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Conserved domains on  [gi|1044516456|gb|ANT65163|]
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hypothetical protein Ptc2401_01397 [Prosthecochloris sp. CIB 2401]

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 ...
150-321 8.38e-13

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: 65.45  E-value: 8.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044516456 150 KEIFTSNYDLIVEKSLEairtpyfdgfvgSYEPFFWPESIDRFVEKSDLTQNWIRLWKIHGSLSWFwkknsdstshnivr 229
Cdd:pfam13289   1 PLIITTNYDDLLEKALA------------GEGKPVSAVSFEDLARLAELESGRPLLYKLHGDLDRP-------------- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044516456 230 vgkisdianldNELVIypSKEKYDSsKKQPFVAYFDRFKNVLLggERLFIFTGYSFSDQHINEIAFNSLRQNN----RLF 305
Cdd:pfam13289  55 -----------ESIVL--TESDYER-LLRFKNPLRRLLRALLR--TRSLLFVGYSFSDPNIRELLREVLAASGgsppRHY 118
                         170
                  ....*....|....*.
gi 1044516456 306 ILVFFYQDSEVEELYK 321
Cdd:pfam13289 119 AILPRPEPEDRERLLE 134
 
Name Accession Description Interval E-value
SIR2_2 pfam13289
SIR2-like domain; This family of proteins are related to the sirtuins.
150-321 8.38e-13

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


Pssm-ID: 433090  Cd Length: 141  Bit Score: 65.45  E-value: 8.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044516456 150 KEIFTSNYDLIVEKSLEairtpyfdgfvgSYEPFFWPESIDRFVEKSDLTQNWIRLWKIHGSLSWFwkknsdstshnivr 229
Cdd:pfam13289   1 PLIITTNYDDLLEKALA------------GEGKPVSAVSFEDLARLAELESGRPLLYKLHGDLDRP-------------- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044516456 230 vgkisdianldNELVIypSKEKYDSsKKQPFVAYFDRFKNVLLggERLFIFTGYSFSDQHINEIAFNSLRQNN----RLF 305
Cdd:pfam13289  55 -----------ESIVL--TESDYER-LLRFKNPLRRLLRALLR--TRSLLFVGYSFSDPNIRELLREVLAASGgsppRHY 118
                         170
                  ....*....|....*.
gi 1044516456 306 ILVFFYQDSEVEELYK 321
Cdd:pfam13289 119 AILPRPEPEDRERLLE 134
SIR2-like cd01406
Sir2-like: Prokaryotic group of uncharacterized Sir2-like proteins which lack certain key ...
25-318 3.00e-03

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: 38.92  E-value: 3.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044516456  25 FFFGAGTSCALGVPNIATLttgvenalqgdhqtnfkkikddlettypdktinIEDILNQLRQIRSITGERSD--KSYLDI 102
Cdd:cd01406     5 IFVGAGVSVSSGLPDWKTL---------------------------------LDEIASELGLEIDGYSVEAKdeNDYLEL 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044516456 103 NGESATEL-DNVICKQIYEIISTSEATVDLSNtKKFFAWLNMQNrVFSKEIFTSNYDLIVEKSLEAIRTPyFDGFVGSYE 181
Cdd:cd01406    52 AELLEKEFgTIGIKINAVLEEKTRPDFEPSPL-HELLLRLFINN-EGDVIIITTNYDRLLETALKEINKV-VKVIVSVQL 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044516456 182 PFFWPESIDRfveksdltqnwirLWKIHGSLswfwkknsdstshnivrvgkisdiaNLDNELVIypSKEKYDSskkqpfv 261
Cdd:cd01406   129 ALSASARFNG-------------VYKIHGDV-------------------------DDDESIVL--TKSDYER------- 161
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1044516456 262 AY-----FDRFKNVLLGgERLFIFTGYSFSDQHINEI--AFNSLRQNNRLFILVFFYQDSEVEE 318
Cdd:cd01406   162 YYlkngwATKFLKSDLE-KYTVLFIGYSLTDPNIRYLleRLRKNYEGKHASHFALLQKPNEEES 224
 
Name Accession Description Interval E-value
SIR2_2 pfam13289
SIR2-like domain; This family of proteins are related to the sirtuins.
150-321 8.38e-13

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


Pssm-ID: 433090  Cd Length: 141  Bit Score: 65.45  E-value: 8.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044516456 150 KEIFTSNYDLIVEKSLEairtpyfdgfvgSYEPFFWPESIDRFVEKSDLTQNWIRLWKIHGSLSWFwkknsdstshnivr 229
Cdd:pfam13289   1 PLIITTNYDDLLEKALA------------GEGKPVSAVSFEDLARLAELESGRPLLYKLHGDLDRP-------------- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044516456 230 vgkisdianldNELVIypSKEKYDSsKKQPFVAYFDRFKNVLLggERLFIFTGYSFSDQHINEIAFNSLRQNN----RLF 305
Cdd:pfam13289  55 -----------ESIVL--TESDYER-LLRFKNPLRRLLRALLR--TRSLLFVGYSFSDPNIRELLREVLAASGgsppRHY 118
                         170
                  ....*....|....*.
gi 1044516456 306 ILVFFYQDSEVEELYK 321
Cdd:pfam13289 119 AILPRPEPEDRERLLE 134
SIR2-like cd01406
Sir2-like: Prokaryotic group of uncharacterized Sir2-like proteins which lack certain key ...
25-318 3.00e-03

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: 38.92  E-value: 3.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044516456  25 FFFGAGTSCALGVPNIATLttgvenalqgdhqtnfkkikddlettypdktinIEDILNQLRQIRSITGERSD--KSYLDI 102
Cdd:cd01406     5 IFVGAGVSVSSGLPDWKTL---------------------------------LDEIASELGLEIDGYSVEAKdeNDYLEL 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044516456 103 NGESATEL-DNVICKQIYEIISTSEATVDLSNtKKFFAWLNMQNrVFSKEIFTSNYDLIVEKSLEAIRTPyFDGFVGSYE 181
Cdd:cd01406    52 AELLEKEFgTIGIKINAVLEEKTRPDFEPSPL-HELLLRLFINN-EGDVIIITTNYDRLLETALKEINKV-VKVIVSVQL 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044516456 182 PFFWPESIDRfveksdltqnwirLWKIHGSLswfwkknsdstshnivrvgkisdiaNLDNELVIypSKEKYDSskkqpfv 261
Cdd:cd01406   129 ALSASARFNG-------------VYKIHGDV-------------------------DDDESIVL--TKSDYER------- 161
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1044516456 262 AY-----FDRFKNVLLGgERLFIFTGYSFSDQHINEI--AFNSLRQNNRLFILVFFYQDSEVEE 318
Cdd:cd01406   162 YYlkngwATKFLKSDLE-KYTVLFIGYSLTDPNIRYLleRLRKNYEGKHASHFALLQKPNEEES 224
 
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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