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Conserved domains on  [gi|521039075|gb|EPQ20851|]
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Dynactin subunit 5 [Myotis brandtii]

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 ...
 1-131 5.21e-78

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: 227.87  E-value: 5.21e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075   1 MNDCIIRGDLANVRVGRHCVVKSRSVIRPLFKKFSKGVAFFPLHIGDHVFIEEDCVVNAAQIGSYVHVGKNCVIGRRCVL 80
Cdd:cd03359   31 QSDVIIRGDLATVSIGRYCILSEGCVIRPPFKKFSKGVAFFPLHIGDYVFIGENCVVNAAQIGSYVHIGKNCVIGRRCII 110

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 521039075  81 KDCCKILDNTVLPPETVVPPFTVFSGCPGLFSGELSECIQELMIDITKSYY 131
Cdd:cd03359  111 KDCVKILDGTVVPPDTVIPPYSVVSGRPARFIGELPECTQELMEEETKEYY 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 ...
 1-131 5.21e-78

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: 227.87  E-value: 5.21e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075   1 MNDCIIRGDLANVRVGRHCVVKSRSVIRPLFKKFSKGVAFFPLHIGDHVFIEEDCVVNAAQIGSYVHVGKNCVIGRRCVL 80
Cdd:cd03359   31 QSDVIIRGDLATVSIGRYCILSEGCVIRPPFKKFSKGVAFFPLHIGDYVFIGENCVVNAAQIGSYVHIGKNCVIGRRCII 110

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 521039075  81 KDCCKILDNTVLPPETVVPPFTVFSGCPGLFSGELSECIQELMIDITKSYY 131
Cdd:cd03359  111 KDCVKILDGTVVPPDTVIPPYSVVSGRPARFIGELPECTQELMEEETKEYY 161
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 4-132 1.07e-09

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 53.49  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075   4 CIIRGDLANVRVGRHCVVKSRSVIRplfkkfskGVAFFPLHIGDHVFIEEDCVVNAAQIGSYVHVGKNCVIGRRCVLKDC 83
Cdd:COG0663   41 AVLRGDVGPIRIGEGSNIQDGVVLH--------VDPGYPLTIGDDVTIGHGAILHGCTIGDNVLIGMGAIVLDGAVIGDG 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 521039075  84 CKILDNTVLPPETVVPPFTVFSGCPGLFSGELSECIQELMIDITKSYYQ 132
Cdd:COG0663  113 SIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRESAENYVE 161
PLN02472 PLN02472
uncharacterized protein
 2-136 8.05e-07

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 46.49  E-value: 8.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075   2 NDCIIRGDLANVRVGRHCVVKSRSVIRPLFKKfskgvaffPLHIGDHVFIEEDCVVNAAQIGSYVHVGKNCVIGRRCVLK 81
Cdd:PLN02472  88 NGAVLRGDLNKITVGFCSNVQERCVLHAAWNS--------PTGLPAETLIDRYVTIGAYSLLRSCTIEPECIIGQHSILM 159

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521039075  82 DCCKILDNTVLPPETVVPP------FTVFSGCPGLFSGELS-ECIQEL------MIDITKSYYQKFLP 136
Cdd:PLN02472 160 EGSLVETHSILEAGSVLPPgrriptGELWAGNPARFVRTLTnEETLEIpklavaINDLSQSHFSEFLP 227
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 1-80 1.01e-06

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: 46.10  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075    1 MNDCIIRGdlaNVRVGRHCVVKSRSVI--RPLFKKFSKGVAFfpLHIGDHVFIEEDCVVNAA--------QIGS------ 64
Cdd:TIGR01852  38 KSHVVILG---HTTIGEGTRIFPGAVIggVPQDLKYKGEKTR--LIIGDNNTIREFVTINRGtasgggvtRIGNnnllma 112

