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Conserved domains on  [gi|124505247|ref|XP_001351365|]
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liver specific protein 2, putative [Plasmodium falciparum 3D7]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 1826-1876 4.85e-04

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


The actual alignment was detected with superfamily member cd03358:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 119  Bit Score: 41.72  E-value: 4.85e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 124505247 1826 IKNDVEINDDVEIKNDVEIKNDVEIKNDVEINDDVEINDDVEIN-NGVEIND 1876
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGpNVVFTND 52
DUF5401 super family cl38662
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 434-755 6.96e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


The actual alignment was detected with superfamily member pfam17380:

Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 44.73  E-value: 6.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505247   434 HKILLEELNKMDKDElyEMYREELNRIEQEKIRNMNK----EEINKTYKDEInnmnsDQVDKIHREELEKiekekinKMD 509
Cdd:pfam17380  280 HQKAVSERQQQEKFE--KMEQERLRQEKEEKAREVERrrklEEAEKARQAEM-----DRQAAIYAEQERM-------AME 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505247   510 KD-EIDKIYRE----ELDKMDRDAIySMYIEdisnkNIKDLIKNEKETNKDKNKKKDIDINKKKKKDIDIDVDIDKDIHK 584
Cdd:pfam17380  346 RErELERIRQEerkrELERIRQEEI-AMEIS-----RMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQK 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505247   585 DHVEELYGEVKNKlSKEELDRMDRD---ALYRVYLEELDRMNRDELYRvyleelekidkeekekihreKLHKIEKEKINK 661
Cdd:pfam17380  420 VEMEQIRAEQEEA-RQREVRRLEEErarEMERVRLEEQERQQQVERLR--------------------QQEEERKRKKLE 478

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505247   662 MDKDQIDKIYEEELNKMD-SDEIQHVRRAILQDIQKEKIQNLELEEIDR-LYKEELDRM-DREARYEIPMRNLSRnekdn 738
Cdd:pfam17380  479 LEKEKRDRKRAEEQRRKIlEKELEERKQAMIEEERKRKLLEKEMEERQKaIYEEERRREaEEERRKQQEMEERRR----- 553

                          330
                   ....*....|....*..
gi 124505247   739 iIHRNIKNESNQKNKKE 755
Cdd:pfam17380  554 -IQEQMRKATEERSRLE 569
 
Name Accession Description Interval E-value
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 1826-1876 4.85e-04

WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 41.72  E-value: 4.85e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 124505247 1826 IKNDVEINDDVEIKNDVEIKNDVEIKNDVEINDDVEINDDVEIN-NGVEIND 1876
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGpNVVFTND 52
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 434-755 6.96e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 44.73  E-value: 6.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505247   434 HKILLEELNKMDKDElyEMYREELNRIEQEKIRNMNK----EEINKTYKDEInnmnsDQVDKIHREELEKiekekinKMD 509
Cdd:pfam17380  280 HQKAVSERQQQEKFE--KMEQERLRQEKEEKAREVERrrklEEAEKARQAEM-----DRQAAIYAEQERM-------AME 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505247   510 KD-EIDKIYRE----ELDKMDRDAIySMYIEdisnkNIKDLIKNEKETNKDKNKKKDIDINKKKKKDIDIDVDIDKDIHK 584
Cdd:pfam17380  346 RErELERIRQEerkrELERIRQEEI-AMEIS-----RMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQK 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505247   585 DHVEELYGEVKNKlSKEELDRMDRD---ALYRVYLEELDRMNRDELYRvyleelekidkeekekihreKLHKIEKEKINK 661
Cdd:pfam17380  420 VEMEQIRAEQEEA-RQREVRRLEEErarEMERVRLEEQERQQQVERLR--------------------QQEEERKRKKLE 478

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505247   662 MDKDQIDKIYEEELNKMD-SDEIQHVRRAILQDIQKEKIQNLELEEIDR-LYKEELDRM-DREARYEIPMRNLSRnekdn 738
Cdd:pfam17380  479 LEKEKRDRKRAEEQRRKIlEKELEERKQAMIEEERKRKLLEKEMEERQKaIYEEERRREaEEERRKQQEMEERRR----- 553

                          330
                   ....*....|....*..
gi 124505247   739 iIHRNIKNESNQKNKKE 755
Cdd:pfam17380  554 -IQEQMRKATEERSRLE 569
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1814-1874 1.26e-03

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: 43.48  E-value: 1.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124505247 1814 IKNDVEIKNDVEIKNDVEINDDVEIKNDVEIKNDVEIKnDVEINDDVEIN----DDVEINNGVEI 1874
Cdd:COG1207   263 IDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTLK-DSTIGDGVVIKysviEDAVVGAGATV 326
mukB PRK04863
chromosome partition protein MukB;
683-750 4.18e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.25  E-value: 4.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124505247  683 IQHVRRAILQDIQK-----EKIQNLELeEIDRLyKEELDRmdREARYEIpmrnlSRNEKDNIIHRNIKNESNQ 750
Cdd:PRK04863 1192 YQHLRERIRQDIIRtddpvEAIEQMEI-ELSRL-TEELTS--REQKLAI-----SSESVANIIRKTIQREQNR 1255
 
