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Conserved domains on  [gi|6322843|ref|NP_012916|]
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Mrt4p [Saccharomyces cerevisiae S288C]

Protein Classification

mRNA turnover 4 family protein( domain architecture ID 10146578)

mRNA turnover 4 (MRT4) family protein is a component of the ribosome assembly machinery

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ribosomal_P0_like cd05796
Ribosomal protein L10 family, P0-like protein subfamily; composed of uncharacterized ...
 21-196 6.57e-79

Ribosomal protein L10 family, P0-like protein subfamily; composed of uncharacterized eukaryotic proteins with similarity to the 60S ribosomal protein P0, including the Saccharomyces cerevisiae protein called mRNA turnover protein 4 (MRT4). MRT4 may be involved in mRNA decay. P0 forms a tight complex with multiple copies of the small acidic protein L12(e). This complex forms a stalk structure on the large subunit of the ribosome. It occupies the L7/L12 stalk of the ribosome. The stalk is known to contain the binding site for elongation factors EF-G and EF-Tu; however, there is disagreement as to whether or not P0 is involved in forming the binding site. The stalk is believed to be associated with GTPase activities in protein synthesis. In a neuroblastoma cell line, P0 has been shown to interact with the SH3 domain of Src and to activate the binding of the Nck1 adaptor protein with skeletal proteins such as the Wiskott-Aldrich Syndrome Protein (WASP) and the WASP-interacting protein (WIP). Some eukaryotic P0 sequences have an additional C-terminal domain homologous with acidic proteins P1 and P2.


:

Pssm-ID: 240222 [Multi-domain]  Cd Length: 163  Bit Score: 234.39  E-value: 6.57e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322843   21 ENKERIFDEVREALDTYRYVWVLHLDDVRTPVLQEIRTSWAGSKLIMGKRKVLQKALGEKREEEYKENLYQLSKLCSGVT 100
Cdd:cd05796   1 ELKQKLVENIREAVDKYKYIYVFSVDNMRNNKLKDIRQEWKDSRFFFGKNKVMQVALGRTPEDEYKPNLHKLSKYLKGQV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322843  101 GLLFTDEDVNTVKEYFKSYVRSDYSRPNTKAPLTFTIPEGivysrggqipaeEDVPMIHSLEPTMRnKFEIPTKIKAGKI 180
Cdd:cd05796  81 GLLFTNEPPEEVIEYFDSYSEPDFARAGSIATETVTLPEG------------PLEQFPHSMEPQLR-KLGLPTKLKKGVI 147

                       170
                ....*....|....*.
gi 6322843  181 TIDSPYLVCTEGEKLD 196
Cdd:cd05796 148 TLEADYVVCEEGKVLT 163
 
Name Accession Description Interval E-value
Ribosomal_P0_like cd05796
Ribosomal protein L10 family, P0-like protein subfamily; composed of uncharacterized ...
 21-196 6.57e-79

Ribosomal protein L10 family, P0-like protein subfamily; composed of uncharacterized eukaryotic proteins with similarity to the 60S ribosomal protein P0, including the Saccharomyces cerevisiae protein called mRNA turnover protein 4 (MRT4). MRT4 may be involved in mRNA decay. P0 forms a tight complex with multiple copies of the small acidic protein L12(e). This complex forms a stalk structure on the large subunit of the ribosome. It occupies the L7/L12 stalk of the ribosome. The stalk is known to contain the binding site for elongation factors EF-G and EF-Tu; however, there is disagreement as to whether or not P0 is involved in forming the binding site. The stalk is believed to be associated with GTPase activities in protein synthesis. In a neuroblastoma cell line, P0 has been shown to interact with the SH3 domain of Src and to activate the binding of the Nck1 adaptor protein with skeletal proteins such as the Wiskott-Aldrich Syndrome Protein (WASP) and the WASP-interacting protein (WIP). Some eukaryotic P0 sequences have an additional C-terminal domain homologous with acidic proteins P1 and P2.