                          90
                  ....*....|....*.
gi 521039075   65 YVHVGKNCVIGRRCVL 80
Cdd:TIGR01852 113 YSHIAHDCVVGNHVIL 128
 
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 ...
 1-131 5.21e-78

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: 227.87  E-value: 5.21e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075   1 MNDCIIRGDLANVRVGRHCVVKSRSVIRPLFKKFSKGVAFFPLHIGDHVFIEEDCVVNAAQIGSYVHVGKNCVIGRRCVL 80
Cdd:cd03359   31 QSDVIIRGDLATVSIGRYCILSEGCVIRPPFKKFSKGVAFFPLHIGDYVFIGENCVVNAAQIGSYVHIGKNCVIGRRCII 110

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 521039075  81 KDCCKILDNTVLPPETVVPPFTVFSGCPGLFSGELSECIQELMIDITKSYY 131
Cdd:cd03359  111 KDCVKILDGTVVPPDTVIPPYSVVSGRPARFIGELPECTQELMEEETKEYY 161
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 4-130 1.48e-14

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: 65.90  E-value: 1.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075   4 CIIRGDLANVRVGRHCVVKSRSVIRPlfkkfSKGvafFPLHIGDHVFIEEDCVVNAAQIGSYVHVGKNCVIGRRCVLKDC 83
Cdd:cd04645   30 AVLRGDVNPIRIGERTNIQDGSVLHV-----DPG---YPTIIGDNVTVGHGAVLHGCTIGDNCLIGMGAIILDGAVIGKG 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 521039075  84 CKILDNTVLPPETVVPPFTVFSGCPGLFSGELSECIQELMIDITKSY 130
Cdd:cd04645  102 SIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAELRESAEHY 148
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 13-98 2.18e-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: 63.81  E-value: 2.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075  13 VRVGRHCVVKSRSVIRPlfkkfskgvaffPLHIGDHVFIEEDCVVNAAQIG---SYVHVGKNCVIGRRCVLKDCCKILDN 89
Cdd:cd00208    1 VFIGEGVKIHPKAVIRG------------PVVIGDNVNIGPGAVIGAATGPnekNPTIIGDNVEIGANAVIHGGVKIGDN 68


                 ....*....
gi 521039075  90 TVLPPETVV 98
Cdd:cd00208   69 AVIGAGAVV 77
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 5-117 5.59e-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: 59.51  E-value: 5.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075   5 IIRGDLANVRVGRHCVVKSRSVIRPlfkkfSKGvafFPLHIGDHVFIEEDCVVNAAQIGSYVHVGKNCVIGRRCVLKDCC 84
Cdd:cd04650   32 VIRGDNDSIYIGKYSNVQENVSIHT-----DHG---YPTEIGDYVTIGHNAVVHGAKVGNYVIVGMGAILLNGAKIGDHV 103

                         90       100       110
                 ....*....|....*....|....*....|...
gi 521039075  85 KILDNTVLPPETVVPPFTVFSGCPGLFSGELSE 117
Cdd:cd04650  104 IIGAGAVVTPGKEIPDYSLVLGVPAKVVRKLTE 136
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 4-132 1.07e-09

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 53.49  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075   4 CIIRGDLANVRVGRHCVVKSRSVIRplfkkfskGVAFFPLHIGDHVFIEEDCVVNAAQIGSYVHVGKNCVIGRRCVLKDC 83
Cdd:COG0663   41 AVLRGDVGPIRIGEGSNIQDGVVLH--------VDPGYPLTIGDDVTIGHGAILHGCTIGDNVLIGMGAIVLDGAVIGDG 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 521039075  84 CKILDNTVLPPETVVPPFTVFSGCPGLFSGELSECIQELMIDITKSYYQ 132
Cdd:COG0663  113 SIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRESAENYVE 161
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 44-92 5.63e-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: 52.71  E-value: 5.63e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 521039075  44 HIGDHVFIEEDCVVNA-AQIGSYVHVGKNCVIGRRCVLKDCCKILDNTVL 92
Cdd:COG1044  116 SIGPFAVIGAGVVIGDgVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVI 165
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 15-125 2.98e-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: 46.93  E-value: 2.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075  15 VGRHCVVKSRSVIRPlfKKFSKGVAFFPLHIGDHVFIEEDCVVNAAQIGSYVHVGKNCVIGRRCVLKDCCKILDNTVLPP 94
Cdd:cd04646   41 IGENNIIEEQVTIVN--KKPKDPAEPKPMIIGSNNVFEVGCKCEALKIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPS 118

