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Conserved domains on  [gi|1830199494|gb|QIY91430|]
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class I SAM-dependent methyltransferase [Chryseobacterium gallinarum]

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; ...
 115-224 1.81e-06

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 pfam13578:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 106  Bit Score: 45.38  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830199494 115 VETGVAYGWSSLASLLSLaKRNGT--LYSSDmpyLAQDGDQYVGYVVPENLRSHWKLFRFADKESLPKIfsENPVFDVLH 192
Cdd:pfam13578   1 VEIGTYSGVSTLWLAAAL-RDNGLgrLTAVD---PDPGAEEAGALLRKAGLDDRVRLIVGDSREALPSL--ADGPIDLLF 74

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1830199494 193 YDSDKSYNGRVWAYSELYKHLKKGGVFISDDI 224
Cdd:pfam13578  75 IDGDHTYEAVLNDLELWLPRLAPGGVILFHDI 106
 
Name Accession Description Interval E-value
Methyltransf_24 pfam13578
Methyltransferase domain; This family appears to be a methyltransferase domain.
 115-224 1.81e-06

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


Pssm-ID: 433324 [Multi-domain]  Cd Length: 106  Bit Score: 45.38  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830199494 115 VETGVAYGWSSLASLLSLaKRNGT--LYSSDmpyLAQDGDQYVGYVVPENLRSHWKLFRFADKESLPKIfsENPVFDVLH 192
Cdd:pfam13578   1 VEIGTYSGVSTLWLAAAL-RDNGLgrLTAVD---PDPGAEEAGALLRKAGLDDRVRLIVGDSREALPSL--ADGPIDLLF 74

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1830199494 193 YDSDKSYNGRVWAYSELYKHLKKGGVFISDDI 224
Cdd:pfam13578  75 IDGDHTYEAVLNDLELWLPRLAPGGVILFHDI 106
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 96-224 1.50e-05

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: 44.02  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830199494  96 PGALELIYYACEFASAQKVVETGVAYG----WsslasLLSLAKRNGTLYSSDMPylaqdgdqyvgyvvPENL---RSHWK 168
Cdd:COG4122     2 PEQGRLLYLLARLLGAKRILEIGTGTGystlW-----LARALPDDGRLTTIEID--------------PERAaiaRENFA 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1830199494 169 LFRFADK---------ESLPKIFSENpvFDVLHYDSDKSYNGRVWAysELYKHLKKGGVFISDDI 224
Cdd:COG4122    63 RAGLADRirlilgdalEVLPRLADGP--FDLVFIDADKSNYPDYLE--LALPLLRPGGLIVADNV 123
 
Name Accession Description Interval E-value
Methyltransf_24 pfam13578
Methyltransferase domain; This family appears to be a methyltransferase domain.
 115-224 1.81e-06

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


Pssm-ID: 433324 [Multi-domain]  Cd Length: 106  Bit Score: 45.38  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830199494 115 VETGVAYGWSSLASLLSLaKRNGT--LYSSDmpyLAQDGDQYVGYVVPENLRSHWKLFRFADKESLPKIfsENPVFDVLH 192
Cdd:pfam13578   1 VEIGTYSGVSTLWLAAAL-RDNGLgrLTAVD---PDPGAEEAGALLRKAGLDDRVRLIVGDSREALPSL--ADGPIDLLF 74

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1830199494 193 YDSDKSYNGRVWAYSELYKHLKKGGVFISDDI 224
Cdd:pfam13578  75 IDGDHTYEAVLNDLELWLPRLAPGGVILFHDI 106
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 96-224 1.50e-05

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: 44.02  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830199494  96 PGALELIYYACEFASAQKVVETGVAYG----WsslasLLSLAKRNGTLYSSDMPylaqdgdqyvgyvvPENL---RSHWK 168
Cdd:COG4122     2 PEQGRLLYLLARLLGAKRILEIGTGTGystlW-----LARALPDDGRLTTIEID--------------PERAaiaRENFA 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1830199494 169 LFRFADK---------ESLPKIFSENpvFDVLHYDSDKSYNGRVWAysELYKHLKKGGVFISDDI 224
Cdd:COG4122    63 RAGLADRirlilgdalEVLPRLADGP--FDLVFIDADKSNYPDYLE--LALPLLRPGGLIVADNV 123
 
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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