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Conserved domains on  [gi|281347500|gb|EFB23084|]
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hypothetical protein PANDA_009120, partial [Ailuropoda melanoleuca]

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 ...
 77-172 8.94e-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: 213.89  E-value: 8.94e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281347500  77 PTLRLLHKYPFILPHQQVDKGAIKFVLSGANIMCPGLTSPGAQLYPA-AVDTVVAIMAEGKQHALCVGVMRMSAEDIEKV 155
Cdd:cd21155    1 PTLRLLHKYPFMLPKVQVDKGAIKFVLSGANIMCPGLTSPGGKLPDDvEKGTVVAIMAEGKEHALAIGITKMSSEDIKKV 80

                         90
                 ....*....|....*..
gi 281347500 156 NKGIGIENIHYLNDGLW 172
Cdd:cd21155   81 NKGIGIENIHYLGDGLW 97
MCT1_N cd11609
N-terminal domain of multiple copies T cell malignancies 1 and related proteins; This ...
 1-77 4.69e-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: 138.05  E-value: 4.69e-43
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281347500   1 KFDEKENVSNCIQLKTSVIKGIKNQLIEQFPGIEPWLNQILPKKDPVKIVRCHEHIEILTVNGELLFFRQREGPFYP 77
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 ...
 77-172 8.94e-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: 213.89  E-value: 8.94e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281347500  77 PTLRLLHKYPFILPHQQVDKGAIKFVLSGANIMCPGLTSPGAQLYPA-AVDTVVAIMAEGKQHALCVGVMRMSAEDIEKV 155
Cdd:cd21155    1 PTLRLLHKYPFMLPKVQVDKGAIKFVLSGANIMCPGLTSPGGKLPDDvEKGTVVAIMAEGKEHALAIGITKMSSEDIKKV 80

                         90
                 ....*....|....*..
gi 281347500 156 NKGIGIENIHYLNDGLW 172
Cdd:cd21155   81 NKGIGIENIHYLGDGLW 97
MCT1_N cd11609
N-terminal domain of multiple copies T cell malignancies 1 and related proteins; This ...
 1-77 4.69e-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: 138.05  E-value: 4.69e-43
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281347500   1 KFDEKENVSNCIQLKTSVIKGIKNQLIEQFPGIEPWLNQILPKKDPVKIVRCHEHIEILTVNGELLFFRQREGPFYP 77
Cdd:cd11609    1 KFFEKEDVSGQTQLKSSVQRGIRAKLLEQYPLLEPYIDEILPKKEPLVLVKCHDHIELLVVNGEPLFFQHRDGPYIP 77
Pre-PUA pfam17832
Pre-PUA-like domain; This Pre-PUA-like domain is found in a wide variety of proteins including ...
 2-86 8.13e-34

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: 114.98  E-value: 8.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281347500    2 FDEKENVSNCIQLKTSVIKGIKNQLIEQFPGIEPWLNQILPKKDPVKIVRCH-EHIEILTVNGELLFFRQREGPFYPTLR 80
Cdd:pfam17832   1 FKKPFKVKSNTQLKSSDRRKLRAKLLEQFPSLEEQLDELLPKKEEVIVIKLHtEHVSLYSVDGEPLFFQVRDGPLYPTLY 80


                  ....*.
gi 281347500   81 LLHKYP 86
Cdd:pfam17832  81 LLWKYP 86
Tma20 COG2016
Predicted ribosome-associated RNA-binding protein Tma20, contains PUA domain [Translation, ...
 13-172 1.57e-32

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: 113.73  E-value: 1.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281347500  13 QLKTSVIKGIKNQLIEQFpGIEPwlnqilpKKDPVKIVRcHEHIEILTVNGELLFFRQREGPFyPTLRLLHKYPFILPHQ 92
Cdd:COG2016    7 HLSKKEIKELLEELEERL-GVDL-------SGDNVEVAE-TDDFEIYLVDGEPLLFKVDDEPF-PTLRGLLKYPPEKPVV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281347500  93 QVDKGAIKFVLSGANIMCPGLTS------PGaqlypaavdTVVAIMAEGKQHALCVGVMRMSAEDIEKVNKGIGIENIHY 166
Cdd:COG2016   77 TVDMGAVKFVSNGADVMRPGIVEadgeikEG---------DIVVIVEEKHGKPLAVGRALVDGEEMVEGKKGKAVKNLHH 147


