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Conserved domains on  [gi|188219518|ref|NP_067621|]
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dynactin subunit 5 [Mus musculus]

Protein Classification

dynactin subunit 5( domain architecture ID 10129731)

dynactin subunit 5 is a member of the pointed-end complex of the dynactin shoulder complex which contains DCTN4, DCTN5 and DCTN6 subunits and ACTR10

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 13-173 1.95e-105

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: 299.13  E-value: 1.95e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  13 YIETASGNKVSRQSVLCGSQNIVLNGKTIIMNDCIIRGDLANVRVGRHCVVKSRSVIRPPFKKFSKGVAFFPLHIGDHVF 92
Cdd:cd03359    1 YIETASGNKVSRKSVICGSQNIVLNGKTIIQSDVIIRGDLATVSIGRYCILSEGCVIRPPFKKFSKGVAFFPLHIGDYVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  93 IEEDCVVNAAQIGSYVHVGKNCVIGRRCVLKDCCKILDNTVLPPETVVPPFTVFSGCPGLFSGELPECTQELMIDVTKSY 172
Cdd:cd03359   81 IGENCVVNAAQIGSYVHIGKNCVIGRRCIIKDCVKILDGTVVPPDTVIPPYSVVSGRPARFIGELPECTQELMEEETKEY 160


                 .
gi 188219518 173 Y 173
Cdd:cd03359  161 Y 161
 
Name Accession Description Interval E-value
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 13-173 1.95e-105

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: 299.13  E-value: 1.95e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  13 YIETASGNKVSRQSVLCGSQNIVLNGKTIIMNDCIIRGDLANVRVGRHCVVKSRSVIRPPFKKFSKGVAFFPLHIGDHVF 92
Cdd:cd03359    1 YIETASGNKVSRKSVICGSQNIVLNGKTIIQSDVIIRGDLATVSIGRYCILSEGCVIRPPFKKFSKGVAFFPLHIGDYVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  93 IEEDCVVNAAQIGSYVHVGKNCVIGRRCVLKDCCKILDNTVLPPETVVPPFTVFSGCPGLFSGELPECTQELMIDVTKSY 172
Cdd:cd03359   81 IGENCVVNAAQIGSYVHIGKNCVIGRRCIIKDCVKILDGTVVPPDTVIPPYSVVSGRPARFIGELPECTQELMEEETKEY 160


                 .
gi 188219518 173 Y 173
Cdd:cd03359  161 Y 161
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 46-151 4.69e-09

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 52.72  E-value: 4.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  46 CIIRGDLANVRVGRHCVVKSRSVIRppfkkfskGVAFFPLHIGDHVFIEEDCVVNAAQIGSYVHVGKNCVIGRRCVLKDC 125
Cdd:COG0663   41 AVLRGDVGPIRIGEGSNIQDGVVLH--------VDPGYPLTIGDDVTIGHGAILHGCTIGDNVLIGMGAIVLDGAVIGDG 112

                         90       100
                 ....*....|....*....|....*.
gi 188219518 126 CKILDNTVLPPETVVPPFTVFSGCPG 151
Cdd:COG0663  113 SIVGAGALVTEGKVVPPGSLVVGSPA 138
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 33-122 1.72e-08

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: 52.26  E-value: 1.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518   33 NIVLNGKTIIMNDCIIRGdlaNVRVGRHCVVKSRSVI--RPPFKKFSKGVAFfpLHIGDHVFIEEDCVVNAA-------- 102
Cdd:TIGR01852  28 GVKIGDGVELKSHVVILG---HTTIGEGTRIFPGAVIggVPQDLKYKGEKTR--LIIGDNNTIREFVTINRGtasgggvt 102

                          90       100
                  ....*....|....*....|....*.
gi 188219518  103 QIGS------YVHVGKNCVIGRRCVL 122
Cdd:TIGR01852 103 RIGNnnllmaYSHIAHDCVVGNHVIL 128
PLN02472 PLN02472
uncharacterized protein
 33-178 1.04e-06

