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Conserved domains on  [gi|227496324|ref|NP_473430|]
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trimethylguanosine synthase [Mus musculus]

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; ...
 683-835 1.78e-46

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: 163.27  E-value: 1.78e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227496324  683 CDVVVDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNAEVYGIADKIEFICGDFL-LLAPC----LKADVVFLSPP 757
Cdd:pfam09445   1 ATRILDVFCGGGGNTIQFANVFDSVISIDINLEHLACAQHNAEVYGVSDRIWLIHGDWFeLLAKLkfekIKYDCVFASPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227496324  758 WGGPDYATAETFDIRTMMSPDGFE-IFRLSQKITNNIVYFLPRNADIDQVAS----LAGLGGQVEIEQNFLNNKLKTITA 832
Cdd:pfam09445  81 WGGPSYKKQNVYDLENKLQPYGLSqLLKEFTKISKNVILFLPRNSDLNQLSAltreVLGPEAKCKVLYIKENGYMKGLLC 160


                  ...
gi 227496324  833 YFG 835
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 ...
 683-835 1.78e-46

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: 163.27  E-value: 1.78e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227496324  683 CDVVVDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNAEVYGIADKIEFICGDFL-LLAPC----LKADVVFLSPP 757
Cdd:pfam09445   1 ATRILDVFCGGGGNTIQFANVFDSVISIDINLEHLACAQHNAEVYGVSDRIWLIHGDWFeLLAKLkfekIKYDCVFASPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227496324  758 WGGPDYATAETFDIRTMMSPDGFE-IFRLSQKITNNIVYFLPRNADIDQVAS----LAGLGGQVEIEQNFLNNKLKTITA 832
Cdd:pfam09445  81 WGGPSYKKQNVYDLENKLQPYGLSqLLKEFTKISKNVILFLPRNSDLNQLSAltreVLGPEAKCKVLYIKENGYMKGLLC 160


                  ...
gi 227496324  833 YFG 835
Cdd:pfam09445 161 YFG 163
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 686-779 9.46e-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: 62.45  E-value: 9.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227496324 686 VVDAFCGVGGNTIQFALT-GKRVIAIDIDPVKIDLARNNAEvYGIADKIEFICGDF--LLLAPCLKADVVFLSPPWGGPD 762
Cdd:cd02440    2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAA-ALLADNVEVLKGDAeeLPPEADESFDVIISDPPLHHLV 80

                         90
                 ....*....|....*...
gi 227496324 763 YATAETFD-IRTMMSPDG 779
Cdd:cd02440   81 EDLARFLEeARRLLKPGG 98
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 660-757 1.33e-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: 67.12  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227496324 660 GWFSVTPEkIAEHIAGRVSQAFRC---DVVVDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNAEVYGIaDKIEFI 736
Cdd:COG2265  209 SFFQVNPE-QAEALYAAALEWLDLtggERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGL-KNVEFV 286

                         90       100
                 ....*....|....*....|....*
gi 227496324 737 CGD---FLL-LAPCLKADVVFLSPP 757
Cdd:COG2265  287 AGDleeVLPeLLWGGRPDVVVLDPP 311
rumA TIGR00479
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ...
 650-762 5.58e-08

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: 55.98  E-value: 5.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227496324  650 FDDGIK--LDKEGWFSVTPEkIAEHIAGRVSQAFRC---DVVVDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNA 724
Cdd:TIGR00479 256 KSGDLSftFSARDFIQVNSG-QNEKLVDRALEWLELqgeERVLDAYCGMGTFTLPLAKQAKSVVGVEGVPESVEKAQQNA 334

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 227496324  725 EVYGIADkIEFICGDFLLLAPCL-----KADVVFLSPPWGGPD 762
Cdd:TIGR00479 335 ELNGIAN-VTFYHGTLETVLPKQpwagnGFDKVLLDPPRKGCA 376
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 681-754 3.03e-07

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 51.72  E-value: 3.03e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 227496324 681 FRCDVVVDAFCGVGGNTIQFAL---TGKRVIAIDIDPVKIDLARNNAEVYGIADKIEFICGDFLLLAPCL--KADVVFL 754
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 ...
 683-835 1.78e-46