                 ....*.
gi 281347500 167 LNDGLW 172
Cdd:COG2016  148 VGDKLW 153
PRK14560 PRK14560
putative RNA-binding protein; Provisional
 13-175 6.36e-29

putative RNA-binding protein; Provisional


Pssm-ID: 237757 [Multi-domain]  Cd Length: 160  Bit Score: 104.55  E-value: 6.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281347500  13 QLKTSVIKGIKNQLIEQFpGIEpwlnqiLPKKDPVKIVRCHEHIEILTVNGELLFFRQREGPFyPTLRLLHKYPFILPHQ 92
Cdd:PRK14560   8 HLSKKEVKEIKEELKEKF-GVD------IDGKDAVEEVETDKKEEIYLVDGEPLFFKVDDELF-PTLRGALKLKPEKRRV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281347500  93 QVDKGAIKFVLSGANIMCPGLTSpgaqlypaaVDT------VVAIMAEGKQHALCVGVMRMSAEDIEKVNKGIGIENIHY 166
Cdd:PRK14560  80 VVDAGAVKFVSNGADVMAPGIVE---------ADEdikegdIVFVVEETHGKPLAVGRALMDGDEMVEEKKGKAVKNIHH 150


                 ....*....
gi 281347500 167 LNDGLWHMK 175
Cdd:PRK14560 151 VGDEIWEFE 159
arCOG00985 TIGR03684
arCOG04150 universal archaeal PUA-domain protein; This universal archaeal protein contains a ...
 13-172 7.29e-29

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: 104.23  E-value: 7.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281347500   13 QLKTSVIKGIKNQLIEQFpgiepwlnQILPKKDPVKIVRCHEhIEILTVNGELLFFrQREGPFYPTLRLLHKYPFILPHQ 92
Cdd:TIGR03684   3 FLSKKEIKELLEELKEYY--------GIDIEKAKLEVAETDK-FEIYLVDGKPLLF-EVDGRLFPTLYGLLELNPDKNVV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281347500   93 QVDKGAIKFVLSGANIMCPGLTSpgaqlypaAVDTV-----VAIMAEGKQHALCVGVMRMSAEDIEKVNKGIGIENIHYL 167
Cdd:TIGR03684  73 VVDEGAVKFIINGADIMAPGIVE--------ADPSIkegdiVFVVDETHGKPLAVGIALMDAEEMVEEKKGKAVKNIHHV 144


                  ....*
gi 281347500  168 NDGLW 172
Cdd:TIGR03684 145 GDKIW 149
PUA pfam01472
PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, ...
 90-167 5.65e-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: 73.67  E-value: 5.65e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281347500   90 PHQQVDKGAIKFVLSGANIMCPGLTSPGAQLypaAVDTVVAIMAEgKQHALCVGVMRMSAEDIEKVNKGIGIENIHYL 167
Cdd:pfam01472   1 GRVVVDDGAVKAILNGASLLAPGVVRVDGDF---RKGDEVVVVTE-KGELVAVGLANYSSEELAKIEGGKAVKVRRVL 74
PUA smart00359
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
94-167 1.05e-10

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


Pssm-ID: 214635 [Multi-domain]  Cd Length: 76  Bit Score: 54.96  E-value: 1.05e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281347500    94 VDKGAIKFVLSGANIMCPGLTSPGAQLYPaavDTVVAIMAEgKQHALCVGVMRMSAEDIEKVN-KGIGIENIHYL 167
Cdd:smart00359   5 VDDGAEKAILNGASLLAPGVVRVDGDIKE---GDVVVIVDE-KGEPLGIGLANMSSEEIARIKgKGLAVKVRRAV 75
 
