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Conserved domains on  [gi|578799212|ref|XP_006710738|]
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mRNA turnover protein 4 homolog isoform X1 [Homo sapiens]

Protein Classification

mRNA turnover protein 4( domain architecture ID 10146578)

mRNA turnover protein 4 (MRT4) 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 ...
 1-136 2.47e-91

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: 263.67  E-value: 2.47e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799212   1 MRNSKLKDIRNAWKHSRMFFGKNKVMMVALGRSPSDEYKDNLHQVSKRLRGEVGLLFTNRTKEEVNEWFTKYTEMDYARA 80
Cdd:cd05796   28 MRNNKLKDIRQEWKDSRFFFGKNKVMQVALGRTPEDEYKPNLHKLSKYLKGQVGLLFTNEPPEEVIEYFDSYSEPDFARA 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578799212  81 GNKAAFTVSLDPGPLEQFPHSMEPQLRQLGLPTALKRGVVTLLSDYEVCKEGDVLT 136
Cdd:cd05796  108 GSIATETVTLPEGPLEQFPHSMEPQLRKLGLPTKLKKGVITLEADYVVCEEGKVLT 163
 
Name Accession Description Interval E-value
Ribosomal_P0_like cd05796
Ribosomal protein L10 family, P0-like protein subfamily; composed of uncharacterized ...
 1-136 2.47e-91

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: 263.67  E-value: 2.47e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799212   1 MRNSKLKDIRNAWKHSRMFFGKNKVMMVALGRSPSDEYKDNLHQVSKRLRGEVGLLFTNRTKEEVNEWFTKYTEMDYARA 80
Cdd:cd05796   28 MRNNKLKDIRQEWKDSRFFFGKNKVMQVALGRTPEDEYKPNLHKLSKYLKGQVGLLFTNEPPEEVIEYFDSYSEPDFARA 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578799212  81 GNKAAFTVSLDPGPLEQFPHSMEPQLRQLGLPTALKRGVVTLLSDYEVCKEGDVLT 136
Cdd:cd05796  108 GSIATETVTLPEGPLEQFPHSMEPQLRKLGLPTKLKKGVITLEADYVVCEEGKVLT 163
RL10P_insert pfam17777
Insertion domain in 60S ribosomal protein L10P; This domain is found in prokaryotic and ...
 78-147 1.86e-33

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: 113.84  E-value: 1.86e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799212   78 ARAGNKAAFTVSLDPGPLEQFPHSMEPQLRQLGLPTALKRGVVTLLSDYEVCKEGDVLTPEQARVLKLFG 147
Cdd:pfam17777   1 ARAGAIATEDVVLPAGPTGLAPGPIEPQLRALGIPTKIKKGKIEITKDYTVCKEGEKLTPEQANLLKLLG 70
rplP0 PRK04019
acidic ribosomal protein P0; Validated
 1-162 2.66e-17

acidic ribosomal protein P0; Validated


Pssm-ID: 179712 [Multi-domain]  Cd Length: 330  Bit Score: 77.98  E-value: 2.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799212   1 MRNSKLKDIR-NAWKHSRMFFGKNKVMMVALGRSPSDEYKDnlhqVSKRLRGEVGLLFTNRTKEEVNEWFTKYTEMDYAR 79
Cdd:PRK04019  33 IPARQLQEIRrKLRGKAELKVSKNTLIKRALEEAGEEDLEK----LEDYLEGQVALIFTNMNPFKLYKLLEKSKTPAPAK 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799212  80 AGNKAAFTV-------SLDPGPleqfphsMEPQLRQLGLPTALKRGVVTLLSDYEVCKEGDVLTPEQARVLKLFGYEMAE 152
Cdd:PRK04019 109 PGDIAPEDIvvpagptGFPPGP-------ILSELQKLGIPARIQKGKIVIKKDTVVAKAGEVISPELANVLQKLGIKPIE 181