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 47.26  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  33 NIVLNGKTIIMNDC------IIRGDLANVRVGRHCVVKSRSVIRPPFKKfskgvaffPLHIGDHVFIEEDCVVNAAQIGS 106
Cdd:PLN02472  71 NVVLAGQVTVWDGAsvwngaVLRGDLNKITVGFCSNVQERCVLHAAWNS--------PTGLPAETLIDRYVTIGAYSLLR 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518 107 YVHVGKNCVIGRRCVLKDCCKILDNTVLPPETVVPP------FTVFSGCPGLFSGELP-ECTQEL------MIDVTKSYY 173
Cdd:PLN02472 143 SCTIEPECIIGQHSILMEGSLVETHSILEAGSVLPPgrriptGELWAGNPARFVRTLTnEETLEIpklavaINDLSQSHF 222


                 ....*
gi 188219518 174 QKFLP 178
Cdd:PLN02472 223 SEFLP 227
 
Name Accession Description Interval E-value
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 13-173 1.95e-105

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: 299.13  E-value: 1.95e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  13 YIETASGNKVSRQSVLCGSQNIVLNGKTIIMNDCIIRGDLANVRVGRHCVVKSRSVIRPPFKKFSKGVAFFPLHIGDHVF 92
Cdd:cd03359    1 YIETASGNKVSRKSVICGSQNIVLNGKTIIQSDVIIRGDLATVSIGRYCILSEGCVIRPPFKKFSKGVAFFPLHIGDYVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  93 IEEDCVVNAAQIGSYVHVGKNCVIGRRCVLKDCCKILDNTVLPPETVVPPFTVFSGCPGLFSGELPECTQELMIDVTKSY 172
Cdd:cd03359   81 IGENCVVNAAQIGSYVHIGKNCVIGRRCIIKDCVKILDGTVVPPDTVIPPYSVVSGRPARFIGELPECTQELMEEETKEY 160


                 .
gi 188219518 173 Y 173
Cdd:cd03359  161 Y 161
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 55-140 2.48e-14

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: 64.58  E-value: 2.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  55 VRVGRHCVVKSRSVIRPPfkkfskgvaffpLHIGDHVFIEEDCVVNAAQIG---SYVHVGKNCVIGRRCVLKDCCKILDN 131
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGP------------VVIGDNVNIGPGAVIGAATGPnekNPTIIGDNVEIGANAVIHGGVKIGDN 68


                 ....*....
gi 188219518 132 TVLPPETVV 140
Cdd:cd00208   69 AVIGAGAVV 77
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 46-172 3.56e-13

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: 63.58  E-value: 3.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  46 CIIRGDLANVRVGRHCVVKSRSVIRPpfkkfSKGvafFPLHIGDHVFIEEDCVVNAAQIGSYVHVGKNCVIGRRCVLKDC 125
Cdd:cd04645   30 AVLRGDVNPIRIGERTNIQDGSVLHV-----DPG---YPTIIGDNVTVGHGAVLHGCTIGDNCLIGMGAIILDGAVIGKG 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 188219518 126 CKILDNTVLPPETVVPPFTVFSGCPGLFSGELPECTQELMIDVTKSY 172
Cdd:cd04645  102 SIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAELRESAEHY 148
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 33-177 2.53e-12

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


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 61.43  E-value: 2.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  33 NIVLNGKTIIMNDCIIRGDLANVRVGRHCVVKSRSVIRPpfkkfSKGvafFPLHIGDHVFIEEDCVVNAAQIGSYVHVGK 112
Cdd:cd04650   18 DVVIGELTSVWHYAVIRGDNDSIYIGKYSNVQENVSIHT-----DHG---YPTEIGDYVTIGHNAVVHGAKVGNYVIVGM 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 188219518 113 NCVIGRRCVLKDCCKILDNTVLPPETVVPPFTVFSGCPGLFSGELPEcTQELMIDVTKSYYQKFL 177
Cdd:cd04650   90 GAILLNGAKIGDHVIIGAGAVVTPGKEIPDYSLVLGVPAKVVRKLTE-EEIEWIKKNAEEYVELA 153
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 46-151 4.69e-09