Pssm-ID: 240222 [Multi-domain]  Cd Length: 163  Bit Score: 234.39  E-value: 6.57e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322843   21 ENKERIFDEVREALDTYRYVWVLHLDDVRTPVLQEIRTSWAGSKLIMGKRKVLQKALGEKREEEYKENLYQLSKLCSGVT 100
Cdd:cd05796   1 ELKQKLVENIREAVDKYKYIYVFSVDNMRNNKLKDIRQEWKDSRFFFGKNKVMQVALGRTPEDEYKPNLHKLSKYLKGQV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322843  101 GLLFTDEDVNTVKEYFKSYVRSDYSRPNTKAPLTFTIPEGivysrggqipaeEDVPMIHSLEPTMRnKFEIPTKIKAGKI 180
Cdd:cd05796  81 GLLFTNEPPEEVIEYFDSYSEPDFARAGSIATETVTLPEG------------PLEQFPHSMEPQLR-KLGLPTKLKKGVI 147

                       170
                ....*....|....*.
gi 6322843  181 TIDSPYLVCTEGEKLD 196
Cdd:cd05796 148 TLEADYVVCEEGKVLT 163
PTZ00135 PTZ00135
60S acidic ribosomal protein P0; Provisional
 12-225 1.97e-23

60S acidic ribosomal protein P0; Provisional


Pssm-ID: 240285 [Multi-domain]  Cd Length: 310  Bit Score: 95.85  E-value: 1.97e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322843    12 LAQTDKKGRenKERIFDEVREALDTYRYVWVLHLDDVRTPVLQEIRTSWAG-SKLIMGKRKVLQKALgeKREEEYKENLY 90
Cdd:PTZ00135   1 MAKPEKKAK--KKAYFEKLYELLEKYKKILIVSVDNVGSKQMQDIRRSLRGkAELLMGKNTLIRKAL--KQRLEELPELE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322843    91 QLSKLCSGVTGLLFTDEDVNTVKEYFKSYVRSDYSRPNTKAPLTFTIPegivysrggqipaeedvPMIHSLEPTMRNKFE 170
Cdd:PTZ00135  77 KLLPHVKGNVGFVFTKDDLFEVKPVILENKVPAPARAGVIAPIDVVIP-----------------AGPTGMDPSQTSFFQ 139

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6322843   171 ---IPTKIKAGKITIDSPYLVCTEGEKLDVRQALILKQFGIAASEFKVKVSAYYDNDS 225
Cdd:PTZ00135 140 algIATKIVKGQIEITNEVHLIKEGQKVGASQAVLLQKLNIKPFSYGLEVLSIYDNGS 197
Ribosomal_L10 pfam00466
Ribosomal protein L10;
18-119 1.13e-19

Ribosomal protein L10;


Pssm-ID: 459822 [Multi-domain]  Cd Length: 99  Bit Score: 80.66  E-value: 1.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322843     18 KGRENKERIFDEVREALDTYRYVWVLHLDDVRTPVLQEIRTSW--AGSKLIMGKRKVLQKALGEKREEEykenlyqLSKL 95
Cdd:pfam00466   1 KTREKKEELVEELKELLKEYKSVVVVDYRGLTVAQLTELRKKLreNGAELKVGKNTLMRRALEETGEEK-------LEDY 73

                          90       100
                  ....*....|....*....|....
gi 6322843     96 CSGVTGLLFTDEDVNTVKEYFKSY 119
Cdd:pfam00466  74 LKGPTALLFTNEDPVAVAKVLEDF 97
 
Name Accession Description Interval E-value
Ribosomal_P0_like cd05796
Ribosomal protein L10 family, P0-like protein subfamily; composed of uncharacterized ...
 21-196 6.57e-79

Ribosomal protein L10 family, P0-like protein subfamily; composed of uncharacterized eukaryotic proteins with similarity to the 60S ribosomal protein P0, including the Saccharomyces cerevisiae protein called mRNA turnover protein 4 (MRT4). MRT4 may be involved in mRNA decay. P0 forms a tight complex with multiple copies of the small acidic protein L12(e). This complex forms a stalk structure on the large subunit of the ribosome. It occupies the L7/L12 stalk of the ribosome. The stalk is known to contain the binding site for elongation factors EF-G and EF-Tu; however, there is disagreement as to whether or not P0 is involved in forming the binding site. The stalk is believed to be associated with GTPase activities in protein synthesis. In a neuroblastoma cell line, P0 has been shown to interact with the SH3 domain of Src and to activate the binding of the Nck1 adaptor protein with skeletal proteins such as the Wiskott-Aldrich Syndrome Protein (WASP) and the WASP-interacting protein (WIP). Some eukaryotic P0 sequences have an additional C-terminal domain homologous with acidic proteins P1 and P2.


