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Conserved domains on  [gi|1622960446|ref|XP_028708511|]
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trimethylguanosine synthase isoform X2 [Macaca mulatta]

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; ...
 692-844 3.21e-49

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: 170.98  E-value: 3.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960446 692 CDVVVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFL-LLAAC----LKADVVFLSPP 766
Cdd:pfam09445   1 ATRILDVFCGGGGNTIQFANVFDSVISIDINLEHLACAQHNAEVYGVSDRIWLIHGDWFeLLAKLkfekIKYDCVFASPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960446 767 WGGPDYATAETFDIRTMMSPDGFE-IFRLSKKITNNIVYFLPRNADIDQVAS----LAGPGGQVEIEQNFLNNKLKTITA 841
Cdd:pfam09445  81 WGGPSYKKQNVYDLENKLQPYGLSqLLKEFTKISKNVILFLPRNSDLNQLSAltreVLGPEAKCKVLYIKENGYMKGLLC 160


                  ...
gi 1622960446 842 YFG 844
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 ...
 692-844 3.21e-49

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: 170.98  E-value: 3.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960446 692 CDVVVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFL-LLAAC----LKADVVFLSPP 766
Cdd:pfam09445   1 ATRILDVFCGGGGNTIQFANVFDSVISIDINLEHLACAQHNAEVYGVSDRIWLIHGDWFeLLAKLkfekIKYDCVFASPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960446 767 WGGPDYATAETFDIRTMMSPDGFE-IFRLSKKITNNIVYFLPRNADIDQVAS----LAGPGGQVEIEQNFLNNKLKTITA 841
Cdd:pfam09445  81 WGGPSYKKQNVYDLENKLQPYGLSqLLKEFTKISKNVILFLPRNSDLNQLSAltreVLGPEAKCKVLYIKENGYMKGLLC 160


                  ...
gi 1622960446 842 YFG 844
Cdd:pfam09445 161 YFG 163
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 693-768 1.14e-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: 64.20  E-value: 1.14e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622960446 693 DVVVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIADkIEFICGDFLLLAACL-KADVVFLSPPWG 768
Cdd:COG1041    28 DTVLDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGARENLEHYGYED-ADVIRGDARDLPLADeSVDAIVTDPPYG 103
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 695-788 2.56e-10

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: 58.21  E-value: 2.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960446 695 VVDAFCGVGGNTIQFALT-GMRVIAIDIDPVKIALARNNAEvYGIADKIEFICGDF--LLLAACLKADVVFLSPPWGGPD 771
Cdd:cd02440     2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAA-ALLADNVEVLKGDAeeLPPEADESFDVIISDPPLHHLV 80

                          90
                  ....*....|....*...
gi 1622960446 772 YATAETFD-IRTMMSPDG 788
Cdd:cd02440    81 EDLARFLEeARRLLKPGG 98
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 690-763 1.18e-06

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 49.80  E-value: 1.18e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622960446 690 FKCDVVVDAFCGVGGNTIQFAL---TGMRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLAACL--KADVVFL 763
Cdd:PRK00377   39 RKGDMILDIGCGTGSVTVEASLlvgETGKVYAVDKDEKAINLTRRNAEKFGVLNNIVLIKGEAPEILFTIneKFDRIFI 117
rumA TIGR00479
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ...
 693-771 4.50e-06

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: 49.82  E-value: 4.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960446 693 DVVVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIADkIEFICGDF-----LLLAACLKADVVFLSPPW 767
Cdd:TIGR00479 294 ERVLDAYCGMGTFTLPLAKQAKSVVGVEGVPESVEKAQQNAELNGIAN-VTFYHGTLetvlpKQPWAGNGFDKVLLDPPR 372


                  ....
gi 1622960446 768 GGPD 771
Cdd:TIGR00479 373 KGCA 376
 
Name Accession Description Interval E-value
Methyltransf_15 pfam09445
RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as ...
 692-844 3.21e-49

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: 170.98  E-value: 3.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960446 692 CDVVVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFL-LLAAC----LKADVVFLSPP 766
Cdd:pfam09445   1 ATRILDVFCGGGGNTIQFANVFDSVISIDINLEHLACAQHNAEVYGVSDRIWLIHGDWFeLLAKLkfekIKYDCVFASPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960446 767 WGGPDYATAETFDIRTMMSPDGFE-IFRLSKKITNNIVYFLPRNADIDQVAS----LAGPGGQVEIEQNFLNNKLKTITA 841
Cdd:pfam09445  81 WGGPSYKKQNVYDLENKLQPYGLSqLLKEFTKISKNVILFLPRNSDLNQLSAltreVLGPEAKCKVLYIKENGYMKGLLC 160


