NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|13385458|ref|NP_080240|]
View 

protein N-lysine methyltransferase METTL21A [Mus musculus]

Protein Classification

protein N-lysine methyltransferase family protein( domain architecture ID 10563300)

protein N-lysine methyltransferase family protein is a class I SAM-dependent methyltransferase that catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; similar to human METTL21D that specifically trimethylates 'Lys-315' of VCP/p97

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 25-190 3.08e-62

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


:

Pssm-ID: 313513  Cd Length: 172  Bit Score: 191.39  E-value: 3.08e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385458    25 SFANHTIQIRQDWRQlGVAAVVWDAAVVLSMYLEM------GAVELRGCSAVELGAGTGLVGIVAALL--GAQVTITDRK 96
Cdd:pfam10294   1 KLDNPGLRIEEDTGN-GIGGHVWDAAVVLSKYLEMkifkelGANNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385458    97 VALEFLKSNVEANlppHIQPKAVVKELTWGQNLES--FSPGEFDLILGADVIYLEDTFTDLLQTLGHLCSNNSVILLACR 174
Cdd:pfam10294  80 EALELLKKNIELN---ALSSKVVVKVLDWGENLPPdlFDGHPVDLILAADCVYNEDSFPLLEKTLKDLLGKESVILVAYK 156

                         170
                  ....*....|....*.
gi 13385458   175 IRYERDSNFLTMLERQ 190
Cdd:pfam10294 157 KRREAEKKFFKLLERF 172
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 25-190 3.08e-62

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 191.39  E-value: 3.08e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385458    25 SFANHTIQIRQDWRQlGVAAVVWDAAVVLSMYLEM------GAVELRGCSAVELGAGTGLVGIVAALL--GAQVTITDRK 96
Cdd:pfam10294   1 KLDNPGLRIEEDTGN-GIGGHVWDAAVVLSKYLEMkifkelGANNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385458    97 VALEFLKSNVEANlppHIQPKAVVKELTWGQNLES--FSPGEFDLILGADVIYLEDTFTDLLQTLGHLCSNNSVILLACR 174
Cdd:pfam10294  80 EALELLKKNIELN---ALSSKVVVKVLDWGENLPPdlFDGHPVDLILAADCVYNEDSFPLLEKTLKDLLGKESVILVAYK 156

                         170
                  ....*....|....*.
gi 13385458   175 IRYERDSNFLTMLERQ 190
Cdd:pfam10294 157 KRREAEKKFFKLLERF 172
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 69-141 3.70e-06

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 45.57  E-value: 3.70e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13385458  69 AVELGAGTGLVGIVAALL--GAQVTITDR-KVALEFLKSNVEANLPPHIQpkaVVkeltWGQNLESFSPGEFDLIL 141
Cdd:COG2813  53 VLDLGCGYGVIGLALAKRnpEARVTLVDVnARAVELARANAAANGLENVE---VL----WSDGLSGVPDGSFDLIL 121
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 63-170 7.48e-04

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 39.84  E-value: 7.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385458   63 ELRGCSAVELGAGTGLVGIVAALLGAQVTITDRKVAL----EFLKSNVEANLPPHIQPKAVVKEltwgqnLESFSpGEFD 138
Cdd:PLN02585 142 SLAGVTVCDAGCGTGSLAIPLALEGAIVSASDISAAMvaeaERRAKEALAALPPEVLPKFEAND------LESLS-GKYD 214

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 13385458  139 LILGADVI--YLEDTFTDLLQtlgHLCS--NNSVIL 170
Cdd:PLN02585 215 TVTCLDVLihYPQDKADGMIA---HLASlaEKRLII 247
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 54-141 4.66e-03

HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 36.76  E-value: 4.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385458    54 SMYLEMGAVELRGCSAVELGAGTGLVGIVAALLGAQVTITD-RKVALEFLKSNVEANlpphiqpkavVKELTWGQNlESF 132
Cdd:TIGR00537   8 SLLLEANLRELKPDDVLEIGAGTGLVAIRLKGKGKCILTTDiNPFAVKELRENAKLN----------NVGLDVVMT-DLF 76

                          90
                  ....*....|.
gi 13385458   133 SP--GEFDLIL 141
Cdd:TIGR00537  77 KGvrGKFDVIL 87
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 70-175 4.94e-03