                         90       100       110
                 ....*....|....*....|....*....|.
gi 521039075  95 ETVVPPFTVFSGcpglfsgelSECIQELMID 125
Cdd:cd04646  119 SEILPENTVIYG---------ADCLRRTQTD 140
PLN02472 PLN02472
uncharacterized protein
 2-136 8.05e-07

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 46.49  E-value: 8.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075   2 NDCIIRGDLANVRVGRHCVVKSRSVIRPLFKKfskgvaffPLHIGDHVFIEEDCVVNAAQIGSYVHVGKNCVIGRRCVLK 81
Cdd:PLN02472  88 NGAVLRGDLNKITVGFCSNVQERCVLHAAWNS--------PTGLPAETLIDRYVTIGAYSLLRSCTIEPECIIGQHSILM 159

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521039075  82 DCCKILDNTVLPPETVVPP------FTVFSGCPGLFSGELS-ECIQEL------MIDITKSYYQKFLP 136
Cdd:PLN02472 160 EGSLVETHSILEAGSVLPPgrriptGELWAGNPARFVRTLTnEETLEIpklavaINDLSQSHFSEFLP 227
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 45-92 8.34e-07

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: 46.25  E-value: 8.34e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 521039075  45 IGDHVFIEEDCVV-NAAQIGSYVHVGKNCVIGRRCVLKDCCKILDNTVL 92
Cdd:cd03352   10 IGPNAVIGEGVVIgDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCII 58
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 1-80 1.01e-06

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: 46.10  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075    1 MNDCIIRGdlaNVRVGRHCVVKSRSVI--RPLFKKFSKGVAFfpLHIGDHVFIEEDCVVNAA--------QIGS------ 64
Cdd:TIGR01852  38 KSHVVILG---HTTIGEGTRIFPGAVIggVPQDLKYKGEKTR--LIIGDNNTIREFVTINRGtasgggvtRIGNnnllma 112

                          90
                  ....*....|....*.
gi 521039075   65 YVHVGKNCVIGRRCVL 80
Cdd:TIGR01852 113 YSHIAHDCVVGNHVIL 128
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
11-108 3.73e-06

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 43.71  E-value: 3.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075  11 ANVRVGRHCVVKSRSVIrplfkkfskgVAFFPLHIGDHVFIEEDCVVNAA-----------QIGSYVHVGKNCVIGRRCV 79
Cdd:COG0110   26 GNITIGDNVYIGPGVTI----------DDPGGITIGDNVLIGPGVTILTGnhpiddpatfpLRTGPVTIGDDVWIGAGAT 95

                         90       100       110
                 ....*....|....*....|....*....|...
gi 521039075  80 LKDCCKILDNTVLPPETVV----PPFTVFSGCP 108
Cdd:COG0110   96 ILPGVTIGDGAVVGAGSVVtkdvPPYAIVAGNP 128
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 44-92 4.25e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 44.74  E-value: 4.25e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 521039075  44 HIGDHVFIEEDCVV-NAAQIGSYVHVGKNCVIGRRCVLKDCCKILDNTVL 92
Cdd:PRK00892 120 SIGPNAVIGAGVVIgDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRI 169
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 4-80 4.42e-06

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: 44.24  E-value: 4.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075   4 CIIRGDL---ANVRVGRHCVVKSRSVIrplfkkfSKGVAFFP-------------------LHIGDHVFIEEDCVVNAA- 60
Cdd:COG1043   26 CVIGPDVeigDGTVIGSHVVIEGPTTI-------GKNNRIFPfasigeepqdlkykgeptrLEIGDNNTIREFVTIHRGt 98

                         90       100       110
                 ....*....|....*....|....*....|...
gi 521039075  61 -------QIGS------YVHVGKNCVIGRRCVL 80
Cdd:COG1043   99 vqgggvtRIGDdnllmaYVHVAHDCVVGNNVIL 131
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
12-80 1.02e-05

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 42.17  E-value: 1.02e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521039075  12 NVRVGRHCVVKSRSVIRPlfkkfskgvafFPLHIGDHVFIEEDCVVNAaqiGSYVHVGKNCVIGRRCVL 80
Cdd:COG0110    8 GARIGDGVVIGPGVRIYG-----------GNITIGDNVYIGPGVTIDD---PGGITIGDNVLIGPGVTI 62
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
4-80 1.26e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 43.16  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075   4 CIIRGDL---ANVRVGRHCVVKSRSVIrplfkkfSKGVAFFP-------------------LHIGDHVFIEEDCVVNAA- 60
Cdd:PRK05289  27 CVIGPNVvigDGTVIGSHVVIDGHTTI-------GKNNRIFPfasigedpqdlkykgeptrLVIGDNNTIREFVTINRGt 99

                         90       100       110
                 ....*....|....*....|....*....|...
gi 521039075  61 -------QIGS------YVHVGKNCVIGRRCVL 80
Cdd:PRK05289 100 vqgggvtRIGDnnllmaYVHVAHDCVVGNHVIL 132
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 44-98 2.44e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 42.43  E-value: 2.44e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 521039075  44 HIGDHVFIEEDCVVNA-AQIGSYVHVGKNCVIGRRCVLKDCCKILDNTVLPPETVV 98
Cdd:PRK00892 108 VIDPSAKIGEGVSIGPnAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTI 163
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 4-80 2.69e-05

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: 42.03  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075   4 CIIRGDL---ANVRVGRHCVVKSRSVIR--------------PLFKKFSKGVAFfpLHIGDHVFIEEDCVVNAA------ 60
Cdd:cd03351   24 CVIGPNVeigDGTVIGSHVVIDGPTTIGknnrifpfasigeaPQDLKYKGEPTR--LEIGDNNTIREFVTIHRGtaqggg 101

                         90       100
                 ....*....|....*....|....*...
gi 521039075  61 --QIGS------YVHVGKNCVIGRRCVL 80
Cdd:cd03351  102 vtRIGNnnllmaYVHVAHDCVIGNNVIL 129
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 12-100 4.00e-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: 4.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075  12 NVRVGRHCVVKsRSVIrplfkkfSKGVaffplHIGDHVFIEEDCVVNAAQIGSYVHVgKNCVIGRRCVLKDCCKILDNTV 91
Cdd:cd03356    5 STVIGENAIIK-NSVI-------GDNV-----RIGDGVTITNSILMDNVTIGANSVI-VDSIIGDNAVIGENVRVVNLCI 70


                 ....*....
gi 521039075  92 LPPETVVPP 100
Cdd:cd03356   71 IGDDVVVED 79
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 11-91 4.45e-05

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: 41.32  E-value: 4.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075  11 ANVRVGRHCVVKSRSvirplfkkfskgvaffplHIGDHVFIEEDCVVNA-AQIGSYVHVGKNCVIGRRCVLKDCCKILDN 89
Cdd:cd03360  113 PDARIGDNVIINTGA------------------VIGHDCVIGDFVHIAPgVVLSGGVTIGEGAFIGAGATIIQGVTIGAG 174


                 ..
gi 521039075  90 TV 91
Cdd:cd03360  175 AI 176
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 45-98 4.50e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 41.66  E-value: 4.50e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 521039075  45 IGDHVFIEEDCVVNA-AQIGSYVHVGKNCVIGRRCVLKDCCKILDNTVLPPETVV 98
Cdd:PRK00892 127 IGAGVVIGDGVVIGAgAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVI 181
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 12-98 4.54e-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: 41.24  E-value: 4.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075  12 NVRVGRHCVVKSRSVIrplfkkfSKGVaffplHIGDHVFIEEDCVvnaaqIGSYVHVGKNCVIGRRCVLKDCCKILDNTV 91
Cdd:cd03352    1 SAKIGENVSIGPNAVI-------GEGV-----VIGDGVVIGPGVV-----IGDGVVIGDDCVIHPNVTIYEGCIIGDRVI 63


