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Conserved domains on  [gi|1972255721|ref|NP_001379028|]
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putative RNA methyltransferase Y17G7B.18 [Caenorhabditis elegans]

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 ...
260-367 2.67e-58

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: 185.05  E-value: 2.67e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972255721 260 FDVILALSITKWIHLNWGDDGMRRFFRRAYAQLHPGGRLIIEPQAFDSYKKRAKMSEELKANYSKIEFKPEDFEMWLIET 339
Cdd:pfam06859   1 YDVILCLSVTKWIHLNWGDEGLKRFFKRIYSLLRPGGVLILEPQPWKSYKKAKRLSETIKANYKTIQLRPEDFEEYLLSE 80
                          90       100
                  ....*....|....*....|....*....
gi 1972255721 340 VGFESVEKLGVVG-AKSKGFERPIDVYLK 367
Cdd:pfam06859  81 VGFESVEELGSTPeGKSKGFDRPIYLFRK 109
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
151-301 9.57e-10

Trans-aconitate methyltransferase [Energy production and conversion];


:

Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 55.21  E-value: 9.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972255721 151 EHKQALDIGCNAGFLTLSIAKDFSPRRIIGIDIDEHLIGVARKNirhycdhetevsgkFPasfGVQFgtvsqrneaprsf 230
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARAR--------------LP---NVRF------------- 50
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972255721 231 stkfpdniwfkkenyvLESDeMLDM-IQPEFDVILALSItkwihLNWGDDgMRRFFRRAYAQLHPGGRLIIE 301
Cdd:COG4106    51 ----------------VVAD-LRDLdPPEPFDLVVSNAA-----LHWLPD-HAALLARLAAALAPGGVLAVQ 99
 
Name Accession Description Interval E-value
Bin3 pfam06859
Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of ...
260-367 2.67e-58

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: 185.05  E-value: 2.67e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972255721 260 FDVILALSITKWIHLNWGDDGMRRFFRRAYAQLHPGGRLIIEPQAFDSYKKRAKMSEELKANYSKIEFKPEDFEMWLIET 339
Cdd:pfam06859   1 YDVILCLSVTKWIHLNWGDEGLKRFFKRIYSLLRPGGVLILEPQPWKSYKKAKRLSETIKANYKTIQLRPEDFEEYLLSE 80
                          90       100
                  ....*....|....*....|....*....
gi 1972255721 340 VGFESVEKLGVVG-AKSKGFERPIDVYLK 367
Cdd:pfam06859  81 VGFESVEELGSTPeGKSKGFDRPIYLFRK 109
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
151-301 9.57e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 55.21  E-value: 9.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972255721 151 EHKQALDIGCNAGFLTLSIAKDFSPRRIIGIDIDEHLIGVARKNirhycdhetevsgkFPasfGVQFgtvsqrneaprsf 230
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARAR--------------LP---NVRF------------- 50
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972255721 231 stkfpdniwfkkenyvLESDeMLDM-IQPEFDVILALSItkwihLNWGDDgMRRFFRRAYAQLHPGGRLIIE 301
Cdd:COG4106    51 ----------------VVAD-LRDLdPPEPFDLVVSNAA-----LHWLPD-HAALLARLAAALAPGGVLAVQ 99
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
156-298 2.49e-08

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 51.21  E-value: 2.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972255721 156 LDIGCNAGFLTLSIAKDFSPRRIIGIDIDEHLIGVARKNIRHYCDHetevsgkfpasfgvqfgtvsqrneaprsfstkfp 235
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLL---------------------------------- 46
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972255721 236 dniwfKKENYVLESDEMLDMIQPEFDVILALSItkwIHlNWGDdgMRRFFRRAYAQLHPGGRL 298
Cdd:pfam08242  47 -----NAVRVELFQLDLGELDPGSFDVVVASNV---LH-HLAD--PRAVLRNIRRLLKPGGVL 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
156-301 6.90e-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: 47.42  E-value: 6.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972255721 156 LDIGCNAGFLTLSIAKdFSPRRIIGIDIDEHLIGVARKNIRHycdhetevsgkfpasfgvqfgtvsqrneaprsfstKFP 235
Cdd:cd02440     3 LDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAAAA-----------------------------------LLA 46
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972255721 236 DNIWFKKENyvleSDEMLDMIQPEFDVILAlsitkWIHLNWGDDGMRRFFRRAYAQLHPGGRLIIE 301
Cdd:cd02440    47 DNVEVLKGD----AEELPPEADESFDVIIS-----DPPLHHLVEDLARFLEEARRLLKPGGVLVLT 103
PRK08317 PRK08317
hypothetical protein; Provisional
154-206 3.65e-05