                  ...
gi 1622960446 842 YFG 844
Cdd:pfam09445 161 YFG 163
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 693-768 1.14e-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: 64.20  E-value: 1.14e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622960446 693 DVVVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIADkIEFICGDFLLLAACL-KADVVFLSPPWG 768
Cdd:COG1041    28 DTVLDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGARENLEHYGYED-ADVIRGDARDLPLADeSVDAIVTDPPYG 103
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 669-766 6.56e-11

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: 65.20  E-value: 6.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960446 669 GWFSVTPEkIAEHIAGRVS---QSFKCDVVVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIaDKIEFI 745
Cdd:COG2265   209 SFFQVNPE-QAEALYAAALewlDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGL-KNVEFV 286

                          90       100
                  ....*....|....*....|....*
gi 1622960446 746 CGD---FLL-LAACLKADVVFLSPP 766
Cdd:COG2265   287 AGDleeVLPeLLWGGRPDVVVLDPP 311
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 695-788 2.56e-10

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: 58.21  E-value: 2.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960446 695 VVDAFCGVGGNTIQFALT-GMRVIAIDIDPVKIALARNNAEvYGIADKIEFICGDF--LLLAACLKADVVFLSPPWGGPD 771
Cdd:cd02440     2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAA-ALLADNVEVLKGDAeeLPPEADESFDVIISDPPLHHLV 80

                          90
                  ....*....|....*...
gi 1622960446 772 YATAETFD-IRTMMSPDG 788
Cdd:cd02440    81 EDLARFLEeARRLLKPGG 98
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 695-764 1.32e-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: 56.95  E-value: 1.32e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622960446 695 VVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEvygiADKIEFICGDFLLLAACL-KADVVFLS 764
Cdd:COG2227    28 VLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAA----ELNVDFVQGDLEDLPLEDgSFDLVICS 94
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 685-748 1.75e-09

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: 60.26  E-value: 1.75e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622960446 685 RVSQSFKCD-VVVDAFCGVGGNTIQFA-LTGMRVIAIDIDPVKIALARNNAEVYGIADKIEFICGD 748
Cdd:COG2520   173 RIAELVKPGeRVLDMFAGVGPFSIPIAkRSGAKVVAIDINPDAVEYLKENIRLNKVEDRVTPILGD 238
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 695-764 2.98e-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: 2.98e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622960446 695 VVDAFCGVGGNTIQFA-LTGMRVIAIDIDPVKIALARNNAEVYGIaDKIEFICGDFL-LLAACL-KADVVFLS 764
Cdd:COG0500    30 VLDLGCGTGRNLLALAaRFGGRVIGIDLSPEAIALARARAAKAGL-GNVEFLVADLAeLDPLPAeSFDLVVAF 101
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 695-764 4.83e-09

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 54.11  E-value: 4.83e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622960446 695 VVDAFCGVGGNTIQFA-LTGMRVIAIDIDPVKIALARNNAEVYGIadKIEFICGDFL-LLAACLKADVVFLS 764
Cdd:pfam13649   1 VLDLGCGTGRLTLALArRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEdLPFPDGSFDLVVSS 70
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
663-769 8.27e-09

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 56.45  E-value: 8.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960446 663 IKLDREGWFS---------VTPEKIAEHI--AGRVSQSFKCDVVVDAFCGVGGNTIQFALTGM-RVIAIDIDPVKIALAR 730
Cdd:COG2263     6 IILEKLPGFSnpkveleqyPTPAELAAELlhLAYLRGDIEGKTVLDLGCGTGMLAIGAALLGAkKVVGVDIDPEALEIAR 85

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1622960446 731 NNAEvyGIADKIEFICGDFLLLAACLKADVVFLSPPWGG 769
Cdd:COG2263    86 ENAE--RLGVRVDFIRADVTRIPLGGSVDTVVMNPPFGA 122
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 693-768 9.51e-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: 55.82  E-value: 9.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960446 693 DVVVDAFCGVGGNTIQFALTGMRVI-------------AIDIDPVKIALARNNAEVYGIADKIEFICGDFLLL-AACLKA 758
Cdd:pfam01170  30 DPLLDPMCGSGTILIEAALMGANIApgkfdarvraplyGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADLpLLEGSV 109

                          90
                  ....*....|
gi 1622960446 759 DVVFLSPPWG 768
Cdd:pfam01170 110 DVIVTNPPYG 119
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 695-762 4.53e-08

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 53.39  E-value: 4.53e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622960446 695 VVDAFCGVGGNTIQFA-LTGMRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLAACLKADVVF 762
Cdd:COG2230    55 VLDIGCGWGGLALYLArRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIV 123
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 701-763 1.22e-07

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: 52.49  E-value: 1.22e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960446 701 GVGGNTIQFALtGM----RVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLAACLKA---DVVFL 763
Cdd:COG4122    26 GTGYSTLWLAR-ALpddgRLTTIEIDPERAAIARENFARAGLADRIRLILGDALEVLPRLADgpfDLVFI 94
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 694-766 3.89e-07

