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Conserved domains on  [gi|20336212|ref|NP_620279|]
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guanidinoacetate N-methyltransferase isoform b [Homo sapiens]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10116212)

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

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 63-166 9.12e-12

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: 60.52  E-value: 9.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20336212  63 RVLEVGFGMAIAASKVQEAPIDEHWIIECNDGVFQRLRD-WAPRQTHKVIPLKGLWEDvAPTLPDGHFDGILYDtypLSE 141
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKaAAALLADNVEVLKGDAEE-LPPEADESFDVIISD---PPL 76

                        90       100
                ....*....|....*....|....*
gi 20336212 142 ETWHTHQFNFIKNhAFRLLKPGGVL 166
Cdd:cd02440  77 HHLVEDLARFLEE-ARRLLKPGGVL 100
 
Name Accession Description Interval E-value
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 63-166 9.12e-12

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: 60.52  E-value: 9.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20336212  63 RVLEVGFGMAIAASKVQEAPIDEHWIIECNDGVFQRLRD-WAPRQTHKVIPLKGLWEDvAPTLPDGHFDGILYDtypLSE 141
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKaAAALLADNVEVLKGDAEE-LPPEADESFDVIISD---PPL 76

                        90       100
                ....*....|....*....|....*
gi 20336212 142 ETWHTHQFNFIKNhAFRLLKPGGVL 166
Cdd:cd02440  77 HHLVEDLARFLEE-ARRLLKPGGVL 100
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
42-166 1.72e-04

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 42.20  E-value: 1.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20336212  42 MER--WETPYMHAL---AAAASSKGGRVLEVGFGM---AIA-----ASKVQEAPIDE--HWIIECNDgvfqrlrdWAPRQ 106
Cdd:COG2521 109 MHRikGTDPLEDARrkvKLVGVRRGDRVLDTCTGLgytAIEalkrgAREVITVEKDPnvLELAELNP--------WSREL 180

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20336212 107 THKVIPLK-GLWEDVAPTLPDGHFDGILYDT---------YplSEETWhthqfnfikNHAFRLLKPGGVL 166
Cdd:COG2521 181 ANERIKIIlGDASEVIKTFPDESFDAIIHDPprfslagelY--SLEFY---------RELYRVLKPGGRL 239
 
Name Accession Description Interval E-value
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 63-166 9.12e-12

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: 60.52  E-value: 9.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20336212  63 RVLEVGFGMAIAASKVQEAPIDEHWIIECNDGVFQRLRD-WAPRQTHKVIPLKGLWEDvAPTLPDGHFDGILYDtypLSE 141
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKaAAALLADNVEVLKGDAEE-LPPEADESFDVIISD---PPL 76

                        90       100
                ....*....|....*....|....*
gi 20336212 142 ETWHTHQFNFIKNhAFRLLKPGGVL 166
Cdd:cd02440  77 HHLVEDLARFLEE-ARRLLKPGGVL 100
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
42-166 1.72e-04

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 42.20  E-value: 1.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20336212  42 MER--WETPYMHAL---AAAASSKGGRVLEVGFGM---AIA-----ASKVQEAPIDE--HWIIECNDgvfqrlrdWAPRQ 106
Cdd:COG2521 109 MHRikGTDPLEDARrkvKLVGVRRGDRVLDTCTGLgytAIEalkrgAREVITVEKDPnvLELAELNP--------WSREL 180

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20336212 107 THKVIPLK-GLWEDVAPTLPDGHFDGILYDT---------YplSEETWhthqfnfikNHAFRLLKPGGVL 166
Cdd:COG2521 181 ANERIKIIlGDASEVIKTFPDESFDAIIHDPprfslagelY--SLEFY---------RELYRVLKPGGRL 239
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 43-166 7.95e-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: 38.46  E-value: 7.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20336212  43 ERWEtPYMHALAAAASSKGGRVLEVGFGMAIAASKVQEAPIDeHWIIECNDGVFQRLRDWAPRQTHKVIPlkGLWEDVAp 122
Cdd:COG2227   8 DFWD-RRLAALLARLLPAGGRVLDVGCGTGRLALALARRGAD-VTGVDISPEALEIARERAAELNVDFVQ--GDLEDLP- 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 20336212 123 tLPDGHFDGIlydtypLSEETWH--THQFNFIKnHAFRLLKPGGVL 166
Cdd:COG2227  83 -LEDGSFDLV------ICSEVLEhlPDPAALLR-ELARLLKPGGLL 120
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 51-166 2.31e-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: 37.67  E-value: 2.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20336212  51 HALAAAASSKGGRVLEVGFGMAIAASKVQEApiDEHWI-IECNDGVFQRLRDWAPRQTHKVIPLKGLWEDVAptLPDGHF 129
Cdd:COG2226  13 ALLAALGLRPGARVLDLGCGTGRLALALAER--GARVTgVDISPEMLELARERAAEAGLNVEFVVGDAEDLP--FPDGSF 88

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 20336212 130 DGIlydtypLSEETWH--THQFNFIKnHAFRLLKPGGVL 166
Cdd:COG2226  89 DLV------ISSFVLHhlPDPERALA-EIARVLKPGGRL 120
 
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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