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Conserved domains on  [gi|344228142|gb|EGV60028|]
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hypothetical protein CANTEDRAFT_111749 [Yamadazyma tenuis ATCC 10573]

Protein Classification

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.

Gene Ontology:  GO:0003723|GO:0003743|GO:0001731
PubMed:  20713520

Graphical summary

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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 ...
 79-176 8.48e-67

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: 198.87  E-value: 8.48e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344228142  79 PHLRLVHQYPECFPRVQVDRGAIKFVLSGANIMCPGLTSAGGQLPEEnLDEGSIVTVYAEGKEHALAIGKLIMSVDDIKS 158
Cdd:cd21155    1 PTLRLLHKYPFMLPKVQVDKGAIKFVLSGANIMCPGLTSPGGKLPDD-VEKGTVVAIMAEGKEHALAIGITKMSSEDIKK 79

                         90
                 ....*....|....*...
gi 344228142 159 KNKGHGIELVHFLGDGLW 176
Cdd:cd21155   80 VNKGIGIENIHYLGDGLW 97
MCT1_N cd11609
N-terminal domain of multiple copies T cell malignancies 1 and related proteins; This ...
 3-79 1.31e-33

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: 114.17  E-value: 1.31e-33
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 344228142   3 KKFTKEDIHSRSNIKSSAQRGLKSNFVGQFEDLEPIIDTIIPKKSQVILIKCEDRIQLYSIDNEVVLFQHFDSNLMP 79
Cdd:cd11609    1 KFFEKEDVSGQTQLKSSVQRGIRAKLLEQYPLLEPYIDEILPKKEPLVLVKCHDHIELLVVNGEPLFFQHRDGPYIP 77
 
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 ...
 79-176 8.48e-67

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: 198.87  E-value: 8.48e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344228142  79 PHLRLVHQYPECFPRVQVDRGAIKFVLSGANIMCPGLTSAGGQLPEEnLDEGSIVTVYAEGKEHALAIGKLIMSVDDIKS 158
Cdd:cd21155    1 PTLRLLHKYPFMLPKVQVDKGAIKFVLSGANIMCPGLTSPGGKLPDD-VEKGTVVAIMAEGKEHALAIGITKMSSEDIKK 79

                         90
                 ....*....|....*...
gi 344228142 159 KNKGHGIELVHFLGDGLW 176
Cdd:cd21155   80 VNKGIGIENIHYLGDGLW 97
unchar_dom_2 TIGR00451
uncharacterized domain 2; This uncharacterized domain is found a number of enzymes and ...
 61-173 3.94e-35

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: 119.08  E-value: 3.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344228142   61 YSIDNEVVLFQHFDsNLMPHLRLVHQYPECFPRVQVDRGAIKFVLSGANIMCPGLTSAGgqlpeENLDEGSIVTVYAEGK 140
Cdd:TIGR00451   1 ILVDGEPLYFIYDD-KVIPSLKGALKLMEDKKIVVVDNGAVKFLKNGADVMRPGIVDAD-----EDIKEGDDVVVVDENK 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 344228142  141 EHALAIGKLIMSVDDIKSKNKGHGIELVHFLGD 173
Cdd:TIGR00451  75 DRPLAVGIALMSGEEMKEMDKGKAVKNIHHIGD 107
MCT1_N cd11609
N-terminal domain of multiple copies T cell malignancies 1 and related proteins; This ...
 3-79 1.31e-33

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: 114.17  E-value: 1.31e-33
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 344228142   3 KKFTKEDIHSRSNIKSSAQRGLKSNFVGQFEDLEPIIDTIIPKKSQVILIKCEDRIQLYSIDNEVVLFQHFDSNLMP 79
Cdd:cd11609    1 KFFEKEDVSGQTQLKSSVQRGIRAKLLEQYPLLEPYIDEILPKKEPLVLVKCHDHIELLVVNGEPLFFQHRDGPYIP 77
Tma20 COG2016
Predicted ribosome-associated RNA-binding protein Tma20, contains PUA domain [Translation, ...
 55-177 4.27e-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: 110.26  E-value: 4.27e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344228142  55 EDRIQLYSIDNEVVLFQhFDSNLMPHLRLVHQYPECFPRVQVDRGAIKFVLSGANIMCPGLTSAggqlpEENLDEGSIVT 134
Cdd:COG2016   38 TDDFEIYLVDGEPLLFK-VDDEPFPTLRGLLKYPPEKPVVTVDMGAVKFVSNGADVMRPGIVEA-----DGEIKEGDIVV 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 344228142 135 VYAEGKEHALAIGKLIMSVDDIKSKNKGHGIELVHFLGDGLWN 177
Cdd:COG2016  112 IVEEKHGKPLAVGRALVDGEEMVEGKKGKAVKNLHHVGDKLWE 154
Pre-PUA pfam17832
Pre-PUA-like domain; This Pre-PUA-like domain is found in a wide variety of proteins including ...
 2-88 4.47e-30