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 52.46  E-value: 3.89e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622960446 694 VVVDAFCGVG--GNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFL-LLAACLKADVVfLS-PP 766
Cdd:COG2890   115 RVLDLGTGSGaiALALAKERPDARVTAVDISPDALAVARRNAERLGLEDRVRFLQGDLFePLPGDGRFDLI-VSnPP 190
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 693-752 6.78e-07

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: 49.61  E-value: 6.78e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960446 693 DVVVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIadKIEFICGDFLLL 752
Cdd:COG2226    24 ARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDL 81
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 690-763 1.18e-06

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 49.80  E-value: 1.18e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622960446 690 FKCDVVVDAFCGVGGNTIQFAL---TGMRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLAACL--KADVVFL 763
Cdd:PRK00377   39 RKGDMILDIGCGTGSVTVEASLlvgETGKVYAVDKDEKAINLTRRNAEKFGVLNNIVLIKGEAPEILFTIneKFDRIFI 117
rumA TIGR00479
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ...
 693-771 4.50e-06

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: 49.82  E-value: 4.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960446 693 DVVVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIADkIEFICGDF-----LLLAACLKADVVFLSPPW 767
Cdd:TIGR00479 294 ERVLDAYCGMGTFTLPLAKQAKSVVGVEGVPESVEKAQQNAELNGIAN-VTFYHGTLetvlpKQPWAGNGFDKVLLDPPR 372


                  ....
gi 1622960446 768 GGPD 771
Cdd:TIGR00479 373 KGCA 376
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 691-767 5.37e-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: 48.60  E-value: 5.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960446 691 KCDVVVDAFCGVGgnTIQFALT----GMRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLAACLKA---DVVFL 763
Cdd:COG4123    37 KGGRVLDLGTGTG--VIALMLAqrspGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAAELPPgsfDLVVS 114


                  ....
gi 1622960446 764 SPPW 767
Cdd:COG4123   115 NPPY 118
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
715-762 6.22e-06

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 49.02  E-value: 6.22e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622960446 715 RVIAIDIDPVKIALARNNAEVYGIADKIEFICGDfllLAACLKADVVF 762
Cdd:COG2264   173 RVLAVDIDPVAVEAARENAELNGVEDRIEVVLGD---LLEDGPYDLVV 217
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 695-748 3.20e-05

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 45.98  E-value: 3.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622960446 695 VVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIADKIEFICGD 748
Cdd:PRK07580   67 ILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLAGNITFEVGD 120
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 714-768 8.88e-05

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: 45.86  E-value: 8.88e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622960446 714 MRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLAACLKADVVFLSPPWG 768
Cdd:COG0116   251 LPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLEPPAEPGLIITNPPYG 305
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
691-761 1.07e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 44.64  E-value: 1.07e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622960446 691 KCDVVVDAFCGVGgntiqfALTGM-------RVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLAACLKADVV 761
Cdd:COG4076    35 PGDVVLDIGTGSG------LLSMLaaragakKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDLPEKADVI 106
rumB PRK03522
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
695-766 1.29e-04

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


Pssm-ID: 235128 [Multi-domain]  Cd Length: 315  Bit Score: 44.86  E-value: 1.29e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622960446 695 VVDAFCGVGGntiqFAL----TGMRVIAIDIDPVKIALARNNAEVYGIaDKIEFICGD---FlLLAACLKADVVFLSPP 766
Cdd:PRK03522  177 MWDLFCGVGG----FGLhcatPGMQLTGIEISAEAIACAKQSAAELGL-TNVQFQALDstqF-ATAQGEVPDLVLVNPP 249
PRK14968 PRK14968
putative methyltransferase; Provisional
 693-766 1.55e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 43.35  E-value: 1.55e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622960446 693 DVVVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIAD-KIEFICGDfllLAACLKA---DVVFLSPP 766
Cdd:PRK14968   25 DRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNnGVEVIRSD---LFEPFRGdkfDVILFNPP 99
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 696-764 1.63e-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: 1.63e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622960446 696 VDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEvygiADKIEFICGDFLLLAacLK---ADVVFLS 764
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAP----REGLTFVVGDAEDLP--FPdnsFDLVLSS 66
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 694-762 1.66e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 42.79  E-value: 1.66e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622960446 694 VVVDAFCGVGGNTIQFA-LTGM--RVIAIDIDPVKIALARNNAEVYGIaDKIEFICGDFLLLAACL---KADVVF 762
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAeELGPnaEVVGIDISEEAIEKARENAQKLGF-DNVEFEQGDIEELPELLeddKFDVVI 79
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 676-809 3.16e-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: 43.50  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960446 676 EKIAEHIAGRVSQSFKCDVVVDAFCGVGGNTIQFALT--GMRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLA 753
Cdd:TIGR00536  99 EELVEKALASLISQPPILHILDLGTGSGCIALALAYEfpNAEVIAVDISPDALAVAEENAEKNQLEHRVEFIQSNLFEPL 178

