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Conserved domains on  [gi|215598561|ref|NP_001135916|]
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enhancer of mRNA-decapping protein 3 isoform 1 [Homo sapiens]

Protein Classification

LSM14 family protein( domain architecture ID 10846049)

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
Edc3_linker pfam16598
Linker region of enhancer of mRNA-decapping protein 3; This region is located between the ...
 102-194 2.95e-59

Linker region of enhancer of mRNA-decapping protein 3; This region is located between the LSM14 pfam12701 (Lsm) and FDF pfam09532 domains of the enhancer of mRNA-decapping protein 3. This region is predicted to be natively unstructured. Its precise functional role is not known.


:

Pssm-ID: 465188  Cd Length: 91  Bit Score: 190.18  E-value: 2.95e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215598561  102 KFVKKPASSSSAPQNIPKRTDVKSQDVAVSPQQqqCSKSYVDRHMESLSQSKSFRRRHNSWSSSSRHPNQATPKKSGLKN 181
Cdd:pfam16598   1 KTLKKPAISSSAPQAIPRRGDAKGQEKVNSPQQ--CSKSYGDRHLDSLGQSKGFRRRHNSWSSSSRGPNQATPKKNGVKN 78

                          90
                  ....*....|...
gi 215598561  182 GQMKNKDDECFGD 194
Cdd:pfam16598  79 GQMKSKDDECFGD 91
FDF pfam09532
FDF domain; The FDF domain, so called because of the conserved FDF at its N termini, is an ...
 198-301 8.46e-31

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: 115.24  E-value: 8.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215598561  198 EIPDTDFDFEGNLALFDKAAVFEEIDTYERRSGTRSRGIPNeRPTRYRHDENILESEPIVYRRIIVPHNVSKEFCTDSGL 277
Cdd:pfam09532   1 IKFDEDFDFESNNAKFNKQEVFAELRKNDKLDEEKRLVNEN-NATRVATNEQPNEEVKGVYKKDDFFDNISSEANDRGIQ 79

                          90       100
                  ....*....|....*....|....*
gi 215598561  278 VVPSISYELHKKLLSV-AEKHGLTL 301
Cdd:pfam09532  80 SGPSPSGRDWREERSLnTETFGVDS 104
LSm16_N cd01737
Like-Sm protein 16, N-terminal domain; LSm16 (also known as enhancer of decapping-3 or EDC3) ...
 2-66 1.14e-28

Like-Sm protein 16, N-terminal domain; LSm16 (also known as enhancer of decapping-3 or EDC3) has been shown to be associated with an mRNA-decapping complex Dcp1-Dcp2, required for removal of the 5-prime cap from mRNA prior to its degradation from the 5-prime end. EDC3 is believed to be a scaffold for decapping complex formation. It belongs to a family of Sm-like proteins that associate with RNA to form complexes involved in a variety of RNA processing events including pre-mRNA splicing, telomere replication, and mRNA degradation. Members of this family share a highly conserved Sm fold, containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet, that associates with other Sm proteins to form hexameric and heptameric ring structures. LSm16 has, in addition to its N-terminal Sm-like domain, a C-terminal Yjef_N-type Rossmann fold domain of unknown function.


:

Pssm-ID: 212484  Cd Length: 65  Bit Score: 107.79  E-value: 1.14e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 215598561   2 ATDWLGSIVSINCGDSLGVYQGRVSAVDQVSQTISLTRPFHNGVKCLVPEVTFRAGDITELKILE 66
Cdd:cd01737    1 AEDFIGSAVSIHCGDTLGVYQGVISNVDPTNQTISLRKAFRNGLKCQVPEVTLSAKDIKDLKIIE 65
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 302-455 7.44e-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: 92.29  E-value: 7.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215598561  302 ERRLEMTGVCASQMALTLLggpnrlnpknVHQRPTVALLCGPHVKGAQGISCGRHLANHDVQVILF-LPNFVKMLESITN 380
Cdd:pfam03853   2 AVLMENAGRAAARVLKALL----------SPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLlLGPEEKLSEDARR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215598561  381 ELSLFSKTQGQ----QVSSLKDLPTSPVDLVINCLDcpeNVFLR--DQPWYKAAVAWANQNRAPVLSIDPPVheveqGID 454
Cdd:pfam03853  72 QLDLFKKLGGKivtdNPDEDLEKLLSPVDLIIDALL---GTGLSgpLRGEYAALIEWINQSGAPVLAVDIPS-----GLD 143


                  .
gi 215598561  455 A 455
Cdd:pfam03853 144 A 144
 
Name Accession Description Interval E-value
Edc3_linker pfam16598
Linker region of enhancer of mRNA-decapping protein 3; This region is located between the ...
 102-194 2.95e-59

Linker region of enhancer of mRNA-decapping protein 3; This region is located between the LSM14 pfam12701 (Lsm) and FDF pfam09532 domains of the enhancer of mRNA-decapping protein 3. This region is predicted to be natively unstructured. Its precise functional role is not known.