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 52.72  E-value: 4.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  46 CIIRGDLANVRVGRHCVVKSRSVIRppfkkfskGVAFFPLHIGDHVFIEEDCVVNAAQIGSYVHVGKNCVIGRRCVLKDC 125
Cdd:COG0663   41 AVLRGDVGPIRIGEGSNIQDGVVLH--------VDPGYPLTIGDDVTIGHGAILHGCTIGDNVLIGMGAIVLDGAVIGDG 112

                         90       100
                 ....*....|....*....|....*.
gi 188219518 126 CKILDNTVLPPETVVPPFTVFSGCPG 151
Cdd:COG0663  113 SIVGAGALVTEGKVVPPGSLVVGSPA 138
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 86-134 9.77e-09

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: 9.77e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 188219518  86 HIGDHVFIEEDCVVNA-AQIGSYVHVGKNCVIGRRCVLKDCCKILDNTVL 134
Cdd:COG1044  116 SIGPFAVIGAGVVIGDgVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVI 165
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 33-122 1.72e-08

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: 52.26  E-value: 1.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518   33 NIVLNGKTIIMNDCIIRGdlaNVRVGRHCVVKSRSVI--RPPFKKFSKGVAFfpLHIGDHVFIEEDCVVNAA-------- 102
Cdd:TIGR01852  28 GVKIGDGVELKSHVVILG---HTTIGEGTRIFPGAVIggVPQDLKYKGEKTR--LIIGDNNTIREFVTINRGtasgggvt 102

                          90       100
                  ....*....|....*....|....*.
gi 188219518  103 QIGS------YVHVGKNCVIGRRCVL 122
Cdd:TIGR01852 103 RIGNnnllmaYSHIAHDCVVGNHVIL 128
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 17-148 1.28e-07

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


Pssm-ID: 100052 [Multi-domain]  Cd Length: 164  Bit Score: 48.86  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  17 ASGNKVSRQSVLCGsqNIVLNGKTIIMNDCIIRGDLANVRVGRHCVVKSRSVIRPPFKKfsKGVAFFPLHIGDHVFIEED 96
Cdd:cd04646    3 APGAVVCQESEIRG--DVTIGPGTVVHPRATIIAEAGPIIIGENNIIEEQVTIVNKKPK--DPAEPKPMIIGSNNVFEVG 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 188219518  97 CVVNAAQIGSYVHVGKNCVIGRRCVLKDCCKILDNTVLPPETVVPPFTVFSG 148
Cdd:cd04646   79 CKCEALKIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPSSEILPENTVIYG 130
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
33-150 1.33e-07

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 48.33  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  33 NIVLNGKTIIMNDCIIRGdlANVRVGRHCVVKSRSVIrppfkkfskgVAFFPLHIGDHVFIEEDCVVNAA---------- 102
Cdd:COG0110    8 GARIGDGVVIGPGVRIYG--GNITIGDNVYIGPGVTI----------DDPGGITIGDNVLIGPGVTILTGnhpiddpatf 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 188219518 103 -QIGSYVHVGKNCVIGRRCVLKDCCKILDNTVLPPETVV----PPFTVFSGCP 150
Cdd:COG0110   76 pLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVtkdvPPYAIVAGNP 128
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 40-122 7.39e-07

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: 47.71  E-value: 7.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  40 TIIMNDCIIRGdlaNVRVGRHCVVKSRSVI--RPPFKKFSKGVAFfpLHIGDHVFIEEDCVVNAA--------QIGS--- 106
Cdd:COG1043   38 TVIGSHVVIEG---PTTIGKNNRIFPFASIgeEPQDLKYKGEPTR--LEIGDNNTIREFVTIHRGtvqgggvtRIGDdnl 112

                         90
                 ....*....|....*....
gi 188219518 107 ---YVHVGKNCVIGRRCVL 122
Cdd:COG1043  113 lmaYVHVAHDCVVGNNVIL 131
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 40-122 7.94e-07

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: 47.43  E-value: 7.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  40 TIIMNDCIIRGdlaNVRVGRHCVVKSRSVI--RPPFKKFSKGVAFfpLHIGDHVFIEEDCVVNAA--------QIGS--- 106
Cdd:cd03351   36 TVIGSHVVIDG---PTTIGKNNRIFPFASIgeAPQDLKYKGEPTR--LEIGDNNTIREFVTIHRGtaqgggvtRIGNnnl 110

