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Conserved domains on  [gi|46402315|ref|NP_997164|]
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protein-lysine methyltransferase METTL21E [Mus musculus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 106779)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 50-216 1.94e-33

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.).


The actual alignment was detected with superfamily member pfam10294:

Pssm-ID: 473071  Cd Length: 172  Bit Score: 118.97  E-value: 1.94e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46402315    50 FAGHEIQITE--GKDCyGAFVWPSALVLCYFLETHAKQ----YNMVDKNVIEIGAGTGLVSIVASLL--GARVIATDLPE 121
Cdd:pfam10294   2 LDNPGLRIEEdtGNGI-GGHVWDAAVVLSKYLEMKIFKelgaNNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46402315   122 LLGNLQYNISRN---TKMkckhlpQVKELSWGVALDRNFPrSSNNFDYILAADVVYAHPFLEELLMTFDHLCKETTIILW 198
Cdd:pfam10294  81 ALELLKKNIELNalsSKV------VVKVLDWGENLPPDLF-DGHPVDLILAADCVYNEDSFPLLEKTLKDLLGKESVILV 153

                         170
                  ....*....|....*...
gi 46402315   199 AMRFRLEKENKFVDKFKE 216
Cdd:pfam10294 154 AYKKRREAEKKFFKLLER 171
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 50-216 1.94e-33

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: 118.97  E-value: 1.94e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46402315    50 FAGHEIQITE--GKDCyGAFVWPSALVLCYFLETHAKQ----YNMVDKNVIEIGAGTGLVSIVASLL--GARVIATDLPE 121
Cdd:pfam10294   2 LDNPGLRIEEdtGNGI-GGHVWDAAVVLSKYLEMKIFKelgaNNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46402315   122 LLGNLQYNISRN---TKMkckhlpQVKELSWGVALDRNFPrSSNNFDYILAADVVYAHPFLEELLMTFDHLCKETTIILW 198
Cdd:pfam10294  81 ALELLKKNIELNalsSKV------VVKVLDWGENLPPDLF-DGHPVDLILAADCVYNEDSFPLLEKTLKDLLGKESVILV 153

                         170
                  ....*....|....*...
gi 46402315   199 AMRFRLEKENKFVDKFKE 216
Cdd:pfam10294 154 AYKKRREAEKKFFKLLER 171
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
78-172 1.55e-06

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 47.84  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46402315   78 FLETHAKQynmvDKNVIEIGAGTGLVSIVASLLGA-RVIATDLPEL-LGNLQYNISRNtkmkckhlpqvkelswGVALDR 155
Cdd:PRK00517 112 ALEKLVLP----GKTVLDVGCGSGILAIAAAKLGAkKVLAVDIDPQaVEAARENAELN----------------GVELNV 171

                         90       100
                 ....*....|....*....|
gi 46402315  156 NFPRSSNNFDYILA---ADV 172
Cdd:PRK00517 172 YLPQGDLKADVIVAnilANP 191
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 75-191 1.94e-05

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: 43.08  E-value: 1.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46402315  75 LCYFLETHAKQynmvDKNVIEIGAGTGLVSIVASLLGARVIATDL-PELLGNLQynisrntkmkcKHLPQVKeLSWGVAL 153
Cdd:COG2227  14 LAALLARLLPA----GGRVLDVGCGTGRLALALARRGADVTGVDIsPEALEIAR-----------ERAAELN-VDFVQGD 77

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 46402315 154 DRNFPRSSNNFDYILAADVVYaH-PFLEELLMTFDHLCK 191
Cdd:COG2227  78 LEDLPLEDGSFDLVICSEVLE-HlPDPAALLRELARLLK 115
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 91-135 4.68e-04

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: 39.84  E-value: 4.68e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 46402315    91 KNVIEIGAGTGLVSIVASLLGARVIATDL-PELLGNLQYNISRNTK 135
Cdd:TIGR00537  21 DDVLEIGAGTGLVAIRLKGKGKCILTTDInPFAVKELRENAKLNNV 66
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 92-183 5.94e-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: 5.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46402315  92 NVIEIGAGTGLVSI-VASLLGARVIATDL-PELLGNLQYNISRNTKMKCKHLPQvkelSWGVALDRNFPRssnnFDYILA 169
Cdd:cd02440   1 RVLDLGCGTGALALaLASGPGARVTGVDIsPVALELARKAAAALLADNVEVLKG----DAEELPPEADES----FDVIIS 72