Name Accession Description Interval E-value
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 1826-1876 4.85e-04

WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 41.72  E-value: 4.85e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 124505247 1826 IKNDVEINDDVEIKNDVEIKNDVEIKNDVEINDDVEINDDVEIN-NGVEIND 1876
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGpNVVFTND 52
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 434-755 6.96e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 44.73  E-value: 6.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505247   434 HKILLEELNKMDKDElyEMYREELNRIEQEKIRNMNK----EEINKTYKDEInnmnsDQVDKIHREELEKiekekinKMD 509
Cdd:pfam17380  280 HQKAVSERQQQEKFE--KMEQERLRQEKEEKAREVERrrklEEAEKARQAEM-----DRQAAIYAEQERM-------AME 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505247   510 KD-EIDKIYRE----ELDKMDRDAIySMYIEdisnkNIKDLIKNEKETNKDKNKKKDIDINKKKKKDIDIDVDIDKDIHK 584
Cdd:pfam17380  346 RErELERIRQEerkrELERIRQEEI-AMEIS-----RMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQK 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505247   585 DHVEELYGEVKNKlSKEELDRMDRD---ALYRVYLEELDRMNRDELYRvyleelekidkeekekihreKLHKIEKEKINK 661
Cdd:pfam17380  420 VEMEQIRAEQEEA-RQREVRRLEEErarEMERVRLEEQERQQQVERLR--------------------QQEEERKRKKLE 478

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505247   662 MDKDQIDKIYEEELNKMD-SDEIQHVRRAILQDIQKEKIQNLELEEIDR-LYKEELDRM-DREARYEIPMRNLSRnekdn 738
Cdd:pfam17380  479 LEKEKRDRKRAEEQRRKIlEKELEERKQAMIEEERKRKLLEKEMEERQKaIYEEERRREaEEERRKQQEMEERRR----- 553

                          330
                   ....*....|....*..
gi 124505247   739 iIHRNIKNESNQKNKKE 755
Cdd:pfam17380  554 -IQEQMRKATEERSRLE 569
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1814-1874 1.26e-03

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: 43.48  E-value: 1.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124505247 1814 IKNDVEIKNDVEIKNDVEINDDVEIKNDVEIKNDVEIKnDVEINDDVEIN----DDVEINNGVEI 1874
Cdd:COG1207   263 IDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTLK-DSTIGDGVVIKysviEDAVVGAGATV 326
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1811-1868 1.49e-03

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: 43.48  E-value: 1.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124505247 1811 DVQIKNDVEIKNDVEIKNDVEINDDVEIKNDVEIKnDVEIKNDVEIN----DDVEINDDVEI 1868
Cdd:COG1207   266 DVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTLK-DSTIGDGVVIKysviEDAVVGAGATV 326
mukB PRK04863
chromosome partition protein MukB;
683-750 4.18e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.25  E-value: 4.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124505247  683 IQHVRRAILQDIQK-----EKIQNLELeEIDRLyKEELDRmdREARYEIpmrnlSRNEKDNIIHRNIKNESNQ 750
Cdd:PRK04863 1192 YQHLRERIRQDIIRtddpvEAIEQMEI-ELSRL-TEELTS--REQKLAI-----SSESVANIIRKTIQREQNR 1255
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 1820-1876 5.12e-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: 40.10  E-value: 5.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 124505247 1820 IKNDVEIKNDVEINDDVEIKNDVEIKNDVEIKNDVEINdDVEINDDVEINNGVEIND 1876
Cdd:cd03353    12 IDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIK-DSTIGDGVVIKASSVIEG 67
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 1811-1877 6.04e-03

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 40.08  E-value: 6.04e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124505247 1811 DVQIKNDVE------IKNDVEIKNDVEINDDVEIKNDVEIKNDVEIKNDVEINDDVEINDDVEINNGVEI-NDG 1877
Cdd:cd03352     1 SAKIGENVSigpnavIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIgSDG 74
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 1812-1874 6.75e-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: 39.71  E-value: 6.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124505247 1812 VQIKNDVEIKNDVEIKNDVEINDDVEIKNDVEIKNDVEIKnDVEINDDVEIN-----DDVEINNGVEI 1874
Cdd:cd03353    10 TYIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIK-DSTIGDGVVIKassviEGAVIGNGATV 76
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 1814-1856 7.18e-03

WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 38.25  E-value: 7.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 124505247 1814 IKNDVEIKNDVEIKNDVEINDDVEIKNDVEIKNDVEIKNDVEI 1856
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFI 43
 
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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