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: 163.27  E-value: 1.78e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227496324  683 CDVVVDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNAEVYGIADKIEFICGDFL-LLAPC----LKADVVFLSPP 757
Cdd:pfam09445   1 ATRILDVFCGGGGNTIQFANVFDSVISIDINLEHLACAQHNAEVYGVSDRIWLIHGDWFeLLAKLkfekIKYDCVFASPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227496324  758 WGGPDYATAETFDIRTMMSPDGFE-IFRLSQKITNNIVYFLPRNADIDQVAS----LAGLGGQVEIEQNFLNNKLKTITA 832
Cdd:pfam09445  81 WGGPSYKKQNVYDLENKLQPYGLSqLLKEFTKISKNVILFLPRNSDLNQLSAltreVLGPEAKCKVLYIKENGYMKGLLC 160


                  ...
gi 227496324  833 YFG 835
Cdd:pfam09445 161 YFG 163
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 686-779 9.46e-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: 62.45  E-value: 9.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227496324 686 VVDAFCGVGGNTIQFALT-GKRVIAIDIDPVKIDLARNNAEvYGIADKIEFICGDF--LLLAPCLKADVVFLSPPWGGPD 762
Cdd:cd02440    2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAA-ALLADNVEVLKGDAeeLPPEADESFDVIISDPPLHHLV 80

                         90
                 ....*....|....*...
gi 227496324 763 YATAETFD-IRTMMSPDG 779
Cdd:cd02440   81 EDLARFLEeARRLLKPGG 98
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 660-757 1.33e-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: 67.12  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227496324 660 GWFSVTPEkIAEHIAGRVSQAFRC---DVVVDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNAEVYGIaDKIEFI 736
Cdd:COG2265  209 SFFQVNPE-QAEALYAAALEWLDLtggERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGL-KNVEFV 286

                         90       100
                 ....*....|....*....|....*
gi 227496324 737 CGD---FLL-LAPCLKADVVFLSPP 757
Cdd:COG2265  287 AGDleeVLPeLLWGGRPDVVVLDPP 311
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 684-759 1.91e-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: 63.43  E-value: 1.91e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 227496324 684 DVVVDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNAEVYGIADkIEFICGDFLLLA-PCLKADVVFLSPPWG 759
Cdd:COG1041   28 DTVLDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGARENLEHYGYED-ADVIRGDARDLPlADESVDAIVTDPPYG 103
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 684-752 2.24e-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: 62.96  E-value: 2.24e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227496324 684 DVVVDAFCGVGGNTIQFA-LTGKRVIAIDIDPVKIDLARNNAEVYGIADKIEFICGDFLLLAPCL--KADVV 752
Cdd:COG2520  182 ERVLDMFAGVGPFSIPIAkRSGAKVVAIDINPDAVEYLKENIRLNKVEDRVTPILGDAREVAPELegKADRI 253
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
654-760 3.39e-10

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 60.30  E-value: 3.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227496324 654 IKLDKEGWFS---------VTPEKIAEHI--AGRVSQAFRCDVVVDAFCGVGGNTIQFALTG-KRVIAIDIDPVKIDLAR 721
Cdd:COG2263    6 IILEKLPGFSnpkveleqyPTPAELAAELlhLAYLRGDIEGKTVLDLGCGTGMLAIGAALLGaKKVVGVDIDPEALEIAR 85

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 227496324 722 NNAEvyGIADKIEFICGDFLLLAPCLKADVVFLSPPWGG 760
Cdd:COG2263   86 ENAE--RLGVRVDFIRADVTRIPLGGSVDTVVMNPPFGA 122
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 686-755 1.53e-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: 1.53e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227496324  686 VVDAFCGVGGNTIQFA-LTGKRVIAIDIDPVKIDLARNNAEVYGIadKIEFICGDFL-LLAPCLKADVVFLS 755
Cdd:pfam13649   1 VLDLGCGTGRLTLALArRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEdLPFPDGSFDLVVSS 70
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 686-755 1.84e-09

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 58.39  E-value: 1.84e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227496324 686 VVDAFCGVGGNTIQFA-LTGKRVIAIDIDPVKIDLARNNAEVYGIaDKIEFICGDF--LLLAPCLKADVVFLS 755
Cdd:COG0500   30 VLDLGCGTGRNLLALAaRFGGRVIGIDLSPEAIALARARAAKAGL-GNVEFLVADLaeLDPLPAESFDLVVAF 101
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 667-755 2.12e-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: 56.18  E-value: 2.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227496324 667 EKIAEHIAGRVSQAFRcdvVVDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNAEvygiADKIEFICGDFLLLAPC 746
Cdd:COG2227   12 RRLAALLARLLPAGGR---VLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAA----ELNVDFVQGDLEDLPLE 84

                         90
                 ....*....|
gi 227496324 747 L-KADVVFLS 755
Cdd:COG2227   85 DgSFDLVICS 94
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 684-759 3.10e-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: 57.37  E-value: 3.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227496324  684 DVVVDAFCGVGGNTIQFALTGKRVI-------------AIDIDPVKIDLARNNAEVYGIADKIEFICGDFLLL-APCLKA 749
Cdd:pfam01170  30 DPLLDPMCGSGTILIEAALMGANIApgkfdarvraplyGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADLpLLEGSV 109

                          90
                  ....*....|
gi 227496324  750 DVVFLSPPWG 759
Cdd:pfam01170 110 DVIVTNPPYG 119
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 686-753 4.88e-08

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 53.01  E-value: 4.88e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 227496324 686 VVDAFCGVGGNTIQFA-LTGKRVIAIDIDPVKIDLARNNAEVYGIADKIEFICGDFLLLAPCLKADVVF 753
Cdd:COG2230   55 VLDIGCGWGGLALYLArRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIV 123
rumA TIGR00479
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ...
 650-762 5.58e-08

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: 55.98  E-value: 5.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227496324  650 FDDGIK--LDKEGWFSVTPEkIAEHIAGRVSQAFRC---DVVVDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNA 724
Cdd:TIGR00479 256 KSGDLSftFSARDFIQVNSG-QNEKLVDRALEWLELqgeERVLDAYCGMGTFTLPLAKQAKSVVGVEGVPESVEKAQQNA 334

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 227496324  725 EVYGIADkIEFICGDFLLLAPCL-----KADVVFLSPPWGGPD 762
Cdd:TIGR00479 335 ELNGIAN-VTFYHGTLETVLPKQpwagnGFDKVLLDPPRKGCA 376
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 692-754 5.91e-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: 53.26  E-value: 5.91e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 227496324 692 GVGGNTIQFAL---TGKRVIAIDIDPVKIDLARNNAEVYGIADKIEFICGDFLLLAPCLKA---DVVFL 754
Cdd:COG4122   26 GTGYSTLWLARalpDDGRLTTIEIDPERAAIARENFARAGLADRIRLILGDALEVLPRLADgpfDLVFI 94
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 681-754 3.03e-07

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 51.72  E-value: 3.03e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 227496324 681 FRCDVVVDAFCGVGGNTIQFAL---TGKRVIAIDIDPVKIDLARNNAEVYGIADKIEFICGDFLLLAPCL--KADVVFL 754
Cdd:PRK00377  39 RKGDMILDIGCGTGSVTVEASLlvgETGKVYAVDKDEKAINLTRRNAEKFGVLNNIVLIKGEAPEILFTIneKFDRIFI 117
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 684-743 5.53e-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: 5.53e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 227496324 684 DVVVDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNAEVYGIadKIEFICGDFLLL 743
Cdd:COG2226   24 ARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDL 81
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
686-755 6.05e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 48.28  E-value: 6.05e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227496324 686 VVDAFCGVGGNTIQFA--LTGKRVIAIDIDPVKIDLARNNAevygiaDKIEFICGDFLLLAPCLKADVVFLS 755
Cdd:COG4106    5 VLDLGCGTGRLTALLAerFPGARVTGVDLSPEMLARARARL------PNVRFVVADLRDLDPPEPFDLVVSN 70
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
705-753 7.71e-07

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 51.71  E-value: 7.71e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 227496324 705 KRVIAIDIDPVKIDLARNNAEVYGIADKIEFICGDfllLAPCLKADVVF 753
Cdd:COG2264  172 KRVLAVDIDPVAVEAARENAELNGVEDRIEVVLGD---LLEDGPYDLVV 217
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 686-758 1.71e-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: 1.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227496324 686 VVDAFCGVGgnTIQFALTGK----RVIAIDIDPVKIDLARNNAEVYGIADKIEFICGDFLLLAPCLKA---DVVFLSPPW 758
Cdd:COG4123   41 VLDLGTGTG--VIALMLAQRspgaRITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAAELPPgsfDLVVSNPPY 118
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 685-757 2.34e-06

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 50.15  E-value: 2.34e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 227496324 685 VVVDAFCGVG--GNTIQFALTGKRVIAIDIDPVKIDLARNNAEVYGIADKIEFICGDFL-LLAPCLKADVVfLS-PP 757
Cdd:COG2890  115 RVLDLGTGSGaiALALAKERPDARVTAVDISPDALAVARRNAERLGLEDRVRFLQGDLFePLPGDGRFDLI-VSnPP 190
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
683-752 7.65e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 48.11  E-value: 7.65e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 227496324 683 CDVVVDAFCGVGGNTIQFALTG-KRVIAIDIDPVKIDLARNNAEVYGIADKIEFICGDFLLLAPCLKADVV 752
Cdd:COG4076   36 GDVVLDIGTGSGLLSMLAARAGaKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDLPEKADVI 106
PRK14968 PRK14968
putative methyltransferase; Provisional
 684-757 7.83e-06

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 47.20  E-value: 7.83e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 227496324 684 DVVVDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNAEVYGIAD-KIEFICGDfllLAPCLKA---DVVFLSPP 757
Cdd:PRK14968  25 DRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNnGVEVIRSD---LFEPFRGdkfDVILFNPP 99
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 706-759 2.68e-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: 47.40  E-value: 2.68e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 227496324 706 RVIAIDIDPVKIDLARNNAEVYGIADKIEFICGDFLLLAPCLKADVVFLSPPWG 759
Cdd:COG0116  252 PIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLEPPAEPGLIITNPPYG 305
Met_10 pfam02475
Met-10+ like-protein; The methionine-10 mutant allele of N. crassa codes for a protein of ...
 684-757 2.88e-05

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: 45.81  E-value: 2.88e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227496324  684 DVVVDAFCGVGGNTIQFALTGK--RVIAIDIDPVKIDLARNNAEVYGIADKIEFICGDFLLLAPCLKADVVFLSPP 757
Cdd:pfam02475 101 EVVVDMFAGIGPFSIPIAKHSKarRVYAIELNPESYKYLKENIKLNKVEDVVKPILGDVREVILEDVADRVVMNLP 176
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 686-739 3.41e-05

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 45.98  E-value: 3.41e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 227496324 686 VVDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNAEVYGIADKIEFICGD 739
Cdd:PRK07580  67 ILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLAGNITFEVGD 120
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 687-755 1.49e-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: 1.49e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227496324  687 VDAFCGVGGNTIQFALTGKRVIAIDIDPVKIDLARNNAEvygiADKIEFICGDFLLLApcLK---ADVVFLS 755
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAP----REGLTFVVGDAEDLP--FPdnsFDLVLSS 66
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 685-753 1.54e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 42.79  E-value: 1.54e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 227496324  685 VVVDAFCGVGGNTIQFAL---TGKRVIAIDIDPVKIDLARNNAEVYGIaDKIEFICGDFLLLAPCL---KADVVF 753
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAEelgPNAEVVGIDISEEAIEKARENAQKLGF-DNVEFEQGDIEELPELLeddKFDVVI 79
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 686-779 1.86e-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: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227496324 686 VVDAFCGVG--GNTIQFALTGKRVIAIDIDPVKIDLARNNAEVYGIADkIEFICGDFLLLAPCLKADVVFLSPPW---GG 760
Cdd:COG2813   53 VLDLGCGYGviGLALAKRNPEARVTLVDVNARAVELARANAAANGLEN-VEVLWSDGLSGVPDGSFDLILSNPPFhagRA 131

                         90       100
                 ....*....|....*....|.
gi 227496324 761 PDYATAETF--DIRTMMSPDG 779
Cdd:COG2813  132 VDKEVAHALiaDAARHLRPGG 152
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 686-753 2.04e-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: 2.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227496324  686 VVDAFCGVGGNTIQFALTG-KRVIAIDIDPVKIDLARNNAEVYGIADKIE-FICGDflllAPCLKADVVF 753
Cdd:pfam06325 165 VLDVGCGSGILAIAALKLGaKKVVGVDIDPVAVRAAKENAELNGVEARLEvYLPGD----LPKEKADVVV 230
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
705-752 4.27e-04

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 42.83  E-value: 4.27e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 227496324 705 KRVIAIDIDPVKIDLARNNAEVYGIADKIEFICGDflllapcLKADVV 752
Cdd:PRK00517 143 KKVLAVDIDPQAVEAARENAELNGVELNVYLPQGD-------LKADVI 183
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 706-757 6.50e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 42.46  E-value: 6.50e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 227496324 706 RVIAIDIDPVKIDLARNNAEvYGIADKIEFICGDFLLLAPCLKADVVfLS-PP 757
Cdd:PRK09328 134 EVTAVDISPEALAVARRNAK-HGLGARVEFLQGDWFEPLPGGRFDLI-VSnPP 184
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 692-770 7.42e-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: 42.62  E-value: 7.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227496324 692 GVGGNTIQFA-LTGKRVIAIDIDPVKIDLARNNAEVYGIADKIEFICGDFLLLAPcLKADVVFlsppwggpDYA-TAETF 769
Cdd:cd08254  176 GLGLNAVQIAkAMGAAVIAVDIKEEKLELAKELGADEVLNSLDDSPKDKKAAGLG-GGFDVIF--------DFVgTQPTF 246


