NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|157822011|ref|NP_001101374|]
View 

trimethylguanosine synthase [Rattus norvegicus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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; ...
685-837 1.69e-48

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 pfam09445:

Pssm-ID: 473071  Cd Length: 165  Bit Score: 169.05  E-value: 1.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822011  685 CDIIVDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNAEVYGVADKIEFICGDFL-LLAPC----LKADVVFLSPP 759
Cdd:pfam09445   1 ATRILDVFCGGGGNTIQFANVFDSVISIDINLEHLACAQHNAEVYGVSDRIWLIHGDWFeLLAKLkfekIKYDCVFASPP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822011  760 WGGPDYATAETFDIRTMMSPDGFE-IFRLSQKITNNIVYFLPRNADVDQVAS----LAGPGGQVEIEQNFLNNKLKTITA 834
Cdd:pfam09445  81 WGGPSYKKQNVYDLENKLQPYGLSqLLKEFTKISKNVILFLPRNSDLNQLSAltreVLGPEAKCKVLYIKENGYMKGLLC 160

                  ...
gi 157822011  835 YFG 837
Cdd:pfam09445 161 YFG 163
 
Name Accession Description Interval E-value
Methyltransf_15 pfam09445
RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as ...
685-837 1.69e-48

RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as Schizosaccharomyces pombe Tgs1 and Giardia lamblia Tgs2 catalyze methylation of the exocyclic N2 amine of 7-methylguanosine.


Pssm-ID: 370496  Cd Length: 165  Bit Score: 169.05  E-value: 1.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822011  685 CDIIVDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNAEVYGVADKIEFICGDFL-LLAPC----LKADVVFLSPP 759
Cdd:pfam09445   1 ATRILDVFCGGGGNTIQFANVFDSVISIDINLEHLACAQHNAEVYGVSDRIWLIHGDWFeLLAKLkfekIKYDCVFASPP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822011  760 WGGPDYATAETFDIRTMMSPDGFE-IFRLSQKITNNIVYFLPRNADVDQVAS----LAGPGGQVEIEQNFLNNKLKTITA 834
Cdd:pfam09445  81 WGGPSYKKQNVYDLENKLQPYGLSqLLKEFTKISKNVILFLPRNSDLNQLSAltreVLGPEAKCKVLYIKENGYMKGLLC 160

                  ...
gi 157822011  835 YFG 837
Cdd:pfam09445 161 YFG 163
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
688-781 5.85e-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: 62.83  E-value: 5.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822011 688 IVDAFCGVGGNTIQFALT-GKRVIAIDIDPVKIDLARNNAEvYGVADKIEFICGDF--LLLAPCLKADVVFLSPPWGGPD 764
Cdd:cd02440    2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAA-ALLADNVEVLKGDAeeLPPEADESFDVIISDPPLHHLV 80
                         90
                 ....*....|....*...
gi 157822011 765 YATAETFD-IRTMMSPDG 781
Cdd:cd02440   81 EDLARFLEeARRLLKPGG 98
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
686-761 8.64e-11

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 61.50  E-value: 8.64e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157822011 686 DIIVDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNAEVYGVADkIEFICGDFLLLA-PCLKADVVFLSPPWG 761
Cdd:COG1041   28 DTVLDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGARENLEHYGYED-ADVIRGDARDLPlADESVDAIVTDPPYG 103
rumA TIGR00479
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ...
652-764 3.87e-07