Pssm-ID: 240222 [Multi-domain]  Cd Length: 163  Bit Score: 234.39  E-value: 6.57e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322843   21 ENKERIFDEVREALDTYRYVWVLHLDDVRTPVLQEIRTSWAGSKLIMGKRKVLQKALGEKREEEYKENLYQLSKLCSGVT 100
Cdd:cd05796   1 ELKQKLVENIREAVDKYKYIYVFSVDNMRNNKLKDIRQEWKDSRFFFGKNKVMQVALGRTPEDEYKPNLHKLSKYLKGQV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322843  101 GLLFTDEDVNTVKEYFKSYVRSDYSRPNTKAPLTFTIPEGivysrggqipaeEDVPMIHSLEPTMRnKFEIPTKIKAGKI 180
Cdd:cd05796  81 GLLFTNEPPEEVIEYFDSYSEPDFARAGSIATETVTLPEG------------PLEQFPHSMEPQLR-KLGLPTKLKKGVI 147

                       170
                ....*....|....*.
gi 6322843  181 TIDSPYLVCTEGEKLD 196
Cdd:cd05796 148 TLEADYVVCEEGKVLT 163
Ribosomal_P0_L10e cd05795
Ribosomal protein L10 family, P0 and L10e subfamily; composed of eukaryotic 60S ribosomal ...
 21-208 1.00e-27

Ribosomal protein L10 family, P0 and L10e subfamily; composed of eukaryotic 60S ribosomal protein P0 and the archaeal P0 homolog, L10e. P0 or L10e forms a tight complex with multiple copies of the small acidic protein L12(e). This complex forms a stalk structure on the large subunit of the ribosome. The stalk is known to contain the binding site for elongation factors G and Tu (EF-G and EF-Tu, respectively); however, there is disagreement as to whether or not L10 is involved in forming the binding site. The stalk is believed to be associated with GTPase activities in protein synthesis. In a neuroblastoma cell line, L10 has been shown to interact with the SH3 domain of Src and to activate the binding of the Nck1 adaptor protein with skeletal proteins such as the Wiskott-Aldrich Syndrome Protein (WASP) and the WASP-interacting protein (WIP). These eukaryotic and archaeal P0 sequences have an additional C-terminal domain homologous with acidic proteins P1 and P2.


Pssm-ID: 240221 [Multi-domain]  Cd Length: 175  Bit Score: 103.81  E-value: 1.00e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322843   21 ENKERIFDEVREALDTYRYVWVLHLDDVRTPVLQEIRTSWAG-SKLIMGK----RKVLQKALGEKREEEYkenlyqLSKL 95
Cdd:cd05795   1 EWKKEYVEKLTELLKSYPKVLIVDADNVGSKQLQKIRRSLRGkAEILMGKntliRRALRNLGDENPELEK------LLPY 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322843   96 CSGVTGLLFTDEDVNTVKEYFKSYVRSDYSRPNTKAPLTFTIPEGIVysrggqipaeedvpmihSLEPTMRNKFE---IP 172
Cdd:cd05795  75 LKGNVGFIFTNGDPFEIRKILEENKVPAPAKPGAIAPCDVVVPAGPT-----------------GMPPGPTSFFQalgIP 137

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 6322843  173 TKIKAGKITIDSPYLVCTEGEKLDVRQALILKQFGI 208
Cdd:cd05795 138 TKIEKGKIEIISDVVVVKKGEKVGASEATLLNKLNI 173
Ribosomal_L10_P0 cd00379
Ribosomal protein L10 family; composed of the large subunit ribosomal protein called L10 in ...
 21-182 1.24e-23

