RecName: Full=Malignant T-cell-amplified sequence 1; Short=MCT-1; AltName: Full=Multiple copies T-cell malignancies 1
malignant T-cell-amplified sequence family protein( domain architecture ID 15300156)
malignant T-cell-amplified sequence family protein similar to MCT-1 (multiple copies T cell malignancies 1), also known as MCTS-1 (malignant T cell-amplified sequence 1), which, together with DENR (density regulated protein), has been shown to have similar function as the eIF2D translation initiation factor (also known as ligatin), which is involved in the recruitment and delivery of aminoacyl-tRNAs to the P-site of the eukaryotic ribosome in a GTP-independent manner.
List of domain hits
Name | Accession | Description | Interval | E-value | |||
PUA_MCTS-1-like | cd21155 | PUA RNA-binding domain of malignant T cell-amplified sequence 1 and related proteins; The ... |
80-175 | 1.68e-73 | |||
PUA RNA-binding domain of malignant T cell-amplified sequence 1 and related proteins; The RNA-binding PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in a number of proteins involved in RNA metabolism. Members of this eukaryotic family, labelled MCT-1 (malignant T cell-amplified sequence 1) or MCTS-1 (multiple copies T-cell lymphoma-1), contain a single PUA domain. They may play roles in the regulation of the cell cycle; human MCT-1 has been characterized for its oncogenic potential. MCT-1/MCTS1 expression is a new poor-prognosis marker in patients with aggressive breast cancers, and thus the MCT-1 pathway is a novel and promising therapeutic target for triple-negative breast cancer (TNBC). : Pssm-ID: 409297 Cd Length: 97 Bit Score: 215.81 E-value: 1.68e-73
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MCT1_N | cd11609 | N-terminal domain of multiple copies T cell malignancies 1 and related proteins; This ... |
4-80 | 7.07e-43 | |||
N-terminal domain of multiple copies T cell malignancies 1 and related proteins; This N-terminal domain of MCT-1 (multiple copies T cell malignancies 1), also known as MCTS-1 (malignant T cell-amplified sequence 1), co-occurs with a PUA domain. MCT-1, together with DENR (density regulated protein), has been shown to have similar function as eIF2D translation initiation factor (also known as ligatin), which is involved in the recruitment and delivery of aminoacyl-tRNAs to the P-site of the eukaryotic ribosome in a GTP-independent manner. : Pssm-ID: 211422 Cd Length: 77 Bit Score: 137.67 E-value: 7.07e-43
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Name | Accession | Description | Interval | E-value | ||||
PUA_MCTS-1-like | cd21155 | PUA RNA-binding domain of malignant T cell-amplified sequence 1 and related proteins; The ... |
80-175 | 1.68e-73 | ||||
PUA RNA-binding domain of malignant T cell-amplified sequence 1 and related proteins; The RNA-binding PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in a number of proteins involved in RNA metabolism. Members of this eukaryotic family, labelled MCT-1 (malignant T cell-amplified sequence 1) or MCTS-1 (multiple copies T-cell lymphoma-1), contain a single PUA domain. They may play roles in the regulation of the cell cycle; human MCT-1 has been characterized for its oncogenic potential. MCT-1/MCTS1 expression is a new poor-prognosis marker in patients with aggressive breast cancers, and thus the MCT-1 pathway is a novel and promising therapeutic target for triple-negative breast cancer (TNBC). Pssm-ID: 409297 Cd Length: 97 Bit Score: 215.81 E-value: 1.68e-73
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MCT1_N | cd11609 | N-terminal domain of multiple copies T cell malignancies 1 and related proteins; This ... |
4-80 | 7.07e-43 | ||||
N-terminal domain of multiple copies T cell malignancies 1 and related proteins; This N-terminal domain of MCT-1 (multiple copies T cell malignancies 1), also known as MCTS-1 (malignant T cell-amplified sequence 1), co-occurs with a PUA domain. MCT-1, together with DENR (density regulated protein), has been shown to have similar function as eIF2D translation initiation factor (also known as ligatin), which is involved in the recruitment and delivery of aminoacyl-tRNAs to the P-site of the eukaryotic ribosome in a GTP-independent manner. Pssm-ID: 211422 Cd Length: 77 Bit Score: 137.67 E-value: 7.07e-43
