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Conserved domains on  [gi|663528520|gb|AIF18557|]
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ubiquitin-associated domain-containing protein (NACA) [uncultured marine thaumarchaeote KM3_83_D12]

Protein Classification

EGD2 family protein( domain architecture ID 11442013)

EGD2 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EGD2 COG1308
Transcription factor homologous to NACalpha-BTF3 [Transcription];
1-113 3.20e-35

Transcription factor homologous to NACalpha-BTF3 [Transcription];


:

Pssm-ID: 440919 [Multi-domain]  Cd Length: 116  Bit Score: 116.87  E-value: 3.20e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528520   1 MMRGGN-RQMRRMMDKMGLDMEEIPnVQEVIIKTDKKEIIIPKPSVTEMKSKENSIFQVIAESFEEK---ELEVPIFSED 76
Cdd:COG1308    1 MFGGMNpRKMKQMMKQMGIKVEEID-AEEVIIRTKDKEIVFENPQVTVMKAQGQETYQIVGEPEEVEkgaEEAEVEIPEE 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 663528520  77 DIMLVCQQANCDEEKAKDALAETKGDIAQAILRLTSG 113
Cdd:COG1308   80 DVELVAEQTGVSEEEAREALEEANGDLAEAILKLEEE 116
 
Name Accession Description Interval E-value
EGD2 COG1308
Transcription factor homologous to NACalpha-BTF3 [Transcription];
1-113 3.20e-35

Transcription factor homologous to NACalpha-BTF3 [Transcription];


Pssm-ID: 440919 [Multi-domain]  Cd Length: 116  Bit Score: 116.87  E-value: 3.20e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528520   1 MMRGGN-RQMRRMMDKMGLDMEEIPnVQEVIIKTDKKEIIIPKPSVTEMKSKENSIFQVIAESFEEK---ELEVPIFSED 76
Cdd:COG1308    1 MFGGMNpRKMKQMMKQMGIKVEEID-AEEVIIRTKDKEIVFENPQVTVMKAQGQETYQIVGEPEEVEkgaEEAEVEIPEE 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 663528520  77 DIMLVCQQANCDEEKAKDALAETKGDIAQAILRLTSG 113
Cdd:COG1308   80 DVELVAEQTGVSEEEAREALEEANGDLAEAILKLEEE 116
nac PRK06369
nascent polypeptide-associated complex protein; Reviewed
 1-113 9.33e-30

nascent polypeptide-associated complex protein; Reviewed


Pssm-ID: 235786 [Multi-domain]  Cd Length: 115  Bit Score: 103.02  E-value: 9.33e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528520   1 MMRGGN-RQMRRMMDKMGLDMEEIpNVQEVIIKTDKKEIIIPKPSVTEMKSKENSIFQVIAESFEEK--ELEVPIFSEDD 77
Cdd:PRK06369   1 GMGGMNpRKMKQMMKQMGIDVEEL-DVEEVIIRLKDKEIVFENPQVTVMDAQGQKTYQIVGEPEEVEkeAEKEVEIPEED 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 663528520  78 IMLVCQQANCDEEKAKDALAETKGDIAQAILRLTSG 113
Cdd:PRK06369  80 IELVAEQTGVSEEEARKALEEANGDLAEAILKLSSE 115
TIGR00264 TIGR00264
alpha-NAC-related protein; This hypothetical protein is found so far only in the Archaea. Its ...
 7-110 1.39e-20

alpha-NAC-related protein; This hypothetical protein is found so far only in the Archaea. Its C-terminal domain of about 40 amino acids is homologous to the C-termini of the nascent polypeptide-associated complex alpha chain (alpha-NAC) and its yeast ortholog Egd2p and to the huntingtin-interacting protein HYPK. It shows weaker similarity, possibly through shared structural constraints rather than through homology, with the amino-terminal domain of elongation factor Ts. Alpha-NAC plays a role in preventing nascent polypeptides from binding inappropriately to membrane-targeting apparatus during translation, but is also active as a transcription regulator. [Unknown function, General]