23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA methyltransferases by homology to the TrmA family. The member from E. coli has now been shown to act as the 23S RNA methyltransferase for the conserved U1939. The gene is now designated rumA and was previously designated ygcA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 129571 [Multi-domain]  Cd Length: 431  Bit Score: 53.29  E-value: 3.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822011  652 FDDGIK--LDKEGWFSVTPEkIAEHIAGRVSQSFNC---DIIVDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNA 726
Cdd:TIGR00479 256 KSGDLSftFSARDFIQVNSG-QNEKLVDRALEWLELqgeERVLDAYCGMGTFTLPLAKQAKSVVGVEGVPESVEKAQQNA 334
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 157822011  727 EVYGVADkIEFICGDFLLLAPCL-----KADVVFLSPPWGGPD 764
Cdd:TIGR00479 335 ELNGIAN-VTFYHGTLETVLPKQpwagnGFDKVLLDPPRKGCA 376
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
683-756 6.33e-07

cobalt-precorrin-6Y C(15)-methyltransferase; Provisional


Pssm-ID: 234740  Cd Length: 198  Bit Score: 50.95  E-value: 6.33e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157822011 683 FNCDIIVDAFCGVGGNTIQFAL---TGKRVIAIDIDPVKIDLARNNAEVYGVADKIEFICGDFLLLAPCL--KADVVFL 756
Cdd:PRK00377  39 RKGDMILDIGCGTGSVTVEASLlvgETGKVYAVDKDEKAINLTRRNAEKFGVLNNIVLIKGEAPEILFTIneKFDRIFI 117
 
Name Accession Description Interval E-value
Methyltransf_15 pfam09445
RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as ...
685-837 1.69e-48

RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as Schizosaccharomyces pombe Tgs1 and Giardia lamblia Tgs2 catalyze methylation of the exocyclic N2 amine of 7-methylguanosine.


Pssm-ID: 370496  Cd Length: 165  Bit Score: 169.05  E-value: 1.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822011  685 CDIIVDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNAEVYGVADKIEFICGDFL-LLAPC----LKADVVFLSPP 759
Cdd:pfam09445   1 ATRILDVFCGGGGNTIQFANVFDSVISIDINLEHLACAQHNAEVYGVSDRIWLIHGDWFeLLAKLkfekIKYDCVFASPP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822011  760 WGGPDYATAETFDIRTMMSPDGFE-IFRLSQKITNNIVYFLPRNADVDQVAS----LAGPGGQVEIEQNFLNNKLKTITA 834
Cdd:pfam09445  81 WGGPSYKKQNVYDLENKLQPYGLSqLLKEFTKISKNVILFLPRNSDLNQLSAltreVLGPEAKCKVLYIKENGYMKGLLC 160

                  ...
gi 157822011  835 YFG 837
Cdd:pfam09445 161 YFG 163
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
688-781 5.85e-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: 62.83  E-value: 5.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822011 688 IVDAFCGVGGNTIQFALT-GKRVIAIDIDPVKIDLARNNAEvYGVADKIEFICGDF--LLLAPCLKADVVFLSPPWGGPD 764
Cdd:cd02440    2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAA-ALLADNVEVLKGDAeeLPPEADESFDVIISDPPLHHLV 80
                         90
                 ....*....|....*...
gi 157822011 765 YATAETFD-IRTMMSPDG 781
Cdd:cd02440   81 EDLARFLEeARRLLKPGG 98
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
686-761 8.64e-11

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 61.50  E-value: 8.64e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157822011 686 DIIVDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNAEVYGVADkIEFICGDFLLLA-PCLKADVVFLSPPWG 761
Cdd:COG1041   28 DTVLDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGARENLEHYGYED-ADVIRGDARDLPlADESVDAIVTDPPYG 103
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
686-754 1.24e-10

tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442010 [Multi-domain]  Cd Length: 333  Bit Score: 63.73  E-value: 1.24e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157822011 686 DIIVDAFCGVGGNTIQFA-LTGKRVIAIDIDPVKIDLARNNAEVYGVADKIEFICGDFLLLAPCL--KADVV 754
Cdd:COG2520  182 ERVLDMFAGVGPFSIPIAkRSGAKVVAIDINPDAVEYLKENIRLNKVEDRVTPILGDAREVAPELegKADRI 253
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
686-759 6.16e-10

