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Conserved domains on  [gi|1907198796|ref|XP_036010984|]
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enhancer of mRNA-decapping protein 3 isoform X3 [Mus musculus]

Protein Classification

LSM14 family protein( domain architecture ID 10560091)

LSM14 family protein having an Sm fold consisting of a five-stranded beta-sheet and an alpha-helix at the N-terminus, may be involved in essential RNA-processing tasks

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FDF pfam09532
FDF domain; The FDF domain, so called because of the conserved FDF at its N termini, is an ...
15-118 1.06e-27

FDF domain; The FDF domain, so called because of the conserved FDF at its N termini, is an entirely alpha-helical domain with multiple exposed hydrophilic loops. It is found at the C terminus of Scd6p-like SM domains. It is also found with other divergent Sm domains and in proteins such as Dcp3p and FLJ21128, where it is found N terminal to the YjeF-N domain, a novel Rossmann fold domain.


:

Pssm-ID: 430668  Cd Length: 104  Bit Score: 104.07  E-value: 1.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198796  15 ELPDTDFDFEGNLALFDKAAVFEEIDTYERRSGSRSRGVPNeRPARYRHDENILESEPIVYRRITVPHSVSKEFCTDSGL 94
Cdd:pfam09532   1 IKFDEDFDFESNNAKFNKQEVFAELRKNDKLDEEKRLVNEN-NATRVATNEQPNEEVKGVYKKDDFFDNISSEANDRGIQ 79
                          90       100
                  ....*....|....*....|....*
gi 1907198796  95 VVPSVSYELHKKLLSV-AEKHGLTL 118
Cdd:pfam09532  80 SGPSPSGRDWREERSLnTETFGVDS 104
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
119-272 7.36e-22

YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a set of catalytic residues and structural features that are different from the conventional dehydrogenases. YjeF-N domain is fused to Ribokinases in bacteria (YjeF), where they may be phosphatases, and to divergent Sm and the FDF domain in eukaryotes (Dcp3p and FLJ21128), where they may be involved in decapping and catalyze hydrolytic RNA-processing reactions.


:

Pssm-ID: 427546 [Multi-domain]  Cd Length: 168  Bit Score: 90.36  E-value: 7.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198796 119 ERRLEMTGVCASQMALTLLggpnrlnpknVHQRPTVALLCGPHVKGAQGISCGRHLANHDVQVILF-LPNFVKMLESITN 197
Cdd:pfam03853   2 AVLMENAGRAAARVLKALL----------SPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLlLGPEEKLSEDARR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198796 198 ELSLFSKTQGQ----QVSSLRDLPASPVDLVINCLDcpENAFLRDQPW-YKAAVAWANQNRAPVLSIDPPVheveqGIDA 272
Cdd:pfam03853  72 QLDLFKKLGGKivtdNPDEDLEKLLSPVDLIIDALL--GTGLSGPLRGeYAALIEWINQSGAPVLAVDIPS-----GLDA 144
 
Name Accession Description Interval E-value
FDF pfam09532
FDF domain; The FDF domain, so called because of the conserved FDF at its N termini, is an ...
15-118 1.06e-27

FDF domain; The FDF domain, so called because of the conserved FDF at its N termini, is an entirely alpha-helical domain with multiple exposed hydrophilic loops. It is found at the C terminus of Scd6p-like SM domains. It is also found with other divergent Sm domains and in proteins such as Dcp3p and FLJ21128, where it is found N terminal to the YjeF-N domain, a novel Rossmann fold domain.


Pssm-ID: 430668  Cd Length: 104  Bit Score: 104.07  E-value: 1.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198796  15 ELPDTDFDFEGNLALFDKAAVFEEIDTYERRSGSRSRGVPNeRPARYRHDENILESEPIVYRRITVPHSVSKEFCTDSGL 94
Cdd:pfam09532   1 IKFDEDFDFESNNAKFNKQEVFAELRKNDKLDEEKRLVNEN-NATRVATNEQPNEEVKGVYKKDDFFDNISSEANDRGIQ 79
                          90       100
                  ....*....|....*....|....*
gi 1907198796  95 VVPSVSYELHKKLLSV-AEKHGLTL 118
Cdd:pfam09532  80 SGPSPSGRDWREERSLnTETFGVDS 104
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
119-272 7.36e-22

YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a set of catalytic residues and structural features that are different from the conventional dehydrogenases. YjeF-N domain is fused to Ribokinases in bacteria (YjeF), where they may be phosphatases, and to divergent Sm and the FDF domain in eukaryotes (Dcp3p and FLJ21128), where they may be involved in decapping and catalyze hydrolytic RNA-processing reactions.


Pssm-ID: 427546 [Multi-domain]  Cd Length: 168  Bit Score: 90.36  E-value: 7.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198796 119 ERRLEMTGVCASQMALTLLggpnrlnpknVHQRPTVALLCGPHVKGAQGISCGRHLANHDVQVILF-LPNFVKMLESITN 197
Cdd:pfam03853   2 AVLMENAGRAAARVLKALL----------SPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLlLGPEEKLSEDARR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198796 198 ELSLFSKTQGQ----QVSSLRDLPASPVDLVINCLDcpENAFLRDQPW-YKAAVAWANQNRAPVLSIDPPVheveqGIDA 272
Cdd:pfam03853  72 QLDLFKKLGGKivtdNPDEDLEKLLSPVDLIIDALL--GTGLSGPLRGeYAALIEWINQSGAPVLAVDIPS-----GLDA 144
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
149-324 5.76e-07

NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and metabolism];