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 ...
 77-172 8.94e-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: 213.89  E-value: 8.94e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281347500  77 PTLRLLHKYPFILPHQQVDKGAIKFVLSGANIMCPGLTSPGAQLYPA-AVDTVVAIMAEGKQHALCVGVMRMSAEDIEKV 155
Cdd:cd21155    1 PTLRLLHKYPFMLPKVQVDKGAIKFVLSGANIMCPGLTSPGGKLPDDvEKGTVVAIMAEGKEHALAIGITKMSSEDIKKV 80

                         90
                 ....*....|....*..
gi 281347500 156 NKGIGIENIHYLNDGLW 172
Cdd:cd21155   81 NKGIGIENIHYLGDGLW 97
MCT1_N cd11609
N-terminal domain of multiple copies T cell malignancies 1 and related proteins; This ...
 1-77 4.69e-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: 138.05  E-value: 4.69e-43
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281347500   1 KFDEKENVSNCIQLKTSVIKGIKNQLIEQFPGIEPWLNQILPKKDPVKIVRCHEHIEILTVNGELLFFRQREGPFYP 77
Cdd:cd11609    1 KFFEKEDVSGQTQLKSSVQRGIRAKLLEQYPLLEPYIDEILPKKEPLVLVKCHDHIELLVVNGEPLFFQHRDGPYIP 77
Pre-PUA pfam17832
Pre-PUA-like domain; This Pre-PUA-like domain is found in a wide variety of proteins including ...
 2-86 8.13e-34

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: 114.98  E-value: 8.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281347500    2 FDEKENVSNCIQLKTSVIKGIKNQLIEQFPGIEPWLNQILPKKDPVKIVRCH-EHIEILTVNGELLFFRQREGPFYPTLR 80
Cdd:pfam17832   1 FKKPFKVKSNTQLKSSDRRKLRAKLLEQFPSLEEQLDELLPKKEEVIVIKLHtEHVSLYSVDGEPLFFQVRDGPLYPTLY 80


                  ....*.
gi 281347500   81 LLHKYP 86
Cdd:pfam17832  81 LLWKYP 86
Tma20 COG2016
Predicted ribosome-associated RNA-binding protein Tma20, contains PUA domain [Translation, ...
 13-172 1.57e-32

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: 113.73  E-value: 1.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281347500  13 QLKTSVIKGIKNQLIEQFpGIEPwlnqilpKKDPVKIVRcHEHIEILTVNGELLFFRQREGPFyPTLRLLHKYPFILPHQ 92
Cdd:COG2016    7 HLSKKEIKELLEELEERL-GVDL-------SGDNVEVAE-TDDFEIYLVDGEPLLFKVDDEPF-PTLRGLLKYPPEKPVV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281347500  93 QVDKGAIKFVLSGANIMCPGLTS------PGaqlypaavdTVVAIMAEGKQHALCVGVMRMSAEDIEKVNKGIGIENIHY 166
Cdd:COG2016   77 TVDMGAVKFVSNGADVMRPGIVEadgeikEG---------DIVVIVEEKHGKPLAVGRALVDGEEMVEGKKGKAVKNLHH 147


                 ....*.
gi 281347500 167 LNDGLW 172
Cdd:COG2016  148 VGDKLW 153
PRK14560 PRK14560
putative RNA-binding protein; Provisional
 13-175 6.36e-29

putative RNA-binding protein; Provisional


Pssm-ID: 237757 [Multi-domain]  Cd Length: 160  Bit Score: 104.55  E-value: 6.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281347500  13 QLKTSVIKGIKNQLIEQFpGIEpwlnqiLPKKDPVKIVRCHEHIEILTVNGELLFFRQREGPFyPTLRLLHKYPFILPHQ 92
Cdd:PRK14560   8 HLSKKEVKEIKEELKEKF-GVD------IDGKDAVEEVETDKKEEIYLVDGEPLFFKVDDELF-PTLRGALKLKPEKRRV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281347500  93 QVDKGAIKFVLSGANIMCPGLTSpgaqlypaaVDT------VVAIMAEGKQHALCVGVMRMSAEDIEKVNKGIGIENIHY 166
Cdd:PRK14560  80 VVDAGAVKFVSNGADVMAPGIVE---------ADEdikegdIVFVVEETHGKPLAVGRALMDGDEMVEEKKGKAVKNIHH 150


