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Conserved domains on  [gi|1932703723|ref|XP_037522932|]
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histone-arginine methyltransferase METTL23 [Rhipicephalus sanguineus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10008106)

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; similar to Homo sapiens electron transfer flavoprotein beta subunit lysine methyltransferase

CATH:  3.40.50.150
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168|GO:0032259|GO:0008757
PubMed:  12826405|12504684
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 46-163 1.87e-26

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 102.27  E-value: 1.87e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932703723  46 DPSYGMYVWPCSPVLAQYLWfNREHIKGKRILEIGAGTGLPGILAALLGA-RVTLSDSSPLGLKNCQRNVEANGLTaneV 124
Cdd:COG3897    45 PPPFWAFLWPSGQALARYLL-DHPEVAGKRVLELGCGLGLVGIAAAKAGAaDVTATDYDPEALAALRLNAALNGVA---I 120

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1932703723 125 PVVSISWGLFNPAlfqlGPIDIILGSDCFYDPKDFENII 163
Cdd:COG3897   121 TTRLGDWRDPPAA----GGFDLILGGDVLYERDLAEPLL 155
 
Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 46-163 1.87e-26

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 102.27  E-value: 1.87e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932703723  46 DPSYGMYVWPCSPVLAQYLWfNREHIKGKRILEIGAGTGLPGILAALLGA-RVTLSDSSPLGLKNCQRNVEANGLTaneV 124
Cdd:COG3897    45 PPPFWAFLWPSGQALARYLL-DHPEVAGKRVLELGCGLGLVGIAAAKAGAaDVTATDYDPEALAALRLNAALNGVA---I 120

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1932703723 125 PVVSISWGLFNPAlfqlGPIDIILGSDCFYDPKDFENII 163
Cdd:COG3897   121 TTRLGDWRDPPAA----GGFDLILGGDVLYERDLAEPLL 155
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 34-186 4.25e-23

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: 92.01  E-value: 4.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932703723  34 KESLTVKIIEMMDPSYGMYVWPCSPVLAQYL------WFNREHIKGKRILEIGAGTGLPGILAALL--GARVTLSDSSPL 105
Cdd:pfam10294   2 LDNPGLRIEEDTGNGIGGHVWDAAVVLSKYLemkifkELGANNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEEA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932703723 106 gLKNCQRNVEANGLTaNEVPVVSISWGL-FNPALFQLGPIDIILGSDCFYDPKDFENIIVTVSYLLhqNPHGRFWCTYQI 184
Cdd:pfam10294  82 -LELLKKNIELNALS-SKVVVKVLDWGEnLPPDLFDGHPVDLILAADCVYNEDSFPLLEKTLKDLL--GKESVILVAYKK 157


                  ..
gi 1932703723 185 RS 186
Cdd:pfam10294 158 RR 159
PRK14968 PRK14968
putative methyltransferase; Provisional
 72-127 1.06e-08

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 53.36  E-value: 1.06e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1932703723  72 KGKRILEIGAGTGLPGILAALLGARVTLSDSSPLGLKNCQRNVEANGLTANEVPVV 127
Cdd:PRK14968   23 KGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNNGVEVI 78
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 67-118 1.91e-06

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: 46.77  E-value: 1.91e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1932703723  67 NREHIKGKRILEIGAGTGLPGILAALLGARVTLSDSSPLGLKNCQRNVEANG 118
Cdd:TIGR00537  14 NLRELKPDDVLEIGAGTGLVAIRLKGKGKCILTTDINPFAVKELRENAKLNN 65
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 75-182 6.54e-05

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: 41.26  E-value: 6.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932703723  75 RILEIGAGTGLPGI-LAALLGARVTLSDSSPLGLKNCQRNVEANGltANEVPVVSISWGLFNPALFqlGPIDIILGSDCF 153
Cdd:cd02440     1 RVLDLGCGTGALALaLASGPGARVTGVDISPVALELARKAAAALL--ADNVEVLKGDAEELPPEAD--ESFDVIISDPPL 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 1932703723 154 -YDPKDFENIIVTVSYLLhqNPHGRFWCTY 182
Cdd:cd02440    77 hHLVEDLARFLEEARRLL--KPGGVLVLTL 104
 
Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 46-163 1.87e-26

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 102.27  E-value: 1.87e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932703723  46 DPSYGMYVWPCSPVLAQYLWfNREHIKGKRILEIGAGTGLPGILAALLGA-RVTLSDSSPLGLKNCQRNVEANGLTaneV 124
Cdd:COG3897    45 PPPFWAFLWPSGQALARYLL-DHPEVAGKRVLELGCGLGLVGIAAAKAGAaDVTATDYDPEALAALRLNAALNGVA---I 120

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1932703723 125 PVVSISWGLFNPAlfqlGPIDIILGSDCFYDPKDFENII 163
Cdd:COG3897   121 TTRLGDWRDPPAA----GGFDLILGGDVLYERDLAEPLL 155
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 34-186 4.25e-23

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: 92.01  E-value: 4.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932703723  34 KESLTVKIIEMMDPSYGMYVWPCSPVLAQYL------WFNREHIKGKRILEIGAGTGLPGILAALL--GARVTLSDSSPL 105
Cdd:pfam10294   2 LDNPGLRIEEDTGNGIGGHVWDAAVVLSKYLemkifkELGANNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEEA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932703723 106 gLKNCQRNVEANGLTaNEVPVVSISWGL-FNPALFQLGPIDIILGSDCFYDPKDFENIIVTVSYLLhqNPHGRFWCTYQI 184
Cdd:pfam10294  82 -LELLKKNIELNALS-SKVVVKVLDWGEnLPPDLFDGHPVDLILAADCVYNEDSFPLLEKTLKDLL--GKESVILVAYKK 157


                  ..
gi 1932703723 185 RS 186
Cdd:pfam10294 158 RR 159
PRK14968 PRK14968
putative methyltransferase; Provisional
 72-127 1.06e-08

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 53.36  E-value: 1.06e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1932703723  72 KGKRILEIGAGTGLPGILAALLGARVTLSDSSPLGLKNCQRNVEANGLTANEVPVV 127
Cdd:PRK14968   23 KGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNNGVEVI 78
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 45-159 1.46e-08

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: 51.94  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932703723  45 MDPSYGMYVWpcSPVLAQYLwfNREHIKGKRILEIGAGTGLPGILAALLGARVTLSDSSPLGLKNCQRNVEANGLTANEV 124
Cdd:COG2227     1 MSDPDARDFW--DRRLAALL--ARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNVDFVQG 76

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1932703723 125 PVVSISwglfnpalFQLGPIDIILGSDCFY---DPKDF 159
Cdd:COG2227    77 DLEDLP--------LEDGSFDLVICSEVLEhlpDPAAL 106
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
72-148 3.85e-07

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 49.79  E-value: 3.85e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1932703723  72 KGKRILEIGAGTGLPGILAALLGA-RVTLSDSSPLGLKNCQRNVEANGLtANEVPVvsiswglFNPALFQLGPIDIIL 148
Cdd:COG2264   148 PGKTVLDVGCGSGILAIAAAKLGAkRVLAVDIDPVAVEAARENAELNGV-EDRIEV-------VLGDLLEDGPYDLVV 217
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 72-122 1.41e-06

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: 46.53  E-value: 1.41e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1932703723  72 KGKRILEIGAGTGLPGILAALLGARVTLSDSSPLGLKNCQRNVEANGLTAN 122
Cdd:COG2226    22 PGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVE 72
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 59-120 1.46e-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: 47.49  E-value: 1.46e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1932703723  59 VLAQYLwfnrEHIKGKRILEIGAGTGLPGILAALL--GARVTLSDSSPLGLKNCQRNVEANGLT 120
Cdd:COG2813    40 LLLEHL----PEPLGGRVLDLGCGYGVIGLALAKRnpEARVTLVDVNARAVELARANAAANGLE 99
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 56-155 1.86e-06