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 44.54  E-value: 3.65e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1972255721 154 QALDIGCNAGFLTLSIAKDFSPR-RIIGIDIDEHLIGVARKnirHYCDHETEVS 206
Cdd:PRK08317   22 RVLDVGCGPGNDARELARRVGPEgRVVGIDRSEAMLALAKE---RAAGLGPNVE 72
 
Name Accession Description Interval E-value
Bin3 pfam06859
Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of ...
260-367 2.67e-58

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: 185.05  E-value: 2.67e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972255721 260 FDVILALSITKWIHLNWGDDGMRRFFRRAYAQLHPGGRLIIEPQAFDSYKKRAKMSEELKANYSKIEFKPEDFEMWLIET 339
Cdd:pfam06859   1 YDVILCLSVTKWIHLNWGDEGLKRFFKRIYSLLRPGGVLILEPQPWKSYKKAKRLSETIKANYKTIQLRPEDFEEYLLSE 80
                          90       100
                  ....*....|....*....|....*....
gi 1972255721 340 VGFESVEKLGVVG-AKSKGFERPIDVYLK 367
Cdd:pfam06859  81 VGFESVEELGSTPeGKSKGFDRPIYLFRK 109
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
151-301 9.57e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 55.21  E-value: 9.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972255721 151 EHKQALDIGCNAGFLTLSIAKDFSPRRIIGIDIDEHLIGVARKNirhycdhetevsgkFPasfGVQFgtvsqrneaprsf 230
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARAR--------------LP---NVRF------------- 50
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972255721 231 stkfpdniwfkkenyvLESDeMLDM-IQPEFDVILALSItkwihLNWGDDgMRRFFRRAYAQLHPGGRLIIE 301
Cdd:COG4106    51 ----------------VVAD-LRDLdPPEPFDLVVSNAA-----LHWLPD-HAALLARLAAALAPGGVLAVQ 99
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
124-320 1.01e-08

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 54.92  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972255721 124 NFDRYYGIRLNPGESDKRLSVFQKDwfEHKQALDIGCNAGFLTLSIAKDFSpRRIIGIDIDEHLIGVARKNIRHYcdhet 203
Cdd:COG0500     1 PWDSYYSDELLPGLAALLALLERLP--KGGRVLDLGCGTGRNLLALAARFG-GRVIGIDLSPEAIALARARAAKA----- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972255721 204 evsgkfpasfgvqfgtvsqrneaprsfstkFPDNIWFKKENYvlesDEMLDMIQPEFDVILALSItkWIHLNwgDDGMRR 283
Cdd:COG0500    73 ------------------------------GLGNVEFLVADL----AELDPLPAESFDLVVAFGV--LHHLP--PEEREA 114
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1972255721 284 FFRRAYAQLHPGGRLIIEPQAFDSYKKRAKMSEELKA 320
Cdd:COG0500   115 LLRELARALKPGGVLLLSASDAAAALSLARLLLLATA 151
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
139-301 1.43e-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: 52.71  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972255721 139 DKRLSVFQKDWF-EHKQALDIGCNAGFLTLSIAKDFSprRIIGIDIDEHLIGVARKNIRHycdhetevsgkfpasFGVQF 217
Cdd:COG2227    11 DRRLAALLARLLpAGGRVLDVGCGTGRLALALARRGA--DVTGVDISPEALEIARERAAE---------------LNVDF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972255721 218 --GTVSQRNEAPRSFstkfpDNIWFkkeNYVLEsdemldmiqpefdvilalsitkwiHLnwgdDGMRRFFRRAYAQLHPG 295
Cdd:COG2227    74 vqGDLEDLPLEDGSF-----DLVIC---SEVLE------------------------HL----PDPAALLRELARLLKPG 117

                  ....*.
gi 1972255721 296 GRLIIE 301
Cdd:COG2227   118 GLLLLS 123
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
156-298 2.49e-08

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 51.21  E-value: 2.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972255721 156 LDIGCNAGFLTLSIAKDFSPRRIIGIDIDEHLIGVARKNIRHYCDHetevsgkfpasfgvqfgtvsqrneaprsfstkfp 235
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLL---------------------------------- 46
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972255721 236 dniwfKKENYVLESDEMLDMIQPEFDVILALSItkwIHlNWGDdgMRRFFRRAYAQLHPGGRL 298
Cdd:pfam08242  47 -----NAVRVELFQLDLGELDPGSFDVVVASNV---LH-HLAD--PRAVLRNIRRLLKPGGVL 98
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
156-296 1.66e-07