Pssm-ID: 465188  Cd Length: 91  Bit Score: 190.18  E-value: 2.95e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215598561  102 KFVKKPASSSSAPQNIPKRTDVKSQDVAVSPQQqqCSKSYVDRHMESLSQSKSFRRRHNSWSSSSRHPNQATPKKSGLKN 181
Cdd:pfam16598   1 KTLKKPAISSSAPQAIPRRGDAKGQEKVNSPQQ--CSKSYGDRHLDSLGQSKGFRRRHNSWSSSSRGPNQATPKKNGVKN 78

                          90
                  ....*....|...
gi 215598561  182 GQMKNKDDECFGD 194
Cdd:pfam16598  79 GQMKSKDDECFGD 91
FDF pfam09532
FDF domain; The FDF domain, so called because of the conserved FDF at its N termini, is an ...
 198-301 8.46e-31

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: 115.24  E-value: 8.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215598561  198 EIPDTDFDFEGNLALFDKAAVFEEIDTYERRSGTRSRGIPNeRPTRYRHDENILESEPIVYRRIIVPHNVSKEFCTDSGL 277
Cdd:pfam09532   1 IKFDEDFDFESNNAKFNKQEVFAELRKNDKLDEEKRLVNEN-NATRVATNEQPNEEVKGVYKKDDFFDNISSEANDRGIQ 79

                          90       100
                  ....*....|....*....|....*
gi 215598561  278 VVPSISYELHKKLLSV-AEKHGLTL 301
Cdd:pfam09532  80 SGPSPSGRDWREERSLnTETFGVDS 104
LSm16_N cd01737
Like-Sm protein 16, N-terminal domain; LSm16 (also known as enhancer of decapping-3 or EDC3) ...
 2-66 1.14e-28

Like-Sm protein 16, N-terminal domain; LSm16 (also known as enhancer of decapping-3 or EDC3) has been shown to be associated with an mRNA-decapping complex Dcp1-Dcp2, required for removal of the 5-prime cap from mRNA prior to its degradation from the 5-prime end. EDC3 is believed to be a scaffold for decapping complex formation. It belongs to a family of Sm-like proteins that associate with RNA to form complexes involved in a variety of RNA processing events including pre-mRNA splicing, telomere replication, and mRNA degradation. Members of this family share a highly conserved Sm fold, containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet, that associates with other Sm proteins to form hexameric and heptameric ring structures. LSm16 has, in addition to its N-terminal Sm-like domain, a C-terminal Yjef_N-type Rossmann fold domain of unknown function.


Pssm-ID: 212484  Cd Length: 65  Bit Score: 107.79  E-value: 1.14e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 215598561   2 ATDWLGSIVSINCGDSLGVYQGRVSAVDQVSQTISLTRPFHNGVKCLVPEVTFRAGDITELKILE 66
Cdd:cd01737    1 AEDFIGSAVSIHCGDTLGVYQGVISNVDPTNQTISLRKAFRNGLKCQVPEVTLSAKDIKDLKIIE 65
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 302-455 7.44e-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: 92.29  E-value: 7.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215598561  302 ERRLEMTGVCASQMALTLLggpnrlnpknVHQRPTVALLCGPHVKGAQGISCGRHLANHDVQVILF-LPNFVKMLESITN 380
Cdd:pfam03853   2 AVLMENAGRAAARVLKALL----------SPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLlLGPEEKLSEDARR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215598561  381 ELSLFSKTQGQ----QVSSLKDLPTSPVDLVINCLDcpeNVFLR--DQPWYKAAVAWANQNRAPVLSIDPPVheveqGID 454
Cdd:pfam03853  72 QLDLFKKLGGKivtdNPDEDLEKLLSPVDLIIDALL---GTGLSgpLRGEYAALIEWINQSGAPVLAVDIPS-----GLD 143


                  .
gi 215598561  455 A 455
Cdd:pfam03853 144 A 144
LSM14 pfam12701
Scd6-like Sm domain; The Scd6-like Sm domain is found in Scd6p from S. cerevisiae, Rap55 from ...
 4-67 1.11e-16

Scd6-like Sm domain; The Scd6-like Sm domain is found in Scd6p from S. cerevisiae, Rap55 from the newt Pleurodeles walt, and its orthologs from fungi, animals, plants and apicomplexans. The domain is also found in Dcp3p and the human EDC3/FLJ21128 protein where it is fused to the the Rossmanoid YjeF-N domain. In addition both EDC3 and Scd6p are found fused to the FDF domain.


