NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|22024252|ref|NP_611704|]
View 

uncharacterized protein Dmel_CG30269, isoform A [Drosophila melanogaster]

Protein Classification

LITAF-like zinc ribbon domain-containing protein( domain architecture ID 10566201)

LITAF (lipopolysaccharide-induced tumor necrosis factor-alpha factor)-like zinc ribbon domain-containing protein similar to vertebrate cell death-inducing p53-target protein 1 that acts as an important p53/TP53-apoptotic effector, and lipopolysaccharide (LPS)-induced tumor necrosis factor (TNF)-alpha factor (LITAF) which plays an important role controlling the expression of TNF-alpha and the other cytokine genes in the presence of LPS

Gene Ontology:  GO:0008270
PubMed:  12527760

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
zf-LITAF-like pfam10601
LITAF-like zinc ribbon domain; Members of this family display a conserved zinc ribbon ...
 73-142 1.38e-20

LITAF-like zinc ribbon domain; Members of this family display a conserved zinc ribbon structure with the motif C-XX-C- separated from the more C-terminal HX-C(P)X-C-X4-G-R motif by a variable region of usually 25-30 (hydrophobic) residues. Although it belongs to one of the zinc finger's fold groups (zinc ribbon), this particular domain was first identified in LPS-induced tumour necrosis alpha factor (LITAF) which is produced in mammalian cells after being challenged with lipopolysaccharide (LPS). The hydrophobic region probably inserts into the membrane rather than traversing it. Such an insertion brings together the N- and C-terminal C-XX-C motifs to form a compact Zn2+-binding structure.


:

Pssm-ID: 463165  Cd Length: 68  Bit Score: 79.18  E-value: 1.38e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024252    73 PEPMDVQCPYCHNYARTRVSFKPNSRTHLIALILCLFqlYCCVCLPYCISSCMNTNHYCGMCDRYLGTYD 142
Cdd:pfam10601   1 PQPQQVTCPHCQQRVTTRVEYEPGLLTWLACLLLCLF--GCLCLIPFCMDSCKDVVHYCPNCGALLGTYK 68
PTZ00144 super family cl36517
dihydrolipoamide succinyltransferase; Provisional
 6-63 2.54e-03

dihydrolipoamide succinyltransferase; Provisional


The actual alignment was detected with superfamily member PTZ00144:

Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 36.58  E-value: 2.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 22024252    6 PAAPLEAPKGSVELQATPEQQHLLPPAPPSYDQATTTPAETTGPAPVPASTSTTQHTV 63
Cdd:PTZ00144 125 PAAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKPPEPAPAAKPPPTPV 182
 
Name Accession Description Interval E-value
zf-LITAF-like pfam10601
LITAF-like zinc ribbon domain; Members of this family display a conserved zinc ribbon ...
 73-142 1.38e-20

LITAF-like zinc ribbon domain; Members of this family display a conserved zinc ribbon structure with the motif C-XX-C- separated from the more C-terminal HX-C(P)X-C-X4-G-R motif by a variable region of usually 25-30 (hydrophobic) residues. Although it belongs to one of the zinc finger's fold groups (zinc ribbon), this particular domain was first identified in LPS-induced tumour necrosis alpha factor (LITAF) which is produced in mammalian cells after being challenged with lipopolysaccharide (LPS). The hydrophobic region probably inserts into the membrane rather than traversing it. Such an insertion brings together the N- and C-terminal C-XX-C motifs to form a compact Zn2+-binding structure.


Pssm-ID: 463165  Cd Length: 68  Bit Score: 79.18  E-value: 1.38e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024252    73 PEPMDVQCPYCHNYARTRVSFKPNSRTHLIALILCLFqlYCCVCLPYCISSCMNTNHYCGMCDRYLGTYD 142
Cdd:pfam10601   1 PQPQQVTCPHCQQRVTTRVEYEPGLLTWLACLLLCLF--GCLCLIPFCMDSCKDVVHYCPNCGALLGTYK 68
LITAF smart00714
Possible membrane-associated motif in LPS-induced tumor necrosis factor alpha factor (LITAF), ...
 75-143 3.67e-19

Possible membrane-associated motif in LPS-induced tumor necrosis factor alpha factor (LITAF), also known as PIG7, and other animal proteins;


Pssm-ID: 197841  Cd Length: 67  Bit Score: 75.82  E-value: 3.67e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024252     75 PMDVQCPYCHNYARTRVSFKpnsRTHLIALILCLFQLYC-CVCLPYCISSCMNTNHYCGMCDRYLGTYDR 143
Cdd:smart00714   1 PYQIFCPRCQNNVTTRVETE---TGVLAWLICFLLFFLCfCCCLPCCLDSFKDVNHYCPNCGAFLGTYNR 67
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 6-63 2.54e-03

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 36.58  E-value: 2.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 22024252    6 PAAPLEAPKGSVELQATPEQQHLLPPAPPSYDQATTTPAETTGPAPVPASTSTTQHTV 63
Cdd:PTZ00144 125 PAAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKPPEPAPAAKPPPTPV 182
 
Name Accession Description Interval E-value
zf-LITAF-like pfam10601
LITAF-like zinc ribbon domain; Members of this family display a conserved zinc ribbon ...
 73-142 1.38e-20

LITAF-like zinc ribbon domain; Members of this family display a conserved zinc ribbon structure with the motif C-XX-C- separated from the more C-terminal HX-C(P)X-C-X4-G-R motif by a variable region of usually 25-30 (hydrophobic) residues. Although it belongs to one of the zinc finger's fold groups (zinc ribbon), this particular domain was first identified in LPS-induced tumour necrosis alpha factor (LITAF) which is produced in mammalian cells after being challenged with lipopolysaccharide (LPS). The hydrophobic region probably inserts into the membrane rather than traversing it. Such an insertion brings together the N- and C-terminal C-XX-C motifs to form a compact Zn2+-binding structure.


Pssm-ID: 463165  Cd Length: 68  Bit Score: 79.18  E-value: 1.38e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024252    73 PEPMDVQCPYCHNYARTRVSFKPNSRTHLIALILCLFqlYCCVCLPYCISSCMNTNHYCGMCDRYLGTYD 142
Cdd:pfam10601   1 PQPQQVTCPHCQQRVTTRVEYEPGLLTWLACLLLCLF--GCLCLIPFCMDSCKDVVHYCPNCGALLGTYK 68
LITAF smart00714
Possible membrane-associated motif in LPS-induced tumor necrosis factor alpha factor (LITAF), ...
 75-143 3.67e-19

Possible membrane-associated motif in LPS-induced tumor necrosis factor alpha factor (LITAF), also known as PIG7, and other animal proteins;


Pssm-ID: 197841  Cd Length: 67  Bit Score: 75.82  E-value: 3.67e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024252     75 PMDVQCPYCHNYARTRVSFKpnsRTHLIALILCLFQLYC-CVCLPYCISSCMNTNHYCGMCDRYLGTYDR 143
Cdd:smart00714   1 PYQIFCPRCQNNVTTRVETE---TGVLAWLICFLLFFLCfCCCLPCCLDSFKDVNHYCPNCGAFLGTYNR 67
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 6-63 2.54e-03

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 36.58  E-value: 2.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 22024252    6 PAAPLEAPKGSVELQATPEQQHLLPPAPPSYDQATTTPAETTGPAPVPASTSTTQHTV 63
Cdd:PTZ00144 125 PAAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKPPEPAPAAKPPPTPV 182
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH