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Conserved domains on  [gi|2065126112|ref|XP_042154502|]
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7SK snRNA methylphosphate capping enzyme [Oncorhynchus tshawytscha]

Protein Classification

BCDIN3 domain-containing RNA methyltransferase( domain architecture ID 11224030)

BCDIN3 domain-containing RNA methyltransferase acts as O-methyltransferase that specifically monomethylates 5'-monophosphate of cytoplasmic histidyl tRNA (tRNA(His)), acting as a capping enzyme by protecting tRNA(His) from cleavage by DICER1

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Bin3 pfam06859
Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of ...
638-740 5.63e-51

Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of approximately 120 residues within eukaryotic Bicoid-interacting protein 3 (Bin3). Bin3, which shows similarity to a number of protein methyltransferases that modify RNA-binding proteins, interacts with Bicoid, which itself directs pattern formation in the early Drosophila embryo. The interaction might allow Bicoid to switch between its dual roles in transcription and translation. Note that family members contain a conserved HLN motif.


:

Pssm-ID: 462022  Cd Length: 109  Bit Score: 173.11  E-value: 5.63e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065126112 638 YDVILCLGVTKWVQLHGGDGGVVRMFRQIYTHLRPGGILLLEPQPWSSYCRSKNITETTYRNYCDIRLRPDNFCCYLTST 717
Cdd:pfam06859   1 YDVILCLSVTKWIHLNWGDEGLKRFFKRIYSLLRPGGVLILEPQPWKSYKKAKRLSETIKANYKTIQLRPEDFEEYLLSE 80
                          90       100
                  ....*....|....*....|....*....
gi 2065126112 718 VGFTCYRLLTDT------GFQRPIYLFHK 740
Cdd:pfam06859  81 VGFESVEELGSTpegkskGFDRPIYLFRK 109
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
443-486 1.24e-10

Trans-aconitate methyltransferase [Energy production and conversion];


:

Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 58.68  E-value: 1.24e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2065126112 443 RGKTVLDIGCSTGHLTLAIARHFNPAHILGIDVDGRLVHAARQN 486
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARAR 44
 
Name Accession Description Interval E-value
Bin3 pfam06859
Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of ...
638-740 5.63e-51

Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of approximately 120 residues within eukaryotic Bicoid-interacting protein 3 (Bin3). Bin3, which shows similarity to a number of protein methyltransferases that modify RNA-binding proteins, interacts with Bicoid, which itself directs pattern formation in the early Drosophila embryo. The interaction might allow Bicoid to switch between its dual roles in transcription and translation. Note that family members contain a conserved HLN motif.


Pssm-ID: 462022  Cd Length: 109  Bit Score: 173.11  E-value: 5.63e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065126112 638 YDVILCLGVTKWVQLHGGDGGVVRMFRQIYTHLRPGGILLLEPQPWSSYCRSKNITETTYRNYCDIRLRPDNFCCYLTST 717
Cdd:pfam06859   1 YDVILCLSVTKWIHLNWGDEGLKRFFKRIYSLLRPGGVLILEPQPWKSYKKAKRLSETIKANYKTIQLRPEDFEEYLLSE 80
                          90       100
                  ....*....|....*....|....*....
gi 2065126112 718 VGFTCYRLLTDT------GFQRPIYLFHK 740
Cdd:pfam06859  81 VGFESVEELGSTpegkskGFDRPIYLFRK 109
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
443-486 1.24e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 58.68  E-value: 1.24e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2065126112 443 RGKTVLDIGCSTGHLTLAIARHFNPAHILGIDVDGRLVHAARQN 486
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARAR 44
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
447-488 2.24e-08

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 52.18  E-value: 2.24e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2065126112 447 VLDIGCSTGHLTLAIARHFNpAHILGIDVDGRLVHAARQNIR 488
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG-ARVTGVDLSPEMLERARERAA 41
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
446-500 2.99e-07

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: 49.35  E-value: 2.99e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2065126112 446 TVLDIGCSTGHLTLAIARHfNPAHILGIDVDGRLVHAARQNIRHFLSER---LTQDAR 500
Cdd:cd02440     1 RVLDLGCGTGALALALASG-PGARVTGVDISPVALELARKAAAALLADNvevLKGDAE 57
PRK08317 PRK08317
hypothetical protein; Provisional
443-485 9.36e-06

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 47.62  E-value: 9.36e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2065126112 443 RGKTVLDIGCSTGHLTLAIARHFNPA-HILGIDVDGRLVHAARQ 485
Cdd:PRK08317   19 PGDRVLDVGCGPGNDARELARRVGPEgRVVGIDRSEAMLALAKE 62
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
612-678 4.92e-05

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 44.15  E-value: 4.92e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2065126112 612 NNVSFITGDYmedRELCPHGddvtaGYDVILCLGVTkwvqLHGGDGGVVRMFRQIYTHLRPGGILLL 678
Cdd:COG2230   101 DRVEVRLADY---RDLPADG-----QFDAIVSIGMF----EHVGPENYPAYFAKVARLLKPGGRLLL 155
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
610-679 1.39e-04

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: 41.65  E-value: 1.39e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065126112 610 FPNNVSFITGDyMEDRELCPHGDdvtagYDVILCLGVtkwvqLHGGDGGVVRMFRQIYTHLRPGGILLLE 679
Cdd:cd02440    45 LADNVEVLKGD-AEELPPEADES-----FDVIISDPP-----LHHLVEDLARFLEEARRLLKPGGVLVLT 103
ovoA_Cterm TIGR04345
putative 4-mercaptohistidine N1-methyltranferase; Ovothiol A is N1-methyl-4-mercaptohistidine. ...
442-493 2.22e-04

putative 4-mercaptohistidine N1-methyltranferase; Ovothiol A is N1-methyl-4-mercaptohistidine. In the absence of S-adenosylmethione, a methyl donor, the intermediate produced is 4-mercaptohistidine. In both Erwinia tasmaniensis and Trypanosoma cruzi, a protein occurs with 5-histidylcysteine sulfoxide synthase activity, but these two enzymes and most homologs share an additional C-terminal methyltransferase domain. Thus OvoA may be a bifunctional enzyme with 5-histidylcysteine sulfoxide synthase and 4-mercaptohistidine N1-methyltranferase activity. This model describes C-terminal putative 4-mercaptohistidine N1-methyltranferase domain. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 275141  Cd Length: 242  Bit Score: 43.36  E-value: 2.22e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2065126112 442 FRGKTVLDIGCSTGHLTLAIARHFNpaHILGIDVDGRLVHAA-----RQNIRHFLSE 493
Cdd:TIGR04345  40 KSRKRALDIGCAVGRASFELARYFD--EVDGIDFSARFIRPAvalkeRGSLRYALKE 94
 
Name Accession Description Interval E-value
Bin3 pfam06859
Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of ...
638-740 5.63e-51

Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of approximately 120 residues within eukaryotic Bicoid-interacting protein 3 (Bin3). Bin3, which shows similarity to a number of protein methyltransferases that modify RNA-binding proteins, interacts with Bicoid, which itself directs pattern formation in the early Drosophila embryo. The interaction might allow Bicoid to switch between its dual roles in transcription and translation. Note that family members contain a conserved HLN motif.


Pssm-ID: 462022  Cd Length: 109  Bit Score: 173.11  E-value: 5.63e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065126112 638 YDVILCLGVTKWVQLHGGDGGVVRMFRQIYTHLRPGGILLLEPQPWSSYCRSKNITETTYRNYCDIRLRPDNFCCYLTST 717
Cdd:pfam06859   1 YDVILCLSVTKWIHLNWGDEGLKRFFKRIYSLLRPGGVLILEPQPWKSYKKAKRLSETIKANYKTIQLRPEDFEEYLLSE 80
                          90       100
                  ....*....|....*....|....*....
gi 2065126112 718 VGFTCYRLLTDT------GFQRPIYLFHK 740
Cdd:pfam06859  81 VGFESVEELGSTpegkskGFDRPIYLFRK 109
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
443-486 1.24e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 58.68  E-value: 1.24e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2065126112 443 RGKTVLDIGCSTGHLTLAIARHFNPAHILGIDVDGRLVHAARQN 486
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARAR 44
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
443-496 8.24e-09

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: 56.69  E-value: 8.24e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2065126112 443 RGKTVLDIGCSTGHLTLAIARHFNPAHILGIDVDGRLVHAARQNIRH-FLSERLT 496
Cdd:COG4123    37 KGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALnGLEDRIT 91
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
431-489 1.63e-08