Pssm-ID: 463675  Cd Length: 75  Bit Score: 74.46  E-value: 1.11e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 215598561    4 DWLGSIVSINCGDSLgVYQGRVSAVDQVSQTISLTRPFHNGVKCLVP------------EVTFRAGDITELKILEI 67
Cdd:pfam12701   1 PFIGSRISLISKSDI-RYEGILHSIDTEDSTITLKNVRSFGTEGRGPgpqeppsdevyeYIVFRGSDIKDLKILEP 75
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 332-443 2.91e-05

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: 46.40  E-value: 2.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215598561 332 HQRPTVALLCGPHVKGAQGISCGRHLANHDVQVILFLPNFVKML--ESITNeLSLFsKTQGQQVSSLKDLPTSP--VDLV 407
Cdd:COG0062   45 SAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLLGDPEKLsgDAAAN-LERL-KAAGIPILELDDELPELaeADLI 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 215598561 408 INCLdcpenvF-------LRDqpWYKAAVAWANQNRAPVLSID 443
Cdd:COG0062  123 VDAL------FgtglsrpLRG--PYAELIEAINASGAPVLAVD 157
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 285-365 2.20e-04

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 42.94  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215598561 285 ELHKKLLSVAekhGLTLERRLEMTGVCASQMALTLLGGPNRLNPKNVHQRptVALLCGPHVKGAQGISCGRHLAN--HDV 362
Cdd:PLN03050  16 ALDEELMSTP---GFSLEQLMELAGLSVAEAVYEVADGEKASNPPGRHPR--VLLVCGPGNNGGDGLVAARHLAHfgYEV 90


                 ...
gi 215598561 363 QVI 365
Cdd:PLN03050  91 TVC 93
 
Name Accession Description Interval E-value
Edc3_linker pfam16598
Linker region of enhancer of mRNA-decapping protein 3; This region is located between the ...
 102-194 2.95e-59

Linker region of enhancer of mRNA-decapping protein 3; This region is located between the LSM14 pfam12701 (Lsm) and FDF pfam09532 domains of the enhancer of mRNA-decapping protein 3. This region is predicted to be natively unstructured. Its precise functional role is not known.


Pssm-ID: 465188  Cd Length: 91  Bit Score: 190.18  E-value: 2.95e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215598561  102 KFVKKPASSSSAPQNIPKRTDVKSQDVAVSPQQqqCSKSYVDRHMESLSQSKSFRRRHNSWSSSSRHPNQATPKKSGLKN 181
Cdd:pfam16598   1 KTLKKPAISSSAPQAIPRRGDAKGQEKVNSPQQ--CSKSYGDRHLDSLGQSKGFRRRHNSWSSSSRGPNQATPKKNGVKN 78

                          90
                  ....*....|...
gi 215598561  182 GQMKNKDDECFGD 194
Cdd:pfam16598  79 GQMKSKDDECFGD 91
FDF pfam09532
FDF domain; The FDF domain, so called because of the conserved FDF at its N termini, is an ...
 198-301 8.46e-31

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: 115.24  E-value: 8.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215598561  198 EIPDTDFDFEGNLALFDKAAVFEEIDTYERRSGTRSRGIPNeRPTRYRHDENILESEPIVYRRIIVPHNVSKEFCTDSGL 277
Cdd:pfam09532   1 IKFDEDFDFESNNAKFNKQEVFAELRKNDKLDEEKRLVNEN-NATRVATNEQPNEEVKGVYKKDDFFDNISSEANDRGIQ 79

                          90       100
                  ....*....|....*....|....*
gi 215598561  278 VVPSISYELHKKLLSV-AEKHGLTL 301
Cdd:pfam09532  80 SGPSPSGRDWREERSLnTETFGVDS 104
LSm16_N cd01737
Like-Sm protein 16, N-terminal domain; LSm16 (also known as enhancer of decapping-3 or EDC3) ...
 2-66 1.14e-28

