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 1002235937 156 EEVDESGVEPKDIELVMTQATVSRSRAVKALKAANGDIVTAIMELT 201
Cdd:cd14415     1 EEVDETGVEVKDIELVMSQANVSRAKAVRALKNNSNDIVNAIMELT 46

NAC domain;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002235937  66 KSRKAMQKLGMKTITGVSRVTIKKSKNILFVISKPDVFKSPNSDTYVIFGEAKI 119
Cdd:pfam01849   1 KLQKALKKLGLKPIPGVEEVNIFKSDGKVLVFNNPKVQKSPGSNTYVVFGEAEE 54

Transcription factor homologous to NACalpha-BTF3 [Transcription];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235937  65 KKSRKAMQKLGMKTIT-GVSRVTIK-KSKNIlfVISKPDV--FKSPNSDTYVIFGEAKIEDLSSQlqtqaaeqfkapdls 140
Cdd:COG1308     8 RKMKQMMKQMGIKVEEiDAEEVIIRtKDKEI--VFENPQVtvMKAQGQETYQIVGEPEEVEKGAE--------------- 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002235937 141 nviskaepsaaaQDDEEVDESgvepkDIELVMTQATVSRSRAVKALKAANGDIVTAIMELTN 202
Cdd:COG1308    71 ------------EAEVEIPEE-----DVELVAEQTGVSEEEAREALEEANGDLAEAILKLEE 115

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 1002235937 162 GVEPKDIELVMTQATVSRSRAVKALKAANGDIVTAIMELT 201
Cdd:pfam19026   2 KVKKEDVELIMTELEVSKAKAERALREHGGDVVAALRALL 41

NAC domain;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002235937  66 KSRKAMQKLGMKTITGVSRVTIKKSKNILFVISKPDVFKSPNSDTYVIFGEAKI 119
Cdd:pfam01849   1 KLQKALKKLGLKPIPGVEEVNIFKSDGKVLVFNNPKVQKSPGSNTYVVFGEAEE 54

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 1002235937 165 PKDIELVMTQATVSRSRAVKALKAANGDIVTAIMELT 201
Cdd:cd14358     1 PKDIELVMQQANVSRAKAVKALKENDNDIVNAIMELT 37

UBA-like domain found in nascent polypeptide-associated complex subunit alpha domain-containing protein 1 (NACAD); The subfamily includes a group of uncharacterized proteins mainly found in vertebrates. Their biological function remains unknown, but they show high sequence similarity to the nascent polypeptide-associated complex (NAC) subunit alpha (NACA) that exists as part of several protein complexes playing a role in proliferation, apoptosis, or degradation. Like NACA, NACAD contains an NAC domain and a C-terminal ubiquitin-associated (UBA) domain.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1002235937 159 DESGVEPKDIELVMTQATVSRSRAVKALKAANGDIVTAIMELT 201
Cdd:cd14416     1 DETGLEVRDIELVMAQANVSRAKAVRALRHNNNDIVNAIMELT 43

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 1002235937 165 PKDIELVMTQATVSRSRAVKALKAANGDIVTAIMELT 201
Cdd:cd14278     1 EEDIELVMSQTGVSREEAIKALRENKGDVVDAILELT 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 1002235937 167 DIELVMTQATVSRSRAVKALKAANGDIVTAIMELT 201
Cdd:cd14359     6 DIELVMEQTGVSREEARKALEESGGDLAEAILKLT 40

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        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235937  62 RSEKKSRKAMQKLGMKTIT-GVSRVTIK-KSKNILFVISKPDVFKSPNSDTYVIFGEAKIEDLssqlqtqaaeqfkapdl 139
Cdd:TIGR00264   9 KMLKQMQKMMKQMGMEMEDlDVEEVIIVfDDEEWIFENPKVQVMDILGVKTYQITGKPKKEKV----------------- 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002235937 140 snviskaepsaaaQDDEEVDEsgvepKDIELVMTQATVSRSRAVKALKAANGDIVTAIMEL 200
Cdd:TIGR00264  72 -------------EEEEEITE-----DDIELVMKQCNVSKEEARRALEECGGDLAEAIMKL 114

basal transcription factor BTF3; Basal transcription factor 3 (BTF3) plays an important role in the transcriptional regulation linked to growth and development in eukaryotes. In mammals, the BTF3 gene encodes two alternative splicing isoforms, BTF3a and BTF3b. The full length BTF3a protein excites transcription. The shortened BTF3b, which lacks the first 44 amino-terminal extension, is a component of the nascent polypeptide-associated complex (NAC), involved in regulating protein localization during translation. BTF3 is involved in oncogenesis; overexpression of BTF3 has been shown to be associated with a variety of malignancies such as cancer of the colon, pancreas, stomach, prostate and breast. It is upregulated in hypopharyngeal squamous cell carcinoma (HSCC) tumors correlating with lymph node metastasis and tumor promotion, thus indicating that BTF3 is a potential therapeutic target and prognostic biomarker for HSCC. BTF3 has also been implicated in the pathogenesis of osteosarcoma (OS), a malignant cancer that affects rapidly proliferating bones, and has a poor prognosis.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235937  51 GGDASGRSKQ-------SRSEKKSRKAMQKLGMKTITGVSRVTIKKSKNILFVISKPDVFKSPNSDTYVIFG---EAKIE 120
Cdd:cd22055    13 GGKGTPRRKKkvvhktaTTDDKKLQSTLKKLGVQPIPGIEEVNMFKDDGTVIHFNNPKVQASIAANTFVISGkpeTKTLT 92

                          90
                  ....*....|....*....
gi 1002235937 121 DL----SSQLQTQAAEQFK 135
Cdd:cd22055    93 ELlpgiLNQLGPENLDNLK 111