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 62.12  E-value: 6.16e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157822011 686 DIIVDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNAEVYGVaDKIEFICGD---FLL-LAPCLKADVVFLSPP 759
Cdd:COG2265  235 ERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGL-KNVEFVAGDleeVLPeLLWGGRPDVVVLDPP 311
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
656-762 1.27e-09

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 58.76  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822011 656 IKLDKEGWFS---------VTPEKIAEHI--AGRVSQSFNCDIIVDAFCGVGGNTIQFALTG-KRVIAIDIDPVKIDLAR 723
Cdd:COG2263    6 IILEKLPGFSnpkveleqyPTPAELAAELlhLAYLRGDIEGKTVLDLGCGTGMLAIGAALLGaKKVVGVDIDPEALEIAR 85
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 157822011 724 NNAEvyGVADKIEFICGDFLLLAPCLKADVVFLSPPWGG 762
Cdd:COG2263   86 ENAE--RLGVRVDFIRADVTRIPLGGSVDTVVMNPPFGA 122
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
688-757 1.41e-09

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 55.65  E-value: 1.41e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157822011  688 IVDAFCGVGGNTIQFA-LTGKRVIAIDIDPVKIDLARNNAEVYGVadKIEFICGDFL-LLAPCLKADVVFLS 757
Cdd:pfam13649   1 VLDLGCGTGRLTLALArRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEdLPFPDGSFDLVVSS 70
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
686-761 1.68e-09

Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 58.14  E-value: 1.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822011  686 DIIVDAFCGVGGNTIQFALTGKRVI-------------AIDIDPVKIDLARNNAEVYGVADKIEFICGDFLLL-APCLKA 751
Cdd:pfam01170  30 DPLLDPMCGSGTILIEAALMGANIApgkfdarvraplyGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADLpLLEGSV 109
                          90
                  ....*....|
gi 157822011  752 DVVFLSPPWG 761
Cdd:pfam01170 110 DVIVTNPPYG 119
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
688-757 3.17e-09

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 57.62  E-value: 3.17e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157822011 688 IVDAFCGVGGNTIQFA-LTGKRVIAIDIDPVKIDLARNNAEVYGvADKIEFICGDF--LLLAPCLKADVVFLS 757
Cdd:COG0500   30 VLDLGCGTGRNLLALAaRFGGRVIGIDLSPEAIALARARAAKAG-LGNVEFLVADLaeLDPLPAESFDLVVAF 101
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
688-757 3.46e-09

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: 55.41  E-value: 3.46e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157822011 688 IVDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNAEvygvADKIEFICGDFLLLAPCL-KADVVFLS 757
Cdd:COG2227   28 VLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAA----ELNVDFVQGDLEDLPLEDgSFDLVICS 94
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
693-755 2.49e-08

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 54.17  E-value: 2.49e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157822011 693 CGVGGNTIQFA-LTGKRVIAIDIDPVKIDLARNNAEVYGVADKIEFICGDFLLLAPCLKADVVF 755
Cdd:COG2230   60 CGWGGLALYLArRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIV 123
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
694-756 3.14e-08

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: 54.03  E-value: 3.14e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157822011 694 GVGGNTIQFAL---TGKRVIAIDIDPVKIDLARNNAEVYGVADKIEFICGDFLLLAPCLKA---DVVFL 756
Cdd:COG4122   26 GTGYSTLWLARalpDDGRLTTIEIDPERAAIARENFARAGLADRIRLILGDALEVLPRLADgpfDLVFI 94
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
707-755 3.80e-07

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 52.48  E-value: 3.80e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 157822011 707 KRVIAIDIDPVKIDLARNNAEVYGVADKIEFICGDfllLAPCLKADVVF 755
Cdd:COG2264  172 KRVLAVDIDPVAVEAARENAELNGVEDRIEVVLGD---LLEDGPYDLVV 217
rumA TIGR00479
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ...
652-764 3.87e-07