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Pre-PUA | pfam17832 | Pre-PUA-like domain; This Pre-PUA-like domain is found in a wide variety of proteins including ... |
5-89 | 1.27e-33 | ||||
Pre-PUA-like domain; This Pre-PUA-like domain is found in a wide variety of proteins including the eukaryotic translation initiation factor 2D, where it is found at the N-terminus. Pssm-ID: 436077 Cd Length: 86 Bit Score: 114.59 E-value: 1.27e-33
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Tma20 | COG2016 | Predicted ribosome-associated RNA-binding protein Tma20, contains PUA domain [Translation, ... |
16-175 | 1.23e-31 | ||||
Predicted ribosome-associated RNA-binding protein Tma20, contains PUA domain [Translation, ribosomal structure and biogenesis]; Pssm-ID: 441619 [Multi-domain] Cd Length: 154 Bit Score: 111.41 E-value: 1.23e-31
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arCOG00985 | TIGR03684 | arCOG04150 universal archaeal PUA-domain protein; This universal archaeal protein contains a ... |
16-175 | 1.33e-28 | ||||
arCOG04150 universal archaeal PUA-domain protein; This universal archaeal protein contains a domain possibly associated with RNA binding (pfam01472, TIGR00451). Pssm-ID: 274723 [Multi-domain] Cd Length: 150 Bit Score: 103.46 E-value: 1.33e-28
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PRK14560 | PRK14560 | putative RNA-binding protein; Provisional |
16-178 | 2.26e-28 | ||||
putative RNA-binding protein; Provisional Pssm-ID: 237757 [Multi-domain] Cd Length: 160 Bit Score: 103.39 E-value: 2.26e-28
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PUA | pfam01472 | PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, ... |
93-170 | 5.55e-18 | ||||
PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, was detected in archaeal and eukaryotic pseudouridine synthases, archaeal archaeosine synthases, a family of predicted ATPases that may be involved in RNA modification, a family of predicted archaeal and bacterial rRNA methylases. Additionally, the PUA domain was detected in a family of eukaryotic proteins that also contain a domain homologous to the translation initiation factor eIF1/SUI1; these proteins may comprise a novel type of translation factors. Unexpectedly, the PUA domain was detected also in bacterial and yeast glutamate kinases; this is compatible with the demonstrated role of these enzymes in the regulation of the expression of other genes. It is predicted that the PUA domain is an RNA binding domain. Pssm-ID: 426278 [Multi-domain] Cd Length: 74 Bit Score: 74.06 E-value: 5.55e-18
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PUA | smart00359 | Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase; |
97-170 | 9.15e-11 | ||||
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase; Pssm-ID: 214635 [Multi-domain] Cd Length: 76 Bit Score: 55.34 E-value: 9.15e-11
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Name | Accession | Description | Interval | E-value | ||||
PUA_MCTS-1-like | cd21155 | PUA RNA-binding domain of malignant T cell-amplified sequence 1 and related proteins; The ... |
80-175 | 1.68e-73 | ||||
PUA RNA-binding domain of malignant T cell-amplified sequence 1 and related proteins; The RNA-binding PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in a number of proteins involved in RNA metabolism. Members of this eukaryotic family, labelled MCT-1 (malignant T cell-amplified sequence 1) or MCTS-1 (multiple copies T-cell lymphoma-1), contain a single PUA domain. They may play roles in the regulation of the cell cycle; human MCT-1 has been characterized for its oncogenic potential. MCT-1/MCTS1 expression is a new poor-prognosis marker in patients with aggressive breast cancers, and thus the MCT-1 pathway is a novel and promising therapeutic target for triple-negative breast cancer (TNBC). Pssm-ID: 409297 Cd Length: 97 Bit Score: 215.81 E-value: 1.68e-73