Pssm-ID: 439832 [Multi-domain]  Cd Length: 499  Bit Score: 51.02  E-value: 5.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198796 149 HQRPTVALLCGPHVKGAQGISCGRHLANHDVQVILFLPNFVKML--ESITNeLSLFsKTQGQQVSSLRDLPASP--VDLV 224
Cdd:COG0062    45 SAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLLGDPEKLsgDAAAN-LERL-KAAGIPILELDDELPELaeADLI 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198796 225 INCLdcpenaF-------LRDqpWYKAAVAWANQNRAPVLSID-P---------------------------PVHEVEQG 269
Cdd:COG0062   123 VDAL------FgtglsrpLRG--PYAELIEAINASGAPVLAVDiPsgldadtgevlgaavradltvtfgapkPGLLLGPG 194
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907198796 270 idakwslalglplplGEHAGRVYLCDIGIPQQVFQELSPAPGKRPEDWEPQLHDR 324
Cdd:COG0062   195 ---------------RDYCGELVVADIGIGIPAAAEAPAALLLLADLLALLLPPR 234
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
102-186 1.41e-04

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 42.56  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198796 102 ELHKKLLSVAekhGLTLERRLEMTGVCASQMALTLLGGPNRLNPKNVHQRptVALLCGPHVKGAQGISCGRHLANHDVQV 181
Cdd:PLN03050   16 ALDEELMSTP---GFSLEQLMELAGLSVAEAVYEVADGEKASNPPGRHPR--VLLVCGPGNNGGDGLVAARHLAHFGYEV 90

                  ....*
gi 1907198796 182 ILFLP 186
Cdd:PLN03050   91 TVCYP 95
 
Name Accession Description Interval E-value
FDF pfam09532
FDF domain; The FDF domain, so called because of the conserved FDF at its N termini, is an ...
15-118 1.06e-27

FDF domain; The FDF domain, so called because of the conserved FDF at its N termini, is an entirely alpha-helical domain with multiple exposed hydrophilic loops. It is found at the C terminus of Scd6p-like SM domains. It is also found with other divergent Sm domains and in proteins such as Dcp3p and FLJ21128, where it is found N terminal to the YjeF-N domain, a novel Rossmann fold domain.


Pssm-ID: 430668  Cd Length: 104  Bit Score: 104.07  E-value: 1.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198796  15 ELPDTDFDFEGNLALFDKAAVFEEIDTYERRSGSRSRGVPNeRPARYRHDENILESEPIVYRRITVPHSVSKEFCTDSGL 94
Cdd:pfam09532   1 IKFDEDFDFESNNAKFNKQEVFAELRKNDKLDEEKRLVNEN-NATRVATNEQPNEEVKGVYKKDDFFDNISSEANDRGIQ 79
                          90       100
                  ....*....|....*....|....*
gi 1907198796  95 VVPSVSYELHKKLLSV-AEKHGLTL 118
Cdd:pfam09532  80 SGPSPSGRDWREERSLnTETFGVDS 104
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
119-272 7.36e-22

YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a set of catalytic residues and structural features that are different from the conventional dehydrogenases. YjeF-N domain is fused to Ribokinases in bacteria (YjeF), where they may be phosphatases, and to divergent Sm and the FDF domain in eukaryotes (Dcp3p and FLJ21128), where they may be involved in decapping and catalyze hydrolytic RNA-processing reactions.


Pssm-ID: 427546 [Multi-domain]  Cd Length: 168  Bit Score: 90.36  E-value: 7.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198796 119 ERRLEMTGVCASQMALTLLggpnrlnpknVHQRPTVALLCGPHVKGAQGISCGRHLANHDVQVILF-LPNFVKMLESITN 197
Cdd:pfam03853   2 AVLMENAGRAAARVLKALL----------SPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLlLGPEEKLSEDARR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198796 198 ELSLFSKTQGQ----QVSSLRDLPASPVDLVINCLDcpENAFLRDQPW-YKAAVAWANQNRAPVLSIDPPVheveqGIDA 272
Cdd:pfam03853  72 QLDLFKKLGGKivtdNPDEDLEKLLSPVDLIIDALL--GTGLSGPLRGeYAALIEWINQSGAPVLAVDIPS-----GLDA 144
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
149-324 5.76e-07

NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and metabolism];


Pssm-ID: 439832 [Multi-domain]  Cd Length: 499  Bit Score: 51.02  E-value: 5.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198796 149 HQRPTVALLCGPHVKGAQGISCGRHLANHDVQVILFLPNFVKML--ESITNeLSLFsKTQGQQVSSLRDLPASP--VDLV 224
Cdd:COG0062    45 SAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLLGDPEKLsgDAAAN-LERL-KAAGIPILELDDELPELaeADLI 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198796 225 INCLdcpenaF-------LRDqpWYKAAVAWANQNRAPVLSID-P---------------------------PVHEVEQG 269
Cdd:COG0062   123 VDAL------FgtglsrpLRG--PYAELIEAINASGAPVLAVDiPsgldadtgevlgaavradltvtfgapkPGLLLGPG 194
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907198796 270 idakwslalglplplGEHAGRVYLCDIGIPQQVFQELSPAPGKRPEDWEPQLHDR 324
Cdd:COG0062   195 ---------------RDYCGELVVADIGIGIPAAAEAPAALLLLADLLALLLPPR 234
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
102-186 1.41e-04

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 42.56  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198796 102 ELHKKLLSVAekhGLTLERRLEMTGVCASQMALTLLGGPNRLNPKNVHQRptVALLCGPHVKGAQGISCGRHLANHDVQV 181
Cdd:PLN03050   16 ALDEELMSTP---GFSLEQLMELAGLSVAEAVYEVADGEKASNPPGRHPR--VLLVCGPGNNGGDGLVAARHLAHFGYEV 90

                  ....*
gi 1907198796 182 ILFLP 186
Cdd:PLN03050   91 TVCYP 95
 
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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