23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA methyltransferases by homology to the TrmA family. The member from E. coli has now been shown to act as the 23S RNA methyltransferase for the conserved U1939. The gene is now designated rumA and was previously designated ygcA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 129571 [Multi-domain]  Cd Length: 431  Bit Score: 53.29  E-value: 3.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822011  652 FDDGIK--LDKEGWFSVTPEkIAEHIAGRVSQSFNC---DIIVDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNA 726
Cdd:TIGR00479 256 KSGDLSftFSARDFIQVNSG-QNEKLVDRALEWLELqgeERVLDAYCGMGTFTLPLAKQAKSVVGVEGVPESVEKAQQNA 334
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 157822011  727 EVYGVADkIEFICGDFLLLAPCL-----KADVVFLSPPWGGPD 764
Cdd:TIGR00479 335 ELNGIAN-VTFYHGTLETVLPKQpwagnGFDKVLLDPPRKGCA 376
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
683-756 6.33e-07

cobalt-precorrin-6Y C(15)-methyltransferase; Provisional


Pssm-ID: 234740  Cd Length: 198  Bit Score: 50.95  E-value: 6.33e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157822011 683 FNCDIIVDAFCGVGGNTIQFAL---TGKRVIAIDIDPVKIDLARNNAEVYGVADKIEFICGDFLLLAPCL--KADVVFL 756
Cdd:PRK00377  39 RKGDMILDIGCGTGSVTVEASLlvgETGKVYAVDKDEKAINLTRRNAEKFGVLNNIVLIKGEAPEILFTIneKFDRIFI 117
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
688-757 6.51e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 48.28  E-value: 6.51e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157822011 688 IVDAFCGVGGNTIQFA--LTGKRVIAIDIDPVKIDLARNNAevygvaDKIEFICGDFLLLAPCLKADVVFLS 757
Cdd:COG4106    5 VLDLGCGTGRLTALLAerFPGARVTGVDLSPEMLARARARL------PNVRFVVADLRDLDPPEPFDLVVSN 70
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
688-745 1.39e-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: 48.45  E-value: 1.39e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157822011 688 IVDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNAEVYGVadKIEFICGDFLLL 745
Cdd:COG2226   26 VLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDL 81
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
684-760 1.39e-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: 50.14  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822011 684 NCDIIVDAFCGVGgnTIQFALTGK----RVIAIDIDPVKIDLARNNAEVYGVADKIEFICGDFLLLAPCLKA---DVVFL 756
Cdd:COG4123   37 KGGRVLDLGTGTG--VIALMLAQRspgaRITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAAELPPgsfDLVVS 114

                 ....
gi 157822011 757 SPPW 760
Cdd:COG4123  115 NPPY 118
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
688-759 1.46e-06

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 50.92  E-value: 1.46e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157822011 688 IVDAFCGVG--GNTIQFALTGKRVIAIDIDPVKIDLARNNAEVYGVADKIEFICGDFL-LLAPCLKADVVfLS-PP 759
Cdd:COG2890  116 VLDLGTGSGaiALALAKERPDARVTAVDISPDALAVARRNAERLGLEDRVRFLQGDLFePLPGDGRFDLI-VSnPP 190
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
688-741 5.04e-06

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 48.68  E-value: 5.04e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157822011 688 IVDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNAEVYGVADKIEFICGD 741
Cdd:PRK07580  67 ILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLAGNITFEVGD 120
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
708-761 5.24e-06

23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA G2445 N2-methylase RlmL is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 439886 [Multi-domain]  Cd Length: 369  Bit Score: 49.71  E-value: 5.24e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157822011 708 RVIAIDIDPVKIDLARNNAEVYGVADKIEFICGDFLLLAPCLKADVVFLSPPWG 761
Cdd:COG0116  252 PIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLEPPAEPGLIITNPPYG 305
PRK14968 PRK14968
putative methyltransferase; Provisional
686-759 1.76e-05