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 35.48  E-value: 4.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385458  70 VELGAGTGLVGI-VAALLGAQVTITDR-KVALEFLKSNVEANLPPHIQpkavVKELTWGQNLEsFSPGEFDLILGADVI- 146
Cdd:cd02440   3 LDLGCGTGALALaLASGPGARVTGVDIsPVALELARKAAAALLADNVE----VLKGDAEELPP-EADESFDVIISDPPLh 77

                        90       100
                ....*....|....*....|....*....
gi 13385458 147 YLEDTFTDLLQTLGHLCSNNSVILLACRI 175
Cdd:cd02440  78 HLVEDLARFLEEARRLLKPGGVLVLTLVL 106
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 25-190 3.08e-62

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 191.39  E-value: 3.08e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385458    25 SFANHTIQIRQDWRQlGVAAVVWDAAVVLSMYLEM------GAVELRGCSAVELGAGTGLVGIVAALL--GAQVTITDRK 96
Cdd:pfam10294   1 KLDNPGLRIEEDTGN-GIGGHVWDAAVVLSKYLEMkifkelGANNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385458    97 VALEFLKSNVEANlppHIQPKAVVKELTWGQNLES--FSPGEFDLILGADVIYLEDTFTDLLQTLGHLCSNNSVILLACR 174
Cdd:pfam10294  80 EALELLKKNIELN---ALSSKVVVKVLDWGENLPPdlFDGHPVDLILAADCVYNEDSFPLLEKTLKDLLGKESVILVAYK 156

                         170
                  ....*....|....*.
gi 13385458   175 IRYERDSNFLTMLERQ 190
Cdd:pfam10294 157 KRREAEKKFFKLLERF 172
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 69-141 3.70e-06

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 45.57  E-value: 3.70e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13385458  69 AVELGAGTGLVGIVAALL--GAQVTITDR-KVALEFLKSNVEANLPPHIQpkaVVkeltWGQNLESFSPGEFDLIL 141
Cdd:COG2813  53 VLDLGCGYGVIGLALAKRnpEARVTLVDVnARAVELARANAAANGLENVE---VL----WSDGLSGVPDGSFDLIL 121
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 69-141 6.47e-05

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 41.81  E-value: 6.47e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13385458    69 AVELGAGTGLVGIVAALLGAQVTIT---DRKVALEFLKSNVEANLPPHIqpkavvkELTWGQNLESFSPGEFDLIL 141
Cdd:pfam05175  35 VLDLGCGAGVLGAALAKESPDAELTmvdINARALESARENLAANGLENG-------EVVASDVYSGVEDGKFDLII 103
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 64-172 1.17e-04

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 40.39  E-value: 1.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385458  64 LRGCSAVELGAGTGLVGIVAALLGAQVTITDR-KVALEFLKSNVEAnLPPHIQPKAVvkeltwgQNLEsFSPGEFDLILG 142
Cdd:COG2227  23 PAGGRVLDVGCGTGRLALALARRGADVTGVDIsPEALEIARERAAE-LNVDFVQGDL-------EDLP-LEDGSFDLVIC 93

                        90       100       110
                ....*....|....*....|....*....|
gi 13385458 143 ADVIYLEDTFTDLLQTLGHLCSNNSVILLA 172
Cdd:COG2227  94 SEVLEHLPDPAALLRELARLLKPGGLLLLS 123
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 63-170 7.48e-04

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 39.84  E-value: 7.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385458   63 ELRGCSAVELGAGTGLVGIVAALLGAQVTITDRKVAL----EFLKSNVEANLPPHIQPKAVVKEltwgqnLESFSpGEFD 138
Cdd:PLN02585 142 SLAGVTVCDAGCGTGSLAIPLALEGAIVSASDISAAMvaeaERRAKEALAALPPEVLPKFEAND------LESLS-GKYD 214

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 13385458  139 LILGADVI--YLEDTFTDLLQtlgHLCS--NNSVIL 170
Cdd:PLN02585 215 TVTCLDVLihYPQDKADGMIA---HLASlaEKRLII 247
PRK14968 PRK14968
putative methyltransferase; Provisional
 61-141 2.48e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 37.57  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385458   61 AVELRGCSAVELGAGTGLVGIVAALLGAQVTITD-----RKVALEFLKSNVEANLPPHIqpkaVVKELtwgqnLESFSPG 135
Cdd:PRK14968  19 AVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDinpyaVECAKCNAKLNNIRNNGVEV----IRSDL-----FEPFRGD 89


