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Conserved domains on  [gi|501038873|ref|WP_012090819|]
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TlyA family RNA methyltransferase [Brucella anthropi]

Protein Classification

TlyA family RNA methyltransferase( domain architecture ID 11439687)

TlyA family RNA methyltransferase similar to Mycobacterium tuberculosis 16S/23S rRNA (cytidine-2'-O)-methyltransferase and Bacillus subtilis rRNA methyltransferase YqxC

CATH:  3.40.50.150
Gene Ontology:  GO:0008168|GO:0032259|GO:0003723
PubMed:  12826405|12504684

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YqxC COG1189
Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure ...
 11-253 9.27e-136

Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure and biogenesis];


:

Pssm-ID: 440802 [Multi-domain]  Cd Length: 248  Bit Score: 382.10  E-value: 9.27e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038873  11 RLDQLLVELGLFATRSRARDAIQRGTVKVDGKPVTKPGQTVLRTAKIAVDDPASAYVSRAALKLIAALDHFELDVKGRTA 90
Cdd:COG1189    2 RLDVLLVERGLAESREKAQRLIMAGRVLVNGQVVDKPGTKVPEDAEIEVKGEELPYVSRGGLKLEGALDAFGIDVAGKVC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038873  91 LDIGASTGGFTQVLLERGASHVLAIDVGHDQLHETLRADPRVTNKEGLNARALELSHLDGReIDCVVSDVSFISLKLALP 170
Cdd:COG1189   82 LDIGASTGGFTDCLLQRGAAKVYAVDVGYGQLAWKLRQDPRVVVLERTNARYLTPEDLPEP-PDLVVIDVSFISLTLVLP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038873 171 PALAFAQKGAICALLVKPQFEAGREAIGKGGILRDPKDGERIAEELKSWLETLpGWRALGLCPSPIEGGDGNREYLLAGK 250
Cdd:COG1189  161 ALLALLKPGGELVALVKPQFEVGRERVGKGGVVRDPALHAEVIEKVLAAAAEL-GLRVLGLTPSPITGPDGNIEFLLWLR 239


                 ...
gi 501038873 251 KDQ 253
Cdd:COG1189  240 KGG 242
 
Name Accession Description Interval E-value
YqxC COG1189
Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure ...
 11-253 9.27e-136

Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440802 [Multi-domain]  Cd Length: 248  Bit Score: 382.10  E-value: 9.27e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038873  11 RLDQLLVELGLFATRSRARDAIQRGTVKVDGKPVTKPGQTVLRTAKIAVDDPASAYVSRAALKLIAALDHFELDVKGRTA 90
Cdd:COG1189    2 RLDVLLVERGLAESREKAQRLIMAGRVLVNGQVVDKPGTKVPEDAEIEVKGEELPYVSRGGLKLEGALDAFGIDVAGKVC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038873  91 LDIGASTGGFTQVLLERGASHVLAIDVGHDQLHETLRADPRVTNKEGLNARALELSHLDGReIDCVVSDVSFISLKLALP 170
Cdd:COG1189   82 LDIGASTGGFTDCLLQRGAAKVYAVDVGYGQLAWKLRQDPRVVVLERTNARYLTPEDLPEP-PDLVVIDVSFISLTLVLP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038873 171 PALAFAQKGAICALLVKPQFEAGREAIGKGGILRDPKDGERIAEELKSWLETLpGWRALGLCPSPIEGGDGNREYLLAGK 250
Cdd:COG1189  161 ALLALLKPGGELVALVKPQFEVGRERVGKGGVVRDPALHAEVIEKVLAAAAEL-GLRVLGLTPSPITGPDGNIEFLLWLR 239


                 ...
gi 501038873 251 KDQ 253
Cdd:COG1189  240 KGG 242
tly TIGR00478
TlyA family rRNA methyltransferase/putative hemolysin; Members of this family include TlyA ...
 11-244 3.68e-64

TlyA family rRNA methyltransferase/putative hemolysin; Members of this family include TlyA from Mycobacterium tuberculosis, an rRNA methylase whose modifications are necessary to confer sensitivity to ribosome-targeting antibiotics capreomycin and viomycin. Homology supports identification as a methyltransferase. However, a parallel literature persists in calling some members hemolysins. Hemolysins are exotoxins that attack blood cell membranes and cause cell rupture, often by forming a pore in the membrane. A recent study (2013) on SCO1782 from Streptomyces coelicolor shows hemolysin activity as earlier described for a homolog from the spirochete Serpula (Treponema) hyodysenteriae and one from Mycobacterium tuberculosis. [Unknown function, General]