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 47.22  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932703723  56 CSPVLAQYLWFNREHIKGKRILEIGAGTG-LPGILAALLGARVTLSDSSPLGLKNCQRNVEANGLTANEVPVVSiswgLF 134
Cdd:COG0500    10 LLPGLAALLALLERLPKGGRVLDLGCGTGrNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVAD----LA 85

                          90       100
                  ....*....|....*....|.
gi 1932703723 135 NPALFQLGPIDIILGSDCFYD 155
Cdd:COG0500    86 ELDPLPAESFDLVVAFGVLHH 106
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 67-118 1.91e-06

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: 46.77  E-value: 1.91e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1932703723  67 NREHIKGKRILEIGAGTGLPGILAALLGARVTLSDSSPLGLKNCQRNVEANG 118
Cdd:TIGR00537  14 NLRELKPDDVLEIGAGTGLVAIRLKGKGKCILTTDINPFAVKELRENAKLNN 65
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 76-122 2.53e-06

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 44.86  E-value: 2.53e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1932703723  76 ILEIGAGTGLPGI-LAALLGARVTLSDSSPLGLKNCQRNVEANGLTAN 122
Cdd:pfam13649   1 VLDLGCGTGRLTLaLARRGGARVTGVDLSPEMLERARERAAEAGLNVE 48
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
58-122 3.62e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 46.44  E-value: 3.62e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1932703723  58 PVLAQYLWFN---REHIKGKRILEIGAGTGLPGILAALLGA-RVTLSDSSPLGLKNCQRNVEANGLTAN 122
Cdd:COG2263    28 AELAAELLHLaylRGDIEGKTVLDLGCGTGMLAIGAALLGAkKVVGVDIDPEALEIARENAERLGVRVD 96
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 72-179 7.48e-06

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 45.52  E-value: 7.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932703723  72 KGKRILEIGAGTGLPGILAA--LLGARVTLSDSSPLGLKNCQRNVEANGLtANEVPVVSISWGLFnPALFQLGPIDIILg 149
Cdd:COG4123    37 KGGRVLDLGTGTGVIALMLAqrSPGARITGVEIQPEAAELARRNVALNGL-EDRITVIHGDLKEF-AAELPPGSFDLVV- 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1932703723 150 sdC---FYDPK-------------------DFENIIVTVSYLLhqNPHGRFW 179
Cdd:COG4123   114 --SnppYFKAGsgrkspdearaiarhedalTLEDLIRAAARLL--KPGGRFA 161
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
72-122 2.09e-05

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 44.37  E-value: 2.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1932703723  72 KGKRILEIGAGTGLPGILAALLGA-RVTLSDSSPLGLKNCQRNVEANGLTAN 122
Cdd:PRK00517  119 PGKTVLDVGCGSGILAIAAAKLGAkKVLAVDIDPQAVEAARENAELNGVELN 170
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
72-122 3.07e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 43.87  E-value: 3.07e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1932703723  72 KGKRILEIGAGTGLPGILAALLGAR-VTLSDSSPLGLKNCQRNVEANGLTAN 122
Cdd:COG4076    35 PGDVVLDIGTGSGLLSMLAARAGAKkVYAVEVNPDIAAVARRIIAANGLSDR 86
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 69-148 5.24e-05

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 43.60  E-value: 5.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932703723  69 EHIKGKRILEIGAGTGlpGILAALL----GARVTLSDSSPLGLKNCQRNVEANGLtANEVPVVSISWglFNPaLFQLGPI 144
Cdd:COG2890   109 PAGAPPRVLDLGTGSG--AIALALAkerpDARVTAVDISPDALAVARRNAERLGL-EDRVRFLQGDL--FEP-LPGDGRF 182


                  ....
gi 1932703723 145 DIIL 148
Cdd:COG2890   183 DLIV 186
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 73-120 5.63e-05

