANAVVTKDVPANSTVVGVP 101
SATase_N pfam06426
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 34-137 5.88e-51

Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a sequence that is conserved in plants and bacteria.


Pssm-ID: 461909 [Multi-domain]  Cd Length: 104  Bit Score: 163.02  E-value: 5.88e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C         34 LWHTIREETAAAAAAEPMLASFLHQTVLRHESLGSVLAYHLSSKLGSPIMDVRALFEIYQQALGSDTQISKCVEADLKAI 113
Cdd:pfam06426   1 VWARLRAEAEEAAEREPLLASFLYATILSHDSLESALAFRLANKLANSTLPATLLRELFEDALEADPEIVEAARADLQAV 80

                          90       100
                  ....*....|....*....|....
7RA4_C        114 YERDPACDEYSLPLLYFKGFHAIQ 137
Cdd:pfam06426  81 YERDPACDRYLTPLLYFKGFHALQ 104
SATase_N smart00971
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 34-138 2.62e-50

Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a sequence that is conserved in plants.and bacteria.


Pssm-ID: 198039 [Multi-domain]  Cd Length: 105  Bit Score: 161.55  E-value: 2.62e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C          34 LWHTIREETAAAAAAEPMLASFLHQTVLRHESLGSVLAYHLSSKLGSPIMDVRALFEIYQQALGSDTQISKCVEADLKAI 113
Cdd:smart00971   1 VWQRIRAEAREAAEREPILASFLYATILNHDSLEAALAYRLANKLGNADMSADLLRELFEDAYAADPEIVEAAAADIQAV 80

                           90       100
                   ....*....|....*....|....*
7RA4_C         114 YERDPACDEYSLPLLYFKGFHAIQA 138
Cdd:smart00971  81 YDRDPACDRYLTPLLYFKGFHALQA 105
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
187-269 8.84e-20

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 83.38  E-value: 8.84e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C      187 FVAGETAVLGNNISILHGVTLGGSGKEGGD--------RHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPS 258
Cdd:COG0110  42 IDDPGGITIGDNVLIGPGVTILTGNHPIDDpatfplrtGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPY 121

                        90
                ....*....|.
7RA4_C      259 ITVVGVPAKPV 269
Cdd:COG0110 122 AIVAGNPARVI 132
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 165-266 4.54e-19

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: 82.93  E-value: 4.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C        165 FGVDIHPAARLGYGLMLDHATGFVAGET----AVLGNNISILH------------------GVTLGGsgkeggdrHPKIG 222
Cdd:TIGR03570  86 FATLIHPSAIVSPSASIGEGTVIMAGAVinpdVRIGDNVIINTgaivehdcvigdfvhiapGVTLSG--------GVVIG 157

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
7RA4_C        223 DGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPSITVVGVPA 266
Cdd:TIGR03570 158 EGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
PRK10191 PRK10191
putative acyl transferase; Provisional
 164-267 8.19e-19

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 81.09  E-value: 8.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C       164 VFGVDIHPAARLGYGLMLDHATGFVAGETAVLGNNISILHGVTLGGSGKEGgDRHPKIGDGVMIGANASILGNIRIGSNA 243
Cdd:PRK10191  39 FFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGVTIGNRGADN-MACPHIGNGVELGANVIILGDITIGNNV 117

                         90       100
                 ....*....|....*....|....
7RA4_C       244 KIGAGSVVVSDVPPSITVVGVPAK 267
Cdd:PRK10191 118 TVGAGSVVLDSVPDNALVVGEKAR 141
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 194-265 1.13e-18

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: 81.76  E-value: 1.13e-18
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7RA4_C      194 VLGNNISILHGVTLGGsgkeggdrHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPSITVVGVP 265
Cdd:cd03360 134 VIGDFVHIAPGVVLSG--------GVTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 197-269 3.41e-17

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: 75.62  E-value: 3.41e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C      197 NNISILHGVTLG-----------------GSGKEGGD--RHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPP 257
Cdd:cd03358  27 SNVSIYEGVTIEddvfigpnvvftndlypRSKIYRKWelKGTTVKRGASIGANATILPGVTIGEYALVGAGAVVTKDVPP 106

                        90
                ....*....|..
7RA4_C      258 SITVVGVPAKPV 269
Cdd:cd03358 107 YALVVGNPARII 118
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 187-269 7.44e-17

