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Conserved domains on  [gi|148703527|gb|EDL35474|]
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RIKEN cDNA 6430573F11, isoform CRA_e [Mus musculus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10789277)

class I SAM-dependent methyltransferase is an enzyme that uses S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyl transfer, creating the product S-adenosyl-L-homocysteine (AdoHcy)

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:1904047
PubMed:  12826405
SCOP:  3000118

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 26-111 2.81e-14

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: 64.63  E-value: 2.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148703527  26 DLQSKAWPRVRQFLQ--DQKPGSLVADIGCGTGKYLK--VNSQVHTLGCDYCGPLVEIARNR------GCEVMVCDNLNL 95
Cdd:COG2226    2 DRVAARYDGREALLAalGLRPGARVLDLGCGTGRLALalAERGARVTGVDISPEMLELARERaaeaglNVEFVVGDAEDL 81

                         90
                 ....*....|....*.
gi 148703527  96 PFRDQGFDAIISIGAI 111
Cdd:COG2226   82 PFPDGSFDLVISSFVL 97
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 26-111 2.81e-14

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: 64.63  E-value: 2.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148703527  26 DLQSKAWPRVRQFLQ--DQKPGSLVADIGCGTGKYLK--VNSQVHTLGCDYCGPLVEIARNR------GCEVMVCDNLNL 95
Cdd:COG2226    2 DRVAARYDGREALLAalGLRPGARVLDLGCGTGRLALalAERGARVTGVDISPEMLELARERaaeaglNVEFVVGDAEDL 81

                         90
                 ....*....|....*.
gi 148703527  96 PFRDQGFDAIISIGAI 111
Cdd:COG2226   82 PFPDGSFDLVISSFVL 97
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 48-111 4.57e-12

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 57.57  E-value: 4.57e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148703527   48 VADIGCGTGKYL-----KVNSQVHtlGCDYCGPLVEIARNRG------CEVMVCDNLNLPFRDQGFDAIISIGAI 111
Cdd:pfam13649   1 VLDLGCGTGRLTlalarRGGARVT--GVDLSPEMLERARERAaeaglnVEFVQGDAEDLPFPDGSFDLVVSSGVL 73
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 13-109 8.79e-09

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 51.31  E-value: 8.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148703527  13 VHSVYENTAP-YftDL--------QSKAWprvRQFLQDQ---KPGSLVADIGCGTGKYL-----KVNSQVHTLGCDYCGP 75
Cdd:PRK00216  13 VAEMFDSIAPkY--DLmndllsfgLHRVW---RRKTIKWlgvRPGDKVLDLACGTGDLAialakAVGKTGEVVGLDFSEG 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 148703527  76 LVEIARNR--------GCEVMVCDNLNLPFRDQGFDAiISIG 109
Cdd:PRK00216  88 MLAVGREKlrdlglsgNVEFVQGDAEALPFPDNSFDA-VTIA 128
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 48-107 6.16e-05

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 40.73  E-value: 6.16e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148703527   48 VADIGCGTG----KYLKVNSQVHTLGCDYCGPLVEIARNRGCEVM--VCDNL-NLPFRDQGFDAIIS 107
Cdd:TIGR02072  38 VLDIGCGTGyltrALLKRFPQAEFIALDISAGMLAQAKTKLSENVqfICGDAeKLPLEDSSFDLIVS 104
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 48-112 3.58e-04

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: 37.41  E-value: 3.58e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148703527  48 VADIGCGTGKY---LKVNSQVHTLGCDYCGPLVEIARNR-------GCEVMVCDNLNLPF-RDQGFDAIISIGAIS 112
Cdd:cd02440    2 VLDLGCGTGALalaLASGPGARVTGVDISPVALELARKAaaalladNVEVLKGDAEELPPeADESFDVIISDPPLH 77
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 26-111 2.81e-14

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: 64.63  E-value: 2.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148703527  26 DLQSKAWPRVRQFLQ--DQKPGSLVADIGCGTGKYLK--VNSQVHTLGCDYCGPLVEIARNR------GCEVMVCDNLNL 95
Cdd:COG2226    2 DRVAARYDGREALLAalGLRPGARVLDLGCGTGRLALalAERGARVTGVDISPEMLELARERaaeaglNVEFVVGDAEDL 81

                         90
                 ....*....|....*.
gi 148703527  96 PFRDQGFDAIISIGAI 111
Cdd:COG2226   82 PFPDGSFDLVISSFVL 97
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 48-111 4.57e-12

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 57.57  E-value: 4.57e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148703527   48 VADIGCGTGKYL-----KVNSQVHtlGCDYCGPLVEIARNRG------CEVMVCDNLNLPFRDQGFDAIISIGAI 111
Cdd:pfam13649   1 VLDLGCGTGRLTlalarRGGARVT--GVDLSPEMLERARERAaeaglnVEFVQGDAEDLPFPDGSFDLVVSSGVL 73
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 25-111 2.15e-10