Pssm-ID: 129570 [Multi-domain]  Cd Length: 228  Bit Score: 199.65  E-value: 3.68e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038873   11 RLDQLLVELGLFATRSRARDAIQRGTVKVDGKPVTKPGQTVLRTAKIAVDDPaSAYVSRAALKLIAALDHFELDVKGRTA 90
Cdd:TIGR00478   1 RLDILLVRRGLFESREKAKRLILKGFVLVNGKKVDKPSALVDFDAKIELLQN-PLFVSRGGEKLKEALEEFNIDVKNKIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038873   91 LDIGASTGGFTQVLLERGASHVLAIDVGHDQLHETLRADPRVTNKEGLNARALELSHLDGreiDCVVSDVSFISLKLALP 170
Cdd:TIGR00478  80 LDVGSSTGGFTDCALQKGAKEVYGVDVGYNQLAEKLRQDERVKVLERTNIRYVTPADIFP---DFATFDVSFISLISILP 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501038873  171 PALAFAQKGAiCALLVKPQFEAGREAIGKGGILRDPKDGERIAEELKSWLETlPGWRALGLCPSPIEGGDGNRE 244
Cdd:TIGR00478 157 ELDLLLNPND-LTLLFKPQFEAGREKKNKKGVVRDKEAIALALHKVIDKGES-PDFQEKKIIFSLTKGKRGNVE 228
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 66-251 1.20e-52

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 168.54  E-value: 1.20e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038873   66 YVSRAALKLIAALDHFELDVKGRTALDIGASTGGFTQVLLERGASHVLAIDVGHDQLhETLRADPRVTNKEGlNARALE- 144
Cdd:pfam01728   1 YRSRAAYKLLEIDEKFGLLKPGKTVLDLGAAPGGWSQVALQRGAGKVVGVDLGPMQL-WKPRNDPGVTFIQG-DIRDPEt 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038873  145 ---LSHLDGREIDCVVSDVS-FISLKLALPPALAFAqkgaicalLVKPQFEAGREAIGKGGILRDPKDGERIAEELKSWL 220
Cdd:pfam01728  79 ldlLEELLGRKVDLVLSDGSpFISGNKVLDHLRSLD--------LVKAALEVALELLRKGGNFVCKVFQGEDFSELLYLL 150

                         170       180       190
                  ....*....|....*....|....*....|.
gi 501038873  221 EtlPGWRALGLCPSPIEGGDGNREYLLAGKK 251
Cdd:pfam01728 151 K--LGFEKVGVFKPPASRPESSEEYLVCLGF 179
S4 cd00165
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ...
 11-62 1.17e-13

S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, charged residues that define a likely RNA-binding site; Found in stress proteins, ribosomal proteins and tRNA synthetases; This may imply a hitherto unrecognized functional similarity between these three protein classes.


Pssm-ID: 238095 [Multi-domain]  Cd Length: 70  Bit Score: 64.19  E-value: 1.17e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 501038873  11 RLDQLLVELGLFATRSRARDAIQRGTVKVDGKPVTKPGQTVLRTAKIAVDDP 62
Cdd:cd00165    2 RLDKILARLGLAPSRSEARQLIKHGHVLVNGKVVTKPSYKVKPGDVIEVDGK 53
S4 smart00363
S4 RNA-binding domain;
10-61 3.36e-10

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 54.52  E-value: 3.36e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 501038873    10 LRLDQLLVELGLFATRSRARDAIQRGTVKVDGKPVTKPGQTVLRTAKIAVDD 61
Cdd:smart00363   1 RRLDKFLARLGLAPSRSQARRLIEQGRVKVNGKKVTKPSYIVKPGDVISVRG 52
rluD PRK11180
23S rRNA pseudouridine(1911/1915/1917) synthase RluD;
11-60 1.14e-04

23S rRNA pseudouridine(1911/1915/1917) synthase RluD;


Pssm-ID: 183020 [Multi-domain]  Cd Length: 325  Bit Score: 42.74  E-value: 1.14e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 501038873  11 RLDQLLVELGLFATRSRARDAIQRGTVKVDGKPVTKPGQTVLRTAKIAVD 60
Cdd:PRK11180  19 RLDQALAELFPDYSRSRIKEWILDQRVLVNGKVINKPKEKVLGGEQVAID 68
 
Name Accession Description Interval E-value
YqxC COG1189
Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure ...
 11-253 9.27e-136

Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440802 [Multi-domain]  Cd Length: 248  Bit Score: 382.10  E-value: 9.27e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038873  11 RLDQLLVELGLFATRSRARDAIQRGTVKVDGKPVTKPGQTVLRTAKIAVDDPASAYVSRAALKLIAALDHFELDVKGRTA 90
Cdd:COG1189    2 RLDVLLVERGLAESREKAQRLIMAGRVLVNGQVVDKPGTKVPEDAEIEVKGEELPYVSRGGLKLEGALDAFGIDVAGKVC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038873  91 LDIGASTGGFTQVLLERGASHVLAIDVGHDQLHETLRADPRVTNKEGLNARALELSHLDGReIDCVVSDVSFISLKLALP 170
Cdd:COG1189   82 LDIGASTGGFTDCLLQRGAAKVYAVDVGYGQLAWKLRQDPRVVVLERTNARYLTPEDLPEP-PDLVVIDVSFISLTLVLP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038873 171 PALAFAQKGAICALLVKPQFEAGREAIGKGGILRDPKDGERIAEELKSWLETLpGWRALGLCPSPIEGGDGNREYLLAGK 250
Cdd:COG1189  161 ALLALLKPGGELVALVKPQFEVGRERVGKGGVVRDPALHAEVIEKVLAAAAEL-GLRVLGLTPSPITGPDGNIEFLLWLR 239


                 ...
gi 501038873 251 KDQ 253
Cdd:COG1189  240 KGG 242
tly TIGR00478
TlyA family rRNA methyltransferase/putative hemolysin; Members of this family include TlyA ...
 11-244 3.68e-64

TlyA family rRNA methyltransferase/putative hemolysin; Members of this family include TlyA from Mycobacterium tuberculosis, an rRNA methylase whose modifications are necessary to confer sensitivity to ribosome-targeting antibiotics capreomycin and viomycin. Homology supports identification as a methyltransferase. However, a parallel literature persists in calling some members hemolysins. Hemolysins are exotoxins that attack blood cell membranes and cause cell rupture, often by forming a pore in the membrane. A recent study (2013) on SCO1782 from Streptomyces coelicolor shows hemolysin activity as earlier described for a homolog from the spirochete Serpula (Treponema) hyodysenteriae and one from Mycobacterium tuberculosis. [Unknown function, General]


Pssm-ID: 129570 [Multi-domain]  Cd Length: 228  Bit Score: 199.65  E-value: 3.68e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038873   11 RLDQLLVELGLFATRSRARDAIQRGTVKVDGKPVTKPGQTVLRTAKIAVDDPaSAYVSRAALKLIAALDHFELDVKGRTA 90
Cdd:TIGR00478   1 RLDILLVRRGLFESREKAKRLILKGFVLVNGKKVDKPSALVDFDAKIELLQN-PLFVSRGGEKLKEALEEFNIDVKNKIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038873   91 LDIGASTGGFTQVLLERGASHVLAIDVGHDQLHETLRADPRVTNKEGLNARALELSHLDGreiDCVVSDVSFISLKLALP 170
Cdd:TIGR00478  80 LDVGSSTGGFTDCALQKGAKEVYGVDVGYNQLAEKLRQDERVKVLERTNIRYVTPADIFP---DFATFDVSFISLISILP 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501038873  171 PALAFAQKGAiCALLVKPQFEAGREAIGKGGILRDPKDGERIAEELKSWLETlPGWRALGLCPSPIEGGDGNRE 244
Cdd:TIGR00478 157 ELDLLLNPND-LTLLFKPQFEAGREKKNKKGVVRDKEAIALALHKVIDKGES-PDFQEKKIIFSLTKGKRGNVE 228
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 66-251 1.20e-52

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 168.54  E-value: 1.20e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038873   66 YVSRAALKLIAALDHFELDVKGRTALDIGASTGGFTQVLLERGASHVLAIDVGHDQLhETLRADPRVTNKEGlNARALE- 144
Cdd:pfam01728   1 YRSRAAYKLLEIDEKFGLLKPGKTVLDLGAAPGGWSQVALQRGAGKVVGVDLGPMQL-WKPRNDPGVTFIQG-DIRDPEt 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038873  145 ---LSHLDGREIDCVVSDVS-FISLKLALPPALAFAqkgaicalLVKPQFEAGREAIGKGGILRDPKDGERIAEELKSWL 220
Cdd:pfam01728  79 ldlLEELLGRKVDLVLSDGSpFISGNKVLDHLRSLD--------LVKAALEVALELLRKGGNFVCKVFQGEDFSELLYLL 150

                         170       180       190
                  ....*....|....*....|....*....|.
gi 501038873  221 EtlPGWRALGLCPSPIEGGDGNREYLLAGKK 251
Cdd:pfam01728 151 K--LGFEKVGVFKPPASRPESSEEYLVCLGF 179
S4 cd00165
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ...
 11-62 1.17e-13

S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, charged residues that define a likely RNA-binding site; Found in stress proteins, ribosomal proteins and tRNA synthetases; This may imply a hitherto unrecognized functional similarity between these three protein classes.