                         90
                 ....*....|....*....
gi 188219518 107 ---YVHVGKNCVIGRRCVL 122
Cdd:cd03351  111 lmaYVHVAHDCVIGNNVIL 129
PLN02472 PLN02472
uncharacterized protein
 33-178 1.04e-06

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 47.26  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  33 NIVLNGKTIIMNDC------IIRGDLANVRVGRHCVVKSRSVIRPPFKKfskgvaffPLHIGDHVFIEEDCVVNAAQIGS 106
Cdd:PLN02472  71 NVVLAGQVTVWDGAsvwngaVLRGDLNKITVGFCSNVQERCVLHAAWNS--------PTGLPAETLIDRYVTIGAYSLLR 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518 107 YVHVGKNCVIGRRCVLKDCCKILDNTVLPPETVVPP------FTVFSGCPGLFSGELP-ECTQEL------MIDVTKSYY 173
Cdd:PLN02472 143 SCTIEPECIIGQHSILMEGSLVETHSILEAGSVLPPgrriptGELWAGNPARFVRTLTnEETLEIpklavaINDLSQSHF 222


                 ....*
gi 188219518 174 QKFLP 178
Cdd:PLN02472 223 SEFLP 227
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 87-134 1.19e-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: 1.19e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 188219518  87 IGDHVFIEEDCVV-NAAQIGSYVHVGKNCVIGRRCVLKDCCKILDNTVL 134
Cdd:cd03352   10 IGPNAVIGEGVVIgDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCII 58
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 40-133 1.35e-06

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: 46.32  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  40 TIIMNDCIIrgdLANVRVGRHCVVKSRSvirppfkkfskgvaffplHIGDHVFIEEDCVVNA-AQIGSYVHVGKNCVIGR 118
Cdd:cd03360  103 CVIMAGAVI---NPDARIGDNVIINTGA------------------VIGHDCVIGDFVHIAPgVVLSGGVTIGEGAFIGA 161

                         90
                 ....*....|....*
gi 188219518 119 RCVLKDCCKILDNTV 133
Cdd:cd03360  162 GATIIQGVTIGAGAI 176
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 33-150 1.80e-06

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: 44.75  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  33 NIVLNGKTIIMNDCIIrGDLANVRVGRHCVVKSRSVIR-------PPFKKFSKGVAFFPLHIGDHVFIEEDCVVNAaqiG 105
Cdd:cd04647    1 NISIGDNVYIGPGCVI-SAGGGITIGDNVLIGPNVTIYdhnhdidDPERPIEQGVTSAPIVIGDDVWIGANVVILP---G 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 188219518 106 syVHVGKNCVIGRRC-VLKDcckildntvlppetvVPPFTVFSGCP 150
Cdd:cd04647   77 --VTIGDGAVVGAGSvVTKD---------------VPPNSIVAGNP 105
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 86-134 7.68e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 45.13  E-value: 7.68e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 188219518  86 HIGDHVFIEEDCVV-NAAQIGSYVHVGKNCVIGRRCVLKDCCKILDNTVL 134
Cdd:PRK00892 120 SIGPNAVIGAGVVIgDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRI 169
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 33-118 1.03e-05

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: 44.63  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  33 NIVLNGKTIIMNDCIIRGD--LANVRVGRHCVVKsRSVIrppfkkfskgvaffplhigDHVFIEEDCVV-------NAAQ 103
Cdd:COG1207  278 NVILEGKTVIGEGVVIGPNctLKDSTIGDGVVIK-YSVI-------------------EDAVVGAGATVgpfarlrPGTV 337

                         90       100
                 ....*....|....*....|
gi 188219518 104 IGSYVHVG-----KNCVIGR 118
Cdd:COG1207  338 LGEGVKIGnfvevKNSTIGE 357
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
40-122 1.55e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 43.93  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  40 TIIMNDCIIRGdlaNVRVGRHCVVKSRSVI--RPPFKKFSKGVAFfpLHIGDHVFIEEDCVVNAA--------QIGS--- 106
Cdd:PRK05289  39 TVIGSHVVIDG---HTTIGKNNRIFPFASIgeDPQDLKYKGEPTR--LVIGDNNTIREFVTINRGtvqgggvtRIGDnnl 113