Like-Sm protein 16, N-terminal domain; LSm16 (also known as enhancer of decapping-3 or EDC3) has been shown to be associated with an mRNA-decapping complex Dcp1-Dcp2, required for removal of the 5-prime cap from mRNA prior to its degradation from the 5-prime end. EDC3 is believed to be a scaffold for decapping complex formation. It belongs to a family of Sm-like proteins that associate with RNA to form complexes involved in a variety of RNA processing events including pre-mRNA splicing, telomere replication, and mRNA degradation. Members of this family share a highly conserved Sm fold, containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet, that associates with other Sm proteins to form hexameric and heptameric ring structures. LSm16 has, in addition to its N-terminal Sm-like domain, a C-terminal Yjef_N-type Rossmann fold domain of unknown function.


Pssm-ID: 212484  Cd Length: 65  Bit Score: 107.79  E-value: 1.14e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 215598561   2 ATDWLGSIVSINCGDSLGVYQGRVSAVDQVSQTISLTRPFHNGVKCLVPEVTFRAGDITELKILE 66
Cdd:cd01737    1 AEDFIGSAVSIHCGDTLGVYQGVISNVDPTNQTISLRKAFRNGLKCQVPEVTLSAKDIKDLKIIE 65
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 302-455 7.44e-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: 92.29  E-value: 7.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215598561  302 ERRLEMTGVCASQMALTLLggpnrlnpknVHQRPTVALLCGPHVKGAQGISCGRHLANHDVQVILF-LPNFVKMLESITN 380
Cdd:pfam03853   2 AVLMENAGRAAARVLKALL----------SPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLlLGPEEKLSEDARR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215598561  381 ELSLFSKTQGQ----QVSSLKDLPTSPVDLVINCLDcpeNVFLR--DQPWYKAAVAWANQNRAPVLSIDPPVheveqGID 454
Cdd:pfam03853  72 QLDLFKKLGGKivtdNPDEDLEKLLSPVDLIIDALL---GTGLSgpLRGEYAALIEWINQSGAPVLAVDIPS-----GLD 143


                  .
gi 215598561  455 A 455
Cdd:pfam03853 144 A 144
LSM14 pfam12701
Scd6-like Sm domain; The Scd6-like Sm domain is found in Scd6p from S. cerevisiae, Rap55 from ...
 4-67 1.11e-16

Scd6-like Sm domain; The Scd6-like Sm domain is found in Scd6p from S. cerevisiae, Rap55 from the newt Pleurodeles walt, and its orthologs from fungi, animals, plants and apicomplexans. The domain is also found in Dcp3p and the human EDC3/FLJ21128 protein where it is fused to the the Rossmanoid YjeF-N domain. In addition both EDC3 and Scd6p are found fused to the FDF domain.


Pssm-ID: 463675  Cd Length: 75  Bit Score: 74.46  E-value: 1.11e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 215598561    4 DWLGSIVSINCGDSLgVYQGRVSAVDQVSQTISLTRPFHNGVKCLVP------------EVTFRAGDITELKILEI 67
Cdd:pfam12701   1 PFIGSRISLISKSDI-RYEGILHSIDTEDSTITLKNVRSFGTEGRGPgpqeppsdevyeYIVFRGSDIKDLKILEP 75
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 332-443 2.91e-05

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: 46.40  E-value: 2.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215598561 332 HQRPTVALLCGPHVKGAQGISCGRHLANHDVQVILFLPNFVKML--ESITNeLSLFsKTQGQQVSSLKDLPTSP--VDLV 407
Cdd:COG0062   45 SAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLLGDPEKLsgDAAAN-LERL-KAAGIPILELDDELPELaeADLI 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 215598561 408 INCLdcpenvF-------LRDqpWYKAAVAWANQNRAPVLSID 443
Cdd:COG0062  123 VDAL------FgtglsrpLRG--PYAELIEAINASGAPVLAVD 157
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 285-365 2.20e-04

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 42.94  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215598561 285 ELHKKLLSVAekhGLTLERRLEMTGVCASQMALTLLGGPNRLNPKNVHQRptVALLCGPHVKGAQGISCGRHLAN--HDV 362
Cdd:PLN03050  16 ALDEELMSTP---GFSLEQLMELAGLSVAEAVYEVADGEKASNPPGRHPR--VLLVCGPGNNGGDGLVAARHLAHfgYEV 90


                 ...
gi 215598561 363 QVI 365
Cdd:PLN03050  91 TVC 93
 
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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