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Conserved domains on  [gi|74150736|dbj|BAE25500|]
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unnamed protein product [Mus musculus]

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 ...
 142-247 4.23e-14

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 pfam13289:

Pssm-ID: 444738  Cd Length: 141  Bit Score: 68.53  E-value: 4.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150736   142 TMVLTTNYDNLLEIFGQQQSKPMESLDLKDKTKVLQWARGHIKygVLHIHGLYTDPCGMVLDPSGYKDV-TQDPEVMEVL 220
Cdd:pfam13289   1 PLIITTNYDDLLEKALAGEGKPVSAVSFEDLARLAELESGRPL--LYKLHGDLDRPESIVLTESDYERLlRFKNPLRRLL 78

                          90       100
                  ....*....|....*....|....*..
gi 74150736   221 QNLYRTKSFLFVGCGetLRDQIFQALF 247
Cdd:pfam13289  79 RALLRTRSLLFVGYS--FSDPNIRELL 103
 
Name Accession Description Interval E-value
SIR2_2 pfam13289
SIR2-like domain; This family of proteins are related to the sirtuins.
 142-247 4.23e-14

SIR2-like domain; This family of proteins are related to the sirtuins.


Pssm-ID: 433090  Cd Length: 141  Bit Score: 68.53  E-value: 4.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150736   142 TMVLTTNYDNLLEIFGQQQSKPMESLDLKDKTKVLQWARGHIKygVLHIHGLYTDPCGMVLDPSGYKDV-TQDPEVMEVL 220
Cdd:pfam13289   1 PLIITTNYDDLLEKALAGEGKPVSAVSFEDLARLAELESGRPL--LYKLHGDLDRPESIVLTESDYERLlRFKNPLRRLL 78

                          90       100
                  ....*....|....*....|....*..
gi 74150736   221 QNLYRTKSFLFVGCGetLRDQIFQALF 247
Cdd:pfam13289  79 RALLRTRSLLFVGYS--FSDPNIRELL 103
SIR2-like cd01406
Sir2-like: Prokaryotic group of uncharacterized Sir2-like proteins which lack certain key ...
 142-272 5.98e-11

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: 62.03  E-value: 5.98e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150736 142 TMVLTTNYDNLLEIfgqqqSKPMESLDLKDKTKVLQWARGHIKY-GVLHIHGLYTDPCGMVLDPSGYKDVTQ-DPEVMEV 219
Cdd:cd01406  98 VIIITTNYDRLLET-----ALKEINKVVKVIVSVQLALSASARFnGVYKIHGDVDDDESIVLTKSDYERYYLkNGWATKF 172

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 74150736 220 LQNLYRTKSFLFVGCgeTLRDQIFQALfLYSVPNKV---DLEHYMVVLKENEDHFF 272
Cdd:cd01406 173 LKSDLEKYTVLFIGY--SLTDPNIRYL-LERLRKNYegkHASHFALLQKPNEEESR 225
 
Name Accession Description Interval E-value
SIR2_2 pfam13289
SIR2-like domain; This family of proteins are related to the sirtuins.
 142-247 4.23e-14

SIR2-like domain; This family of proteins are related to the sirtuins.


Pssm-ID: 433090  Cd Length: 141  Bit Score: 68.53  E-value: 4.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150736   142 TMVLTTNYDNLLEIFGQQQSKPMESLDLKDKTKVLQWARGHIKygVLHIHGLYTDPCGMVLDPSGYKDV-TQDPEVMEVL 220
Cdd:pfam13289   1 PLIITTNYDDLLEKALAGEGKPVSAVSFEDLARLAELESGRPL--LYKLHGDLDRPESIVLTESDYERLlRFKNPLRRLL 78

                          90       100
                  ....*....|....*....|....*..
gi 74150736   221 QNLYRTKSFLFVGCGetLRDQIFQALF 247
Cdd:pfam13289  79 RALLRTRSLLFVGYS--FSDPNIRELL 103
SIR2-like cd01406
Sir2-like: Prokaryotic group of uncharacterized Sir2-like proteins which lack certain key ...
 142-272 5.98e-11

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: 62.03  E-value: 5.98e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150736 142 TMVLTTNYDNLLEIfgqqqSKPMESLDLKDKTKVLQWARGHIKY-GVLHIHGLYTDPCGMVLDPSGYKDVTQ-DPEVMEV 219
Cdd:cd01406  98 VIIITTNYDRLLET-----ALKEINKVVKVIVSVQLALSASARFnGVYKIHGDVDDDESIVLTKSDYERYYLkNGWATKF 172

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 74150736 220 LQNLYRTKSFLFVGCgeTLRDQIFQALfLYSVPNKV---DLEHYMVVLKENEDHFF 272
Cdd:cd01406 173 LKSDLEKYTVLFIGY--SLTDPNIRYL-LERLRKNYegkHASHFALLQKPNEEESR 225
SIR2 cd00296
SIR2 superfamily of proteins includes silent information regulator 2 (Sir2) enzymes which ...
 30-283 1.56e-03

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.


Pssm-ID: 238184 [Multi-domain]  Cd Length: 222  Bit Score: 39.63  E-value: 1.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150736  30 LLLVIGTGVSAAvaPGIRalcSWRScieAVIEAAEQLEVLHPGDVAEFRRKvmkDRDLlvvAHDLIRKMSPRTGDTKPNF 109
Cdd:cd00296   3 VVVFTGAGISTE--SGIP---DFRG---LGTGLWTRLDPEELAFSPEAFRR---DPEL---FWLFYKERRYTPLDAKPNP 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150736 110 FqdclmevfdsleqHiqnpvvlRSILSLMDRG--TMVLTTNYDNLLEIFGQQQSKpmesldlkdktkvlqwarghikygV 187
Cdd:cd00296  69 A-------------H-------RALAELERKGklKRIITQNVDGLHERAGSRRNR------------------------V 104

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150736 188 LHIHG-LYTD---PCGMVLDPSGYKDVTQDP-----------------------EVMEVLQNLYRTKSFLFVGCgeTLRD 240
Cdd:cd00296 105 IELHGsLDRVrctSCGKEYPRDEVLEREKPPrcpkcggllrpdvvdfgealpkeWFDRALEALLEADLVLVIGT--SLTV 182

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 74150736 241 QIFQALFLYSVPNKVdleHYMVVLKENEDHFFKHQADMLLHGI 283
Cdd:cd00296 183 YPAARLLLRAPERGA---PVVIINREPTPADALKKADLVILGD 222
 
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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