                         90
                 ....*....|....*....
gi 188219518 107 ---YVHVGKNCVIGRRCVL 122
Cdd:PRK05289 114 lmaYVHVAHDCVVGNHVIL 132
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 40-122 1.65e-05

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 43.86  E-value: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  40 TIIMNDCIIRGdlaNVRVGRHCVVKSRSVI--RPPFKKFSKGVAFfpLHIGDHVFIEEDCVV-------NAAQIGS---- 106
Cdd:PRK12461  36 TWIGPHAVILG---PTRIGKNNKIHQGAVVgdEPQDFTYKGEESR--LEIGDRNVIREGVTIhrgtkggGVTRIGNdnll 110

                         90
                 ....*....|....*...
gi 188219518 107 --YVHVGKNCVIGRRCVL 122
Cdd:PRK12461 111 maYSHVAHDCQIGNNVIL 128
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 40-134 3.30e-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: 42.40  E-value: 3.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  40 TIIMNDCIIrGD----LANVRVGRHCVVKSRSVIRP---------PFKKFSKGVAFFP----LHIGDHVFIEEDCVVNAA 102
Cdd:cd03352   32 VVIGDGVVI-GDdcviHPNVTIYEGCIIGDRVIIHSgavigsdgfGFAPDGGGWVKIPqlggVIIGDDVEIGANTTIDRG 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 188219518 103 -----QIGSY------VHVGKNCVIGRRCVLKDCCKILDNTVL 134
Cdd:cd03352  111 algdtVIGDGtkidnlVQIAHNVRIGENCLIAAQVGIAGSTTI 153
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 86-140 4.42e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 42.82  E-value: 4.42e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 188219518  86 HIGDHVFIEEDCVVNA-AQIGSYVHVGKNCVIGRRCVLKDCCKILDNTVLPPETVV 140
Cdd:PRK00892 108 VIDPSAKIGEGVSIGPnAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTI 163
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 54-140 5.45e-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: 42.01  E-value: 5.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  54 NVRVGRHCVVKSRSVIrppfkkfSKGVaffplHIGDHVFIEEDCVvnaaqIGSYVHVGKNCVIGRRCVLKDCCKILDNTV 133
Cdd:cd03352    1 SAKIGENVSIGPNAVI-------GEGV-----VIGDGVVIGPGVV-----IGDGVVIGDDCVIHPNVTIYEGCIIGDRVI 63


                 ....*..
gi 188219518 134 LPPETVV 140
Cdd:cd03352   64 IHSGAVI 70
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 54-142 6.78e-05

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


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 39.53  E-value: 6.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  54 NVRVGRHCVVKsRSVIrppfkkfSKGVaffplHIGDHVFIEEDCVVNAAQIGSYVHVgKNCVIGRRCVLKDCCKILDNTV 133
Cdd:cd03356    5 STVIGENAIIK-NSVI-------GDNV-----RIGDGVTITNSILMDNVTIGANSVI-VDSIIGDNAVIGENVRVVNLCI 70


                 ....*....
gi 188219518 134 LPPETVVPP 142
Cdd:cd03356   71 IGDDVVVED 79
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 53-134 8.00e-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: 41.62  E-value: 8.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  53 ANVRVGRHCVVKSRSVIRPpfkkfskgvaffplhigdHVFIEEDCVvnaaqIGSYVHVGKNCVIGRRCVLKDCCKILDNT 132
Cdd:cd03352   12 PNAVIGEGVVIGDGVVIGP------------------GVVIGDGVV-----IGDDCVIHPNVTIYEGCIIGDRVIIHSGA 68


                 ..
gi 188219518 133 VL 134
Cdd:cd03352   69 VI 70
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 87-140 8.05e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 42.05  E-value: 8.05e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 188219518  87 IGDHVFIEEDCVVNA-AQIGSYVHVGKNCVIGRRCVLKDCCKILDNTVLPPETVV 140
Cdd:PRK00892 127 IGAGVVIGDGVVIGAgAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVI 181
PRK10502 PRK10502
putative acyl transferase; Provisional
 56-122 1.38e-04