                 ....*..
gi 521039075  92 LPPETVV 98
Cdd:cd03352   64 IHSGAVI 70
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 2-108 5.95e-05

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


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 39.75  E-value: 5.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075   2 NDCIIrGDLANVRVGRHCVVKSRSVIR-------PLFKKFSKGVAFFPLHIGDHVFIEEDCVvnaaqIGSYVHVGKNCVI 74
Cdd:cd04647   12 PGCVI-SAGGGITIGDNVLIGPNVTIYdhnhdidDPERPIEQGVTSAPIVIGDDVWIGANVV-----ILPGVTIGDGAVV 85

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 521039075  75 GRRC-VLKDcckildntvlppetvVPPFTVFSGCP 108
Cdd:cd04647   86 GAGSvVTKD---------------VPPNSIVAGNP 105
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 2-92 6.10e-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: 40.85  E-value: 6.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075   2 NDCIIRgdlANVRVGRHCVVKSRSVIRP---------LFKKFSKGVAFFP----LHIGDHVFIEEDCVVNAA-----QIG 63
Cdd:cd03352   42 DDCVIH---PNVTIYEGCIIGDRVIIHSgavigsdgfGFAPDGGGWVKIPqlggVIIGDDVEIGANTTIDRGalgdtVIG 118

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 521039075  64 SY------VHVGKNCVIGRRCVLKDCCKILDNTVL 92
Cdd:cd03352  119 DGtkidnlVQIAHNVRIGENCLIAAQVGIAGSTTI 153
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 11-92 6.59e-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: 40.85  E-value: 6.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075  11 ANVRVGRHCVVKSRSVIRPlfkkfskgvaffplhigdHVFIEEDCVvnaaqIGSYVHVGKNCVIGRRCVLKDCCKILDNT 90
Cdd:cd03352   12 PNAVIGEGVVIGDGVVIGP------------------GVVIGDGVV-----IGDDCVIHPNVTIYEGCIIGDRVIIHSGA 68


                 ..
gi 521039075  91 VL 92
Cdd:cd03352   69 VI 70
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 15-80 1.52e-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: 37.94  E-value: 1.52e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521039075  15 VGRHCVVKSRSVIRPLFkkfskgvaffplhIGDHVFIEEDCVVNAAQIGSYVHVGKNCVIGRRCVL 80
Cdd:cd05787   19 IGRNCKIGKNVVIDNSY-------------IWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPGSLI 71
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 10-80 1.99e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 39.62  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075  10 LANVRVGRHCVVKSRSVI--RPLFKKFSKGVAFfpLHIGDHVFIEEDCVV-------NAAQIGS------YVHVGKNCVI 74
Cdd:PRK12461  45 LGPTRIGKNNKIHQGAVVgdEPQDFTYKGEESR--LEIGDRNVIREGVTIhrgtkggGVTRIGNdnllmaYSHVAHDCQI 122


                 ....*.
gi 521039075  75 GRRCVL 80
Cdd:PRK12461 123 GNNVIL 128
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 44-86 3.33e-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: 38.62  E-value: 3.33e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 521039075  44 HIGDHVFIEEDCVVNA-AQIGSYVHVGKNCVIGRRCVLKDCCKI 86
Cdd:cd03360   98 VIGEGCVIMAGAVINPdARIGDNVIINTGAVIGHDCVIGDFVHI 141
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 44-108 6.53e-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: 37.77  E-value: 6.53e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521039075  44 HIGDHVFIEEDCVVnAAQ--IGSYVHVGKNCVIGRRCVLKDCCKILDNTVLPPETVV----PPFTVFSGCP 108
Cdd:cd03352  128 QIAHNVRIGENCLI-AAQvgIAGSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVtsivPPGEYVSGTP 197
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 11-80 1.15e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 37.43  E-value: 1.15e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075  11 ANVRVGRHCVVKSRSVirplfkkfskgvaffplhIGDHVFIEEDCVvnaaqIGSYVHVGKNCVIGRRCVL 80
Cdd:PRK00892 129 AGVVIGDGVVIGAGAV------------------IGDGVKIGADCR-----LHANVTIYHAVRIGNRVII 175
PRK10502 PRK10502
putative acyl transferase; Provisional
 26-80 1.17e-03