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: 53.48  E-value: 1.63e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065126112 431 DPRL-GLLRPDWFRGKTVLDIGCSTGHLTLAIARHFnpAHILGIDVDGRLVHAARQNIRH 489
Cdd:COG2227    11 DRRLaALLARLLPAGGRVLDVGCGTGRLALALARRG--ADVTGVDISPEALEIARERAAE 68
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
447-488 2.24e-08

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 52.18  E-value: 2.24e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2065126112 447 VLDIGCSTGHLTLAIARHFNpAHILGIDVDGRLVHAARQNIR 488
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG-ARVTGVDLSPEMLERARERAA 41
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
443-488 1.07e-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: 51.53  E-value: 1.07e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2065126112 443 RGKTVLDIGCSTGHLTLAIARHFnpAHILGIDVDGRLVHAARQNIR 488
Cdd:COG2226    22 PGARVLDLGCGTGRLALALAERG--ARVTGVDISPEMLELARERAA 65
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
444-496 2.37e-07

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 50.88  E-value: 2.37e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2065126112 444 GKTVLDIGCSTGHLTLAIARHFNP-AHILGIDVDGRLVHAARQNIRHFLSERLT 496
Cdd:pfam13847   4 GMRVLDLGCGTGHLSFELAEELGPnAEVVGIDISEEAIEKARENAQKLGFDNVE 57
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
446-500 2.99e-07

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: 49.35  E-value: 2.99e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2065126112 446 TVLDIGCSTGHLTLAIARHfNPAHILGIDVDGRLVHAARQNIRHFLSER---LTQDAR 500
Cdd:cd02440     1 RVLDLGCGTGALALALASG-PGARVTGVDISPVALELARKAAAALLADNvevLKGDAE 57
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
448-490 6.57e-07

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 48.13  E-value: 6.57e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2065126112 448 LDIGCSTGHLTLAIARHFNPAHILGIDVDGRLVHAARQNIRHF 490
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAAL 43
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
433-500 8.60e-07

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 49.16  E-value: 8.60e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2065126112 433 RLGLLRPdwfrGKTVLDIGCSTGHLTLAIARHFNpAHILGIDVDGRLVHAARQNIR-HFLSERLT---QDAR 500
Cdd:COG2230    45 RKLGLKP----GMRVLDIGCGWGGLALYLARRYG-VRVTGVTLSPEQLEYARERAAeAGLADRVEvrlADYR 111
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
443-490 2.51e-06

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 48.76  E-value: 2.51e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2065126112 443 RGKTVLDIGCSTGHLTLAIARHFNpAHILGIDVDGRLVHAARQNIRHF 490
Cdd:COG0500    26 KGGRVLDLGCGTGRNLLALAARFG-GRVIGIDLSPEAIALARARAAKA 72
PRK08317 PRK08317
hypothetical protein; Provisional
443-485 9.36e-06

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 47.62  E-value: 9.36e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2065126112 443 RGKTVLDIGCSTGHLTLAIARHFNPA-HILGIDVDGRLVHAARQ 485
Cdd:PRK08317   19 PGDRVLDVGCGPGNDARELARRVGPEgRVVGIDRSEAMLALAKE 62
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
443-485 1.55e-05

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 46.14  E-value: 1.55e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2065126112 443 RGKTVLDIGCSTGHLTLAIARHFnpAHILGIDVDGRLVHAARQ 485
Cdd:COG4976    46 PFGRVLDLGCGTGLLGEALRPRG--YRLTGVDLSEEMLAKARE 86
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
442-488 3.29e-05

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 45.91  E-value: 3.29e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2065126112 442 FRGKTVLDIGCSTGhlTLAI-ARHFNPAHILGIDVDGRLVHAARQNIR 488
Cdd:PRK00517  118 LPGKTVLDVGCGSG--ILAIaAAKLGAKKVLAVDIDPQAVEAARENAE 163
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
444-488 4.02e-05

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: 45.18  E-value: 4.02e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2065126112 444 GKTVLDIGCSTGHLTLAIARHFNPAHILGIDVDGRLVHAARQNIR 488
Cdd:COG2813    50 GGRVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAA 94
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
612-678 4.92e-05