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 40.70  E-value: 1.38e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188219518  56 RVGRHCVVKSRSVIRPPFKkfskgvaffpLHIGDHVFIEEDCVV-NAAQIgsyvHVGKNCVIGRRCVL 122
Cdd:PRK10502  53 KIGKGVVIRPSVRITYPWK----------LTIGDYAWIGDDVWLyNLGEI----TIGAHCVISQKSYL 106
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 35-122 1.41e-04

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 38.71  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  35 VLNGKTIIMNDCIIRgdlaNVRVGRHCVVKSRSVIRPPFkkfskgvaffplhIGDHVFIEEDCVVNAAQIGSYVHVGKNC 114
Cdd:cd05787    1 VIGRGTSIGEGTTIK----NSVIGRNCKIGKNVVIDNSY-------------IWDDVTIEDGCTIHHSIVADGAVIGKGC 63


                 ....*...
gi 188219518 115 VIGRRCVL 122
Cdd:cd05787   64 TIPPGSLI 71
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 35-130 3.33e-04

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: 37.61  E-value: 3.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  35 VLNGKTIIMNDCIIrgdlANVRVGRHCVVKSRSVIRPPFkkfskgvaffplhIGDHVFIEEDCVVNAAQIGSYVHVGKNC 114
Cdd:cd03356    1 LIGESTVIGENAII----KNSVIGDNVRIGDGVTITNSI-------------LMDNVTIGANSVIVDSIIGDNAVIGENV 63

                         90
                 ....*....|....*.
gi 188219518 115 VIGRRCVLKDCCKILD 130
Cdd:cd03356   64 RVVNLCIIGDDVVVED 79
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 86-126 3.55e-04

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


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 39.39  E-value: 3.55e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 188219518  86 HIGDHVFIEEDCVVNA-AQIGSYVHVGKNCVIGRRCVLKDCC 126
Cdd:cd03360   98 VIGEGCVIMAGAVINPdARIGDNVIINTGAVIGHDCVIGDFV 139
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 37-155 7.67e-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: 38.95  E-value: 7.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  37 NGKTIIMNDCIIrgdLANVRVGRHCVvksrsvirppfkkfskgvaffplhIGDHVFIeedcvVNAAQIGSYVHVGKNCVI 116
Cdd:cd03351  100 GGVTRIGNNNLL---MAYVHVAHDCV------------------------IGNNVIL-----ANNATLAGHVEIGDYAII 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 188219518 117 GRRCVLKDCCKILDNTVLPPETV----VPPFTVFSGCPGLFSG 155
Cdd:cd03351  148 GGLSAVHQFCRIGRHAMVGGGSGvvqdVPPYVIAAGNRARLRG 190
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 86-150 8.56e-04

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: 38.54  E-value: 8.56e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 188219518  86 HIGDHVFIEEDCVVnAAQ--IGSYVHVGKNCVIGRRCVLKDCCKILDNTVLPPETVV----PPFTVFSGCP 150
Cdd:cd03352  128 QIAHNVRIGENCLI-AAQvgIAGSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVtsivPPGEYVSGTP 197
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 33-120 9.07e-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: 38.17  E-value: 9.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  33 NIVLNGKTIIMNDCIIRGD--LANVRVGRHCVVKSRSVIrppfkkfskgvaffplhigdhvfieEDCVV-NAAQIGSYVH 109
Cdd:cd03353   27 GVILEGKTVIGEDCVIGPNcvIKDSTIGDGVVIKASSVI-------------------------EGAVIgNGATVGPFAH 81

                         90
                 ....*....|.
gi 188219518 110 VGKNCVIGRRC 120
Cdd:cd03353   82 LRPGTVLGEGV 92
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 30-133 1.02e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 38.67  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  30 GSQNIVLNgkTIIMNDCIIRGdlANVRvgrhcvvksRSVIrppfkkFSKgvaffplhigdhVFIEEDCVVNAAQIGSYVH 109
Cdd:PRK00725 320 GRRGMAIN--SLVSGGCIISG--AVVR---------RSVL------FSR------------VRVNSFSNVEDSVLLPDVN 368

