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Conserved domains on  [gi|2217284624|ref|XP_011541280|]
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protein FAM118B isoform X3 [Homo sapiens]

Protein Classification

SIR2 family protein( domain architecture ID 1222)

SIR2 family protein similar to NAD-dependent deacetylase that catalyzes NAD+-dependent protein/histone deacetylation, where the acetyl group from the lysine epsilon-amino group is transferred to the ADP-ribose moiety of NAD+, producing nicotinamide and the novel metabolite O-acetyl-ADP-ribose

PubMed:  7498786

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SIR2 super family cl00195
SIR2 superfamily of proteins includes silent information regulator 2 (Sir2) enzymes which ...
 43-178 2.38e-04

SIR2 superfamily of proteins includes silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation, where the acetyl group from the lysine epsilon-amino group is transferred to the ADP-ribose moiety of NAD+, producing nicotinamide and the novel metabolite O-acetyl-ADP-ribose. Sir2 proteins, also known as sirtuins, are found in all eukaryotes and many archaea and prokaryotes and have been shown to regulate gene silencing, DNA repair, metabolic enzymes, and life span. The most-studied function, gene silencing, involves the inactivation of chromosome domains containing key regulatory genes by packaging them into a specialized chromatin structure that is inaccessible to DNA-binding proteins. The oligomerization state of Sir2 appears to be organism-dependent, sometimes occurring as a monomer and sometimes as a multimer. Also included in this superfamily is a group of uncharacterized Sir2-like proteins which lack certain key catalytic residues and conserved zinc binding cysteines.


The actual alignment was detected with superfamily member cd01406:

Pssm-ID: 444738 [Multi-domain]  Cd Length: 242  Bit Score: 40.85  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284624  43 LVLVIGTGISaaVAPQVPalkSWKGLIQALLDaaidfDLLEDEESKKFQKCLHEDknLVHVAHDLIQKLSPRTSNVRstf 122
Cdd:cd01406     3 VVIFVGAGVS--VSSGLP---DWKTLLDEIAS-----ELGLEIDGYSVEAKDEND--YLELAELLEKEFGTIGIKIN--- 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217284624 123 fkdcLYEVFDDLESKMEDSGKQLLQSVLHLMENGALVLTTNFDNLLELYAADQGKQ 178
Cdd:cd01406    68 ----AVLEEKTRPDFEPSPLHELLLRLFINNEGDVIIITTNYDRLLETALKEINKV 119
 
Name Accession Description Interval E-value
SIR2-like cd01406
Sir2-like: Prokaryotic group of uncharacterized Sir2-like proteins which lack certain key ...
 43-178 2.38e-04

Sir2-like: Prokaryotic group of uncharacterized Sir2-like proteins which lack certain key catalytic residues and conserved zinc binding cysteines; and are members of the SIR2 superfamily of proteins, silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation.


Pssm-ID: 238697 [Multi-domain]  Cd Length: 242  Bit Score: 40.85  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284624  43 LVLVIGTGISaaVAPQVPalkSWKGLIQALLDaaidfDLLEDEESKKFQKCLHEDknLVHVAHDLIQKLSPRTSNVRstf 122
Cdd:cd01406     3 VVIFVGAGVS--VSSGLP---DWKTLLDEIAS-----ELGLEIDGYSVEAKDEND--YLELAELLEKEFGTIGIKIN--- 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217284624 123 fkdcLYEVFDDLESKMEDSGKQLLQSVLHLMENGALVLTTNFDNLLELYAADQGKQ 178
Cdd:cd01406    68 ----AVLEEKTRPDFEPSPLHELLLRLFINNEGDVIIITTNYDRLLETALKEINKV 119
 
Name Accession Description Interval E-value
SIR2-like cd01406
Sir2-like: Prokaryotic group of uncharacterized Sir2-like proteins which lack certain key ...
 43-178 2.38e-04

Sir2-like: Prokaryotic group of uncharacterized Sir2-like proteins which lack certain key catalytic residues and conserved zinc binding cysteines; and are members of the SIR2 superfamily of proteins, silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation.


Pssm-ID: 238697 [Multi-domain]  Cd Length: 242  Bit Score: 40.85  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284624  43 LVLVIGTGISaaVAPQVPalkSWKGLIQALLDaaidfDLLEDEESKKFQKCLHEDknLVHVAHDLIQKLSPRTSNVRstf 122
Cdd:cd01406     3 VVIFVGAGVS--VSSGLP---DWKTLLDEIAS-----ELGLEIDGYSVEAKDEND--YLELAELLEKEFGTIGIKIN--- 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217284624 123 fkdcLYEVFDDLESKMEDSGKQLLQSVLHLMENGALVLTTNFDNLLELYAADQGKQ 178
Cdd:cd01406    68 ----AVLEEKTRPDFEPSPLHELLLRLFINNEGDVIIITTNYDRLLETALKEINKV 119
 
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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