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Conserved domains on  [gi|292627291|ref|XP_001921729|]
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7SK snRNA methylphosphate capping enzyme-like [Danio rerio]

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

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008173|GO:0001510|GO:0032259|GO:0008757|GO:0008168|GO:1904047|GO:0008171|GO:0090486
PubMed:  12504684|12826405
SCOP:  3000118

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 ...
 515-622 3.69e-59

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: 193.14  E-value: 3.69e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291  515 YDVILCLSLTKWVHLNYGDAGIQRLFGRIYRHLLPGGVLILEPQPWSSYSRHKRLTDVTRRNYSSIRLKPDKFSSFLMAE 594
Cdd:pfam06859   1 YDVILCLSVTKWIHLNWGDEGLKRFFKRIYSLLRPGGVLILEPQPWKSYKKAKRLSETIKANYKTIQLRPEDFEEYLLSE 80

                          90       100
                  ....*....|....*....|....*....
gi 292627291  595 VGFSSYELIG-TPRASPKGLQRSVYLFHK 622
Cdd:pfam06859  81 VGFESVEELGsTPEGKSKGFDRPIYLFRK 109
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
385-556 6.03e-10

Trans-aconitate methyltransferase [Energy production and conversion];


:

Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 56.37  E-value: 6.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291 385 GKKVLDVGCNTGHVTLAIAKHCSPAHILGLDIDGALVQAARQNLRHflselqdrqqagagegsevtglvplmdlqlvlpr 464
Cdd:COG4106    2 PRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLPN---------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291 465 fpVSFMRcrgpiaappimhqslgqfpsnvcflkgdyvpdSDAEVVSQSAEYDVILCLSLTKWVhlnygdAGIQRLFGRIY 544
Cdd:COG4106   48 --VRFVV--------------------------------ADLRDLDPPEPFDLVVSNAALHWL------PDHAALLARLA 87

                        170
                 ....*....|..
gi 292627291 545 RHLLPGGVLILE 556
Cdd:COG4106   88 AALAPGGVLAVQ 99
 
Name Accession Description Interval E-value
Bin3 pfam06859
Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of ...
 515-622 3.69e-59

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: 193.14  E-value: 3.69e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291  515 YDVILCLSLTKWVHLNYGDAGIQRLFGRIYRHLLPGGVLILEPQPWSSYSRHKRLTDVTRRNYSSIRLKPDKFSSFLMAE 594
Cdd:pfam06859   1 YDVILCLSVTKWIHLNWGDEGLKRFFKRIYSLLRPGGVLILEPQPWKSYKKAKRLSETIKANYKTIQLRPEDFEEYLLSE 80

                          90       100
                  ....*....|....*....|....*....
gi 292627291  595 VGFSSYELIG-TPRASPKGLQRSVYLFHK 622
Cdd:pfam06859  81 VGFESVEELGsTPEGKSKGFDRPIYLFRK 109
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
385-556 6.03e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 56.37  E-value: 6.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291 385 GKKVLDVGCNTGHVTLAIAKHCSPAHILGLDIDGALVQAARQNLRHflselqdrqqagagegsevtglvplmdlqlvlpr 464
Cdd:COG4106    2 PRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLPN---------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291 465 fpVSFMRcrgpiaappimhqslgqfpsnvcflkgdyvpdSDAEVVSQSAEYDVILCLSLTKWVhlnygdAGIQRLFGRIY 544
Cdd:COG4106   48 --VRFVV--------------------------------ADLRDLDPPEPFDLVVSNAALHWL------PDHAALLARLA 87

                        170
                 ....*....|..
gi 292627291 545 RHLLPGGVLILE 556
Cdd:COG4106   88 AALAPGGVLAVQ 99
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 388-551 5.89e-08

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 50.64  E-value: 5.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291  388 VLDVGCNTGHVTLAIAKHCSpAHILGLDIDGALVQAARQNLRHflselqdrqqagagegsevtglvplmdlqlvlprfpv 467
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG-ARVTGVDLSPEMLERARERAAE------------------------------------- 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291  468 sfmrcRGPiaappimhqslgqfpsNVCFLKGDY--VPDSDaevvsqsAEYDVILCLSLtkWVHLNygDAGIQRLFGRIYR 545
Cdd:pfam13649  43 -----AGL----------------NVEFVQGDAedLPFPD-------GSFDLVVSSGV--LHHLP--DPDLEAALREIAR 90