                         90       100
                 ....*....|....*....|....
gi 188219518 110 VGKNCVIgRRCVLKDCCKILDNTV 133
Cdd:PRK00725 369 VGRSCRL-RRCVIDRGCVIPEGMV 391
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 39-117 1.08e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 38.70  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  39 KTIIMNDCIIRGDL------ANVRVGRHCVVKsRSVIRPpfkkfskgvaffplhigdHVFIEEDCVVNAAQIGSYVHVGK 112
Cdd:PRK05293 293 NSLVVEGCVVYGTVehsvlfQGVQVGEGSVVK-DSVIMP------------------GAKIGENVVIERAIIGENAVIGD 353


                 ....*
gi 188219518 113 NCVIG 117
Cdd:PRK05293 354 GVIIG 358
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 7-140 1.22e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 38.65  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518   7 LYNKSEYIETASGN----KVSRqsvlcGSQNIVLNGKTIIMNDCIIRGdlANVRvgrhcvvksRSVIRPpfkkfskgvaf 82
Cdd:PRK00844 284 LYNREWPIYTSSPNlppaKFVD-----GGGRVGSAQDSLVSAGSIISG--ATVR---------NSVLSP----------- 336

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 188219518  83 fplhigdHVFIEEDCVVNAAQIGSYVHVGKNCVIgRRCvlkdcckILD-NTVLPPETVV 140
Cdd:PRK00844 337 -------NVVVESGAEVEDSVLMDGVRIGRGAVV-RRA-------ILDkNVVVPPGATI 380
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 37-155 1.30e-03

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 38.08  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  37 NGKTIIMNDCIIrgdLANVRVGRHCVvksrsvirppfkkfskgvaffplhIGDHVFIeedcvVNAAQIGSYVHVGKN--- 113
Cdd:COG1043  102 GGVTRIGDDNLL---MAYVHVAHDCV------------------------VGNNVIL-----ANNATLAGHVEVGDHaii 149

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 188219518 114 ---------CVIGRRCVLKDCCKIL-DntvlppetvVPPFTVFSGCPGLFSG 155
Cdd:COG1043  150 gglsavhqfVRIGAHAMVGGGSGVVkD---------VPPYVLAAGNPARLRG 192
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 35-174 2.30e-03

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


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 36.96  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  35 VLNGKTIIMNDCII------RGDLANVRVGRHCVVKSRSVIrppfkkfskgvaffplhigdHVFIEEDCVVNA-AQIG-- 105
Cdd:cd04745   14 VLIGDVIIGKNCYIgphaslRGDFGRIVIRDGANVQDNCVI--------------------HGFPGQDTVLEEnGHIGhg 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188219518 106 SYVH---VGKNCVIGRRCVLKDCCKILDNTVL------PPETVVPPFTVFSGCPGLFSGELPECTQELMIDVTKSYYQ 174
Cdd:cd04745   74 AILHgctIGRNALVGMNAVVMDGAVIGEESIVgamafvKAGTVIPPRSLIAGSPAKVIRELSDEEVAWKTRGTKEYQQ 151
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 53-125 2.96e-03

eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 35.25  E-value: 2.96e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 188219518  53 ANVRVGRHCVVKsRSVIRPPFKkFSKGVAFFPLHIGDHVFIEEDCVVNAAQIgsyvhvGKNCVIGRRCVLKDC 125
Cdd:cd04652    4 ENTQVGEKTSIK-RSVIGANCK-IGKRVKITNCVIMDNVTIEDGCTLENCII------GNGAVIGEKCKLKDC 68
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 93-150 3.07e-03