                        90
                ....*....|....*....
gi 46402315 170 ADVVYA-----HPFLEELL 183
Cdd:cd02440  73 DPPLHHlvedlARFLEEAR 91
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 50-216 1.94e-33

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: 118.97  E-value: 1.94e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46402315    50 FAGHEIQITE--GKDCyGAFVWPSALVLCYFLETHAKQ----YNMVDKNVIEIGAGTGLVSIVASLL--GARVIATDLPE 121
Cdd:pfam10294   2 LDNPGLRIEEdtGNGI-GGHVWDAAVVLSKYLEMKIFKelgaNNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46402315   122 LLGNLQYNISRN---TKMkckhlpQVKELSWGVALDRNFPrSSNNFDYILAADVVYAHPFLEELLMTFDHLCKETTIILW 198
Cdd:pfam10294  81 ALELLKKNIELNalsSKV------VVKVLDWGENLPPDLF-DGHPVDLILAADCVYNEDSFPLLEKTLKDLLGKESVILV 153

                         170
                  ....*....|....*...
gi 46402315   199 AMRFRLEKENKFVDKFKE 216
Cdd:pfam10294 154 AYKKRREAEKKFFKLLER 171
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
78-172 1.55e-06

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 47.84  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46402315   78 FLETHAKQynmvDKNVIEIGAGTGLVSIVASLLGA-RVIATDLPEL-LGNLQYNISRNtkmkckhlpqvkelswGVALDR 155
Cdd:PRK00517 112 ALEKLVLP----GKTVLDVGCGSGILAIAAAKLGAkKVLAVDIDPQaVEAARENAELN----------------GVELNV 171

                         90       100
                 ....*....|....*....|
gi 46402315  156 NFPRSSNNFDYILA---ADV 172
Cdd:PRK00517 172 YLPQGDLKADVIVAnilANP 191
PRK14968 PRK14968
putative methyltransferase; Provisional
 90-119 5.52e-06

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 45.66  E-value: 5.52e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 46402315   90 DKNVIEIGAGTGLVSIVASLLGARVIATDL 119
Cdd:PRK14968  24 GDRVLEVGTGSGIVAIVAAKNGKKVVGVDI 53
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 74-133 1.57e-05

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: 44.95  E-value: 1.57e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46402315    74 VLC-YFLETHAKQynmvDKNVIEIGAGTGLVSIVASLLGA-RVIATDLPEL-LGNLQYNISRN 133
Cdd:pfam06325 149 KLClEALERLVKP----GESVLDVGCGSGILAIAALKLGAkKVVGVDIDPVaVRAAKENAELN 207
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 75-191 1.94e-05

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: 43.08  E-value: 1.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46402315  75 LCYFLETHAKQynmvDKNVIEIGAGTGLVSIVASLLGARVIATDL-PELLGNLQynisrntkmkcKHLPQVKeLSWGVAL 153
Cdd:COG2227  14 LAALLARLLPA----GGRVLDVGCGTGRLALALARRGADVTGVDIsPEALEIAR-----------ERAAELN-VDFVQGD 77

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 46402315 154 DRNFPRSSNNFDYILAADVVYaH-PFLEELLMTFDHLCK 191
Cdd:COG2227  78 LEDLPLEDGSFDLVICSEVLE-HlPDPAALLRELARLLK 115
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
78-133 3.97e-05

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 43.62  E-value: 3.97e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 46402315  78 FLETHAKQynmvDKNVIEIGAGTGLVSIVASLLGA-RVIATDL-PELLGNLQYNISRN 133
Cdd:COG2264 141 ALEKLLKP----GKTVLDVGCGSGILAIAAAKLGAkRVLAVDIdPVAVEAARENAELN 194
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 91-135 4.68e-04

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: 39.84  E-value: 4.68e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 46402315    91 KNVIEIGAGTGLVSIVASLLGARVIATDL-PELLGNLQYNISRNTK 135
Cdd:TIGR00537  21 DDVLEIGAGTGLVAIRLKGKGKCILTTDInPFAVKELRENAKLNNV 66
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 93-172 6.05e-04