                  ....*.
gi 292627291  546 HLLPGG 551
Cdd:pfam13649  91 VLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 387-556 6.13e-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: 48.20  E-value: 6.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291 387 KVLDVGCNTGHVTLAIAKHCsPAHILGLDIDGALVQAARQNLRHFLselqdrqqagagegsevtglvplmdlqlvlprfp 466
Cdd:cd02440    1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALELARKAAAALL---------------------------------- 45

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291 467 vsfmrcrgpiaappimhqslgqfPSNVCFLKGDYVPDSDAEVvsqsAEYDVILCLSLTKWVHLNYgdagiQRLFGRIYRH 546
Cdd:cd02440   46 -----------------------ADNVEVLKGDAEELPPEAD----ESFDVIISDPPLHHLVEDL-----ARFLEEARRL 93

                        170
                 ....*....|
gi 292627291 547 LLPGGVLILE 556
Cdd:cd02440   94 LKPGGVLVLT 103
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
374-429 6.79e-06

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 47.84  E-value: 6.79e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 292627291 374 RLALfnpEW-----FSGKKVLDVGCNTGhvTLAI-AKHCSPAHILGLDIDGALVQAARQNLR 429
Cdd:PRK00517 107 RLCL---EAleklvLPGKTVLDVGCGSG--ILAIaAAKLGAKKVLAVDIDPQAVEAARENAE 163
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 383-423 3.40e-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: 39.58  E-value: 3.40e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 292627291  383 FSGKKVLDVGCNTGHVTLAIAKHCSPAHILGLDI-DGALVQA 423
Cdd:TIGR02072  33 FIPASVLDIGCGTGYLTRALLKRFPQAEFIALDIsAGMLAQA 74
 
Name Accession Description Interval E-value
Bin3 pfam06859
Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of ...
 515-622 3.69e-59

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: 193.14  E-value: 3.69e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291  515 YDVILCLSLTKWVHLNYGDAGIQRLFGRIYRHLLPGGVLILEPQPWSSYSRHKRLTDVTRRNYSSIRLKPDKFSSFLMAE 594
Cdd:pfam06859   1 YDVILCLSVTKWIHLNWGDEGLKRFFKRIYSLLRPGGVLILEPQPWKSYKKAKRLSETIKANYKTIQLRPEDFEEYLLSE 80

                          90       100
                  ....*....|....*....|....*....
gi 292627291  595 VGFSSYELIG-TPRASPKGLQRSVYLFHK 622
Cdd:pfam06859  81 VGFESVEELGsTPEGKSKGFDRPIYLFRK 109
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
385-556 6.03e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 56.37  E-value: 6.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291 385 GKKVLDVGCNTGHVTLAIAKHCSPAHILGLDIDGALVQAARQNLRHflselqdrqqagagegsevtglvplmdlqlvlpr 464
Cdd:COG4106    2 PRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLPN---------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291 465 fpVSFMRcrgpiaappimhqslgqfpsnvcflkgdyvpdSDAEVVSQSAEYDVILCLSLTKWVhlnygdAGIQRLFGRIY 544
Cdd:COG4106   48 --VRFVV--------------------------------ADLRDLDPPEPFDLVVSNAALHWL------PDHAALLARLA 87

                        170
                 ....*....|..
gi 292627291 545 RHLLPGGVLILE 556
Cdd:COG4106   88 AALAPGGVLAVQ 99
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 384-438 3.04e-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: 57.85  E-value: 3.04e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 292627291 384 SGKKVLDVGCNTGHVTLAIAKHCSPAHILGLDIDGALVQAARQNLRhfLSELQDR 438
Cdd:COG4123   37 KGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVA--LNGLEDR 89
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 372-430 4.23e-09