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: 54.25  E-value: 2.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148703527  25 TDLQSKAW-PRVRQFLQDQ-KPGSLVADIGCGTGKYLKV----NSQVHtlGCDYCGPLVEIARNR----GCEVMVCDNLN 94
Cdd:COG2227    3 DPDARDFWdRRLAALLARLlPAGGRVLDVGCGTGRLALAlarrGADVT--GVDISPEALEIARERaaelNVDFVQGDLED 80

                         90
                 ....*....|....*..
gi 148703527  95 LPFRDQGFDAIISIGAI 111
Cdd:COG2227   81 LPLEDGSFDLVICSEVL 97
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 50-111 6.00e-09

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 49.59  E-value: 6.00e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148703527   50 DIGCGTGKYLKVNSQV--HTLGCDYCGPLVEIAR----NRGCEVMVCDNLNLPFRDQGFDAIISIGAI 111
Cdd:pfam08241   2 DVGCGTGLLTELLARLgaRVTGVDISPEMLELARekapREGLTFVVGDAEDLPFPDNSFDLVLSSEVL 69
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 23-112 8.42e-09

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 51.07  E-value: 8.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148703527  23 YFTDLQSKAWPRVRQFLQDQKPGSLVADIGCGTGKYL-----KVNSQVhtLGCDYCGPLVEIARNR-------GCEVMVC 90
Cdd:COG0500    5 YYSDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLlalaaRFGGRV--IGIDLSPEAIALARARaakaglgNVEFLVA 82

                         90       100
                 ....*....|....*....|...
gi 148703527  91 DNLNL-PFRDQGFDAIISIGAIS 112
Cdd:COG0500   83 DLAELdPLPAESFDLVVAFGVLH 105
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 13-109 8.79e-09

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 51.31  E-value: 8.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148703527  13 VHSVYENTAP-YftDL--------QSKAWprvRQFLQDQ---KPGSLVADIGCGTGKYL-----KVNSQVHTLGCDYCGP 75
Cdd:PRK00216  13 VAEMFDSIAPkY--DLmndllsfgLHRVW---RRKTIKWlgvRPGDKVLDLACGTGDLAialakAVGKTGEVVGLDFSEG 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 148703527  76 LVEIARNR--------GCEVMVCDNLNLPFRDQGFDAiISIG 109
Cdd:PRK00216  88 MLAVGREKlrdlglsgNVEFVQGDAEALPFPDNSFDA-VTIA 128
PRK08317 PRK08317
hypothetical protein; Provisional
 22-107 6.42e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 49.16  E-value: 6.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148703527  22 PYFTDLQSkawpRVRQFLQDQkPGSLVADIGCGTG---KYLK--VNSQVHTLGCDYCGPLVEIARNRGC------EVMVC 90
Cdd:PRK08317   2 PDFRRYRA----RTFELLAVQ-PGDRVLDVGCGPGndaRELArrVGPEGRVVGIDRSEAMLALAKERAAglgpnvEFVRG 76

                         90
                 ....*....|....*..
gi 148703527  91 DNLNLPFRDQGFDAIIS 107
Cdd:PRK08317  77 DADGLPFPDGSFDAVRS 93
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
10-125 9.11e-08

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 48.07  E-value: 9.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148703527  10 RRHVHSVYENTAPYF-----TDLQSKAWPRVRQFLQDQ---KPGSLVADIGCGTG---KYLKvNSQVHTLGCDYCGPLVE 78
Cdd:COG4976    4 DAYVEALFDQYADSYdaalvEDLGYEAPALLAEELLARlppGPFGRVLDLGCGTGllgEALR-PRGYRLTGVDLSEEMLA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 148703527  79 IARNRGC--EVMVCDNLNLPFRDQGFDAIISIGaisggslkVLTYADPL 125
Cdd:COG4976   83 KAREKGVydRLLVADLADLAEPDGRFDLIVAAD--------VLTYLGDL 123
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 43-111 3.31e-06

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 43.76  E-value: 3.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148703527  43 KPGSLVADIGCGTG---KYLKVNSQVHTLGCDYCGPLVEIARNR--------GCEVMVCDNLNLPFrDQGFDAIISIGAI 111
Cdd:COG2230   50 KPGMRVLDIGCGWGglaLYLARRYGVRVTGVTLSPEQLEYARERaaeagladRVEVRLADYRDLPA-DGQFDAIVSIGMF 128
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
44-111 4.49e-06

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 42.12  E-value: 4.49e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148703527  44 PGSLVADIGCGTGKYLKV----NSQVHTLGCDYCGPLVEIARNR--GCEVMVCDNLNLPFrDQGFDAIISIGAI 111
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALlaerFPGARVTGVDLSPEMLARARARlpNVRFVVADLRDLDP-PEPFDLVVSNAAL 73
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 43-121 1.98e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 41.25  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148703527   43 KPGSLVADIGCGTGKYL-----KVNSQVHTLGCDYCGPLVEIARNR-------GCEVMVCDNLNLP--FRDQGFDAIISI 108
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSfelaeELGPNAEVVGIDISEEAIEKARENaqklgfdNVEFEQGDIEELPelLEDDKFDVVISN 81

