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Conserved domains on  [gi|18490987|ref|NP_057267|]
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mRNA turnover protein 4 homolog [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 ...
 21-183 1.31e-106

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: 304.50  E-value: 1.31e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490987  21 ELKQNLIEELRKCVDTYKYLFIFSVANMRNSKLKDIRNAWKHSRMFFGKNKVMMVALGRSPSDEYKDNLHQVSKRLRGEV 100
Cdd:cd05796   1 ELKQKLVENIREAVDKYKYIYVFSVDNMRNNKLKDIRQEWKDSRFFFGKNKVMQVALGRTPEDEYKPNLHKLSKYLKGQV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490987 101 GLLFTNRTKEEVNEWFTKYTEMDYARAGNKAAFTVSLDPGPLEQFPHSMEPQLRQLGLPTALKRGVVTLLSDYEVCKEGD 180
Cdd:cd05796  81 GLLFTNEPPEEVIEYFDSYSEPDFARAGSIATETVTLPEGPLEQFPHSMEPQLRKLGLPTKLKKGVITLEADYVVCEEGK 160


                ...
gi 18490987 181 VLT 183
Cdd:cd05796 161 VLT 163
 
Name Accession Description Interval E-value
Ribosomal_P0_like cd05796
Ribosomal protein L10 family, P0-like protein subfamily; composed of uncharacterized ...
 21-183 1.31e-106

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: 304.50  E-value: 1.31e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490987  21 ELKQNLIEELRKCVDTYKYLFIFSVANMRNSKLKDIRNAWKHSRMFFGKNKVMMVALGRSPSDEYKDNLHQVSKRLRGEV 100
Cdd:cd05796   1 ELKQKLVENIREAVDKYKYIYVFSVDNMRNNKLKDIRQEWKDSRFFFGKNKVMQVALGRTPEDEYKPNLHKLSKYLKGQV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490987 101 GLLFTNRTKEEVNEWFTKYTEMDYARAGNKAAFTVSLDPGPLEQFPHSMEPQLRQLGLPTALKRGVVTLLSDYEVCKEGD 180
Cdd:cd05796  81 GLLFTNEPPEEVIEYFDSYSEPDFARAGSIATETVTLPEGPLEQFPHSMEPQLRKLGLPTKLKKGVITLEADYVVCEEGK 160


                ...
gi 18490987 181 VLT 183
Cdd:cd05796 161 VLT 163
RL10P_insert pfam17777
Insertion domain in 60S ribosomal protein L10P; This domain is found in prokaryotic and ...
 125-194 7.50e-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: 7.50e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490987   125 ARAGNKAAFTVSLDPGPLEQFPHSMEPQLRQLGLPTALKRGVVTLLSDYEVCKEGDVLTPEQARVLKLFG 194
Cdd:pfam17777   1 ARAGAIATEDVVLPAGPTGLAPGPIEPQLRALGIPTKIKKGKIEITKDYTVCKEGEKLTPEQANLLKLLG 70
rplP0 PRK04019
acidic ribosomal protein P0; Validated
 23-209 1.20e-23

acidic ribosomal protein P0; Validated


Pssm-ID: 179712 [Multi-domain]  Cd Length: 330  Bit Score: 96.86  E-value: 1.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490987   23 KQNLIEELRKCVDTYKYLFIFSVANMRNSKLKDIR-NAWKHSRMFFGKNKVMMVALGRSPSDEYKDnlhqVSKRLRGEVG 101
Cdd:PRK04019   8 KKEEVEELKELIKSYPVVGIVDLEGIPARQLQEIRrKLRGKAELKVSKNTLIKRALEEAGEEDLEK----LEDYLEGQVA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490987  102 LLFTNRTKEEVNEWFTKYTEMDYARAGNKAAFTV-------SLDPGPleqfphsMEPQLRQLGLPTALKRGVVTLLSDYE 174
Cdd:PRK04019  84 LIFTNMNPFKLYKLLEKSKTPAPAKPGDIAPEDIvvpagptGFPPGP-------ILSELQKLGIPARIQKGKIVIKKDTV 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 18490987  175 VCKEGDVLTPEQARVLKLFGYEMAEFKVTIKYMWD 209
Cdd:PRK04019 157 VAKAGEVISPELANVLQKLGIKPIEVGLDLKAAYE 191
 
Name Accession Description Interval E-value
Ribosomal_P0_like cd05796
Ribosomal protein L10 family, P0-like protein subfamily; composed of uncharacterized ...
 21-183 1.31e-106