                 ....*....
gi 281347500 167 LNDGLWHMK 175
Cdd:PRK14560 151 VGDEIWEFE 159
arCOG00985 TIGR03684
arCOG04150 universal archaeal PUA-domain protein; This universal archaeal protein contains a ...
 13-172 7.29e-29

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: 104.23  E-value: 7.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281347500   13 QLKTSVIKGIKNQLIEQFpgiepwlnQILPKKDPVKIVRCHEhIEILTVNGELLFFrQREGPFYPTLRLLHKYPFILPHQ 92
Cdd:TIGR03684   3 FLSKKEIKELLEELKEYY--------GIDIEKAKLEVAETDK-FEIYLVDGKPLLF-EVDGRLFPTLYGLLELNPDKNVV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281347500   93 QVDKGAIKFVLSGANIMCPGLTSpgaqlypaAVDTV-----VAIMAEGKQHALCVGVMRMSAEDIEKVNKGIGIENIHYL 167
Cdd:TIGR03684  73 VVDEGAVKFIINGADIMAPGIVE--------ADPSIkegdiVFVVDETHGKPLAVGIALMDAEEMVEEKKGKAVKNIHHV 144


                  ....*
gi 281347500  168 NDGLW 172
Cdd:TIGR03684 145 GDKIW 149
eIF2D_N_like cd11580
N-terminal domain of eIF2D, malignant T cell-amplified sequence 1 and related proteins; This ...
 6-77 3.40e-28

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: 100.12  E-value: 3.40e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281347500   6 ENVSNCIQLKTSVIKGIKNQLIEQFPGIEPWLNQILPKKDPVKIVRCHEHIEILTVNGELLFFRQREGPFYP 77
Cdd:cd11580    1 EKLKNKTQLSKKDVKKLREQLIEQFPLLEEILDEIFPKKAPVKVQKFDTHYEIYTVDGEPVFFELDEGEVFP 72
unchar_dom_2 TIGR00451
uncharacterized domain 2; This uncharacterized domain is found a number of enzymes and ...
 61-169 1.06e-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: 99.82  E-value: 1.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281347500   61 VNGELLFFrQREGPFYPTLRLLHKYPFILPHQQVDKGAIKFVLSGANIMCPGLTSPGAQLypaAVDTVVAIMAEGKQHAL 140
Cdd:TIGR00451   3 VDGEPLYF-IYDDKVIPSLKGALKLMEDKKIVVVDNGAVKFLKNGADVMRPGIVDADEDI---KEGDDVVVVDENKDRPL 78

                          90       100
                  ....*....|....*....|....*....
gi 281347500  141 CVGVMRMSAEDIEKVNKGIGIENIHYLND 169
Cdd:TIGR00451  79 AVGIALMSGEEMKEMDKGKAVKNIHHIGD 107
PUA cd07953
PUA RNA binding domain; The PUA (PseudoUridine synthase and Archaeosine transglycosylase) ...
 90-166 5.18e-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: 79.26  E-value: 5.18e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281347500  90 PHQQVDKGAIKFVLSGANIMCPGLTSPgaqLYPAAVDTVVAIMAEGKqHALCVGVMRMSAEDIEKVNKGIGIENIHY 166
Cdd:cd07953    1 PVVVVDKGAEKAVLNGADLMAPGVVSA---DGDFKRGDLVRIVSEGG-RPLAIGVAEMSSDEMKEELKGIAVRVLHF 73
PUA_MJ1432-like cd21154
PUA RNA-binding domain of MJ1432, TA1423, PH0734, and similar proteins; The RNA-binding PUA ...
 89-174 6.54e-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: 76.39  E-value: 6.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281347500  89 LPHQQVDKGAIKFVLSGANIMCPGLTSpgaqlypaaVDT------VVAIMAEGKQHALCVGVMRMSAEDIEKVNKGIGIE 162
Cdd:cd21154    2 LPRVVVDMGAVKFVANGADVMRPGIVE---------ADEeikkgdIVVVVDERHGKPLAVGIALMSGEEMVEMKKGKAVK 72