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MCT1_N | cd11609 | N-terminal domain of multiple copies T cell malignancies 1 and related proteins; This ... |
4-80 | 7.07e-43 | ||||
N-terminal domain of multiple copies T cell malignancies 1 and related proteins; This N-terminal domain of MCT-1 (multiple copies T cell malignancies 1), also known as MCTS-1 (malignant T cell-amplified sequence 1), co-occurs with a PUA domain. MCT-1, together with DENR (density regulated protein), has been shown to have similar function as eIF2D translation initiation factor (also known as ligatin), which is involved in the recruitment and delivery of aminoacyl-tRNAs to the P-site of the eukaryotic ribosome in a GTP-independent manner. Pssm-ID: 211422 Cd Length: 77 Bit Score: 137.67 E-value: 7.07e-43
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Pre-PUA | pfam17832 | Pre-PUA-like domain; This Pre-PUA-like domain is found in a wide variety of proteins including ... |
5-89 | 1.27e-33 | ||||
Pre-PUA-like domain; This Pre-PUA-like domain is found in a wide variety of proteins including the eukaryotic translation initiation factor 2D, where it is found at the N-terminus. Pssm-ID: 436077 Cd Length: 86 Bit Score: 114.59 E-value: 1.27e-33
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Tma20 | COG2016 | Predicted ribosome-associated RNA-binding protein Tma20, contains PUA domain [Translation, ... |
16-175 | 1.23e-31 | ||||
Predicted ribosome-associated RNA-binding protein Tma20, contains PUA domain [Translation, ribosomal structure and biogenesis]; Pssm-ID: 441619 [Multi-domain] Cd Length: 154 Bit Score: 111.41 E-value: 1.23e-31
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arCOG00985 | TIGR03684 | arCOG04150 universal archaeal PUA-domain protein; This universal archaeal protein contains a ... |
16-175 | 1.33e-28 | ||||
arCOG04150 universal archaeal PUA-domain protein; This universal archaeal protein contains a domain possibly associated with RNA binding (pfam01472, TIGR00451). Pssm-ID: 274723 [Multi-domain] Cd Length: 150 Bit Score: 103.46 E-value: 1.33e-28
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PRK14560 | PRK14560 | putative RNA-binding protein; Provisional |
16-178 | 2.26e-28 | ||||
putative RNA-binding protein; Provisional Pssm-ID: 237757 [Multi-domain] Cd Length: 160 Bit Score: 103.39 E-value: 2.26e-28
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unchar_dom_2 | TIGR00451 | uncharacterized domain 2; This uncharacterized domain is found a number of enzymes and ... |
64-172 | 2.50e-27 | ||||
uncharacterized domain 2; This uncharacterized domain is found a number of enzymes and uncharacterized proteins, often at the C-terminus. It is found in some but not all members of a family of related tRNA-guanine transglycosylases (tgt), which exchange a guanine base for some modified base without breaking the phosphodiester backbone of the tRNA. It is also found in rRNA pseudouridine synthase, another enzyme of RNA base modification not otherwise homologous to tgt. It is found, again at the C-terminus, in two putative glutamate 5-kinases. It is also found in a family of small, uncharacterized archaeal proteins consisting mostly of this domain. Pssm-ID: 129543 [Multi-domain] Cd Length: 107 Bit Score: 99.04 E-value: 2.50e-27
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eIF2D_N_like | cd11580 | N-terminal domain of eIF2D, malignant T cell-amplified sequence 1 and related proteins; This ... |
9-80 | 3.60e-27 | ||||
N-terminal domain of eIF2D, malignant T cell-amplified sequence 1 and related proteins; This N-terminal domain of various proteins co-occurs with a PUA domain. Members of this family are: (1) MCTS-1 (malignant T cell-amplified sequence 1) or MCT-1 (multiple copies T cell malignancies), which may play roles in the regulation of the cell cycle, (2) the eukayotic translation initiation factor 2D, and (3) an uncharacterized archaeal family. Pssm-ID: 211421 Cd Length: 72 Bit Score: 97.42 E-value: 3.60e-27