Pssm-ID: 272988 [Multi-domain]  Cd Length: 116  Bit Score: 79.61  E-value: 1.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528520    7 RQMRRMMDKMGLDMEEIpNVQEVIIKTDKKEIIIPKPSVTEMKSKENSIFQVIAESFEEKELEVPIFSEDDIMLVCQQAN 86
Cdd:TIGR00264  12 KQMQKMMKQMGMEMEDL-DVEEVIIVFDDEEWIFENPKVQVMDILGVKTYQITGKPKKEKVEEEEEITEDDIELVMKQCN 90

                          90       100
                  ....*....|....*....|....
gi 663528520   87 CDEEKAKDALAETKGDIAQAILRL 110
Cdd:TIGR00264  91 VSKEEARRALEECGGDLAEAIMKL 114
UBA_AeNAC cd14359
UBA-like domain found in archaeal nascent polypeptide-associated complex homolog from ...
 72-111 4.81e-12

UBA-like domain found in archaeal nascent polypeptide-associated complex homolog from Methanothermobacter marburgensis (AeNAC) and similar proteins; AeNAC is a functional archaeal homolog of eukaryotic nascent polypeptide-associated complex (NAC). Both AeNAC and eukaryotic NAC function as the cytosolic chaperone that can bind to ribosomal RNA, interact with the nascent polypeptide chains as they emerge from the ribosome, and assist in post-translational processes. They all contain a NAC domain and an ubiquitin-associated (UBA) domain in the C-terminus. However, unlike eukaryotic NAC, AeNAC forms a ribosome associated homodimer, but not heterodimer. The NAC domain of AeNAC is responsible for the homodimer formation.


Pssm-ID: 270542 [Multi-domain]  Cd Length: 40  Bit Score: 55.69  E-value: 4.81e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 663528520  72 IFSEDDIMLVCQQANCDEEKAKDALAETKGDIAQAILRLT 111
Cdd:cd14359    1 EISEEDIELVMEQTGVSREEARKALEESGGDLAEAILKLT 40
NAC pfam01849
NAC domain;
8-61 2.46e-08

NAC domain;


Pssm-ID: 426474  Cd Length: 54  Bit Score: 46.69  E-value: 2.46e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 663528520    8 QMRRMMDKMGldMEEIPNVQEVIIKTDK-KEIIIPKPSVTemKSKENSIFQVIAE 61
Cdd:pfam01849   1 KLQKALKKLG--LKPIPGVEEVNIFKSDgKVLVFNNPKVQ--KSPGSNTYVVFGE 51
 
Name Accession Description Interval E-value
EGD2 COG1308
Transcription factor homologous to NACalpha-BTF3 [Transcription];
1-113 3.20e-35

Transcription factor homologous to NACalpha-BTF3 [Transcription];


Pssm-ID: 440919 [Multi-domain]  Cd Length: 116  Bit Score: 116.87  E-value: 3.20e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528520   1 MMRGGN-RQMRRMMDKMGLDMEEIPnVQEVIIKTDKKEIIIPKPSVTEMKSKENSIFQVIAESFEEK---ELEVPIFSED 76
Cdd:COG1308    1 MFGGMNpRKMKQMMKQMGIKVEEID-AEEVIIRTKDKEIVFENPQVTVMKAQGQETYQIVGEPEEVEkgaEEAEVEIPEE 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 663528520  77 DIMLVCQQANCDEEKAKDALAETKGDIAQAILRLTSG 113
Cdd:COG1308   80 DVELVAEQTGVSEEEAREALEEANGDLAEAILKLEEE 116
nac PRK06369
nascent polypeptide-associated complex protein; Reviewed
 1-113 9.33e-30

nascent polypeptide-associated complex protein; Reviewed


Pssm-ID: 235786 [Multi-domain]  Cd Length: 115  Bit Score: 103.02  E-value: 9.33e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528520   1 MMRGGN-RQMRRMMDKMGLDMEEIpNVQEVIIKTDKKEIIIPKPSVTEMKSKENSIFQVIAESFEEK--ELEVPIFSEDD 77
Cdd:PRK06369   1 GMGGMNpRKMKQMMKQMGIDVEEL-DVEEVIIRLKDKEIVFENPQVTVMDAQGQKTYQIVGEPEEVEkeAEKEVEIPEED 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 663528520  78 IMLVCQQANCDEEKAKDALAETKGDIAQAILRLTSG 113
Cdd:PRK06369  80 IELVAEQTGVSEEEARKALEEANGDLAEAILKLSSE 115
TIGR00264 TIGR00264
alpha-NAC-related protein; This hypothetical protein is found so far only in the Archaea. Its ...
 7-110 1.39e-20