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: 105.35  E-value: 4.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344228142    2 FKKftKEDIHSRSNIKSSAQRGLKSNFVGQFEDLEPIIDTIIPKKSQVILIKCE-DRIQLYSIDNEVVLFQHFDSNLMPH 80
Cdd:pfam17832   1 FKK--PFKVKSNTQLKSSDRRKLRAKLLEQFPSLEEQLDELLPKKEEVIVIKLHtEHVSLYSVDGEPLFFQVRDGPLYPT 78


                  ....*...
gi 344228142   81 LRLVHQYP 88
Cdd:pfam17832  79 LYLLWKYP 86
PRK14560 PRK14560
putative RNA-binding protein; Provisional
 32-178 5.58e-29

putative RNA-binding protein; Provisional


Pssm-ID: 237757 [Multi-domain]  Cd Length: 160  Bit Score: 104.93  E-value: 5.58e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344228142  32 FEDLEPIIDTIIPKKSQVILIKCEDRIQLYSIDNEVVLFQhFDSNLMPHLRLVHQYPECFPRVQVDRGAIKFVLSGANIM 111
Cdd:PRK14560  18 KEELKEKFGVDIDGKDAVEEVETDKKEEIYLVDGEPLFFK-VDDELFPTLRGALKLKPEKRRVVVDAGAVKFVSNGADVM 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 344228142 112 CPGLTSAggqlpEENLDEGSIVTVYAEGKEHALAIGKLIMSVDDIKSKNKGHGIELVHFLGDGLWNM 178
Cdd:PRK14560  97 APGIVEA-----DEDIKEGDIVFVVEETHGKPLAVGRALMDGDEMVEEKKGKAVKNIHHVGDEIWEF 158
PUA pfam01472
PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, ...
 92-171 8.24e-17

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: 70.98  E-value: 8.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344228142   92 PRVQVDRGAIKFVLSGANIMCPGLTSAggqlpEENLDEGSIVTVYAEgKEHALAIGKLIMSVDDIKSKNKGHGIELVHFL 171
Cdd:pfam01472   1 GRVVVDDGAVKAILNGASLLAPGVVRV-----DGDFRKGDEVVVVTE-KGELVAVGLANYSSEELAKIEGGKAVKVRRVL 74
PUA smart00359
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
92-172 3.82e-11

Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;


Pssm-ID: 214635 [Multi-domain]  Cd Length: 76  Bit Score: 56.11  E-value: 3.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344228142    92 PRVQVDRGAIKFVLSGANIMCPGLTSAggqlpEENLDEGSIVTVYAEgKEHALAIGKLIMSVDDIKS-KNKGHGIELVHF 170
Cdd:smart00359   1 GKVVVDDGAEKAILNGASLLAPGVVRV-----DGDIKEGDVVVIVDE-KGEPLGIGLANMSSEEIARiKGKGLAVKVRRA 74


                   ..
gi 344228142   171 LG 172
Cdd:smart00359  75 VM 76
 
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 ...
 79-176 8.48e-67

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: 198.87  E-value: 8.48e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344228142  79 PHLRLVHQYPECFPRVQVDRGAIKFVLSGANIMCPGLTSAGGQLPEEnLDEGSIVTVYAEGKEHALAIGKLIMSVDDIKS 158
Cdd:cd21155    1 PTLRLLHKYPFMLPKVQVDKGAIKFVLSGANIMCPGLTSPGGKLPDD-VEKGTVVAIMAEGKEHALAIGITKMSSEDIKK 79

                         90
                 ....*....|....*...
gi 344228142 159 KNKGHGIELVHFLGDGLW 176
Cdd:cd21155   80 VNKGIGIENIHYLGDGLW 97
unchar_dom_2 TIGR00451
uncharacterized domain 2; This uncharacterized domain is found a number of enzymes and ...
 61-173 3.94e-35

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: 119.08  E-value: 3.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344228142   61 YSIDNEVVLFQHFDsNLMPHLRLVHQYPECFPRVQVDRGAIKFVLSGANIMCPGLTSAGgqlpeENLDEGSIVTVYAEGK 140
Cdd:TIGR00451   1 ILVDGEPLYFIYDD-KVIPSLKGALKLMEDKKIVVVDNGAVKFLKNGADVMRPGIVDAD-----EDIKEGDDVVVVDENK 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 344228142  141 EHALAIGKLIMSVDDIKSKNKGHGIELVHFLGD 173
Cdd:TIGR00451  75 DRPLAVGIALMSGEEMKEMDKGKAVKNIHHIGD 107
MCT1_N cd11609
N-terminal domain of multiple copies T cell malignancies 1 and related proteins; This ...
 3-79 1.31e-33