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 44.15  E-value: 4.92e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2065126112 612 NNVSFITGDYmedRELCPHGddvtaGYDVILCLGVTkwvqLHGGDGGVVRMFRQIYTHLRPGGILLL 678
Cdd:COG2230   101 DRVEVRLADY---RDLPADG-----QFDAIVSIGMF----EHVGPENYPAYFAKVARLLKPGGRLLL 155
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
442-488 5.85e-05

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 45.55  E-value: 5.85e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2065126112 442 FRGKTVLDIGCSTGhlTLAI-ARHFNPAHILGIDVDGRLVHAARQNIR 488
Cdd:COG2264   147 KPGKTVLDVGCGSG--ILAIaAAKLGAKRVLAVDIDPVAVEAARENAE 192
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
444-496 6.92e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 45.03  E-value: 6.92e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2065126112 444 GKTVLDIGCSTGHLTLAIARHfNPAHILGIDVDGRLVHAARQNIRHF-LSERLT 496
Cdd:COG4076    36 GDVVLDIGTGSGLLSMLAARA-GAKKVYAVEVNPDIAAVARRIIAANgLSDRIT 88
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
425-488 8.22e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 44.12  E-value: 8.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065126112 425 QVGRFEDPRLGL------------------LRPDwFRGKTVLDIGCSTGHLTLAiARHFNPAHILGIDVDGRLVHAARQN 486
Cdd:COG2263    10 KLPGFSNPKVELeqyptpaelaaellhlayLRGD-IEGKTVLDLGCGTGMLAIG-AALLGAKKVVGVDIDPEALEIAREN 87

                  ..
gi 2065126112 487 IR 488
Cdd:COG2263    88 AE 89
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
444-487 9.64e-05

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: 44.95  E-value: 9.64e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2065126112 444 GKTVLDIGCSTGHLTLAIARhFNPAHILGIDVDGRLVHAARQNI 487
Cdd:pfam06325 162 GESVLDVGCGSGILAIAALK-LGAKKVVGVDIDPVAVRAAKENA 204
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
443-500 1.06e-04

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: 43.63  E-value: 1.06e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2065126112 443 RGKTVLDIGCSTGHLTLAIARHFNP-AHILGIDVDGRLVHAARQNIRHF-LSERLTQ---DAR 500
Cdd:COG4122    16 GAKRILEIGTGTGYSTLWLARALPDdGRLTTIEIDPERAAIARENFARAgLADRIRLilgDAL 78
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
610-679 1.39e-04

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: 41.65  E-value: 1.39e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065126112 610 FPNNVSFITGDyMEDRELCPHGDdvtagYDVILCLGVtkwvqLHGGDGGVVRMFRQIYTHLRPGGILLLE 679
Cdd:cd02440    45 LADNVEVLKGD-AEELPPEADES-----FDVIISDPP-----LHHLVEDLARFLEEARRLLKPGGVLVLT 103
ovoA_Cterm TIGR04345
putative 4-mercaptohistidine N1-methyltranferase; Ovothiol A is N1-methyl-4-mercaptohistidine. ...
442-493 2.22e-04

putative 4-mercaptohistidine N1-methyltranferase; Ovothiol A is N1-methyl-4-mercaptohistidine. In the absence of S-adenosylmethione, a methyl donor, the intermediate produced is 4-mercaptohistidine. In both Erwinia tasmaniensis and Trypanosoma cruzi, a protein occurs with 5-histidylcysteine sulfoxide synthase activity, but these two enzymes and most homologs share an additional C-terminal methyltransferase domain. Thus OvoA may be a bifunctional enzyme with 5-histidylcysteine sulfoxide synthase and 4-mercaptohistidine N1-methyltranferase activity. This model describes C-terminal putative 4-mercaptohistidine N1-methyltranferase domain. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 275141  Cd Length: 242  Bit Score: 43.36  E-value: 2.22e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2065126112 442 FRGKTVLDIGCSTGHLTLAIARHFNpaHILGIDVDGRLVHAA-----RQNIRHFLSE 493
Cdd:TIGR04345  40 KSRKRALDIGCAVGRASFELARYFD--EVDGIDFSARFIRPAvalkeRGSLRYALKE 94
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
448-500 3.05e-04