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: 304.50  E-value: 1.31e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490987  21 ELKQNLIEELRKCVDTYKYLFIFSVANMRNSKLKDIRNAWKHSRMFFGKNKVMMVALGRSPSDEYKDNLHQVSKRLRGEV 100
Cdd:cd05796   1 ELKQKLVENIREAVDKYKYIYVFSVDNMRNNKLKDIRQEWKDSRFFFGKNKVMQVALGRTPEDEYKPNLHKLSKYLKGQV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490987 101 GLLFTNRTKEEVNEWFTKYTEMDYARAGNKAAFTVSLDPGPLEQFPHSMEPQLRQLGLPTALKRGVVTLLSDYEVCKEGD 180
Cdd:cd05796  81 GLLFTNEPPEEVIEYFDSYSEPDFARAGSIATETVTLPEGPLEQFPHSMEPQLRKLGLPTKLKKGVITLEADYVVCEEGK 160


                ...
gi 18490987 181 VLT 183
Cdd:cd05796 161 VLT 163
Ribosomal_L10_P0 cd00379
Ribosomal protein L10 family; composed of the large subunit ribosomal protein called L10 in ...
 21-179 3.47e-35

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: 122.67  E-value: 3.47e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490987  21 ELKQNLIEELRKCVDTYKYLFIFSVANMRNSKLKDIRNAWKHS--RMFFGKNKVMMVALGRSPSDEYKDnlhqvskRLRG 98
Cdd:cd00379   1 EKKEELVEELKELLKKYKSVVVVDYRGLTVAQLTELRKELRESgaKLKVGKNTLMRRALKGTGFEELKP-------LLKG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490987  99 EVGLLFTNRTKEEVNEWFTKYT---EMDYARAGNKaAFTVSLdpgPLEQFPHSMEP-QLRQLGLPTALKRGVVT-LLSDY 173
Cdd:cd00379  74 PTALAFTNEDPVEVAKVLKDFAkenKKLFAKGGVV-AGKVLD---PAGVTALAKLPsREELLAMLIGLLKAPIAkLARLL 149


                ....*.
gi 18490987 174 EVCKEG 179
Cdd:cd00379 150 NALGIG 155
RL10P_insert pfam17777
Insertion domain in 60S ribosomal protein L10P; This domain is found in prokaryotic and ...
 125-194 7.50e-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: 7.50e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490987   125 ARAGNKAAFTVSLDPGPLEQFPHSMEPQLRQLGLPTALKRGVVTLLSDYEVCKEGDVLTPEQARVLKLFG 194
Cdd:pfam17777   1 ARAGAIATEDVVLPAGPTGLAPGPIEPQLRALGIPTKIKKGKIEITKDYTVCKEGEKLTPEQANLLKLLG 70
Ribosomal_P0_L10e cd05795
Ribosomal protein L10 family, P0 and L10e subfamily; composed of eukaryotic 60S ribosomal ...
 21-194 1.29e-25

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: 98.41  E-value: 1.29e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490987  21 ELKQNLIEELRKCVDTYKYLFIFSVANMRNSKLKDIRNAWK-HSRMFFGKNKVMMVALgrspsDEYKDNLHQVSKRL--- 96
Cdd:cd05795   1 EWKKEYVEKLTELLKSYPKVLIVDADNVGSKQLQKIRRSLRgKAEILMGKNTLIRRAL-----RNLGDENPELEKLLpyl 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490987  97 RGEVGLLFTNRTKEEVNEWFTKYTEMDYARAGNKAAFTVSLDPGPLeqfphSMEP----QLRQLGLPTALKRGVVTLLSD 172
Cdd:cd05795  76 KGNVGFIFTNGDPFEIRKILEENKVPAPAKPGAIAPCDVVVPAGPT-----GMPPgptsFFQALGIPTKIEKGKIEIISD 150

                       170       180
                ....*....|....*....|..
gi 18490987 173 YEVCKEGDVLTPEQARVLKLFG 194
Cdd:cd05795 151 VVVVKKGEKVGASEATLLNKLN 172
rplP0 PRK04019
acidic ribosomal protein P0; Validated
 23-209 1.20e-23