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 48.71  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972255721 156 LDIGCNAGFLTLSIAKDFSpRRIIGIDIDEHLIGVARKNIRHycdhetevsgkfpASFGVQF--GTVSQrneaprsfsTK 233
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGG-ARVTGVDLSPEMLERARERAAE-------------AGLNVEFvqGDAED---------LP 58
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972255721 234 FPDNiwfkkenyvlesdemldmiqpEFDVILALSItkwIHLNWGDDgMRRFFRRAYAQLHPGG 296
Cdd:pfam13649  59 FPDG---------------------SFDLVVSSGV---LHHLPDPD-LEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
156-301 6.90e-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: 47.42  E-value: 6.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972255721 156 LDIGCNAGFLTLSIAKdFSPRRIIGIDIDEHLIGVARKNIRHycdhetevsgkfpasfgvqfgtvsqrneaprsfstKFP 235
Cdd:cd02440     3 LDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAAAA-----------------------------------LLA 46
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972255721 236 DNIWFKKENyvleSDEMLDMIQPEFDVILAlsitkWIHLNWGDDGMRRFFRRAYAQLHPGGRLIIE 301
Cdd:cd02440    47 DNVEVLKGD----AEELPPEADESFDVIIS-----DPPLHHLVEDLARFLEEARRLLKPGGVLVLT 103
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
153-300 1.89e-06

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 46.91  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972255721 153 KQALDIGCNAGFLTLSIAKDFSprRIIGIDIDEHLIGVARKNIRHycdhetevsgkfpASFGVQF--GTVSQrneaprsf 230
Cdd:COG2226    24 ARVLDLGCGTGRLALALAERGA--RVTGVDISPEMLELARERAAE-------------AGLNVEFvvGDAED-------- 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972255721 231 sTKFPDNiwfkkenyvlesdemldmiqpEFDVILALSItkwihLNWGDDgMRRFFRRAYAQLHPGGRLII 300
Cdd:COG2226    81 -LPFPDG---------------------SFDLVISSFV-----LHHLPD-PERALAEIARVLKPGGRLVV 122
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
155-358 3.46e-06

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: 47.11  E-value: 3.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972255721 155 ALDIGCNAGFLTLSIAKDFSPRRIIGIDIDEHLIGVARKNIRHYcdhetevsgkfpasfGVQFGTvsqrneaprsfstkf 234
Cdd:COG2813    53 VLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAAN---------------GLENVE--------------- 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972255721 235 pdniwfkkenyVLESDEMLDMIQPEFDVIlalsitkW----IH--LNWGDDGMRRFFRRAYAQLHPGGRLIIEPQAFDSY 308
Cdd:COG2813   103 -----------VLWSDGLSGVPDGSFDLI-------LsnppFHagRAVDKEVAHALIADAARHLRPGGELWLVANRHLPY 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1972255721 309 KKrakmseelkanyskiefkpedfemWLIETvgFESVEKLgvvgAKSKGF 358
Cdd:COG2813   165 ER------------------------KLEEL--FGNVEVL----ARNKGF 184
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
156-300 4.77e-06

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 44.58  E-value: 4.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972255721 156 LDIGCNAGFLTLSIAKDFSprRIIGIDIDEHLIGVARKNIRhycdhetevsgkfPASFGVQFGTVSQrneaprsfsTKFP 235
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMLELAREKAP-------------REGLTFVVGDAED---------LPFP 56
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972255721 236 DNiwfkkenyvlesdemldmiqpEFDVILALSItkwihLNWGDDgMRRFFRRAYAQLHPGGRLII 300
Cdd:pfam08241  57 DN---------------------SFDLVLSSEV-----LHHVED-PERALREIARVLKPGGILII 94
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
153-197 9.69e-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: 46.29  E-value: 9.69e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1972255721 153 KQALDIGCNAGFLTLSIAKDFSPRRIIGIDIDEHLIGVARKNIRH 197
Cdd:COG4123    39 GRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVAL 83
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
156-197 1.66e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 44.33  E-value: 1.66e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1972255721 156 LDIGCNAGFLTLSIA-KDFSPRRIIGIDIDEHLIGVARKNIRH 197
Cdd:pfam13847   8 LDLGCGTGHLSFELAeELGPNAEVVGIDISEEAIEKARENAQK 50
PRK08317 PRK08317
hypothetical protein; Provisional
154-206 3.65e-05