                 ....*.
gi 13385458  136 EFDLIL 141
Cdd:PRK14968  90 KFDVIL 95
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
70-107 4.11e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 36.81  E-value: 4.11e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 13385458  70 VELGAGTGLVGIVAALLGAQVTI---TDRKvALEFLKSNVE 107
Cdd:COG2263  50 LDLGCGTGMLAIGAALLGAKKVVgvdIDPE-ALEIARENAE 89
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 57-146 4.65e-03

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 37.25  E-value: 4.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385458    57 LEMgaVELRGCSAVELGAGTGLVGIVAALLGAQ-VTITD-RKVALEFLKSNVEANlppHIQPKAVVKeLTWGQNLEsfsp 134
Cdd:pfam06325 155 LER--LVKPGESVLDVGCGSGILAIAALKLGAKkVVGVDiDPVAVRAAKENAELN---GVEARLEVY-LPGDLPKE---- 224

                          90
                  ....*....|....*
gi 13385458   135 gEFDLILG---ADVI 146
Cdd:pfam06325 225 -KADVVVAnilADPL 238
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 54-141 4.66e-03

HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 36.76  E-value: 4.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385458    54 SMYLEMGAVELRGCSAVELGAGTGLVGIVAALLGAQVTITD-RKVALEFLKSNVEANlpphiqpkavVKELTWGQNlESF 132
Cdd:TIGR00537   8 SLLLEANLRELKPDDVLEIGAGTGLVAIRLKGKGKCILTTDiNPFAVKELRENAKLN----------NVGLDVVMT-DLF 76

                          90
                  ....*....|.
gi 13385458   133 SP--GEFDLIL 141
Cdd:TIGR00537  77 KGvrGKFDVIL 87
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 70-175 4.94e-03

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 35.48  E-value: 4.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385458  70 VELGAGTGLVGI-VAALLGAQVTITDR-KVALEFLKSNVEANLPPHIQpkavVKELTWGQNLEsFSPGEFDLILGADVI- 146
Cdd:cd02440   3 LDLGCGTGALALaLASGPGARVTGVDIsPVALELARKAAAALLADNVE----VLKGDAEELPP-EADESFDVIISDPPLh 77

                        90       100
                ....*....|....*....|....*....
gi 13385458 147 YLEDTFTDLLQTLGHLCSNNSVILLACRI 175
Cdd:cd02440  78 HLVEDLARFLEEARRLLKPGGVLVLTLVL 106
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
64-141 7.40e-03

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 36.69  E-value: 7.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385458  64 LRGCSAVELGAGTGLVGIVAALLGA-QVTITD-RKVALEFLKSNVEANlppHIQPKAVVKEltwgqnLESFSPGEFDLIL 141
Cdd:COG2264 147 KPGKTVLDVGCGSGILAIAAAKLGAkRVLAVDiDPVAVEAARENAELN---GVEDRIEVVL------GDLLEDGPYDLVV 217
NAD_bind_H4MPT_DH cd01078
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ...
 57-96 8.97e-03

NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene Tetrahydromethanopterin Dehydrogenase (H4MPT DH) NADP binding domain. NADP-dependent H4MPT DH catalyzes the dehydrogenation of methylene- H4MPT and methylene-tetrahydrofolate (H4F) with NADP+ as cofactor. H4F and H4MPT are both cofactors that carry the one-carbon units between the formyl and methyl oxidation level. H4F and H4MPT are structurally analogous to each other with respect to the pterin moiety, but each has distinct side chain. H4MPT is present only in anaerobic methanogenic archaea and aerobic methylotrophic proteobacteria. H4MPT seems to have evolved independently from H4F and functions as a distinct carrier in C1 metabolism. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133446 [Multi-domain]  Cd Length: 194  Bit Score: 35.83  E-value: 8.97e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 13385458  57 LEMGAVELRGCSAVELGaGTGLVGIVAALL----GAQVTITDRK 96
Cdd:cd01078  19 LELMGKDLKGKTAVVLG-GTGPVGQRAAVLlareGARVVLVGRD 61
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH