UBA-like domain found in nascent polypeptide-associated complex subunit alpha (NACA) and putative NACA-like protein (NACP1); 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. Both NACA and BTF3 harbor an NAC domain that mediates the dimerization of the two subunits. By contrast, NACA has an extra ubiquitin-associated (UBA) domain in the C-terminus. In addition to NACA, the family includes NACP1, also called Alpha-NAC pseudogene 1 or NAC-alpha pseudogene 1. The biological function of NACP1 remains unclear.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 71151997 169 EEVDETGVEVKDIELVMSQANVSRAKAVRALKNNSNDIVNAIMELT 214
Cdd:cd14415   1 EEVDETGVEVKDIELVMSQANVSRAKAVRALKNNSNDIVNAIMELT 46

UBA-like domain found in nascent polypeptide-associated complex subunit alpha (NACA) and putative NACA-like protein (NACP1); 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. Both NACA and BTF3 harbor an NAC domain that mediates the dimerization of the two subunits. By contrast, NACA has an extra ubiquitin-associated (UBA) domain in the C-terminus. In addition to NACA, the family includes NACP1, also called Alpha-NAC pseudogene 1 or NAC-alpha pseudogene 1. The biological function of NACP1 remains unclear.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 71151997 169 EEVDETGVEVKDIELVMSQANVSRAKAVRALKNNSNDIVNAIMELT 214
Cdd:cd14415   1 EEVDETGVEVKDIELVMSQANVSRAKAVRALKNNSNDIVNAIMELT 46

Transcription factor homologous to NACalpha-BTF3 [Transcription];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71151997  74 KKARKAMSKLGLRQVT-GVTRVTIR-KSKNIlfVITKPDVY--KSPASDTYIVFGEAKIEDLSQQAQlaaaekfkvqgea 149
Cdd:COG1308   8 RKMKQMMKQMGIKVEEiDAEEVIIRtKDKEI--VFENPQVTvmKAQGQETYQIVGEPEEVEKGAEEA------------- 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71151997 150 vsniqentqtptvqeeseeeevdetGVEVK--DIELVMSQANVSRAKAVRALKNNSNDIVNAIMELT 214
Cdd:COG1308  73 -------------------------EVEIPeeDVELVAEQTGVSEEEAREALEEANGDLAEAILKLE 114

nascent polypeptide-associated complex protein; Reviewed

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71151997   74 KKARKAMSKLGLR-QVTGVTRVTIR-KSKNIlfVITKPDV--YKSPASDTYIVFGEAKIEDLSQQAQLAAAEKfkvqgea 149
Cdd:PRK06369   8 RKMKQMMKQMGIDvEELDVEEVIIRlKDKEI--VFENPQVtvMDAQGQKTYQIVGEPEEVEKEAEKEVEIPEE------- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71151997  150 vsniqentqtptvqeeseeeevdetgvevkDIELVMSQANVSRAKAVRALKNNSNDIVNAIMELT 214
Cdd:PRK06369  79 ------------------------------DIELVAEQTGVSEEEARKALEEANGDLAEAILKLS 113

UBA-like domain found in nascent polypeptide-associated complex subunit alpha (NACA) and putative NACA-like protein (NACP1); 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. Both NACA and BTF3 harbor an NAC domain that mediates the dimerization of the two subunits. By contrast, NACA has an extra ubiquitin-associated (UBA) domain in the C-terminus. In addition to NACA, the family includes NACP1, also called Alpha-NAC pseudogene 1 or NAC-alpha pseudogene 1. The biological function of NACP1 remains unclear.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 71151997 169 EEVDETGVEVKDIELVMSQANVSRAKAVRALKNNSNDIVNAIMELT 214
Cdd:cd14415   1 EEVDETGVEVKDIELVMSQANVSRAKAVRALKNNSNDIVNAIMELT 46

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.

                        10        20        30
                ....*....|....*....|....*....|....*.
gi 71151997 179 KDIELVMSQANVSRAKAVRALKNNSNDIVNAIMELT 214
Cdd:cd14358   2 KDIELVMQQANVSRAKAVKALKENDNDIVNAIMELT 37

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.

                        10        20        30
                ....*....|....*....|....*....|....*.
gi 71151997 179 KDIELVMSQANVSRAKAVRALKNNSNDIVNAIMELT 214
Cdd:cd14278   2 EDIELVMSQTGVSREEAIKALRENKGDVVDAILELT 37

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.

                        10        20        30
                ....*....|....*....|....*....|....*
gi 71151997 180 DIELVMSQANVSRAKAVRALKNNSNDIVNAIMELT 214
Cdd:cd14359   6 DIELVMEQTGVSREEARKALEESGGDLAEAILKLT 40

HYPK UBA domain; This entry represents the UBA domain found at the C-terminus of the HYPK protein and its homologs. This domain in HYPK mediates a protein interaction with the Naa15 C-terminus.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 71151997   174 TGVEVKDIELVMSQANVSRAKAVRALKNNSNDIVNAIMELT 214
Cdd:pfam19026   1 VKVKKEDVELIMTELEVSKAKAERALREHGGDVVAALRALL 41

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]

                          10        20        30
                  ....*....|....*....|....*....|....
gi 71151997   180 DIELVMSQANVSRAKAVRALKNNSNDIVNAIMEL 213
Cdd:TIGR00264  81 DIELVMKQCNVSKEEARRALEECGGDLAEAIMKL 114