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 42.22  E-value: 5.63e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1932703723  73 GKRILEIGAGTGLPGI-LAALLGARVTLSDSSPLGLKNCQRNVEANGLT 120
Cdd:COG2230    52 GMRVLDIGCGWGGLALyLARRYGVRVTGVTLSPEQLEYARERAAEAGLA 100
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 75-182 6.54e-05

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: 41.26  E-value: 6.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932703723  75 RILEIGAGTGLPGI-LAALLGARVTLSDSSPLGLKNCQRNVEANGltANEVPVVSISWGLFNPALFqlGPIDIILGSDCF 153
Cdd:cd02440     1 RVLDLGCGTGALALaLASGPGARVTGVDISPVALELARKAAAALL--ADNVEVLKGDAEELPPEAD--ESFDVIISDPPL 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 1932703723 154 -YDPKDFENIIVTVSYLLhqNPHGRFWCTY 182
Cdd:cd02440    77 hHLVEDLARFLEEARRLL--KPGGVLVLTL 104
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 57-124 8.04e-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: 8.04e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932703723  57 SPVLAQYLwfnrEHIKGKRILEIGAGTGLPGILAALLG--ARVTLSDSSPLGLKNCQRNVEANGLTANEV 124
Cdd:pfam05175  20 SRLLLEHL----PKDLSGKVLDLGCGAGVLGAALAKESpdAELTMVDINARALESARENLAANGLENGEV 85
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
72-114 5.13e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 38.27  E-value: 5.13e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1932703723  72 KGKRILEIGAGTG--LPGILAALLGARVTLSDSSPLGLKNCQRNV 114
Cdd:COG4106     1 PPRRVLDLGCGTGrlTALLAERFPGARVTGVDLSPEMLARARARL 45
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 77-153 1.05e-03

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 37.35  E-value: 1.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1932703723  77 LEIGAGTG--LPGILAALLGARVTLSDSSPLGLKNCQRNVEANGLTANEVpvvsISWGLFNPALFQLGPIDIILGSDCF 153
Cdd:pfam08242   1 LEIGCGTGtlLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVR----VELFQLDLGELDPGSFDVVVASNVL 75
TRM1 COG1867
tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N, ...
 66-124 2.03e-03

tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N,N-dimethylase Trm1 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441472  Cd Length: 383  Bit Score: 38.70  E-value: 2.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932703723  66 FNREHIKGKRILEIGAGTGLPGILAAL-LGARVTLSDSSPLGLKNCQRNVEANGLTANEV 124
Cdd:COG1867    51 YRERLKREISYLDALAASGIRGLRYALeVGIKVTLNDIDPEAVELIRENLELNGLEDVEV 110
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 68-122 2.08e-03

23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 39.01  E-value: 2.08e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1932703723  68 REHIKGKRILEIGAGTGLPGILAALLGARVTLS-DSSPLGLKNCQRNVEANGLTAN 122
Cdd:COG1092   212 AELAKGKRVLNLFSYTGGFSVHAAAGGAKSVTSvDLSATALEWAKENAALNGLDDR 267
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 72-198 2.59e-03

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 37.41  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932703723  72 KGKRILEIGAGTGLPGILAALLGARVTLSDSSPlglkncqRNVEANGLTANEVPVVSISWglfnpaLFQLGPIDIILGSD 151
Cdd:pfam13489  22 SPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSP-------IAIERALLNVRFDQFDEQEA------AVPAGKFDVIVARE 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1932703723 152 CFYDPKDFENIIVTVSYLLhqNPHGrfWCTYQIRSADYSMEGLLRQW 198
Cdd:pfam13489  89 VLEHVPDPPALLRQIAALL--KPGG--LLLLSTPLASDEADRLLLEW 131
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 77-120 3.24e-03