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


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 55.02  E-value: 4.23e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291 372 DPRLALFNPEWF-SGKKVLDVGCNTGHVTLAIAKHCspAHILGLDIDGALVQAARQNLRH 430
Cdd:COG2227   11 DRRLAALLARLLpAGGRVLDVGCGTGRLALALARRG--ADVTGVDISPEALEIARERAAE 68
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
357-555 4.99e-09

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 56.16  E-value: 4.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291 357 AYSRYY--------GYRTPSMTADPRLALFNPEwfSGKKVLDVGCNTGHVTLAIAKHCspAHILGLDIDGALVQAARQNl 428
Cdd:COG4976   13 QYADSYdaalvedlGYEAPALLAEELLARLPPG--PFGRVLDLGCGTGLLGEALRPRG--YRLTGVDLSEEMLAKAREK- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291 429 rhflsELQDRqqagagegsevtglvplmdlqlvlprfpvsfmrcrgpiaappimhqslgqfpsnvcFLKGDYvpdsdAEV 508
Cdd:COG4976   88 -----GVYDR--------------------------------------------------------LLVADL-----ADL 101

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 292627291 509 VSQSAEYDVILCLSLtkwvhLNYGDAgIQRLFGRIYRHLLPGGVLIL 555
Cdd:COG4976  102 AEPDGRFDLIVAADV-----LTYLGD-LAAVFAGVARALKPGGLFIF 142
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 388-551 5.89e-08

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 50.64  E-value: 5.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291  388 VLDVGCNTGHVTLAIAKHCSpAHILGLDIDGALVQAARQNLRHflselqdrqqagagegsevtglvplmdlqlvlprfpv 467
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG-ARVTGVDLSPEMLERARERAAE------------------------------------- 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291  468 sfmrcRGPiaappimhqslgqfpsNVCFLKGDY--VPDSDaevvsqsAEYDVILCLSLtkWVHLNygDAGIQRLFGRIYR 545
Cdd:pfam13649  43 -----AGL----------------NVEFVQGDAedLPFPD-------GSFDLVVSSGV--LHHLP--DPDLEAALREIAR 90


                  ....*.
gi 292627291  546 HLLPGG 551
Cdd:pfam13649  91 VLKPGG 96
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 384-440 7.54e-08

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 52.03  E-value: 7.54e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 292627291  384 SGKKVLDVGCNTGHVTLAIA-KHCSPAHILGLDIDGALVQAARQNLR-HFLSELQDRQQ 440
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAeELGPNAEVVGIDISEEAIEKARENAQkLGFDNVEFEQG 61
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 385-429 2.04e-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: 50.38  E-value: 2.04e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 292627291 385 GKKVLDVGCNTGHVTLAIAKHcsPAHILGLDIDGALVQAARQNLR 429
Cdd:COG2226   23 GARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAA 65
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 389-431 4.09e-07

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 48.52  E-value: 4.09e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 292627291  389 LDVGCNTGHVTLAIAKHCSPAHILGLDIDGALVQAARQNLRHF 431
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAAL 43
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 387-556 6.13e-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: 48.20  E-value: 6.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291 387 KVLDVGCNTGHVTLAIAKHCsPAHILGLDIDGALVQAARQNLRHFLselqdrqqagagegsevtglvplmdlqlvlprfp 466
Cdd:cd02440    1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALELARKAAAALL---------------------------------- 45

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291 467 vsfmrcrgpiaappimhqslgqfPSNVCFLKGDYVPDSDAEVvsqsAEYDVILCLSLTKWVHLNYgdagiQRLFGRIYRH 546
Cdd:cd02440   46 -----------------------ADNVEVLKGDAEELPPEAD----ESFDVIISDPPLHHLVEDL-----ARFLEEARRL 93

                        170
                 ....*....|
gi 292627291 547 LLPGGVLILE 556
Cdd:cd02440   94 LKPGGVLVLT 103
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 357-574 1.31e-06

