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Conserved domains on  [gi|2462585144|ref|XP_054181735|]
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protein FAM118A isoform X23 [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 ...
 144-248 5.25e-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: 65.84  E-value: 5.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585144 144 MVLTTNYDNLLEAFGRRQNKPMESLDLKDKTKVLEWARGHMKygVLHIHGLYTDPCGVVLDPSGYKDV-TQDAEVMEVLQ 222
Cdd:pfam13289   2 LIITTNYDDLLEKALAGEGKPVSAVSFEDLARLAELESGRPL--LYKLHGDLDRPESIVLTESDYERLlRFKNPLRRLLR 79

                          90       100
                  ....*....|....*....|....*.
gi 2462585144 223 NLYRTKSFLFVGCGetLHDQIFQALF 248
Cdd:pfam13289  80 ALLRTRSLLFVGYS--FSDPNIRELL 103
 
Name Accession Description Interval E-value
SIR2_2 pfam13289
SIR2-like domain; This family of proteins are related to the sirtuins.
 144-248 5.25e-13

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


Pssm-ID: 433090  Cd Length: 141  Bit Score: 65.84  E-value: 5.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585144 144 MVLTTNYDNLLEAFGRRQNKPMESLDLKDKTKVLEWARGHMKygVLHIHGLYTDPCGVVLDPSGYKDV-TQDAEVMEVLQ 222
Cdd:pfam13289   2 LIITTNYDDLLEKALAGEGKPVSAVSFEDLARLAELESGRPL--LYKLHGDLDRPESIVLTESDYERLlRFKNPLRRLLR 79

                          90       100
                  ....*....|....*....|....*.
gi 2462585144 223 NLYRTKSFLFVGCGetLHDQIFQALF 248
Cdd:pfam13289  80 ALLRTRSLLFVGYS--FSDPNIRELL 103
SIR2-like cd01406
Sir2-like: Prokaryotic group of uncharacterized Sir2-like proteins which lack certain key ...
 35-273 1.35e-10

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: 61.26  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585144  35 IGTGVSaaVAPGIPalcSWRSCIEAVIEAAEQLEVlhpgdvaEFRRKVTKDRDLLVVAhDLIRKmspRTGDAKPSFfQDC 114
Cdd:cd01406     7 VGAGVS--VSSGLP---DWKTLLDEIASELGLEID-------GYSVEAKDENDYLELA-ELLEK---EFGTIGIKI-NAV 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585144 115 LMEVF-DDLEqhirsPLVLQSILSLMDR----GAMVLTTNYDNLLEAFGRRQNKPMesldlkDKTKVLEWA--RGHMKYG 187
Cdd:cd01406    70 LEEKTrPDFE-----PSPLHELLLRLFInnegDVIIITTNYDRLLETALKEINKVV------KVIVSVQLAlsASARFNG 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585144 188 VLHIHGLYTDPCGVVLDPSGYKDVTQDAEVMEV-LQNLYRTKSFLFVGCgeTLHDQIFQALfLYSVPNKV---DLEHYML 263
Cdd:cd01406   139 VYKIHGDVDDDESIVLTKSDYERYYLKNGWATKfLKSDLEKYTVLFIGY--SLTDPNIRYL-LERLRKNYegkHASHFAL 215

                         250
                  ....*....|
gi 2462585144 264 VLKENEDHFF 273
Cdd:cd01406   216 LQKPNEEESR 225
 
Name Accession Description Interval E-value
SIR2_2 pfam13289
SIR2-like domain; This family of proteins are related to the sirtuins.
 144-248 5.25e-13

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


Pssm-ID: 433090  Cd Length: 141  Bit Score: 65.84  E-value: 5.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585144 144 MVLTTNYDNLLEAFGRRQNKPMESLDLKDKTKVLEWARGHMKygVLHIHGLYTDPCGVVLDPSGYKDV-TQDAEVMEVLQ 222
Cdd:pfam13289   2 LIITTNYDDLLEKALAGEGKPVSAVSFEDLARLAELESGRPL--LYKLHGDLDRPESIVLTESDYERLlRFKNPLRRLLR 79

                          90       100
                  ....*....|....*....|....*.
gi 2462585144 223 NLYRTKSFLFVGCGetLHDQIFQALF 248
Cdd:pfam13289  80 ALLRTRSLLFVGYS--FSDPNIRELL 103
SIR2-like cd01406
Sir2-like: Prokaryotic group of uncharacterized Sir2-like proteins which lack certain key ...
 35-273 1.35e-10

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: 61.26  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585144  35 IGTGVSaaVAPGIPalcSWRSCIEAVIEAAEQLEVlhpgdvaEFRRKVTKDRDLLVVAhDLIRKmspRTGDAKPSFfQDC 114
Cdd:cd01406     7 VGAGVS--VSSGLP---DWKTLLDEIASELGLEID-------GYSVEAKDENDYLELA-ELLEK---EFGTIGIKI-NAV 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585144 115 LMEVF-DDLEqhirsPLVLQSILSLMDR----GAMVLTTNYDNLLEAFGRRQNKPMesldlkDKTKVLEWA--RGHMKYG 187
Cdd:cd01406    70 LEEKTrPDFE-----PSPLHELLLRLFInnegDVIIITTNYDRLLETALKEINKVV------KVIVSVQLAlsASARFNG 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585144 188 VLHIHGLYTDPCGVVLDPSGYKDVTQDAEVMEV-LQNLYRTKSFLFVGCgeTLHDQIFQALfLYSVPNKV---DLEHYML 263
Cdd:cd01406   139 VYKIHGDVDDDESIVLTKSDYERYYLKNGWATKfLKSDLEKYTVLFIGY--SLTDPNIRYL-LERLRKNYegkHASHFAL 215

                         250
                  ....*....|
gi 2462585144 264 VLKENEDHFF 273
Cdd:cd01406   216 LQKPNEEESR 225
SIR2 cd00296
SIR2 superfamily of proteins includes silent information regulator 2 (Sir2) enzymes which ...
 31-284 1.47e-05

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: 45.80  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585144  31 LLLVIGTGVSAAvaPGIPalcSWRScieAVIEAAEQLEVLHPGDVAEFRRKVTKdrdllvVAHDLIRKMSPRTGDAKPSF 110
Cdd:cd00296     3 VVVFTGAGISTE--SGIP---DFRG---LGTGLWTRLDPEELAFSPEAFRRDPE------LFWLFYKERRYTPLDAKPNP 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585144 111 FqdclmevfddleqHirsplvlQSILSLMDRG--AMVLTTNYDNLLEAFGRRQNKPME---SLD----LKDKTKVlEWAR 181
Cdd:cd00296    69 A-------------H-------RALAELERKGklKRIITQNVDGLHERAGSRRNRVIElhgSLDrvrcTSCGKEY-PRDE 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585144 182 GHMKYGVLHIhglytDPCGVVLDPS--GYKDVTQDAEVMEVLQNLYRTKSFLFVGCgeTLHDQIFQALFLYSVPNKVdle 259
Cdd:cd00296   128 VLEREKPPRC-----PKCGGLLRPDvvDFGEALPKEWFDRALEALLEADLVLVIGT--SLTVYPAARLLLRAPERGA--- 197

                         250       260
                  ....*....|....*....|....*
gi 2462585144 260 HYMLVLKENEDHFFKHQADMLLHGI 284
Cdd:cd00296   198 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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