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 46.43  E-value: 1.76e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157822011 686 DIIVDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNAEVYGVAD-KIEFICGDfllLAPCLKA---DVVFLSPP 759
Cdd:PRK14968  25 DRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNnGVEVIRSD---LFEPFRGdkfDVILFNPP 99
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
707-754 3.52e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 46.18  E-value: 3.52e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 157822011 707 KRVIAIDIDPVKIDLARNNAEVYGVADKIEFICGDFLLLAPCLKADVV 754
Cdd:COG4076   59 KKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDLPEKADVI 106
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
708-759 1.11e-04

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 44.77  E-value: 1.11e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157822011 708 RVIAIDIDPVKIDLARNNAEvYGVADKIEFICGDFLLLAPCLKADVVfLS-PP 759
Cdd:PRK09328 134 EVTAVDISPEALAVARRNAK-HGLGARVEFLQGDWFEPLPGGRFDLI-VSnPP 184
Met_10 pfam02475
Met-10+ like-protein; The methionine-10 mutant allele of N. crassa codes for a protein of ...
686-759 1.17e-04

Met-10+ like-protein; The methionine-10 mutant allele of N. crassa codes for a protein of unknown function, Swiss:O27901. However, homologous proteins have been found in yeast suggesting this protein may be involved in methionine biosynthesis, transport and/or utilization.


Pssm-ID: 396850 [Multi-domain]  Cd Length: 198  Bit Score: 43.88  E-value: 1.17e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157822011  686 DIIVDAFCGVGGNTIQFALTGK--RVIAIDIDPVKIDLARNNAEVYGVADKIEFICGDFLLLAPCLKADVVFLSPP 759
Cdd:pfam02475 101 EVVVDMFAGIGPFSIPIAKHSKarRVYAIELNPESYKYLKENIKLNKVEDVVKPILGDVREVILEDVADRVVMNLP 176
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
669-760 1.44e-04

HemK family putative methylases; 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. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 44.65  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822011  669 EKIAEHIAGRVSQSFNCDIIVDAFCGVGGNTIQFALT--GKRVIAIDIDPVKIDLARNNAEVYGVADKIEFICGDFLLLA 746
Cdd:TIGR00536  99 EELVEKALASLISQPPILHILDLGTGSGCIALALAYEfpNAEVIAVDISPDALAVAEENAEKNQLEHRVEFIQSNLFEPL 178
                          90
                  ....*....|....
gi 157822011  747 PCLKADVVFLSPPW 760
Cdd:TIGR00536 179 AGQKIDIIVSNPPY 192
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
689-757 1.48e-04

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 41.50  E-value: 1.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157822011  689 VDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNAEvygvADKIEFICGDFLLLApcLK---ADVVFLS 757
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAP----REGLTFVVGDAEDLP--FPdnsFDLVLSS 66
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
693-781 2.00e-04

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: 43.25  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822011 693 CGVG--GNTIQFALTGKRVIAIDIDPVKIDLARNNAEVYGVADkIEFICGDFLLLAPCLKADVVFLSPPW---GGPDYAT 767
Cdd:COG2813   58 CGYGviGLALAKRNPEARVTLVDVNARAVELARANAAANGLEN-VEVLWSDGLSGVPDGSFDLILSNPPFhagRAVDKEV 136
                         90
                 ....*....|....*.
gi 157822011 768 AETF--DIRTMMSPDG 781
Cdd:COG2813  137 AHALiaDAARHLRPGG 152
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
707-754 2.16e-04

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 43.60  E-value: 2.16e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 157822011 707 KRVIAIDIDPVKIDLARNNAEVYGVADKIEFICGDflllapcLKADVV 754
Cdd:PRK00517 143 KKVLAVDIDPQAVEAARENAELNGVELNVYLPQGD-------LKADVI 183
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
686-755 2.24e-04

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: 44.18  E-value: 2.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157822011  686 DIIVDAFCGVGGNTIQFALTG-KRVIAIDIDPVKIDLARNNAEVYGVADKIEFicgdFLLL-APCLKADVVF 755
Cdd:pfam06325 163 ESVLDVGCGSGILAIAALKLGaKKVVGVDIDPVAVRAAKENAELNGVEARLEV----YLPGdLPKEKADVVV 230
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
705-761 2.72e-04

bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2))-methyltransferase RlmL;