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 37.24  E-value: 1.17e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 521039075  26 VIRPlfkkfskGVAF-FP--LHIGDHVFIEEDCVV-NAAQIgsyvHVGKNCVIGRRCVL 80
Cdd:PRK10502  59 VIRP-------SVRItYPwkLTIGDYAWIGDDVWLyNLGEI----TIGAHCVISQKSYL 106
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 11-75 1.29e-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: 37.30  E-value: 1.29e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521039075  11 ANVRVGRHCVVKSRSVIRPlfkkfskGVaffplHIGDHVFIEEDCVVNA-AQIGSYVHVGK------NCVIG 75
Cdd:COG1044  119 PFAVIGAGVVIGDGVVIGP-------GV-----VIGDGVVIGDDCVLHPnVTIYERCVIGDrviihsGAVIG 178
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 62-107 1.65e-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: 1.65e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 521039075  62 IGSYVHVGKNCVIGRRCVLKDcCKILDNTVLPPETVVPPFTVFSGC 107
Cdd:PRK09451 280 IEGNVTLGNRVKIGAGCVLKN-CVIGDDCEISPYSVVEDANLGAAC 324
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 12-132 2.03e-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: 36.19  E-value: 2.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075  12 NVRVGRHCVVKSRSVIRPLFKK--FSKGVaffplHIGD----HVFIEEDCVVNA-AQIG--SYVH---VGKNCVIGRRCV 79
Cdd:cd04745   18 DVIIGKNCYIGPHASLRGDFGRivIRDGA-----NVQDncviHGFPGQDTVLEEnGHIGhgAILHgctIGRNALVGMNAV 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 521039075  80 LKDCCKILDNTVL------PPETVVPPFTVFSGCPGLFSGELSECIQELMIDITKSYYQ 132
Cdd:cd04745   93 VMDGAVIGEESIVgamafvKAGTVIPPRSLIAGSPAKVIRELSDEEVAWKTRGTKEYQQ 151
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 4-75 2.09e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 36.77  E-value: 2.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521039075   4 CIIRGDL------ANVRVGRHCVVKsRSVIRPlfkkfskgvaffplhigdHVFIEEDCVVNAAQIGSYVHVGKNCVIG 75
Cdd:PRK05293 300 CVVYGTVehsvlfQGVQVGEGSVVK-DSVIMP------------------GAKIGENVVIERAIIGENAVIGDGVIIG 358
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 11-83 2.31e-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: 34.86  E-value: 2.31e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521039075  11 ANVRVGRHCVVKsRSVIRPlFKKFSKGVAFFPLHIGDHVFIEEDCVVNAAQIgsyvhvGKNCVIGRRCVLKDC 83
Cdd:cd04652    4 ENTQVGEKTSIK-RSVIGA-NCKIGKRVKITNCVIMDNVTIEDGCTLENCII------GNGAVIGEKCKLKDC 68
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 51-108 2.31e-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: 36.53  E-value: 2.31e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 521039075  51 IEEDCVvnaaqIGSYVHVGKNCVIGRRCVLKDCCKILDNTVLPPETVVPPFTVFSGCP 108
Cdd:COG1043   16 LGENVE-----IGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEEP 68
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 45-91 2.49e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 36.74  E-value: 2.49e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 521039075  45 IGDHVFIEEDCVVNAAQIGSYVHVGKNCVIgRRCVLKDCCKILDNTV 91
Cdd:PRK00725 346 LFSRVRVNSFSNVEDSVLLPDVNVGRSCRL-RRCVIDRGCVIPEGMV 391
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 3-88 3.24e-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: 3.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075   3 DCIIrgdlANVRVGRHCVVKSRSVIRPLFkkfskgvaffplhIGDHVFIEEDCVVNAAQIGSYVHVGKNCVIGRRCVLKD 82
Cdd:cd03356   11 NAII----KNSVIGDNVRIGDGVTITNSI-------------LMDNVTIGANSVIVDSIIGDNAVIGENVRVVNLCIIGD 73