                        170
                 ....*....|
gi 578799212 153 FKVTIKYMWD 162
Cdd:PRK04019 182 VGLDLKAAYE 191
 
Name Accession Description Interval E-value
Ribosomal_P0_like cd05796
Ribosomal protein L10 family, P0-like protein subfamily; composed of uncharacterized ...
 1-136 2.47e-91

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: 263.67  E-value: 2.47e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799212   1 MRNSKLKDIRNAWKHSRMFFGKNKVMMVALGRSPSDEYKDNLHQVSKRLRGEVGLLFTNRTKEEVNEWFTKYTEMDYARA 80
Cdd:cd05796   28 MRNNKLKDIRQEWKDSRFFFGKNKVMQVALGRTPEDEYKPNLHKLSKYLKGQVGLLFTNEPPEEVIEYFDSYSEPDFARA 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578799212  81 GNKAAFTVSLDPGPLEQFPHSMEPQLRQLGLPTALKRGVVTLLSDYEVCKEGDVLT 136
Cdd:cd05796  108 GSIATETVTLPEGPLEQFPHSMEPQLRKLGLPTKLKKGVITLEADYVVCEEGKVLT 163
RL10P_insert pfam17777
Insertion domain in 60S ribosomal protein L10P; This domain is found in prokaryotic and ...
 78-147 1.86e-33

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: 113.84  E-value: 1.86e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799212   78 ARAGNKAAFTVSLDPGPLEQFPHSMEPQLRQLGLPTALKRGVVTLLSDYEVCKEGDVLTPEQARVLKLFG 147
Cdd:pfam17777   1 ARAGAIATEDVVLPAGPTGLAPGPIEPQLRALGIPTKIKKGKIEITKDYTVCKEGEKLTPEQANLLKLLG 70
Ribosomal_L10_P0 cd00379
Ribosomal protein L10 family; composed of the large subunit ribosomal protein called L10 in ...
 1-132 1.79e-25

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: 96.09  E-value: 1.79e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799212   1 MRNSKLKDIRNAWKHS--RMFFGKNKVMMVALGRSPSDEYKDnlhqvskRLRGEVGLLFTNRTKEEVNEWFTKYT---EM 75
Cdd:cd00379   28 LTVAQLTELRKELRESgaKLKVGKNTLMRRALKGTGFEELKP-------LLKGPTALAFTNEDPVEVAKVLKDFAkenKK 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578799212  76 DYARAGNKaAFTVSLdpgPLEQFPHSMEP-QLRQLGLPTALKRGVVT-LLSDYEVCKEG 132
Cdd:cd00379  101 LFAKGGVV-AGKVLD---PAGVTALAKLPsREELLAMLIGLLKAPIAkLARLLNALGIG 155
Ribosomal_P0_L10e cd05795
Ribosomal protein L10 family, P0 and L10e subfamily; composed of eukaryotic 60S ribosomal ...
 1-147 1.93e-17

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: 75.69  E-value: 1.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799212   1 MRNSKLKDIRNAWK-HSRMFFGKNKVMMVALgrspsDEYKDNLHQVSKRL---RGEVGLLFTNRTKEEVNEWFTKYTEMD 76
Cdd:cd05795   28 VGSKQLQKIRRSLRgKAEILMGKNTLIRRAL-----RNLGDENPELEKLLpylKGNVGFIFTNGDPFEIRKILEENKVPA 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578799212  77 YARAGNKAAFTVSLDPGPLeqfphSMEP----QLRQLGLPTALKRGVVTLLSDYEVCKEGDVLTPEQARVLKLFG 147
Cdd:cd05795  103 PAKPGAIAPCDVVVPAGPT-----GMPPgptsFFQALGIPTKIEKGKIEIISDVVVVKKGEKVGASEATLLNKLN 172
rplP0 PRK04019
acidic ribosomal protein P0; Validated
 1-162 2.66e-17