Pssm-ID: 236981 [Multi-domain]  Cd Length: 702  Bit Score: 44.41  E-value: 2.72e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822011 705 TGKRVIAIDIDPVKIDLARNNAEVYGVADKIEFICGDFLLLAPCLKAD---VVFLSPPWG 761
Cdd:PRK11783 255 LPSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKNPLPKGptgLVISNPPYG 314
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
694-733 3.80e-04

6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, and other MDR family members; This group contains enzymes of the zinc-dependent alcohol dehydrogenase family, including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA,NADH, and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176216 [Multi-domain]  Cd Length: 338  Bit Score: 43.39  E-value: 3.80e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 157822011 694 GVGGNTIQFA-LTGKRVIAIDIDPVKIDLARNnaevYGVAD 733
Cdd:cd08254  176 GLGLNAVQIAkAMGAAVIAVDIKEEKLELAKE----LGADE 212
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
688-755 4.79e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 41.25  E-value: 4.79e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157822011  688 IVDAFCGVGGNTIQFAL---TGKRVIAIDIDPVKIDLARNNAEVYGVaDKIEFICGDFLLLAPCL---KADVVF 755
Cdd:pfam13847   7 VLDLGCGTGHLSFELAEelgPNAEVVGIDISEEAIEKARENAQKLGF-DNVEFEQGDIEELPELLeddKFDVVI 79
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
686-762 6.03e-04

Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 43.23  E-value: 6.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822011 686 DIIVDAFCGVGGNTIQFALTGK--RVIAIDIDPVKIDLARNNAEVYGVADkIEFICGDflllAP-CL----KADVVFLsp 758
Cdd:COG2242  249 DVLWDIGAGSGSVSIEAARLAPggRVYAIERDPERAALIRANARRFGVPN-VEVVEGE----APeALadlpDPDAVFI-- 321

                 ....
gi 157822011 759 pwGG 762
Cdd:COG2242  322 --GG 323
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
637-757 1.27e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 40.75  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822011 637 ELAKYWAQRYRLFS-RFDDGI--KLDKEGWFSVTPEKIAEHIAGRVSQsfncdiIVDAFCGVGGNTIQFALTGKRVIAID 713
Cdd:COG4976    2 ALDAYVEALFDQYAdSYDAALveDLGYEAPALLAEELLARLPPGPFGR------VLDLGCGTGLLGEALRPRGYRLTGVD 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 157822011 714 IDPVKIDLARNNAeVYgvadkIEFICGDFL-LLAPCLKADVVFLS 757
Cdd:COG4976   76 LSEEMLAKAREKG-VY-----DRLLVADLAdLAEPDGRFDLIVAA 114
PRK08317 PRK08317
hypothetical protein; Provisional
684-742 1.96e-03

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 40.69  E-value: 1.96e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822011 684 NCDIIVDAFCGVGGNTIQFA-LTGK--RVIAIDIDPVKIDLARNNAE--------VYGVADKIEFICGDF 742
Cdd:PRK08317  19 PGDRVLDVGCGPGNDARELArRVGPegRVVGIDRSEAMLALAKERAAglgpnvefVRGDADGLPFPDGSF 88
rumB PRK03522
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
690-759 3.99e-03

23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;


Pssm-ID: 235128 [Multi-domain]  Cd Length: 315  Bit Score: 40.24  E-value: 3.99e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157822011 690 DAFCGVGGntiqFAL----TGKRVIAIDIDPVKIDLARNNAEVYGvADKIEFICGD---FLLLAPcLKADVVFLSPP 759
Cdd:PRK03522 179 DLFCGVGG----FGLhcatPGMQLTGIEISAEAIACAKQSAAELG-LTNVQFQALDstqFATAQG-EVPDLVLVNPP 249
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH
HHS Vulnerability Disclosure