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 36.92  E-value: 3.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 188219518  93 IEEDCVvnaaqIGSYVHVGKNCVIGRRCVLKDCCKILDNTVLPPETVVPPFTVFSGCP 150
Cdd:COG1043   16 LGENVE-----IGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEEP 68
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 104-149 3.54e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 37.31  E-value: 3.54e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 188219518 104 IGSYVHVGKNCVIGRRCVLKDcCKILDNTVLPPETVVPPFTVFSGC 149
Cdd:PRK09451 280 IEGNVTLGNRVKIGAGCVLKN-CVIGDDCEISPYSVVEDANLGAAC 324
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 33-117 4.02e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 37.12  E-value: 4.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  33 NIVLNGKTIIMNDCII--RGDLANVRVGRHCVVKSrSVI-----------------RPPfKKFSKGVaffplHIGDhvFI 93
Cdd:PRK14354 277 GVVIKGNTVIGEDCVIgpGSRIVDSTIGDGVTITN-SVIeeskvgdnvtvgpfahlRPG-SVIGEEV-----KIGN--FV 347

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 188219518  94 EedcvVNAAQIG--------SYV---HVGKNCVIG 117
Cdd:PRK14354 348 E----IKKSTIGegtkvshlTYIgdaEVGENVNIG 378
PRK10502 PRK10502
putative acyl transferase; Provisional
 52-150 4.76e-03

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 36.08  E-value: 4.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  52 LANVRVGRHCVVKSRSVI--------RPPFKKFSKgvaffPLHIGDHVFIEEDCVVNAAqigsyVHVGKNCVIG-RRCVL 122
Cdd:PRK10502  89 LGEITIGAHCVISQKSYLctgshdysDPHFDLNTA-----PIVIGEGCWLAADVFVAPG-----VTIGSGAVVGaRSSVF 158

                         90       100
                 ....*....|....*....|....*...
gi 188219518 123 KDcckildntvlppetvVPPFTVFSGCP 150
Cdd:PRK10502 159 KS---------------LPANTICRGNP 171
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 32-122 5.84e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 36.27  E-value: 5.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  32 QNIVLNGKTIIMNDCIIrGDlaNVRVGRHCVVKSRSVIR-------------------------PPFKKFSK-----GVA 81
Cdd:PRK00892 129 AGVVIGDGVVIGAGAVI-GD--GVKIGADCRLHANVTIYhavrignrviihsgavigsdgfgfaNDRGGWVKipqlgRVI 205

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  82 ffplhIGDHV----------------FIEEDCVV-NAAQIGSYVHVGKNCV------------IGRRCVL 122
Cdd:PRK00892 206 -----IGDDVeiganttidrgalddtVIGEGVKIdNLVQIAHNVVIGRHTAiaaqvgiagstkIGRYCMI 270
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 84-142 6.93e-03

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


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 35.68  E-value: 6.93e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 188219518  84 PLHIGDHVFIEEDCVVNAAQIgsyvhvGKNCVIGRRCVLKDcCKILDNTVLPPETVVPP 142
Cdd:cd00710   82 PAYIGDNCFIGFRSVVFNAKV------GDNCVIGHNAVVDG-VEIPPGRYVPAGAVITS 133
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 102-140 8.79e-03

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: 35.76  E-value: 8.79e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 188219518 102 AQIGSYVHVGKNCVIGRRCVLKDCCKILDNTVLPPETVV 140
Cdd:COG1044  109 AKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVI 147
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 41-117 9.74e-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: 34.36  E-value: 9.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  41 IIMNDCIIRGDLA-------NVRVGRHCVVKSrSVIRPpfkkfskgvaffplhigdHVFIEEDCVVNAAQIGSYVHVGKN 113
Cdd:cd04651   14 LVSEGCIISGGTVensvlfrGVRVGSGSVVED-SVIMP------------------NVGIGRNAVIRRAIIDKNVVIPDG 74


                 ....
gi 188219518 114 CVIG 117
Cdd:cd04651   75 VVIG 78
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
37-117 9.94e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 35.46  E-value: 9.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219518  37 NGKTIIMNDCIIrgdLANVRVGRHCVvksrsvirppfkkfskgvaffplhIGDHVFIeedcvVNAAQIGSYVHVGKNCVI 116
Cdd:PRK05289 103 GGVTRIGDNNLL---MAYVHVAHDCV------------------------VGNHVIL-----ANNATLAGHVEVGDYAII 150


                 .
gi 188219518 117 G 117
Cdd:PRK05289 151 G 151
 
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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