                          90
                  ....*....|...
gi 148703527  109 GAISGGSLKVLTY 121
Cdd:pfam13847  82 CVLNHIPDPDKVL 94
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 48-107 6.16e-05

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 40.73  E-value: 6.16e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148703527   48 VADIGCGTG----KYLKVNSQVHTLGCDYCGPLVEIARNRGCEVM--VCDNL-NLPFRDQGFDAIIS 107
Cdd:TIGR02072  38 VLDIGCGTGyltrALLKRFPQAEFIALDISAGMLAQAKTKLSENVqfICGDAeKLPLEDSSFDLIVS 104
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 13-109 6.38e-05

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 40.71  E-value: 6.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148703527   13 VHSVYENTAPYFTDL-------QSKAWprvRQFLQDQ---KPGSLVADIGCGTG----KYLKVNSQV-HTLGCDYCGPLV 77
Cdd:TIGR01934   1 VQEMFDRIAPKYDLLndllsfgLHRLW---RRRAVKLigvFKGQKVLDVACGTGdlaiELAKSAPDRgKVTGVDFSSEML 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 148703527   78 EIARNRGC-----EVMVCDNLNLPFRDQGFDAI-ISIG 109
Cdd:TIGR01934  78 EVAKKKSElplniEFIQADAEALPFEDNSFDAVtIAFG 115
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 41-107 2.28e-04

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 39.35  E-value: 2.28e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148703527  41 DQKPGSLVADIGCGTGK---YLKVNSQVHTLGCDYCGPLVEIA------RNRGCEVMVCDNLNLPFRDQGFDAIIS 107
Cdd:PLN02336 263 DLKPGQKVLDVGCGIGGgdfYMAENFDVHVVGIDLSVNMISFAleraigRKCSVEFEVADCTKKTYPDNSFDVIYS 338
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 48-112 3.58e-04

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: 37.41  E-value: 3.58e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148703527  48 VADIGCGTGKY---LKVNSQVHTLGCDYCGPLVEIARNR-------GCEVMVCDNLNLPF-RDQGFDAIISIGAIS 112
Cdd:cd02440    2 VLDLGCGTGALalaLASGPGARVTGVDISPVALELARKAaaalladNVEVLKGDAEELPPeADESFDVIISDPPLH 77
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 50-112 4.44e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 36.96  E-value: 4.44e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148703527   50 DIGCGTG----KYLKVNSQVHTLGCDYCGPLVEIARNR--GCEVMVCDNLNLPFRD------QGFDAIISIGAIS 112
Cdd:pfam08242   2 EIGCGTGtllrALLEALPGLEYTGLDISPAALEAARERlaALGLLNAVRVELFQLDlgeldpGSFDVVVASNVLH 76
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 44-111 7.96e-04

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 37.64  E-value: 7.96e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148703527  44 PGSLVADIGCGTG---KYLKVNSQVHTLGCDYCGPLVEIA--RNRG---CEVMVCDNLNLPFRDQGFDAIISIGAI 111
Cdd:PTZ00098  52 ENSKVLDIGSGLGggcKYINEKYGAHVHGVDICEKMVNIAklRNSDknkIEFEANDILKKDFPENTFDMIYSRDAI 127
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 34-110 2.44e-03

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 36.04  E-value: 2.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148703527  34 RVRQFLQDQKPGS--LVADIGCGTGKY----LKVNSQVHTL---GCDYCGPLVEIARNR--GCEVMVCDNLNLPFRDQGF 102
Cdd:PRK11088  73 AVANLLAERLDEKatALLDIGCGEGYYthalADALPEITTMqlfGLDISKVAIKYAAKRypQVTFCVASSHRLPFADQSL 152


                 ....*...
gi 148703527 103 DAIISIGA 110
Cdd:PRK11088 153 DAIIRIYA 160
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 9-105 6.90e-03

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 34.87  E-value: 6.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148703527   9 ERRHVHS----VYENTAPYFTDLQSKAWPRVRQFLQDQKPGSLVADIGCGTGK--YL---KVNSQVHTLGCDYCGPLVEI 79
Cdd:PLN02233  34 ERQALFNriapVYDNLNDLLSLGQHRIWKRMAVSWSGAKMGDRVLDLCCGSGDlaFLlseKVGSDGKVMGLDFSSEQLAV 113

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 148703527  80 A------RNRGC----EVMVCDNLNLPFRDQGFDAI 105
Cdd:PLN02233 114 AasrqelKAKSCykniEWIEGDATDLPFDDCYFDAI 149
 
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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