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PUA | cd07953 | PUA RNA binding domain; The PUA (PseudoUridine synthase and Archaeosine transglycosylase) ... |
93-169 | 6.89e-20 | ||||
PUA RNA binding domain; The PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in archaeal and eukaryotic pseudouridine synthases, archaeal archaeosine synthases, a family of predicted ATPases that may be involved in RNA modification, and a family of predicted archaeal and bacterial rRNA methylases. Additionally, the PUA domain was detected in a family of eukaryotic proteins that also contain a domain homologous to the translation initiation factor eIF1/SUI1; these proteins may comprise a novel type of translation factors. Unexpectedly, the PUA domain was also found in bacterial and yeast glutamate kinases; this is compatible with the demonstrated role of these enzymes in regulating the expression of other genes. It has been shown that the PUA domain acts as an RNA binding domain in at least some of the proteins involved in RNA metabolism. Pssm-ID: 409289 [Multi-domain] Cd Length: 73 Bit Score: 78.88 E-value: 6.89e-20
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PUA_MJ1432-like | cd21154 | PUA RNA-binding domain of MJ1432, TA1423, PH0734, and similar proteins; The RNA-binding PUA ... |
92-177 | 1.69e-19 | ||||
PUA RNA-binding domain of MJ1432, TA1423, PH0734, and similar proteins; The RNA-binding PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in a number of proteins involved in RNA metabolism. Members of this mostly archaeal family have not been characterized functionally; they may bind to RNA. This family includes Pyrococcus horikoshii PH0734 where the N-terminal domain may modulate the binding target of the C-terminal PUA domain using its characteristic electropositive surface. Pssm-ID: 409296 [Multi-domain] Cd Length: 84 Bit Score: 78.31 E-value: 1.69e-19
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PUA | pfam01472 | PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, ... |
93-170 | 5.55e-18 | ||||
PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, was detected in archaeal and eukaryotic pseudouridine synthases, archaeal archaeosine synthases, a family of predicted ATPases that may be involved in RNA modification, a family of predicted archaeal and bacterial rRNA methylases. Additionally, the PUA domain was detected in a family of eukaryotic proteins that also contain a domain homologous to the translation initiation factor eIF1/SUI1; these proteins may comprise a novel type of translation factors. Unexpectedly, the PUA domain was detected also in bacterial and yeast glutamate kinases; this is compatible with the demonstrated role of these enzymes in the regulation of the expression of other genes. It is predicted that the PUA domain is an RNA binding domain. Pssm-ID: 426278 [Multi-domain] Cd Length: 74 Bit Score: 74.06 E-value: 5.55e-18
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PUA | smart00359 | Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase; |
97-170 | 9.15e-11 | ||||
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase; Pssm-ID: 214635 [Multi-domain] Cd Length: 76 Bit Score: 55.34 E-value: 9.15e-11
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PUA_eIF2d-like | cd21156 | PUA RNA-binding domain of eukaryotic translation initiation factor 2D and similar proteins; ... |
89-171 | 1.05e-08 | ||||