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 49.53  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291 357 AYSRYYGYRTPSMTADPRLALFNPEwfSGKKVLDVGCNTGHVTLAIAKHCSpAHILGLDIDGALVQAARQNLrhflselq 436
Cdd:COG0500    1 PWDSYYSDELLPGLAALLALLERLP--KGGRVLDLGCGTGRNLLALAARFG-GRVIGIDLSPEAIALARARA-------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291 437 drQQAGAGegsevtglvplmdlqlvlprfpvsfmrcrgpiaappimhqslgqfpsNVCFLKGDYVPDSDAEvvsqSAEYD 516
Cdd:COG0500   70 --AKAGLG-----------------------------------------------NVEFLVADLAELDPLP----AESFD 96

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 292627291 517 VILCLSLtkWVHLNygDAGIQRLFGRIYRHLLPGGVLILEPQPWSSYSRHKRLTDVTR 574
Cdd:COG0500   97 LVVAFGV--LHHLP--PEEREALLRELARALKPGGVLLLSASDAAAALSLARLLLLAT 150
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
374-429 6.79e-06

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 47.84  E-value: 6.79e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 292627291 374 RLALfnpEW-----FSGKKVLDVGCNTGhvTLAI-AKHCSPAHILGLDIDGALVQAARQNLR 429
Cdd:PRK00517 107 RLCL---EAleklvLPGKTVLDVGCGSG--ILAIaAAKLGAKKVLAVDIDPQAVEAARENAE 163
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
383-448 7.50e-06

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 48.25  E-value: 7.50e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 292627291 383 FSGKKVLDVGCNTGhVtLAI-AKHCSPAHILGLDIDGALVQAARQNLRhfLSELQDRQQAGAGEGSE 448
Cdd:COG2264  147 KPGKTVLDVGCGSG-I-LAIaAAKLGAKRVLAVDIDPVAVEAARENAE--LNGVEDRIEVVLGDLLE 209
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 385-429 2.62e-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: 2.62e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 292627291 385 GKKVLDVGCNTGHVTLAIAKHCSPAHILGLDIDGALVQAARQNLR 429
Cdd:COG2813   50 GGRVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAA 94
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
385-429 3.31e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 45.28  E-value: 3.31e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 292627291 385 GKKVLDVGCNTGhvTLAI-AKHCSPAHILGLDIDGALVQAARQNLR 429
Cdd:COG2263   46 GKTVLDLGCGTG--MLAIgAALLGAKKVVGVDIDPEALEIARENAE 89
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 385-555 4.28e-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: 4.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291 385 GKKVLDVGCNTGHVTLAIAKHCSpAHILGLDIDGALVQAARQNLRHFlsELQDRqqagagegseVTglvplmdlqlvlpr 464
Cdd:COG2230   52 GMRVLDIGCGWGGLALYLARRYG-VRVTGVTLSPEQLEYARERAAEA--GLADR----------VE-------------- 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291 465 fpvsfmrcrgpiaappimhqslgqfpsnvcFLKGDYvpdsdaEVVSQSAEYDVILCLSLTKWVhlnyGDAGIQRLFGRIY 544
Cdd:COG2230  105 ------------------------------VRLADY------RDLPADGQFDAIVSIGMFEHV----GPENYPAYFAKVA 144

                        170
                 ....*....|.
gi 292627291 545 RHLLPGGVLIL 555
Cdd:COG2230  145 RLLKPGGRLLL 155
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 389-429 5.18e-05

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 42.27  E-value: 5.18e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 292627291  389 LDVGCNTGHVTLAIAKHCspAHILGLDIDGALVQAARQNLR 429
Cdd:pfam08241   1 LDVGCGTGLLTELLARLG--ARVTGVDISPEMLELAREKAP 39
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 360-434 6.13e-05

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: 43.78  E-value: 6.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291 360 RYYGYRTpSMtaDPRLA--LFN----PEwfsGKKVLDVGCNTGhvTLAIAKHCSPAHILGLDIDGALVQAARQNLRHFLS 433
Cdd:COG1041    2 KYFFYPG-SL--DPRLAraLVNlagaKE---GDTVLDPFCGTG--TILIEAGLLGRRVIGSDIDPKMVEGARENLEHYGY 73


                 .
gi 292627291 434 E 434
Cdd:COG1041   74 E 74
PRK08317 PRK08317
hypothetical protein; Provisional
 385-426 1.22e-04