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 36.10  E-value: 3.24e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1932703723  77 LEIGAGTGLPGILAALLGARVTLSDSSPLGLKNCQRNVEANGLT 120
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLT 44
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 72-147 3.58e-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: 38.02  E-value: 3.58e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1932703723  72 KGKRILEIGAGTGLPGILAALLGA-RVTLSDSSPLGLKNCQRNVEANGLTANEVpvvsiswgLFNPALFQLGPIDII 147
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAkKVVGVDIDPVAVRAAKENAELNGVEARLE--------VYLPGDLPKEKADVV 229
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
 67-171 3.61e-03

Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member of the medium chain dehydrogenase/ reductase (MDR) family. Riticulons are endoplasmic reticulum associated proteins involved in membrane trafficking and neuroendocrine secretion. The MDR/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176210 [Multi-domain]  Cd Length: 350  Bit Score: 37.97  E-value: 3.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932703723  67 NREHIKGKRILEIGAGTGLPGILAALL---GARVT---LSDSSPLglkncqrnveANGLTANEvpVVSISWGLFNPALFQ 140
Cdd:cd08248   157 NPKNAAGKRVLILGGSGGVGTFAIQLLkawGAHVTttcSTDAIPL----------VKSLGADD--VIDYNNEDFEEELTE 224

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1932703723 141 LGPIDIILgsDC-------FYDP--KDFENIIVTVSYLLH 171
Cdd:cd08248   225 RGKFDVIL--DTvggdtekWALKllKKGGTYVTLVSPLLK 262
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
70-121 3.85e-03

16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 38.00  E-value: 3.85e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1932703723  70 HIKGKrILEIGAGTGlpgILAALLG-----ARVTLSDSSPLGLKNCQRNVEANGLTA 121
Cdd:PRK09489  195 HTKGK-VLDVGCGAG---VLSAVLArhspkIRLTLSDVSAAALESSRATLAANGLEG 247
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 72-124 3.92e-03

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 36.54  E-value: 3.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1932703723  72 KGKRILEIGAGTGLPGILAALL--GARVTLSDSSPLGLKNCQRNVEANGLTANEV 124
Cdd:TIGR02469  19 PGDVLWDIGAGTGSVTIEAARLvpNGRVYAIERNPEALDLIERNLRRFGVSNIVI 73
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 72-182 5.49e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 36.24  E-value: 5.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932703723  72 KGKRILEIGAGTGLPGILAALL---GARVTLSDSSPLGLKNCQRNVEANGLTANEVPVVSIswglFN-PALFQLGPIDII 147
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEElgpNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDI----EElPELLEDDKFDVV 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1932703723 148 LGSDCFYDPKDFENIIVTVSYLLHqnPHGRFWCTY 182
Cdd:pfam13847  79 ISNCVLNHIPDPDKVLQEILRVLK--PGGRLIISD 111
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 72-111 5.98e-03

16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ribosomal structure and biogenesis]; 16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440126  Cd Length: 211  Bit Score: 36.67  E-value: 5.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1932703723  72 KGKRILEIGAGTGLPGI-LAALL-GARVTLSDSSP------------LGLKNCQ 111
Cdd:COG0357    67 EGARVLDVGSGAGFPGIpLAIARpDLQVTLVDSLGkkiaflrevvreLGLKNVT 120
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 72-104 6.40e-03

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 36.74  E-value: 6.40e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1932703723  72 KGKRILEIGAGTGLPGILAALLGARVTLSDSSP 104
Cdd:PRK07580   63 TGLRILDAGCGVGSLSIPLARRGAKVVASDISP 95
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 71-148 7.06e-03

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 36.32  E-value: 7.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932703723  71 IKGKRILEIGAGTGLPGI-LAALL--GARVTLSDSSPLGLKNCQRNVEANGLTANevpvVSISWGlfnPALFQL-----G 142
Cdd:COG4122    15 LGAKRILEIGTGTGYSTLwLARALpdDGRLTTIEIDPERAAIARENFARAGLADR----IRLILG---DALEVLprladG 87


                  ....*.
gi 1932703723 143 PIDIIL 148
Cdd:COG4122    88 PFDLVF 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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