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: 114.17  E-value: 1.31e-33
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 344228142   3 KKFTKEDIHSRSNIKSSAQRGLKSNFVGQFEDLEPIIDTIIPKKSQVILIKCEDRIQLYSIDNEVVLFQHFDSNLMP 79
Cdd:cd11609    1 KFFEKEDVSGQTQLKSSVQRGIRAKLLEQYPLLEPYIDEILPKKEPLVLVKCHDHIELLVVNGEPLFFQHRDGPYIP 77
Tma20 COG2016
Predicted ribosome-associated RNA-binding protein Tma20, contains PUA domain [Translation, ...
 55-177 4.27e-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: 110.26  E-value: 4.27e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344228142  55 EDRIQLYSIDNEVVLFQhFDSNLMPHLRLVHQYPECFPRVQVDRGAIKFVLSGANIMCPGLTSAggqlpEENLDEGSIVT 134
Cdd:COG2016   38 TDDFEIYLVDGEPLLFK-VDDEPFPTLRGLLKYPPEKPVVTVDMGAVKFVSNGADVMRPGIVEA-----DGEIKEGDIVV 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 344228142 135 VYAEGKEHALAIGKLIMSVDDIKSKNKGHGIELVHFLGDGLWN 177
Cdd:COG2016  112 IVEEKHGKPLAVGRALVDGEEMVEGKKGKAVKNLHHVGDKLWE 154
Pre-PUA pfam17832
Pre-PUA-like domain; This Pre-PUA-like domain is found in a wide variety of proteins including ...
 2-88 4.47e-30

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: 105.35  E-value: 4.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344228142    2 FKKftKEDIHSRSNIKSSAQRGLKSNFVGQFEDLEPIIDTIIPKKSQVILIKCE-DRIQLYSIDNEVVLFQHFDSNLMPH 80
Cdd:pfam17832   1 FKK--PFKVKSNTQLKSSDRRKLRAKLLEQFPSLEEQLDELLPKKEEVIVIKLHtEHVSLYSVDGEPLFFQVRDGPLYPT 78


                  ....*...
gi 344228142   81 LRLVHQYP 88
Cdd:pfam17832  79 LYLLWKYP 86
PRK14560 PRK14560
putative RNA-binding protein; Provisional
 32-178 5.58e-29

putative RNA-binding protein; Provisional


Pssm-ID: 237757 [Multi-domain]  Cd Length: 160  Bit Score: 104.93  E-value: 5.58e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344228142  32 FEDLEPIIDTIIPKKSQVILIKCEDRIQLYSIDNEVVLFQhFDSNLMPHLRLVHQYPECFPRVQVDRGAIKFVLSGANIM 111
Cdd:PRK14560  18 KEELKEKFGVDIDGKDAVEEVETDKKEEIYLVDGEPLFFK-VDDELFPTLRGALKLKPEKRRVVVDAGAVKFVSNGADVM 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 344228142 112 CPGLTSAggqlpEENLDEGSIVTVYAEGKEHALAIGKLIMSVDDIKSKNKGHGIELVHFLGDGLWNM 178
Cdd:PRK14560  97 APGIVEA-----DEDIKEGDIVFVVEETHGKPLAVGRALMDGDEMVEEKKGKAVKNIHHVGDEIWEF 158
PUA_MJ1432-like cd21154
PUA RNA-binding domain of MJ1432, TA1423, PH0734, and similar proteins; The RNA-binding PUA ...
 91-178 1.11e-23

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: 88.72  E-value: 1.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344228142  91 FPRVQVDRGAIKFVLSGANIMCPGLTSAggqlpEENLDEGSIVTVYAEGKEHALAIGKLIMSVDDIKSKNKGHGIELVHF 170
Cdd:cd21154    2 LPRVVVDMGAVKFVANGADVMRPGIVEA-----DEEIKKGDIVVVVDERHGKPLAVGIALMSGEEMVEMKKGKAVKNLHY 76


                 ....*...
gi 344228142 171 LGDGLWNM 178
Cdd:cd21154   77 VGDKIWKL 84
PUA cd07953
PUA RNA binding domain; The PUA (PseudoUridine synthase and Archaeosine transglycosylase) ...
 92-170 1.46e-18

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: 75.41  E-value: 1.46e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 344228142  92 PRVQVDRGAIKFVLSGANIMCPGLTSaggqlPEENLDEGSIVTVYAEGKeHALAIGKLIMSVDDIKSKNKGHGIELVHF 170
Cdd:cd07953    1 PVVVVDKGAEKAVLNGADLMAPGVVS-----ADGDFKRGDLVRIVSEGG-RPLAIGVAEMSSDEMKEELKGIAVRVLHF 73
PUA pfam01472
PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, ...
 92-171 8.24e-17