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 40.34  E-value: 3.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2065126112 448 LDIGCSTGHLTLAIARHFnpAHILGIDVDGRLVHAARQNIRHFLSERLTQDAR 500
Cdd:pfam08241   1 LDVGCGTGLLTELLARLG--ARVTGVDISPEMLELAREKAPREGLTFVVGDAE 51
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
436-489 7.15e-04

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 41.79  E-value: 7.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2065126112 436 LLRPDWFRGKTVLDIGCSTGHLTLAIARHFNpAHILGIDVDGRLVHAARQNIRH 489
Cdd:COG3897    63 LLDHPEVAGKRVLELGCGLGLVGIAAAKAGA-ADVTATDYDPEALAALRLNAAL 115
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
443-496 7.52e-04

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 42.06  E-value: 7.52e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2065126112 443 RGKTVLDIGCSTGHLTLAIARHFNPAHILGIDVDGRLVHAARQNI-RHFLSERLT 496
Cdd:COG2890   112 APPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAeRLGLEDRVR 166
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
443-496 8.12e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 42.07  E-value: 8.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2065126112 443 RGKTVLDIGCSTGHLTLAIARHFNPAHILGIDVDGRLVHAARQNIRHFLSERLT 496
Cdd:PRK09328  108 EPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGLGARVE 161
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
613-679 8.44e-04

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 40.00  E-value: 8.44e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2065126112 613 NVSFITGDyMEDRELCPhgddvtAGYDVILCLGVTKWVQlhggdgGVVRMFRQIYTHLRPGGILLLE 679
Cdd:COG2227    70 NVDFVQGD-LEDLPLED------GSFDLVICSEVLEHLP------DPAALLRELARLLKPGGLLLLS 123
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
612-680 9.30e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 41.06  E-value: 9.30e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2065126112 612 NNVSFITGDYMEDRELCPhgddvtAGYDVILCLGVTKWVQLHGGDggvvRMFRQIYTHLRPGGILLLEP 680
Cdd:COG0500    75 GNVEFLVADLAELDPLPA------ESFDLVVAFGVLHHLPPEERE----ALLRELARALKPGGVLLLSA 133
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
442-491 1.38e-03

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 41.12  E-value: 1.38e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2065126112 442 FRGKTVLDIGCSTGHLTLAIARHFNPAHILGID-VDGRLVHAARQN--IRHFL 491
Cdd:TIGR02072  33 FIPASVLDIGCGTGYLTRALLKRFPQAEFIALDiSAGMLAQAKTKLseNVQFI 85
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
423-494 1.66e-03

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 39.72  E-value: 1.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2065126112 423 DGQVGRFEDPRLGLLRPDWFRGKTVLDIGCSTGHLTLAIARHFnpAHILGIDVDGRLVHAARQNIRHFLSER 494
Cdd:pfam13489   2 AHQRERLLADLLLRLLPKLPSPGRVLDFGCGTGIFLRLLRAQG--FSVTGVDPSPIAIERALLNVRFDQFDE 71
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
445-485 2.45e-03

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


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 38.71  E-value: 2.45e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2065126112 445 KTVLDIGCSTGHLTLAIARHFNPAHILGIDVDGRLVHAARQ 485
Cdd:pfam13679  27 ITIVDHGAGKGYLGFILYYLKYGVRVYGIDTRAELVEKANA 67
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
443-488 4.19e-03

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 38.73  E-value: 4.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2065126112 443 RGKTVLDIGCSTGHLTLAIARHFNPAHILGIDVDGRLVHAARQNIR 488
Cdd:pfam05175  31 LSGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLA 76
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
434-490 6.79e-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: 39.38  E-value: 6.79e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2065126112 434 LGLLRPdwFRGKTVLDIGCSTGHLTLAIARHFNPAHILGIDVDGRLVHAARQNIRHF 490
Cdd:COG2242   240 LAKLAL--RPGDVLWDIGAGSGSVSIEAARLAPGGRVYAIERDPERAALIRANARRF 294
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
613-674 8.38e-03

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 36.39  E-value: 8.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2065126112 613 NVSFITGDYMEdrelCPHGDdvtAGYDVILCLGVTkwvqLHGGDGGVVRMFRQIYTHLRPGG 674
Cdd:pfam13649  46 NVEFVQGDAED----LPFPD---GSFDLVVSSGVL----HHLPDPDLEAALREIARVLKPGG 96
 
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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