acidic ribosomal protein P0; Validated


Pssm-ID: 179712 [Multi-domain]  Cd Length: 330  Bit Score: 96.86  E-value: 1.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490987   23 KQNLIEELRKCVDTYKYLFIFSVANMRNSKLKDIR-NAWKHSRMFFGKNKVMMVALGRSPSDEYKDnlhqVSKRLRGEVG 101
Cdd:PRK04019   8 KKEEVEELKELIKSYPVVGIVDLEGIPARQLQEIRrKLRGKAELKVSKNTLIKRALEEAGEEDLEK----LEDYLEGQVA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490987  102 LLFTNRTKEEVNEWFTKYTEMDYARAGNKAAFTV-------SLDPGPleqfphsMEPQLRQLGLPTALKRGVVTLLSDYE 174
Cdd:PRK04019  84 LIFTNMNPFKLYKLLEKSKTPAPAKPGDIAPEDIvvpagptGFPPGP-------ILSELQKLGIPARIQKGKIVIKKDTV 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 18490987  175 VCKEGDVLTPEQARVLKLFGYEMAEFKVTIKYMWD 209
Cdd:PRK04019 157 VAKAGEVISPELANVLQKLGIKPIEVGLDLKAAYE 191
Ribosomal_L10 pfam00466
Ribosomal protein L10;
18-120 2.02e-20

Ribosomal protein L10;


Pssm-ID: 459822 [Multi-domain]  Cd Length: 99  Bit Score: 82.59  E-value: 2.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490987    18 KGLELKQNLIEELRKCVDTYKYLFIFSVANMRNSKLKDIRNAWK--HSRMFFGKNKVMMVALGRSPSDEykdnlhqVSKR 95
Cdd:pfam00466   1 KTREKKEELVEELKELLKEYKSVVVVDYRGLTVAQLTELRKKLRenGAELKVGKNTLMRRALEETGEEK-------LEDY 73

                          90       100
                  ....*....|....*....|....*
gi 18490987    96 LRGEVGLLFTNRTKEEVNEWFTKYT 120
Cdd:pfam00466  74 LKGPTALLFTNEDPVAVAKVLEDFA 98
PTZ00135 PTZ00135
60S acidic ribosomal protein P0; Provisional
 14-194 2.39e-17

60S acidic ribosomal protein P0; Provisional


Pssm-ID: 240285 [Multi-domain]  Cd Length: 310  Bit Score: 79.29  E-value: 2.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490987   14 KTAKKglELKQNLIEELRKCVDTYKYLFIFSVANMRNSKLKDIRNAWK-HSRMFFGKNKVMMVALGRSPSDeyKDNLHQV 92
Cdd:PTZ00135   3 KPEKK--AKKKAYFEKLYELLEKYKKILIVSVDNVGSKQMQDIRRSLRgKAELLMGKNTLIRKALKQRLEE--LPELEKL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490987   93 SKRLRGEVGLLFTNRTKEEVNEWFTKYTEMDYARAGNKAAFTVSLDPGPLeqfphSMEPQ----LRQLGLPTALKRGVVT 168
Cdd:PTZ00135  79 LPHVKGNVGFVFTKDDLFEVKPVILENKVPAPARAGVIAPIDVVIPAGPT-----GMDPSqtsfFQALGIATKIVKGQIE 153

                        170       180
                 ....*....|....*....|....*.
gi 18490987  169 LLSDYEVCKEGDVLTPEQARVLKLFG 194
Cdd:PTZ00135 154 ITNEVHLIKEGQKVGASQAVLLQKLN 179
PTZ00240 PTZ00240
60S ribosomal protein P0; Provisional
 21-209 1.30e-06

60S ribosomal protein P0; Provisional


Pssm-ID: 140267 [Multi-domain]  Cd Length: 323  Bit Score: 48.42  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490987   21 ELKQNLIEELRKCVDTYKYLFIFSVANMRNSKLKDIRNAWKhsrmffGKNKVMM------------VALGRSPSDEYKdN 88
Cdd:PTZ00240   6 TAKREYEERLVDCLTKYSCVLFVGMDNVRSQQVHDVRRALR------GKAEFVMgkktlqakivekRAQAKKASAEAK-L 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490987   89 LHQV---SKRLRGEVGLLFTNRTKEEVNEWFTKYTEMDYARAGNKAAFTVSLDPGPLeqfphSMEPQ----LRQLGLPTA 161
Cdd:PTZ00240  79 FNDQceeKNLLSGNTGLIFTNNEVQEITSVLDSHRVKAPARVGAIAPCDVIVPAGST-----GMEPTqtsfFQALNIATK 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 18490987  162 LKRGVVTLLSDYEVCKEGDVLTPEQARVLKLFGYEMAEFKVTIKYMWD 209
Cdd:PTZ00240 154 IAKGMVEIVTEKKVLSVGDKVDNSTATLLQKLNISPFYYQVEVLSVWD 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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