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622960446 754 ACLKADVVFLSPPwggpdYATAETFDIRTMM-----------SPDGFEIfrlSKKITNNIVYFLPRN 809
Cdd:TIGR00536 179 AGQKIDIIVSNPP-----YIDEEDLADLPNVvrfepllalvgGDDGLNI---LRQIIELAPDYLKPN 237
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 694-766 3.58e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 43.23  E-value: 3.58e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622960446 694 VVVDAFCGVG--GNTIQFALTGMRVIAIDIDPVKIALARNNAEvYGIADKIEFICGDFLLLAACLKADVVfLS-PP 766
Cdd:PRK09328  111 RVLDLGTGSGaiALALAKERPDAEVTAVDISPEALAVARRNAK-HGLGARVEFLQGDWFEPLPGGRFDLI-VSnPP 184
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 695-788 3.78e-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: 42.48  E-value: 3.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960446 695 VVDAFCGVG--GNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIADkIEFICGDFLLLAACLKADVVFLSPPW---GG 769
Cdd:COG2813    53 VLDLGCGYGviGLALAKRNPEARVTLVDVNARAVELARANAAANGLEN-VEVLWSDGLSGVPDGSFDLILSNPPFhagRA 131

                          90       100
                  ....*....|....*....|.
gi 1622960446 770 PDYATAETF--DIRTMMSPDG 788
Cdd:COG2813   132 VDKEVAHALiaDAARHLRPGG 152
Met_10 pfam02475
Met-10+ like-protein; The methionine-10 mutant allele of N. crassa codes for a protein of ...
 693-748 7.32e-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: 41.57  E-value: 7.32e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622960446 693 DVVVDAFCGVGGNTIQFALTG--MRVIAIDIDPVKIALARNNAEVYGIADKIEFICGD 748
Cdd:pfam02475 101 EVVVDMFAGIGPFSIPIAKHSkaRRVYAIELNPESYKYLKENIKLNKVEDVVKPILGD 158
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 715-768 1.70e-03

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: 42.10  E-value: 1.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622960446 715 RVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLAACLKAD---VVFLSPPWG 768
Cdd:PRK11783  258 KFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKNPLPKGptgLVISNPPYG 314
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 693-769 2.91e-03

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: 40.92  E-value: 2.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960446 693 DVVVDAFCGVGGNTIQFALT--GMRVIAIDIDPVKIALARNNAEVYGIADkIEFICGDflllA-ACL----KADVVFLsp 765
Cdd:COG2242   249 DVLWDIGAGSGSVSIEAARLapGGRVYAIERDPERAALIRANARRFGVPN-VEVVEGE----ApEALadlpDPDAVFI-- 321


                  ....
gi 1622960446 766 pwGG 769
Cdd:COG2242   322 --GG 323
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 701-730 6.00e-03

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: 39.92  E-value: 6.00e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1622960446 701 GVGGNTIQFA-LTGMRVIAIDIDPVKIALAR 730
Cdd:cd08254   176 GLGLNAVQIAkAMGAAVIAVDIKEEKLELAK 206
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
644-764 6.22e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 38.44  E-value: 6.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960446 644 ELAKYWAQRYRLFS-RFDDGIkldREGWFSVTPEKIAEHIAGRVsQSFKCDVVVDAFCGVGGNTIQFALTGMRVIAIDID 722
Cdd:COG4976     2 ALDAYVEALFDQYAdSYDAAL---VEDLGYEAPALLAEELLARL-PPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLS 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622960446 723 PVKIALARNNAeVYgiadkIEFICGDFL-LLAACLKADVVFLS 764
Cdd:COG4976    78 EEMLAKAREKG-VY-----DRLLVADLAdLAEPDGRFDLIVAA 114
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
715-761 6.55e-03

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 39.36  E-value: 6.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1622960446 715 RVIAIDIDPVKIALARNNAEVYGIADKIEFICGDflllaacLKADVV 761
Cdd:PRK00517  144 KVLAVDIDPQAVEAARENAELNGVELNVYLPQGD-------LKADVI 183
PRK08317 PRK08317
hypothetical protein; Provisional
 691-748 9.42e-03

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 38.76  E-value: 9.42e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622960446 691 KCDVVVDAFCGVGGNTIQFAL----TGmRVIAIDIDPVKIALARNNAEvyGIADKIEFICGD 748
Cdd:PRK08317   19 PGDRVLDVGCGPGNDARELARrvgpEG-RVVGIDRSEAMLALAKERAA--GLGPNVEFVRGD 77
 
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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