Ribosomal protein L10 family; composed of the large subunit ribosomal protein called L10 in bacteria, P0 in eukaryotes, and L10e in archaea, as well as uncharacterized P0-like eukaryotic proteins. In all three kingdoms, L10 forms a tight complex with multiple copies of the small acidic protein L12(e). This complex forms a stalk structure on the large subunit of the ribosome. The N-terminal domain (NTD) of L10 interacts with L11 protein and forms the base of the L7/L12 stalk, while the extended C-terminal helix binds to two or three dimers of the NTD of L7/L12 (L7 and L12 are identical except for an acetylated N-terminus). The L7/L12 stalk is known to contain the binding site for elongation factors G and Tu (EF-G and EF-Tu, respectively); however, there is disagreement as to whether or not L10 is involved in forming the binding site. The stalk is believed to be associated with GTPase activities in protein synthesis. In a neuroblastoma cell line, L10 has been shown to interact with the SH3 domain of Src and to activate the binding of the Nck1 adaptor protein with skeletal proteins such as the Wiskott-Aldrich Syndrome Protein (WASP) and the WASP-interacting protein (WIP). Some eukaryotic P0 sequences have an additional C-terminal domain homologous with acidic proteins P1 and P2.


Pssm-ID: 238222 [Multi-domain]  Cd Length: 155  Bit Score: 92.63  E-value: 1.24e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322843   21 ENKERIFDEVREALDTYRYVWVLHLDDVRTPVLQEIRTSW--AGSKLIMGKRKVLQKALGEKREEEYKENLyqlsklcSG 98
Cdd:cd00379   1 EKKEELVEELKELLKKYKSVVVVDYRGLTVAQLTELRKELreSGAKLKVGKNTLMRRALKGTGFEELKPLL-------KG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322843   99 VTGLLFTDEDVNTVKEYFKsyvrsDYSRPNTKAPLtftipegivysRGGQIpaEEDV-----PMIHSLEPTMRNKfeIPT 173
Cdd:cd00379  74 PTALAFTNEDPVEVAKVLK-----DFAKENKKLFA-----------KGGVV--AGKVldpagVTALAKLPSREEL--LAM 133


                ....*....
gi 6322843  174 KIKAGKITI 182
Cdd:cd00379 134 LIGLLKAPI 142
PTZ00135 PTZ00135
60S acidic ribosomal protein P0; Provisional
 12-225 1.97e-23

60S acidic ribosomal protein P0; Provisional


Pssm-ID: 240285 [Multi-domain]  Cd Length: 310  Bit Score: 95.85  E-value: 1.97e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322843    12 LAQTDKKGRenKERIFDEVREALDTYRYVWVLHLDDVRTPVLQEIRTSWAG-SKLIMGKRKVLQKALgeKREEEYKENLY 90
Cdd:PTZ00135   1 MAKPEKKAK--KKAYFEKLYELLEKYKKILIVSVDNVGSKQMQDIRRSLRGkAELLMGKNTLIRKAL--KQRLEELPELE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322843    91 QLSKLCSGVTGLLFTDEDVNTVKEYFKSYVRSDYSRPNTKAPLTFTIPegivysrggqipaeedvPMIHSLEPTMRNKFE 170
Cdd:PTZ00135  77 KLLPHVKGNVGFVFTKDDLFEVKPVILENKVPAPARAGVIAPIDVVIP-----------------AGPTGMDPSQTSFFQ 139

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6322843   171 ---IPTKIKAGKITIDSPYLVCTEGEKLDVRQALILKQFGIAASEFKVKVSAYYDNDS 225
Cdd:PTZ00135 140 algIATKIVKGQIEITNEVHLIKEGQKVGASQAVLLQKLNIKPFSYGLEVLSIYDNGS 197
Ribosomal_L10 pfam00466
Ribosomal protein L10;
18-119 1.13e-19

Ribosomal protein L10;


Pssm-ID: 459822 [Multi-domain]  Cd Length: 99  Bit Score: 80.66  E-value: 1.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322843     18 KGRENKERIFDEVREALDTYRYVWVLHLDDVRTPVLQEIRTSW--AGSKLIMGKRKVLQKALGEKREEEykenlyqLSKL 95
Cdd:pfam00466   1 KTREKKEELVEELKELLKEYKSVVVVDYRGLTVAQLTELRKKLreNGAELKVGKNTLMRRALEETGEEK-------LEDY 73