PUA RNA-binding domain of eukaryotic translation initiation factor 2D and similar proteins; The RNA-binding PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in a number of proteins involved in RNA metabolism. Most members of this eukaryotic translation initiation factor 2D (eIF2d)-like family of eukaryotic proteins also contain a domain homologous to the translation initiation factor eIF1/SUI1, and a short uncharacterized N-terminal domain. eIF2D may function as a cytosolic GTP-independent initiation factor which delivers Met-tRNA (and non-initiating tRNAs) to the 40S ribosomal subunit. The family member from Drosophila melanogaster has been named ligatin, and this alias has been adopted for other family members as well, which are not homologous to the vertebrate ligatin (LGTN) that is a trafficking receptor for phosphoglycoproteins. Pssm-ID: 409298 [Multi-domain] Cd Length: 82 Bit Score: 49.87 E-value: 1.05e-08
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PRK13795 | PRK13795 | hypothetical protein; Provisional |
97-165 | 1.16e-04 | ||||
hypothetical protein; Provisional Pssm-ID: 237510 [Multi-domain] Cd Length: 636 Bit Score: 41.52 E-value: 1.16e-04
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eIF2D_N | cd11610 | N-terminal domain of eIF2D and related proteins; This N-terminal domain of eIF2D co-occurs ... |
16-80 | 2.16e-03 | ||||
N-terminal domain of eIF2D and related proteins; This N-terminal domain of eIF2D co-occurs with a PUA domain. eIF2D translation initiation factor (also known as ligatin) is involved in the recruitment and delivery of aminoacyl-tRNAs to the P-site of the eukaryotic ribosome in a GTP-independent manner. Pssm-ID: 211423 Cd Length: 76 Bit Score: 35.33 E-value: 2.16e-03
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PUA_archaeosine_TGT | cd21149 | PUA RNA-binding domain of archaeosine tRNA-guanine transglycosylase; The RNA-binding PUA ... |
97-165 | 4.54e-03 | ||||
PUA RNA-binding domain of archaeosine tRNA-guanine transglycosylase; The RNA-binding PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in a number of proteins involved in RNA metabolism. Members of this archaeosine tRNA-guanine transglycosylase (TGT) family are responsible for the exchange of a guanine residue in archaeal tRNAs with a preQ0 base (7-cyano-7-deazaguanine), which constitutes the initial step in archaeosine biosynthesis. Archaeosine is a modified RNA base specific to archaea (7-formamidino-7deazaguanosine), found at position 15 in tRNAs. It has been shown that the PUA domain of archaeosine TGT is not required for its specificity for position 15. Pssm-ID: 409291 [Multi-domain] Cd Length: 75 Bit Score: 34.51 E-value: 4.54e-03
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PUA_Cbf5 | cd21148 | PUA RNA-binding domain of the archaeal pseudouridine synthase component Cbf5; The RNA-binding ... |
108-162 | 4.73e-03 | ||||
PUA RNA-binding domain of the archaeal pseudouridine synthase component Cbf5; The RNA-binding PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in a number of proteins involved in RNA metabolism. Members of the archaeal and eukaryotic subfamily of pseudouridine synthases, including Cbf5 (dyskerin in humans) and similar proteins, are modules that assist in the binding and positioning (guide and/or substrate) of RNA to the pseudouridine synthase complex. Pseudouridine synthases are enzymes that are responsible for post-translational modifications of RNAs by specifically isomerizing uracil residues. In Pyrococcus furiosus H/ACA ribonucleoprotein (RNP) assembly with a single-hairpin H/ACA RNA, the lower stem and the ACA motif of the guide RNA are anchored at the PUA domain of Cbf5. In addition, the N-terminal extension of Cbf5, which is a hot spot for dyskeratosis congenita (a rare genetic form of bone marrow failure) mutation, forms an extra structural layer on the PUA domain. Pssm-ID: 409290 [Multi-domain] Cd Length: 75 Bit Score: 34.37 E-value: 4.73e-03
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PRK04270 | PRK04270 | RNA-guided pseudouridylation complex pseudouridine synthase subunit Cbf5; |
92-165 | 6.01e-03 | ||||
RNA-guided pseudouridylation complex pseudouridine synthase subunit Cbf5; Pssm-ID: 179806 [Multi-domain] Cd Length: 300 Bit Score: 36.37 E-value: 6.01e-03
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Blast search parameters | ||||
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