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: 74.42  E-value: 7.44e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C      187 FVAGETAVLGNNISILHGVTL-GGSGKEGGDRHP----------KIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDV 255
Cdd:cd04647  16 ISAGGGITIGDNVLIGPNVTIyDHNHDIDDPERPieqgvtsapiVIGDDVWIGANVVILPGVTIGDGAVVGAGSVVTKDV 95

                        90
                ....*....|....
7RA4_C      256 PPSITVVGVPAKPV 269
Cdd:cd04647  96 PPNSIVAGNPAKVI 109
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 221-269 2.53e-15

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: 72.07  E-value: 2.53e-15
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
7RA4_C      221 IGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPSITVVGVPAKPV 269
Cdd:cd03357 121 IGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 220-269 8.73e-14

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


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 67.18  E-value: 8.73e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
7RA4_C      220 KIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPP-SItVVGVPAKPV 269
Cdd:cd03349  75 IIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPyAI-VGGNPAKVI 124
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 173-251 1.11e-13

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: 64.96  E-value: 1.11e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
7RA4_C      173 ARLGYGLMLDHATgfVAGETAVLGNNISILHGVTLGGSGKEGGDRHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVV 251
Cdd:cd00208   1 VFIGEGVKIHPKA--VIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVV 77
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 220-275 8.26e-13

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: 67.74  E-value: 8.26e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
7RA4_C      220 KIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPSITVVGVPAKPVARSLKT 275
Cdd:COG1044 260 KIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQPHREWLRN 315
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 220-268 4.14e-12

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: 63.97  E-value: 4.14e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
7RA4_C      220 KIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPSITVVGVPAKP 268
Cdd:cd03352 152 TIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQP 200
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 194-269 8.79e-12

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: 63.61  E-value: 8.79e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
7RA4_C      194 VLGNNISILHGVTLGGsgkeggdrHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPSITVVGVPAKPV 269
Cdd:cd03351 122 VIGNNVILANNATLAG--------HVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLR 189
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 194-269 9.68e-12

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: 63.50  E-value: 9.68e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
7RA4_C      194 VLGNNISILHGVTLGGsgkeggdrHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPSITVVGVPAKPV 269
Cdd:COG1043 124 VVGNNVILANNATLAG--------HVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARLR 191
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
194-268 6.38e-11

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 61.27  E-value: 6.38e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
7RA4_C       194 VLGNNISILHGVTLGGsgkeggdrHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPSITVVGVPAKP 268
Cdd:PRK05289 125 VVGNHVILANNATLAG--------HVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDVPPYVLAEGNPARL 191
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 194-269 7.94e-11

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: 59.35  E-value: 7.94e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
7RA4_C      194 VLGNNISILHGVTLGGSgkeggdrhpKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSD--VPPSITVVGVPAKPV 269
Cdd:cd04645  62 IIGDNVTVGHGAVLHGC---------TIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGkvIPPGSLVAGSPAKVV 130
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 183-269 1.21e-10

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 58.89  E-value: 1.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C      183 HATGfvaGETAVLGNNISILHGVTLGGSgkeggdrhpKIGDGVMIGANASILGNIRIGSNAKIGAGSVVV--SDVPPSIT 260
Cdd:COG0663  65 HVDP---GYPLTIGDDVTIGHGAILHGC---------TIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGSL 132


                ....*....
7RA4_C      261 VVGVPAKPV 269
Cdd:COG0663 133 VVGSPAKVV 141
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 192-267 2.23e-10

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 58.86  E-value: 2.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C       192 TAVLGNNISILHGVTLGGSG-------KEGGDRHP---KIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPSITV 261
Cdd:PRK09527  95 TVTIGDNVLIAPNVTLSVTGhpvhhelRKNGEMYSfpiTIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVA 174


                 ....*.
7RA4_C       262 VGVPAK 267
Cdd:PRK09527 175 AGVPCR 180
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 221-269 4.17e-10

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


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 56.07  E-value: 4.17e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
7RA4_C      221 IGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPSITVVGVPAKPV 269
Cdd:cd05825  59 IGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 139-271 8.41e-10