                          90       100
                  ....*....|....*....|....
gi 6322843     96 CSGVTGLLFTDEDVNTVKEYFKSY 119
Cdd:pfam00466  74 LKGPTALLFTNEDPVAVAKVLEDF 97
RL10P_insert pfam17777
Insertion domain in 60S ribosomal protein L10P; This domain is found in prokaryotic and ...
 126-208 2.54e-18

Insertion domain in 60S ribosomal protein L10P; This domain is found in prokaryotic and archaeal ribosomal L10 protein.


Pssm-ID: 465500 [Multi-domain]  Cd Length: 71  Bit Score: 76.09  E-value: 2.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322843    126 RPNTKAPLTFTIPEGIVysrgGQIPaeedvpmiHSLEPTMRnKFEIPTKIKAGKITIDSPYLVCTEGEKLDVRQALILKQ 205
Cdd:pfam17777   2 RAGAIATEDVVLPAGPT----GLAP--------GPIEPQLR-ALGIPTKIKKGKIEITKDYTVCKEGEKLTPEQANLLKL 68


                  ...
gi 6322843    206 FGI 208
Cdd:pfam17777  69 LGI 71
PTZ00240 PTZ00240
60S ribosomal protein P0; Provisional
 20-222 9.51e-15

60S ribosomal protein P0; Provisional


Pssm-ID: 140267 [Multi-domain]  Cd Length: 323  Bit Score: 71.92  E-value: 9.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322843    20 RENKERIFDevreALDTYRYVWVLHLDDVRTPVLQEIRTSWAG-SKLIMGKrKVLQKALGEKREE-----EYKENLYQL- 92
Cdd:PTZ00240   9 REYEERLVD----CLTKYSCVLFVGMDNVRSQQVHDVRRALRGkAEFVMGK-KTLQAKIVEKRAQakkasAEAKLFNDQc 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322843    93 --SKLCSGVTGLLFTDEDVNTVKEYFKSYVRSDYSRPNTKAPLTFTIPEGivySRGgqipaeedvpmihsLEPTMRNKFE 170
Cdd:PTZ00240  84 eeKNLLSGNTGLIFTNNEVQEITSVLDSHRVKAPARVGAIAPCDVIVPAG---STG--------------MEPTQTSFFQ 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6322843   171 ---IPTKIKAGKITIDSPYLVCTEGEKLDVRQALILKQFGIAASEFKVKVSAYYD 222
Cdd:PTZ00240 147 alnIATKIAKGMVEIVTEKKVLSVGDKVDNSTATLLQKLNISPFYYQVEVLSVWD 201
rplP0 PRK04019
acidic ribosomal protein P0; Validated
 20-223 3.62e-14

acidic ribosomal protein P0; Validated


Pssm-ID: 179712 [Multi-domain]  Cd Length: 330  Bit Score: 70.28  E-value: 3.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322843    20 RENKERIFDEVREALDTYRYVWVLHLDDVRTPVLQEIRTSWAG-SKLIMGKRKVLQKALgekrEEEYKENLYQLSKLCSG 98
Cdd:PRK04019   5 PEWKKEEVEELKELIKSYPVVGIVDLEGIPARQLQEIRRKLRGkAELKVSKNTLIKRAL----EEAGEEDLEKLEDYLEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322843    99 VTGLLFTDED-VNTVKEYFKSYVRSdYSRPNTKAPLTFTIPEGIVYSRGGqipaeedvPMIHSLeptmrNKFEIPTKIKA 177
Cdd:PRK04019  81 QVALIFTNMNpFKLYKLLEKSKTPA-PAKPGDIAPEDIVVPAGPTGFPPG--------PILSEL-----QKLGIPARIQK 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 6322843   178 GKITIDSPYLVCTEGEKLDVRQALILKQFGIAASEFKVKVSAYYDN 223
Cdd:PRK04019 147 GKIVIKKDTVVAKAGEVISPELANVLQKLGIKPIEVGLDLKAAYED 192
 
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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