alpha-NAC-related protein; This hypothetical protein is found so far only in the Archaea. Its C-terminal domain of about 40 amino acids is homologous to the C-termini of the nascent polypeptide-associated complex alpha chain (alpha-NAC) and its yeast ortholog Egd2p and to the huntingtin-interacting protein HYPK. It shows weaker similarity, possibly through shared structural constraints rather than through homology, with the amino-terminal domain of elongation factor Ts. Alpha-NAC plays a role in preventing nascent polypeptides from binding inappropriately to membrane-targeting apparatus during translation, but is also active as a transcription regulator. [Unknown function, General]


Pssm-ID: 272988 [Multi-domain]  Cd Length: 116  Bit Score: 79.61  E-value: 1.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528520    7 RQMRRMMDKMGLDMEEIpNVQEVIIKTDKKEIIIPKPSVTEMKSKENSIFQVIAESFEEKELEVPIFSEDDIMLVCQQAN 86
Cdd:TIGR00264  12 KQMQKMMKQMGMEMEDL-DVEEVIIVFDDEEWIFENPKVQVMDILGVKTYQITGKPKKEKVEEEEEITEDDIELVMKQCN 90

                          90       100
                  ....*....|....*....|....
gi 663528520   87 CDEEKAKDALAETKGDIAQAILRL 110
Cdd:TIGR00264  91 VSKEEARRALEECGGDLAEAIMKL 114
UBA_AeNAC cd14359
UBA-like domain found in archaeal nascent polypeptide-associated complex homolog from ...
 72-111 4.81e-12

UBA-like domain found in archaeal nascent polypeptide-associated complex homolog from Methanothermobacter marburgensis (AeNAC) and similar proteins; AeNAC is a functional archaeal homolog of eukaryotic nascent polypeptide-associated complex (NAC). Both AeNAC and eukaryotic NAC function as the cytosolic chaperone that can bind to ribosomal RNA, interact with the nascent polypeptide chains as they emerge from the ribosome, and assist in post-translational processes. They all contain a NAC domain and an ubiquitin-associated (UBA) domain in the C-terminus. However, unlike eukaryotic NAC, AeNAC forms a ribosome associated homodimer, but not heterodimer. The NAC domain of AeNAC is responsible for the homodimer formation.


Pssm-ID: 270542 [Multi-domain]  Cd Length: 40  Bit Score: 55.69  E-value: 4.81e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 663528520  72 IFSEDDIMLVCQQANCDEEKAKDALAETKGDIAQAILRLT 111
Cdd:cd14359    1 EISEEDIELVMEQTGVSREEARKALEESGGDLAEAILKLT 40
UBA_NAC_like cd14278
UBA-like domain found in nascent polypeptide-associated complex subunit alpha (NACA) and ...
 75-111 5.09e-09

UBA-like domain found in nascent polypeptide-associated complex subunit alpha (NACA) and similar proteins; The family contains nascent polypeptide-associated complex subunit alpha (NACA), putative NACA-like protein (NACP1), nascent polypeptide-associated complex subunit alpha domain-containing protein 1 (NACAD), and similar proteins found in archaea and bacteria. NACA, also called NAC-alpha or Alpha-NAC, together with BTF3, also called Beta-NAC, form the nascent polypeptide-associated complex (NAC) which is a cytosolic protein chaperone that contacts the nascent polypeptide chains as they emerge from the ribosome. Besides, NACA has a high affinity for nucleic acids and exists as part of several protein complexes playing a role in proliferation, apoptosis, or degradation. It is a cytokine-modulated specific transcript in the human TF-1 erythroleukemic cell line. It also acts as a transcriptional co-activator in osteoblasts by binding to phosphorylated c-Jun, a member of the activator-protein-1 (AP-1) family. Moreover, NACA binds to and regulates the adaptor protein Fas-associated death domain (FADD). In addition, NACA functions as a novel factor participating in the positive regulation of human erythroid-cell differentiation. The biological function of NACP1 (also called Alpha-NAC pseudogene 1 or NAC-alpha pseudogene 1) and NACAD remain unclear. The family also includes huntingtin-interacting protein K (HYPK), also called Huntingtin yeast partner K or Huntingtin yeast two-hybrid protein K. It is an intrinsically unstructured Huntingtin (HTT)-interacting protein with chaperone-like activity. It may be involved in regulating cell growth, cell cycle, unfolded protein response and cell death. All members in this family contain an ubiquitin-associated (UBA) domain.