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 57.13  E-value: 8.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C       139 HRINHRLyLDGRKTLAYFLQNRMSEVFGVDIHPAARLGYGLMLDHATGFVAGETAVL--------GNNISILHGV----- 205
Cdd:PRK10092  33 HRYNHSL-PDEHTLRQQILADLFGQVTEAYIEPTFRCDYGYNIFLGNNFYANFDCVMldvcpiriGDNCMLAPGVhiyta 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7RA4_C       206 ------TLGGSGKEGGdRHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPSITVVGVPAKPVAR 271
Cdd:PRK10092 112 thpldpVARNSGAELG-KPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKK 182
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 162-257 1.02e-09

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 58.62  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C       162 SEVFG------VDIHPAARLGYGLMLDHAT---GFVAGETAVLGNNISILHGVTLG----------GSGK-----EGGDR 217
Cdd:PRK14357 302 SECEKsvieddVSVGPFSRLREGTVLKKSVkigNFVEIKKSTIGENTKAQHLTYLGdatvgknvniGAGTitcnyDGKKK 381

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
7RA4_C       218 HPK-IGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPP 257
Cdd:PRK14357 382 NPTfIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPP 422
PRK10502 PRK10502
putative acyl transferase; Provisional
 166-269 2.42e-09

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 55.73  E-value: 2.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C       166 GVDIHPAARLGYGLML---DHATgfvAGETAVL--------GNNISILHGVTLGGSGKEGGDRH------P-KIGDGVMI 227
Cdd:PRK10502  57 GVVIRPSVRITYPWKLtigDYAW---IGDDVWLynlgeitiGAHCVISQKSYLCTGSHDYSDPHfdlntaPiVIGEGCWL 133

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
7RA4_C       228 GANASILGNIRIGSNAKIGAGSVVVSDVPPSITVVGVPAKPV 269
Cdd:PRK10502 134 AADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPI 175
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 220-275 4.54e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 56.30  E-value: 4.54e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
7RA4_C       220 KIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPS-ITVVGVPAKPVARSLKT 275
Cdd:PRK00892 263 KIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPgEYSSGIPAQPNKEWLRT 319
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 171-256 6.60e-09

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 56.27  E-value: 6.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C       171 PAARLGYGLMLD---HATGFVAGETAVLGNNISILHGVTLG----GSGK-----------EGGDRHPK-IGDGVMIGANA 231
Cdd:PRK14356 332 PYARLRPGAVLEegaRVGNFVEMKKAVLGKGAKANHLTYLGdaeiGAGAnigagtitcnyDGVNKHRTvIGEGAFIGSNT 411

                         90       100
                 ....*....|....*....|....*
7RA4_C       232 SILGNIRIGSNAKIGAGSVVVSDVP 256
Cdd:PRK14356 412 ALVAPVTIGDGALVGAGSVITKDVP 436
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 194-268 9.83e-09

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: 54.96  E-value: 9.83e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
7RA4_C        194 VLGNNISILHGVTLGGsgkeggdrHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPSITVVGVPAKP 268
Cdd:TIGR01852 121 VVGNHVILANNATLAG--------HVEVGDYAIIGGLVAVHQFVRIGRYAMIGGLSAVSKDVPPYCLAEGNRARL 187
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 220-263 1.77e-08

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: 53.19  E-value: 1.77e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
7RA4_C      220 KIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPSITVVG 263
Cdd:cd03353 146 VIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALAIA 189
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 160-255 2.30e-08

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 54.37  E-value: 2.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C       160 RMSEVFGVDIHPAARLGYglmldHATGFVAgETAVLGNNISILHGVTLGgsgkeggdRHPKIGDGVMIGANASILGNIRI 239
Cdd:PRK00892  86 RLAQLFDPPATPSPAAGI-----HPSAVID-PSAKIGEGVSIGPNAVIG--------AGVVIGDGVVIGAGAVIGDGVKI 151

                         90
                 ....*....|....*.
7RA4_C       240 GSNAKIGAGSVVVSDV 255
Cdd:PRK00892 152 GADCRLHANVTIYHAV 167
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 183-255 4.30e-08

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: 53.48  E-value: 4.30e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
7RA4_C      183 HATGFVAgETAVLGNNISILHGVTLGgsgkeggdRHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDV 255
Cdd:COG1044 100 HPSAVID-PSAKIGEGVSIGPFAVIG--------AGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERC 163
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 169-254 5.69e-08

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 53.22  E-value: 5.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C       169 IHPAARLGYGLMLDHatGFVAGETAVLGNNISILHGVTLGgsgkeggdRHPKIGDGVMIGANASILGNIRIGSNAKIGAG 248
Cdd:PRK00892 109 IDPSAKIGEGVSIGP--NAVIGAGVVIGDGVVIGAGAVIG--------DGVKIGADCRLHANVTIYHAVRIGNRVIIHSG 178


                 ....*.
7RA4_C       249 SVVVSD 254
Cdd:PRK00892 179 AVIGSD 184
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
218-247 3.49e-07

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 45.79  E-value: 3.49e-07
                          10        20        30
                  ....*....|....*....|....*....|
7RA4_C        218 HPKIGDGVMIGANASILGNIRIGSNAKIGA 247
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 220-267 6.48e-07

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 48.72  E-value: 6.48e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
7RA4_C       220 KIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPSITVVGVPAK 267
Cdd:PRK09677 132 VIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAK 179
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 220-257 1.52e-06

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: 49.25  E-value: 1.52e-06
                        10        20        30
                ....*....|....*....|....*....|....*...
7RA4_C      220 KIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPP 257
Cdd:COG1207 396 VIGDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDVPA 433
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 195-274 1.78e-06

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: 46.79  E-value: 1.78e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C      195 LGNNISILHGVTLGGSgkeggdrhpKIGDGVMIGANASILGNIRIGSNAKIGAGSVVV--SDVPPSITVVGVPAKpVARS 272
Cdd:cd04650  64 IGDYVTIGHNAVVHGA---------KVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAK-VVRK 133


                ..
7RA4_C      273 LK 274
Cdd:cd04650 134 LT 135
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 173-266 2.45e-06

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


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 46.22  E-value: 2.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C      173 ARLGYGLMLDhaTGFVAGETAVLGNNISILHGVTLGGSGKEGGDRHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVV 252
Cdd:cd03350  32 AYVDEGTMVD--SWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLT 109

                        90       100       110
                ....*....|....*....|....*....|
7RA4_C      253 S---------------DVPPSITVV-GVPA 266
Cdd:cd03350 110 QstpiydretgeiyygRVPPGSVVVaGSLP 139
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 221-257 3.07e-06

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 47.93  E-value: 3.07e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
7RA4_C       221 IGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPP 257
Cdd:PRK14353 383 IGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPD 419
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 166-268 3.08e-06

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 47.32  E-value: 3.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C       166 GVDIHPAARLGYGLMLDHATGFVA----GETAVLGNNISILHGVTLGGsgkeggdrHPKIGDGVMIGANASILGNIRIGS 241
Cdd:PRK12461  89 GVTIHRGTKGGGVTRIGNDNLLMAyshvAHDCQIGNNVILVNGALLAG--------HVTVGDRAIISGNCLVHQFCRIGA 160

                         90       100
                 ....*....|....*....|....*..
7RA4_C       242 NAKIGAGSVVVSDVPPSITVVGVPAKP 268
Cdd:PRK12461 161 LAMMAGGSRISKDVPPYCMMAGHPTNV 187
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 188-254 3.77e-06

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: 46.63  E-value: 3.77e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
7RA4_C      188 VAGETAVLGNNISILHGVTLGgsgkeggdRHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSD 254
Cdd:cd03352  15 VIGEGVVIGDGVVIGPGVVIG--------DGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSD 73
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 166-256 4.22e-06

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 47.67  E-value: 4.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C       166 GVDIHPAARLGYGLMLD---HATGFVAGETA-----VLGNNISILHGVTLG-----GSGK-----EGGDRH-PKIGDGVM 226
Cdd:PRK14358 328 GSDVGPFARLRPGTVLGegvHIGNFVETKNArldagVKAGHLAYLGDVTIGaetnvGAGTivanfDGVNKHqSKVGAGVF 407

                         90       100       110
                 ....*....|....*....|....*....|
7RA4_C       227 IGANASILGNIRIGSNAKIGAGSVVVSDVP 256
Cdd:PRK14358 408 IGSNTTLIAPRVVGDAAFIAAGSAVHDDVP 437
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 190-273 4.84e-06

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


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 45.44  E-value: 4.84e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C      190 GETAVLGNNISILHGVTLGGSgkeggdrhpKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVS--DVPPSITVVGVPAK 267
Cdd:cd04745  59 GQDTVLEENGHIGHGAILHGC---------TIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAK 129


                ....*.
7RA4_C      268 pVARSL 273
Cdd:cd04745 130 -VIREL 134
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 193-256 2.56e-05

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 45.30  E-value: 2.56e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C       193 AVLGNNISIlhgvtlgGSGK-----EGGDRHP-KIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVP 256
Cdd:PRK14360 366 ATLGEQVNI-------GAGTitanyDGVKKHRtVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVP 428
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 218-261 2.66e-05

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: 43.77  E-value: 2.66e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
7RA4_C      218 HPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPPSITV 261
Cdd:cd00710   2 EPVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADEGTPIII 45
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 192-255 2.80e-05

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 43.94  E-value: 2.80e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
7RA4_C      192 TAVLGNNISILHGVTLGgsgkeggdRHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDV 255
Cdd:cd03352   1 SAKIGENVSIGPNAVIG--------EGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGC 56
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 173-271 5.44e-05

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: 44.36  E-value: 5.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C        173 ARLGYGLMLdHATGFVAGETAVLGNNISILHGVTLGGSGKEGGDRHP---KIGDGVMIGANASILGNIRIGSNAKIGAGS 249
Cdd:TIGR02353 113 AKIGKGVDI-GSLPPVCTDLLTIGAGTIVRKEVMLLGYRAERGRLHTgpvTLGRDAFIGTRSTLDIDTSIGDGAQLGHGS 191

                          90       100
                  ....*....|....*....|....
7RA4_C        250 VVVSD--VPPSITVVGVPAKPVAR 271
Cdd:TIGR02353 192 ALQGGqsIPDGERWHGSPAQKTGA 215
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 218-257 7.73e-05

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 43.67  E-value: 7.73e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
7RA4_C       218 HPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPP 257
Cdd:PRK14354 393 KTIIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPE 432
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 221-257 1.01e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 43.58  E-value: 1.01e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
7RA4_C       221 IGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPP 257
Cdd:PRK14355 400 IEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPP 436
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 126-289 1.15e-04

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: 42.80  E-value: 1.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C      126 PLLYFKgFHAIQAHRINHRLYLD--GRKTlAYFLQNrmsevfGVDIHPAARLGYG--------LMldhaTGFV---AG-- 190
Cdd:COG2171  63 ILLSFR-LEDNRVLEGGGVTYHDkvPLKF-DYFKPA------GVRIVPGARVRLGaylapgvvLM----PSFVnigAYvd 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C      191 -----ET-------AVLGNNISILHGVTLGGSgKEGGDRHP-KIGDGVMIGANASILGNIRIGSNAKIGAGSVV-----V 252
Cdd:COG2171 131 egtmvDTwatvgscAQIGKNVHLSGGAGIGGV-LEPLQAAPvIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLtastkI 209

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
7RA4_C      253 SDVP-PSITVVGVPAKPV--ARSLktPSADMDQNIQFAEI 289
Cdd:COG2171 210 YDRVtGEVYYGRVPAGSVvvPGSL--PGKDGDYGLYCAVI 247
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
183-251 1.88e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 42.01  E-value: 1.88e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
7RA4_C       183 HATGFVAgETAVLGNNISILHGVTLGGsgkeggdrHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVV 251
Cdd:PRK05289   6 HPTAIVE-PGAKIGENVEIGPFCVIGP--------NVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASI 65
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
220-251 2.20e-04

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 37.80  E-value: 2.20e-04
                          10        20        30
                  ....*....|....*....|....*....|..
7RA4_C        220 KIGDGVMIGANASIlgNIRIGSNAKIGAGSVV 251
Cdd:pfam14602   2 IIGDNCLIGANSGI--GVSLGDNCVVGAGVVI 31
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 183-251 2.48e-04

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: 41.54  E-value: 2.48e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
7RA4_C      183 HATGFVAgETAVLGNNISILHGVTLGGsgkeggdrHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVV 251
Cdd:COG1043   5 HPTAIVD-PGAKLGENVEIGPFCVIGP--------DVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASI 64
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 191-271 2.50e-04