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 37.93  E-value: 6.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46402315    93 VIEIGAGTGLVSI-VASLLGARVIATDL-PELLGNLQYNISRNTkmkckhlPQVKelsWGVALDRNFPRSSNNFDYILAA 170
Cdd:pfam13649   1 VLDLGCGTGRLTLaLARRGGARVTGVDLsPEMLERARERAAEAG-------LNVE---FVQGDAEDLPFPDGSFDLVVSS 70


                  ..
gi 46402315   171 DV 172
Cdd:pfam13649  71 GV 72
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
90-132 2.24e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 37.96  E-value: 2.24e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 46402315  90 DKNVIEIGAGTGLVSIVASLLGA-RVIATDL-PELLGNLQYNISR 132
Cdd:COG2263  46 GKTVLDLGCGTGMLAIGAALLGAkKVVGVDIdPEALEIARENAER 90
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 64-177 2.69e-03

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 37.97  E-value: 2.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46402315  64 YGAFVWPSALVLCYFLETHAKqynmvDKNVIEIGAGTGLVSIV-ASLLGARVIATDL-PELLGNLQyniSRNTKMKCKHL 141
Cdd:COG0500   6 YSDELLPGLAALLALLERLPK-----GGRVLDLGCGTGRNLLAlAARFGGRVIGIDLsPEAIALAR---ARAAKAGLGNV 77

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 46402315 142 pQVKELSWGVALDRNFPRssnnFDYILAADVVYAHP 177
Cdd:COG0500  78 -EFLVADLAELDPLPAES----FDLVVAFGVLHHLP 108
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 90-189 2.80e-03

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 36.90  E-value: 2.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46402315  90 DKNVIEIGAGTGLVSIVASLLGARVIATDL-PELLGNLQYNISRntkmkckhlpQVKELSWGVALDRNFPRSSNNFDYIL 168
Cdd:COG2226  23 GARVLDLGCGTGRLALALAERGARVTGVDIsPEMLELARERAAE----------AGLNVEFVVGDAEDLPFPDGSFDLVI 92

                        90       100
                ....*....|....*....|.
gi 46402315 169 AADVVYahpFLEELLMTFDHL 189
Cdd:COG2226  93 SSFVLH---HLPDPERALAEI 110
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
90-189 3.20e-03

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 37.29  E-value: 3.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46402315  90 DKNVIEIGAGTGLVSIVASLLGARVIATDlpellgnlqynISRNtkMkckhLPQVKELSWGVAL---D-RNFPRSSNNFD 165
Cdd:COG4976  47 FGRVLDLGCGTGLLGEALRPRGYRLTGVD-----------LSEE--M----LAKAREKGVYDRLlvaDlADLAEPDGRFD 109

                        90       100
                ....*....|....*....|....
gi 46402315 166 YILAADVVyahPFLEELLMTFDHL 189
Cdd:COG4976 110 LIVAADVL---TYLGDLAAVFAGV 130
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
90-189 4.46e-03

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 35.57  E-value: 4.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46402315  90 DKNVIEIGAGTGLVS--IVASLLGARVIATDL-PELLGNLQynisrntkmkcKHLPQVkelSWGVALDRNFPRSSnNFDY 166
Cdd:COG4106   2 PRRVLDLGCGTGRLTalLAERFPGARVTGVDLsPEMLARAR-----------ARLPNV---RFVVADLRDLDPPE-PFDL 66

                        90       100
                ....*....|....*....|...
gi 46402315 167 ILAADVVYahpFLEELLMTFDHL 189
Cdd:COG4106  67 VVSNAALH---WLPDHAALLARL 86
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 92-183 5.94e-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: 5.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46402315  92 NVIEIGAGTGLVSI-VASLLGARVIATDL-PELLGNLQYNISRNTKMKCKHLPQvkelSWGVALDRNFPRssnnFDYILA 169
Cdd:cd02440   1 RVLDLGCGTGALALaLASGPGARVTGVDIsPVALELARKAAAALLADNVEVLKG----DAEELPPEADES----FDVIIS 72

                        90
                ....*....|....*....
gi 46402315 170 ADVVYA-----HPFLEELL 183
Cdd:cd02440  73 DPPLHHlvedlARFLEEAR 91
 
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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