                 ....*.
gi 521039075  83 CCKILD 88
Cdd:cd03356   74 DVVVED 79
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 4-78 3.33e-03

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: 35.86  E-value: 3.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075   4 CIIRGdlaNVRVGRHCVVKSRSVIRPlfkkfSKgvaffplhIGDHVFIE-----EDCVV-NAAQIGSYVHVGKNCVIGRR 77
Cdd:cd03353   28 VILEG---KTVIGEDCVIGPNCVIKD-----ST--------IGDGVVIKassviEGAVIgNGATVGPFAHLRPGTVLGEG 91


                 .
gi 521039075  78 C 78
Cdd:cd03353   92 V 92
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
44-86 3.59e-03

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 35.23  E-value: 3.59e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 521039075  44 HIGDHVFIEEDCVVNaaqiGSYVHVGKNCVIGRRCVLKDCCKI 86
Cdd:COG0110   10 RIGDGVVIGPGVRIY----GGNITIGDNVYIGPGVTIDDPGGI 48
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
61-119 5.20e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 35.46  E-value: 5.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521039075  61 QIGSYVHVGKNCVIGRRCVLKDCCKILDNTVLPPETVVPPFTVFSGCP-GL-FSGELSECI 119
Cdd:PRK05289  22 EIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEDPqDLkYKGEPTRLV 82
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 4-98 5.24e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 35.57  E-value: 5.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075   4 CIIRGdlANVRvgrhcvvksRSVIRPlfkkfskgvaffplhigdHVFIEEDCVVNAAQIGSYVHVGKNCVIgRRCvlkdc 83
Cdd:PRK00844 322 SIISG--ATVR---------NSVLSP------------------NVVVESGAEVEDSVLMDGVRIGRGAVV-RRA----- 366

                         90
                 ....*....|....*.
gi 521039075  84 ckILD-NTVLPPETVV 98
Cdd:PRK00844 367 --ILDkNVVVPPGATI 380
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 60-98 5.40e-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: 5.40e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 521039075  60 AQIGSYVHVGKNCVIGRRCVLKDCCKILDNTVLPPETVV 98
Cdd:COG1044  109 AKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVI 147
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 42-100 6.79e-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: 34.91  E-value: 6.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 521039075  42 PLHIGDHVFIEEDCVVNAAQIgsyvhvGKNCVIGRRCVLKDcCKILDNTVLPPETVVPP 100
Cdd:cd00710   82 PAYIGDNCFIGFRSVVFNAKV------GDNCVIGHNAVVDG-VEIPPGRYVPAGAVITS 133
PRK10502 PRK10502
putative acyl transferase; Provisional
 10-108 7.58e-03

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 34.93  E-value: 7.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075  10 LANVRVGRHCVVKSRSVI--------RPLFKKFSKgvaffPLHIGDHVFIEEDCVVNAAqigsyVHVGKNCVIG-RRCVL 80
Cdd:PRK10502  89 LGEITIGAHCVISQKSYLctgshdysDPHFDLNTA-----PIVIGEGCWLAADVFVAPG-----VTIGSGAVVGaRSSVF 158

                         90       100
                 ....*....|....*....|....*...
gi 521039075  81 KDcckildntvlppetvVPPFTVFSGCP 108
Cdd:PRK10502 159 KS---------------LPANTICRGNP 171
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 10-98 8.43e-03

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: 33.73  E-value: 8.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521039075  10 LANVRVGRHCVVKSRSVI--------RPLFKKFSKgvaffPLHIGDHVFIEEDCVVnaaqiGSYVHVGKNCVIG-RRCVL 80
Cdd:cd05825   21 LAPVTIGSDACISQGAYLctgshdyrSPAFPLITA-----PIVIGDGAWVAAEAFV-----GPGVTIGEGAVVGaRSVVV 90

                         90
                 ....*....|....*...
gi 521039075  81 KDcckildntvLPPETVV 98
Cdd:cd05825   91 RD---------LPAWTVY 99
 
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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