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 44.54  E-value: 3.65e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1972255721 154 QALDIGCNAGFLTLSIAKDFSPR-RIIGIDIDEHLIGVARKnirHYCDHETEVS 206
Cdd:PRK08317   22 RVLDVGCGPGNDARELARRVGPEgRVVGIDRSEAMLALAKE---RAAGLGPNVE 72
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
156-301 1.01e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 43.61  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972255721 156 LDIGCNAGFLTLSIAKDFSPRRIIGIDIDEHLIGVARKNIRHYCDHETEVsgkFPASF--GVQFGT----VSqrNeaPrs 229
Cdd:PRK09328  113 LDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGLGARVEF---LQGDWfePLPGGRfdliVS--N--P-- 183
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972255721 230 fstkfPdniwfkkenYVLESDemLDMIQPE---FDVILALSItkwihlnwGDDGM---RRFFRRAYAQLHPGGRLIIE 301
Cdd:PRK09328  184 -----P---------YIPEAD--IHLLQPEvrdHEPHLALFG--------GEDGLdfyRRIIEQAPRYLKPGGWLLLE 237
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
156-301 1.33e-03

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 40.13  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972255721 156 LDIGCNAGFLTLSIAKDFSPRRIIGIDIDEHLIGVARKNIRHYCdhetevsgkfpASFGVQF--Gtvsqrneaprsfstk 233
Cdd:COG2890   117 LDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLG-----------LEDRVRFlqG--------------- 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972255721 234 fpDniWFKKenyvLESDEMLDMI---------------QPE---FDVILAL-SitkwihlnwGDDGM---RRFFRRAYAQ 291
Cdd:COG2890   171 --D--LFEP----LPGDGRFDLIvsnppyipedeiallPPEvrdHEPRLALdG---------GEDGLdfyRRIIAQAPRL 233
                         170
                  ....*....|
gi 1972255721 292 LHPGGRLIIE 301
Cdd:COG2890   234 LKPGGWLLLE 243
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
176-205 1.39e-03

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: 39.16  E-value: 1.39e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1972255721 176 RRIIGIDIDEHLIGVARKNIRHYCDHETEV 205
Cdd:COG1041    49 RRVIGSDIDPKMVEGARENLEHYGYEDADV 78
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
142-196 2.40e-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: 38.34  E-value: 2.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1972255721 142 LSVFQKDWFehKQALDIGCNAGFLTLSIAKdFSPRRII-GIDIDEHLIGVARKNIR 196
Cdd:pfam05175  24 LEHLPKDLS--GKVLDLGCGAGVLGAALAK-ESPDAELtMVDINARALESARENLA 76
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
153-198 4.74e-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: 37.47  E-value: 4.74e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1972255721 153 KQALDIGCNAGFLTLSIAKDFSPR-RIIGIDIDEHLIGVARKNIRHY 198
Cdd:COG4122    18 KRILEIGTGTGYSTLWLARALPDDgRLTTIEIDPERAAIARENFARA 64
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
153-324 5.26e-03

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: 38.40  E-value: 5.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972255721 153 KQALDIGCNAGFLTLSIAKdFSPRRIIGIDIDEHLIGVARKNIrhycdhetevsgkfpasfgvqfgtvsQRNEAPRSFST 232
Cdd:pfam06325 163 ESVLDVGCGSGILAIAALK-LGAKKVVGVDIDPVAVRAAKENA--------------------------ELNGVEARLEV 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972255721 233 KFPDNIwfkkenyvlesdemldmIQPEFDVILAlsitkwihlNWGDDGMRRFFRRAYAQLHPGGRL----IIEPQAfdsy 308
Cdd:pfam06325 216 YLPGDL-----------------PKEKADVVVA---------NILADPLIELAPDIYALVKPGGYLilsgILKEQA---- 265
                         170
                  ....*....|....*.
gi 1972255721 309 kkrakmsEELKANYSK 324
Cdd:pfam06325 266 -------QMVAEAYSQ 274
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
150-196 5.87e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 37.58  E-value: 5.87e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1972255721 150 FEHKQALDIGCNAGflTLSI-AKDFSPRRIIGIDIDEHLIGVARKNIR 196
Cdd:COG2263    44 IEGKTVLDLGCGTG--MLAIgAALLGAKKVVGVDIDPEALEIARENAE 89
 
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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