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: 41.25  E-value: 2.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C      191 ETAVLGNNISILHGVTLGGsgkeggdrHPKIGDGVMIGANaSILGNIRIGSNAKIGAGSVVVSDVPPSITVVGvpakPVA 270
Cdd:cd03353  14 GDVEIGVDVVIDPGVILEG--------KTVIGEDCVIGPN-CVIKDSTIGDGVVIKASSVIEGAVIGNGATVG----PFA 80


                .
7RA4_C      271 R 271
Cdd:cd03353  81 H 81
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 183-251 3.17e-04

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 41.26  E-value: 3.17e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
7RA4_C      183 HATGFVAgETAVLGNNISILHGVTLGGsgkeggdrHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVV 251
Cdd:cd03351   3 HPTAIVD-PGAKIGENVEIGPFCVIGP--------NVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASI 62
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 217-257 7.31e-04

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 40.69  E-value: 7.31e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
7RA4_C       217 RHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDVPP 257
Cdd:PRK14352 398 HRTTIGSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPP 438
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 193-251 8.86e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 40.01  E-value: 8.86e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
7RA4_C       193 AVLGNNISILHGVTLGgsgkeggdRHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVV 251
Cdd:PRK12461  12 AKLGSGVEIGPFAVIG--------ANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVV 62
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 215-255 1.20e-03

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 38.85  E-value: 1.20e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
7RA4_C      215 GDRHPKIGDGVMIGANASILGNIRIGSNAKIGAGSVVVSDV 255
Cdd:COG0663   7 DGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDV 47
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 191-246 1.52e-03

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 39.91  E-value: 1.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
7RA4_C       191 ETAVLGNNISILHGVTlggsgkeggdRHPKIGDGVMIGANASILGNIRIGSNAKIG 246
Cdd:PRK14360 296 ENSQIGENVTVLYSVV----------SDSQIGDGVKIGPYAHLRPEAQIGSNCRIG 341
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 193-255 2.90e-03

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 36.07  E-value: 2.90e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
7RA4_C      193 AVLGNNISILHGVTLGGSgkeggdrhpKIGDGVMIGANASILGNIrIGSNAKIGAGSVVVSDV 255
Cdd:cd03356  17 SVIGDNVRIGDGVTITNS---------ILMDNVTIGANSVIVDSI-IGDNAVIGENVRVVNLC 69
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 221-251 6.40e-03

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: 36.80  E-value: 6.40e-03
                        10        20        30
                ....*....|....*....|....*....|.
7RA4_C      221 IGDGVMIGANASILGNIRIGSNAKIGAGSVV 251
Cdd:cd05636 132 IGDGVKTGINVSLNPGVKIGPGSWVYPGCVV 162
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 190-255 8.30e-03

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 34.52  E-value: 8.30e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
7RA4_C      190 GETAVLGNNISILHGVtlggsgkeggdrhpkIGDGVMIGANASILGNIrIGSNAKIGAGSVVVSDV 255
Cdd:cd03356   3 GESTVIGENAIIKNSV---------------IGDNVRIGDGVTITNSI-LMDNVTIGANSVIVDSI 52
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 220-270 9.15e-03

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


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 36.04  E-value: 9.15e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C      220 KIGDGVMIGAN-----ASILGNIRIGSNAKIG------------AGSVVVSD--VPPSITVVGVPAKPVA 270
Cdd:cd03359  74 HIGDYVFIGENcvvnaAQIGSYVHIGKNCVIGrrciikdcvkilDGTVVPPDtvIPPYSVVSGRPARFIG 143
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 149-250 9.32e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 37.42  E-value: 9.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7RA4_C       149 GRKTLAYFLQNRMsEVFGVD----IHPAARLGYG-----LMLDHATgFVAGET------AVLGNNISILHGVTLGGSgke 213
Cdd:PRK14355 212 GLRCLAFPVADPD-EIMGVNdraqLAEAARVLRRrinreLMLAGVT-LIDPETtyidrgVVIGRDTTIYPGVCISGD--- 286

                         90       100       110
                 ....*....|....*....|....*....|....*..
7RA4_C       214 ggdrhPKIGDGVMIGANASILGnIRIGSNAKIGAGSV 250
Cdd:PRK14355 287 -----TRIGEGCTIEQGVVIKG-CRIGDDVTVKAGSV 317
 
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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