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 44.16  E-value: 1.22e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 292627291 385 GKKVLDVGCNTGHVTLAIAKHCSPA-HILGLDIDGALVQAARQ 426
Cdd:PRK08317  20 GDRVLDVGCGPGNDARELARRVGPEgRVVGIDRSEAMLALAKE 62
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 385-429 1.72e-04

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: 42.58  E-value: 1.72e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 292627291  385 GKKVLDVGCNTGHVTLAIAKHCSPAHILGLDIDGALVQAARQNLR 429
Cdd:pfam05175  32 SGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLA 76
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 384-432 2.37e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 43.23  E-value: 2.37e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 292627291 384 SGKKVLDVGCNTGHVTLAIAKHCSPAHILGLDIDGALVQAARQNLRHFL 432
Cdd:PRK09328 108 EPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGL 156
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 371-440 2.65e-04

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 42.03  E-value: 2.65e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292627291  371 ADPRLALFNPEWFSGKKVLDVGCNTGHVTLAIAKHcsPAHILGLDIDGALVQAARQNLRHFLSELQDRQQ 440
Cdd:pfam13489   9 LADLLLRLLPKLPSPGRVLDFGCGTGIFLRLLRAQ--GFSVTGVDPSPIAIERALLNVRFDQFDEQEAAV 76
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 383-431 3.41e-04

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 42.45  E-value: 3.41e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 292627291 383 FSGKKVLDVGCNTGHVTLAIAKH-CSPAHILGLDIDGALVQAARQNLRHF 431
Cdd:PRK00216  50 RPGDKVLDLACGTGDLAIALAKAvGKTGEVVGLDFSEGMLAVGREKLRDL 99
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 385-427 5.89e-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: 42.25  E-value: 5.89e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 292627291  385 GKKVLDVGCNTGHVTLAIAKhCSPAHILGLDIDGALVQAARQN 427
Cdd:pfam06325 162 GESVLDVGCGSGILAIAALK-LGAKKVVGVDIDPVAVRAAKEN 203
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 383-423 3.40e-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: 39.58  E-value: 3.40e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 292627291  383 FSGKKVLDVGCNTGHVTLAIAKHCSPAHILGLDI-DGALVQA 423
Cdd:TIGR02072  33 FIPASVLDIGCGTGYLTRALLKRFPQAEFIALDIsAGMLAQA 74
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 386-438 4.31e-03

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: 38.63  E-value: 4.31e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 292627291 386 KKVLDVGCNTGHVTLAIAKHCSP-AHILGLDIDGALVQAARQNLRHflSELQDR 438
Cdd:COG4122   18 KRILEIGTGTGYSTLWLARALPDdGRLTTIEIDPERAAIARENFAR--AGLADR 69
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 384-430 5.08e-03

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 39.36  E-value: 5.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 292627291 384 SGKKVLDVGCNTGHVTLAIAKHCSPAHILGLDIDGALVQAARQNLRH 430
Cdd:COG2890  112 APPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAER 158
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
375-437 5.30e-03

Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 38.66  E-value: 5.30e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 292627291 375 LALFNPEWfsgKKVLDVGCNTGHVTLAIAKHCSPAHILGLDIDGALVQAARQNLRHFLSELQD 437
Cdd:COG0421   31 PLLFHPNP---KRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFPLLAPAFDD 90
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 384-430 5.88e-03

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 38.53  E-value: 5.88e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 292627291 384 SGKKVLDVGCNTGHVTLAIAKHCspAHILGLDIDGALVQAARQNLRH 430
Cdd:COG2518   66 PGDRVLEIGTGSGYQAAVLARLA--GRVYSVERDPELAERARERLAA 110
PRK14968 PRK14968
putative methyltransferase; Provisional
 385-429 9.53e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 37.57  E-value: 9.53e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 292627291 385 GKKVLDVGCNTGHVTLAIAKhcSPAHILGLDIDGALVQAARQNLR 429
Cdd:PRK14968  24 GDRVLEVGTGSGIVAIVAAK--NGKKVVGVDINPYAVECAKCNAK 66
 
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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