                 .
gi 227496324 770 D 770
Cdd:cd08254  247 E 247
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 684-760 8.13e-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: 42.85  E-value: 8.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227496324 684 DVVVDAFCGVGGNTIQFALTGK--RVIAIDIDPVKIDLARNNAEVYGIADkIEFICGDflllAP-CL----KADVVFLsp 756
Cdd:COG2242  249 DVLWDIGAGSGSVSIEAARLAPggRVYAIERDPERAALIRANARRFGVPN-VEVVEGE----APeALadlpDPDAVFI-- 321


                 ....
gi 227496324 757 pwGG 760
Cdd:COG2242  322 --GG 323
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
635-755 9.58e-04

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 41.14  E-value: 9.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227496324 635 ELAKYWAQRYRLFS-RFDDGIKldkEGWFSVTPEKIAEHIAGRVsQAFRCDVVVDAFCGVGGNTIQFALTGKRVIAIDID 713
Cdd:COG4976    2 ALDAYVEALFDQYAdSYDAALV---EDLGYEAPALLAEELLARL-PPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLS 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 227496324 714 PVKIDLARNNAeVYgiadkIEFICGDFL-LLAPCLKADVVFLS 755
Cdd:COG4976   78 EEMLAKAREKG-VY-----DRLLVADLAdLAEPDGRFDLIVAA 114
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 703-759 9.84e-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: 42.87  E-value: 9.84e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 227496324 703 TGKRVIAIDIDPVKIDLARNNAEVYGIADKIEFICGDFLLLAPCLKAD---VVFLSPPWG 759
Cdd:PRK11783 255 LPSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKNPLPKGptgLVISNPPYG 314
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 667-758 1.52e-03

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: 41.57  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227496324  667 EKIAEHIAGRVSQAFRCDVVVDAFCGVGGNTIQFALT--GKRVIAIDIDPVKIDLARNNAEVYGIADKIEFICGDFLLLA 744
Cdd:TIGR00536  99 EELVEKALASLISQPPILHILDLGTGSGCIALALAYEfpNAEVIAVDISPDALAVAEENAEKNQLEHRVEFIQSNLFEPL 178

                          90
                  ....*....|....
gi 227496324  745 PCLKADVVFLSPPW 758
Cdd:TIGR00536 179 AGQKIDIIVSNPPY 192
PRK08317 PRK08317
hypothetical protein; Provisional
 679-739 2.21e-03

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 40.69  E-value: 2.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227496324 679 QAFRCDVVVDAFCGVGGNTIQFA-LTGK--RVIAIDIDPVKIDLARNNAEvyGIADKIEFICGD 739
Cdd:PRK08317  16 AVQPGDRVLDVGCGPGNDARELArRVGPegRVVGIDRSEAMLALAKERAA--GLGPNVEFVRGD 77
rumB PRK03522
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
686-757 2.65e-03

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


Pssm-ID: 235128 [Multi-domain]  Cd Length: 315  Bit Score: 40.62  E-value: 2.65e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 227496324 686 VVDAFCGVGGntiqFAL----TGKRVIAIDIDPVKIDLARNNAEVYGIaDKIEFICGD---FLLLAPcLKADVVFLSPP 757
Cdd:PRK03522 177 MWDLFCGVGG----FGLhcatPGMQLTGIEISAEAIACAKQSAAELGL-TNVQFQALDstqFATAQG-EVPDLVLVNPP 249
PTZ00338 PTZ00338
dimethyladenosine transferase-like protein; Provisional
 684-741 5.40e-03

dimethyladenosine transferase-like protein; Provisional


Pssm-ID: 240367 [Multi-domain]  Cd Length: 294  Bit Score: 39.60  E-value: 5.40e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227496324 684 DVVVDAFCGVGGNTIQFALTGKRVIAIDIDPvkidlaRNNAEV------YGIADKIEFICGDFL 741
Cdd:PTZ00338  38 DTVLEIGPGTGNLTEKLLQLAKKVIAIEIDP------RMVAELkkrfqnSPLASKLEVIEGDAL 95
 
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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