acidic ribosomal protein P0; Validated


Pssm-ID: 179712 [Multi-domain]  Cd Length: 330  Bit Score: 77.98  E-value: 2.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799212   1 MRNSKLKDIR-NAWKHSRMFFGKNKVMMVALGRSPSDEYKDnlhqVSKRLRGEVGLLFTNRTKEEVNEWFTKYTEMDYAR 79
Cdd:PRK04019  33 IPARQLQEIRrKLRGKAELKVSKNTLIKRALEEAGEEDLEK----LEDYLEGQVALIFTNMNPFKLYKLLEKSKTPAPAK 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799212  80 AGNKAAFTV-------SLDPGPleqfphsMEPQLRQLGLPTALKRGVVTLLSDYEVCKEGDVLTPEQARVLKLFGYEMAE 152
Cdd:PRK04019 109 PGDIAPEDIvvpagptGFPPGP-------ILSELQKLGIPARIQKGKIVIKKDTVVAKAGEVISPELANVLQKLGIKPIE 181

                        170
                 ....*....|
gi 578799212 153 FKVTIKYMWD 162
Cdd:PRK04019 182 VGLDLKAAYE 191
Ribosomal_L10 pfam00466
Ribosomal protein L10;
1-73 1.03e-11

Ribosomal protein L10;


Pssm-ID: 459822 [Multi-domain]  Cd Length: 99  Bit Score: 58.71  E-value: 1.03e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578799212    1 MRNSKLKDIRNAWK--HSRMFFGKNKVMMVALGRSPSDEykdnlhqVSKRLRGEVGLLFTNRTKEEVNEWFTKYT 73
Cdd:pfam00466  31 LTVAQLTELRKKLRenGAELKVGKNTLMRRALEETGEEK-------LEDYLKGPTALLFTNEDPVAVAKVLEDFA 98
PTZ00135 PTZ00135
60S acidic ribosomal protein P0; Provisional
 2-147 1.26e-10

60S acidic ribosomal protein P0; Provisional


Pssm-ID: 240285 [Multi-domain]  Cd Length: 310  Bit Score: 58.88  E-value: 1.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799212   2 RNSKLKDIRNAWK-HSRMFFGKNKVMMVALGRSPSDeyKDNLHQVSKRLRGEVGLLFTNRTKEEVNEWFTKYTEMDYARA 80
Cdd:PTZ00135  36 GSKQMQDIRRSLRgKAELLMGKNTLIRKALKQRLEE--LPELEKLLPHVKGNVGFVFTKDDLFEVKPVILENKVPAPARA 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578799212  81 GNKAAFTVSLDPGPLeqfphSMEPQ----LRQLGLPTALKRGVVTLLSDYEVCKEGDVLTPEQARVLKLFG 147
Cdd:PTZ00135 114 GVIAPIDVVIPAGPT-----GMDPSqtsfFQALGIATKIVKGQIEITNEVHLIKEGQKVGASQAVLLQKLN 179
PTZ00240 PTZ00240
60S ribosomal protein P0; Provisional
 1-162 3.73e-04

60S ribosomal protein P0; Provisional


Pssm-ID: 140267 [Multi-domain]  Cd Length: 323  Bit Score: 40.33  E-value: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799212   1 MRNSKLKDIRNAWKhsrmffGKNKVMM------------VALGRSPSDEYKdNLHQV---SKRLRGEVGLLFTNRTKEEV 65
Cdd:PTZ00240  33 VRSQQVHDVRRALR------GKAEFVMgkktlqakivekRAQAKKASAEAK-LFNDQceeKNLLSGNTGLIFTNNEVQEI 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799212  66 NEWFTKYTEMDYARAGNKAAFTVSLDPGPLeqfphSMEPQ----LRQLGLPTALKRGVVTLLSDYEVCKEGDVLTPEQAR 141
Cdd:PTZ00240 106 TSVLDSHRVKAPARVGAIAPCDVIVPAGST-----GMEPTqtsfFQALNIATKIAKGMVEIVTEKKVLSVGDKVDNSTAT 180

                        170       180
                 ....*....|....*....|.
gi 578799212 142 VLKLFGYEMAEFKVTIKYMWD 162
Cdd:PTZ00240 181 LLQKLNISPFYYQVEVLSVWD 201
 
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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