Pssm-ID: 270464 [Multi-domain]  Cd Length: 37  Bit Score: 47.86  E-value: 5.09e-09
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 663528520  75 EDDIMLVCQQANCDEEKAKDALAETKGDIAQAILRLT 111
Cdd:cd14278    1 EEDIELVMSQTGVSREEAIKALRENKGDVVDAILELT 37
NAC pfam01849
NAC domain;
8-61 2.46e-08

NAC domain;


Pssm-ID: 426474  Cd Length: 54  Bit Score: 46.69  E-value: 2.46e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 663528520    8 QMRRMMDKMGldMEEIPNVQEVIIKTDK-KEIIIPKPSVTemKSKENSIFQVIAE 61
Cdd:pfam01849   1 KLQKALKKLG--LKPIPGVEEVNIFKSDgKVLVFNNPKVQ--KSPGSNTYVVFGE 51
UBA_NAC_euk cd14358
UBA-like domain found in nascent polypeptide-associated complex subunit alpha (NACA) and its ...
 75-111 3.05e-06

UBA-like domain found in nascent polypeptide-associated complex subunit alpha (NACA) and its homologs mainly found in eukaryotes; The subfamily contains nascent polypeptide-associated complex subunit alpha (NACA), putative NACA-like protein (NACP1), nascent polypeptide-associated complex subunit alpha domain-containing protein 1 (NACAD), and similar proteins. NACA, also called NAC-alpha or Alpha-NAC, together with BTF3, also called Beta-NAC, form the nascent polypeptide-associated complex (NAC) which is a cytosolic protein chaperone that contacts the nascent polypeptide chains as they emerge from the ribosome. Besides, NACA has a high affinity for nucleic acids and exists as part of several protein complexes playing a role in proliferation, apoptosis, or degradation. It is a cytokine-modulated specific transcript in the human TF-1 erythroleukemic cell line. It also acts as a transcriptional co-activator in osteoblasts by binding to phosphorylated c-Jun, a member of the activator-protein-1 (AP-1) family. Moreover, NACA binds to and regulates the adaptor protein Fas-associated death domain (FADD). In addition, NACA functions as a novel factor participating in the positive regulation of human erythroid-cell differentiation. The biological function of NACP1 (also called Alpha-NAC pseudogene 1 or NAC-alpha pseudogene 1) and NACAD remain unclear. All family members contain an NAC domain and a C-terminal ubiquitin-associated (UBA) domain.


Pssm-ID: 270541 [Multi-domain]  Cd Length: 37  Bit Score: 40.68  E-value: 3.05e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 663528520  75 EDDIMLVCQQANCDEEKAKDALAETKGDIAQAILRLT 111
Cdd:cd14358    1 PKDIELVMQQANVSRAKAVKALKENDNDIVNAIMELT 37
NAC_NACA cd22054
nascent polypeptide-associated complex (NAC), alpha subunit; The nascent ...
 19-56 6.25e-06

nascent polypeptide-associated complex (NAC), alpha subunit; The nascent polypeptide-associated complex (NAC) is a complex, conserved from archaea to human, that plays an important role in co translational targeting of nascent polypeptides to the endoplasmic reticulum (ER). In eukaryotes, under physiological conditions, the complex is a stable heterodimer of the NAC alpha subunit and the NAC beta subunit, also known as basal transcription factor 3b (BTF3b). An imbalance of the relative concentrations has been observed in diseases, like Alzheimer's, AIDS, and ulcerative colitis. NAC alpha consists of a NAC domain, also present in BTF3, and a unique C-terminal ubiquitin-associated (UBA) domain.


Pssm-ID: 409233  Cd Length: 48  Bit Score: 40.24  E-value: 6.25e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 663528520  19 DMEEIPNVQEVIIKTDK-KEIIIPKPSVTEMKSKENSIF 56
Cdd:cd22054    1 GLKPVPGVTRVTIKKSKnILFVINKPDVYKSPGSDTYIV 39
 
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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