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: 70.98  E-value: 8.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344228142   92 PRVQVDRGAIKFVLSGANIMCPGLTSAggqlpEENLDEGSIVTVYAEgKEHALAIGKLIMSVDDIKSKNKGHGIELVHFL 171
Cdd:pfam01472   1 GRVVVDDGAVKAILNGASLLAPGVVRV-----DGDFRKGDEVVVVTE-KGELVAVGLANYSSEELAKIEGGKAVKVRRVL 74
PUA smart00359
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
92-172 3.82e-11

Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;


Pssm-ID: 214635 [Multi-domain]  Cd Length: 76  Bit Score: 56.11  E-value: 3.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344228142    92 PRVQVDRGAIKFVLSGANIMCPGLTSAggqlpEENLDEGSIVTVYAEgKEHALAIGKLIMSVDDIKS-KNKGHGIELVHF 170
Cdd:smart00359   1 GKVVVDDGAEKAILNGASLLAPGVVRV-----DGDIKEGDVVVIVDE-KGEPLGIGLANMSSEEIARiKGKGLAVKVRRA 74


                   ..
gi 344228142   171 LG 172
Cdd:smart00359  75 VM 76
eIF2D_N_like cd11580
N-terminal domain of eIF2D, malignant T cell-amplified sequence 1 and related proteins; This ...
 8-70 4.37e-09

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: 50.82  E-value: 4.37e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 344228142   8 EDIHSRSNIKSSAQRGLKSNFVGQFEDLEPIIDTIIPKKSQVILIKCEDRIQLYSIDNEVVLF 70
Cdd:cd11580    1 EKLKNKTQLSKKDVKKLREQLIEQFPLLEEILDEIFPKKAPVKVQKFDTHYEIYTVDGEPVFF 63
PUA_eIF2d-like cd21156
PUA RNA-binding domain of eukaryotic translation initiation factor 2D and similar proteins; ...
 99-172 3.20e-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: 48.72  E-value: 3.20e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 344228142  99 GAIKFVLSGANIMCPGLTSAGGQLPEenLDEGSIVTVYAEGKEHALAIGKLIMSVDDIKSKN-KGHGIELVHFLG 172
Cdd:cd21156   10 PVSEKLLGGADLMLPGVIVPPPGLPP--FEKGSLVAVAVLGNPAPVAVGRAAMSSEDMYASGmKGKGVEVLHTYG 82
eIF2D_N cd11610
N-terminal domain of eIF2D and related proteins; This N-terminal domain of eIF2D co-occurs ...
 12-79 1.64e-07

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: 46.50  E-value: 1.64e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 344228142  12 SRSNIKSSAQRGLKSNFVGQFEDL-EPIIDTIIPKKSQVILIK---CEDRIQLYSIDNEVVLFQHFDSNLMP 79
Cdd:cd11610    5 SNTALKGSDRKKLRARVLKAFPLLtEEDLDELVPNKEELSVVKlvtHGERVTVYSVDGVPLFFELSDGNLYP 76
PRK13795 PRK13795
hypothetical protein; Provisional
 94-169 6.98e-07

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 48.07  E-value: 6.98e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 344228142  94 VQVDRGAIKFVLSGANIMCPGLTSAggQLPEENLDEGSIVTvyAEGKEHALAIGKliMSVDDIKSKNKGHGIELVH 169
Cdd:PRK13795 129 VIVDKGALEPIKNGKNVLAPGVVEA--DLDIKKGDEVVVVT--EDGEVVGVGRAK--MDGDDMIKRFRGRAVKVRK 198
PUA_archaeosine_TGT cd21149
PUA RNA-binding domain of archaeosine tRNA-guanine transglycosylase; The RNA-binding PUA ...
 93-170 3.69e-05

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: 40.29  E-value: 3.69e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 344228142  93 RVQVDRGAIKFVLSGANIMCPGLTSAGgqlpeENLDEGSIVTVYAEGKEhALAIGKLIMSVDDIKSKNKGHGIELVHF 170
Cdd:cd21149    4 RVVVNKESAPFVRKGGSVFAKGVVDAD-----ENIRPGDEVLVVDEDDR-LLAVGRAVLSGKEMKEFERGVAVKVRHG 75
PUA_Cbf5 cd21148
PUA RNA-binding domain of the archaeal pseudouridine synthase component Cbf5; The RNA-binding ...
 91-162 1.66e-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: 35.52  E-value: 1.66e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 344228142  91 FPRVQVDRGAIKFVLSGANIMCPGLTSAggqlpEENLDEGSIVTVYAEGKEhALAIGKLIMSVDDIKSKNKG 162
Cdd:cd21148    2 LPRIVIKDSAVNAICYGAKLAIPGVLRY-----EDGIEKGDEVVIMTTKGE-AVALGIALMTTAEIATCDHG 67
 
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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