                         90
                 ....*....|..
gi 281347500 163 NIHYLNDGLWHM 174
Cdd:cd21154   73 NLHYVGDKIWKL 84
PUA pfam01472
PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, ...
 90-167 5.65e-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: 73.67  E-value: 5.65e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281347500   90 PHQQVDKGAIKFVLSGANIMCPGLTSPGAQLypaAVDTVVAIMAEgKQHALCVGVMRMSAEDIEKVNKGIGIENIHYL 167
Cdd:pfam01472   1 GRVVVDDGAVKAILNGASLLAPGVVRVDGDF---RKGDEVVVVTE-KGELVAVGLANYSSEELAKIEGGKAVKVRRVL 74
PUA smart00359
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
94-167 1.05e-10

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


Pssm-ID: 214635 [Multi-domain]  Cd Length: 76  Bit Score: 54.96  E-value: 1.05e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281347500    94 VDKGAIKFVLSGANIMCPGLTSPGAQLYPaavDTVVAIMAEgKQHALCVGVMRMSAEDIEKVN-KGIGIENIHYL 167
Cdd:smart00359   5 VDDGAEKAILNGASLLAPGVVRVDGDIKE---GDVVVIVDE-KGEPLGIGLANMSSEEIARIKgKGLAVKVRRAV 75
PUA_eIF2d-like cd21156
PUA RNA-binding domain of eukaryotic translation initiation factor 2D and similar proteins; ...
 86-168 1.10e-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: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281347500  86 PFILPHQQVdkgaIKFVLSGANIMCPGLTSPGAQLYPAAVDTVVAIMAEGKQHALCVGVMRMSAEDIEKVN-KGIGIENI 164
Cdd:cd21156    3 PVFTTHPPV----SEKLLGGADLMLPGVIVPPPGLPPFEKGSLVAVAVLGNPAPVAVGRAAMSSEDMYASGmKGKGVEVL 78


                 ....
gi 281347500 165 HYLN 168
Cdd:cd21156   79 HTYG 82
PRK13795 PRK13795
hypothetical protein; Provisional
 94-162 3.12e-05

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 43.44  E-value: 3.12e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281347500  94 VDKGAIKFVLSGANIMCPGLTS--PGAQLYpaavDTVVAIMAEGKQHAlcVGVMRMSAEDIEKVNKGIGIE 162
Cdd:PRK13795 131 VDKGALEPIKNGKNVLAPGVVEadLDIKKG----DEVVVVTEDGEVVG--VGRAKMDGDDMIKRFRGRAVK 195
PUA_archaeosine_TGT cd21149
PUA RNA-binding domain of archaeosine tRNA-guanine transglycosylase; The RNA-binding PUA ...
 94-162 1.39e-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: 36.05  E-value: 1.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281347500  94 VDKGAIKFVLSGANIMCPGLTSPGAQLYPAavDTVVAIMAEGKqhALCVGVMRMSAEDIEKVNKGIGIE 162
Cdd:cd21149    7 VNKESAPFVRKGGSVFAKGVVDADENIRPG--DEVLVVDEDDR--LLAVGRAVLSGKEMKEFERGVAVK 71
eIF2D_N cd11610
N-terminal domain of eIF2D and related proteins; This N-terminal domain of eIF2D co-occurs ...
 13-77 1.84e-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: 35.71  E-value: 1.84e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281347500  13 QLKTSVIKGIKNQLIEQFPGI-EPWLNQILPKKDPVKIVRCHEHIEILTV---NGELLFFRQREGPFYP 77
Cdd:cd11610    8 ALKGSDRKKLRARVLKAFPLLtEEDLDELVPNKEELSVVKLVTHGERVTVysvDGVPLFFELSDGNLYP 76
 
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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