Pssm-ID: 238095 [Multi-domain]  Cd Length: 70  Bit Score: 64.19  E-value: 1.17e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 501038873  11 RLDQLLVELGLFATRSRARDAIQRGTVKVDGKPVTKPGQTVLRTAKIAVDDP 62
Cdd:cd00165    2 RLDKILARLGLAPSRSEARQLIKHGHVLVNGKVVTKPSYKVKPGDVIEVDGK 53
RlmM COG2933
23S rRNA C2498 (ribose-2'-O)-methylase RlmM [Translation, ribosomal structure and biogenesis]; ...
 62-133 3.01e-11

23S rRNA C2498 (ribose-2'-O)-methylase RlmM [Translation, ribosomal structure and biogenesis]; 23S rRNA C2498 (ribose-2'-O)-methylase RlmM is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 442177 [Multi-domain]  Cd Length: 356  Bit Score: 62.56  E-value: 3.01e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501038873  62 PASAyVSRAALKLIAALDHF------ELDVK-GRTALDIGASTGGFTQVLLERGAsHVLAIDVGhdQLHETLRADPRVT 133
Cdd:COG2933  181 PADA-PSRSTLKLEEAFHVFlprdewEERLRpGMRAVDLGAAPGGWTWQLVRRGM-FVTAVDNG--PMAPSLMDTGQVE 255
S4 smart00363
S4 RNA-binding domain;
10-61 3.36e-10

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 54.52  E-value: 3.36e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 501038873    10 LRLDQLLVELGLFATRSRARDAIQRGTVKVDGKPVTKPGQTVLRTAKIAVDD 61
Cdd:smart00363   1 RRLDKFLARLGLAPSRSQARRLIEQGRVKVNGKKVTKPSYIVKPGDVISVRG 52
S4 pfam01479
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ...
 10-51 3.55e-10

S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was detected in the bacterial ribosomal protein S4, eukaryotic ribosomal S9, two families of pseudouridine synthases, a novel family of predicted RNA methylases, a yeast protein containing a pseudouridine synthetase and a deaminase domain, bacterial tyrosyl-tRNA synthetases, and a number of uncharacterized, small proteins that may be involved in translation regulation. The S4 domain probably mediates binding to RNA.


Pssm-ID: 396182 [Multi-domain]  Cd Length: 48  Bit Score: 54.04  E-value: 3.55e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 501038873   10 LRLDQLLVELGLFATRSRARDAIQRGTVKVDGKPVTKPGQTV 51
Cdd:pfam01479   1 RRLDKVLARLGLASSRSQARQLIEHGRVLVNGKVVKDPSYRV 42
RlmE COG0293
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ...
 66-159 1.05e-07

23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and biogenesis]; 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440062 [Multi-domain]  Cd Length: 208  Bit Score: 50.84  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038873  66 YVSRAALKLIAALDHFELDVKGRTALDIGASTGGFTQVLLER--GASHVLAIDVghdqLH-------ETLRADprVTNKE 136
Cdd:COG0293   30 YRSRAAYKLLEIDEKDKLIKPGMRVVDLGAAPGGWSQVAAKRvgGKGRVIALDL----LPmepipgvEFIQGD--FREDE 103

                         90       100
                 ....*....|....*....|...
gi 501038873 137 GLNarALeLSHLDGREIDCVVSD 159
Cdd:COG0293  104 VLD--QL-LEALGGRKVDLVLSD 123
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 89-203 1.37e-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: 48.58  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038873  89 TALDIGASTGGFTQVLLERGASHVLAIDVGHDQLH--ETLRADPRVTNKEGLNARALELSHLDGREIDCVVSDVSFISLK 166
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALElaRKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLHHLV 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 501038873 167 LALPPALafaqkgaicallvkpqfEAGREAIGKGGIL 203
Cdd:cd02440   81 EDLARFL-----------------EEARRLLKPGGVL 100
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 4-51 9.80e-06

Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439932 [Multi-domain]  Cd Length: 409  Bit Score: 46.18  E-value: 9.80e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 501038873   4 ETSDKNLRLDQLLVELGLFATRSRARDAIQRGTVKVDGKPVTKPGQTV 51
Cdd:COG0162  336 SAAEGGIPLVDLLVEAGLAASKSEARRLIKQGGVSVNGEKVTDPDAVL 383
rluD PRK11180
23S rRNA pseudouridine(1911/1915/1917) synthase RluD;
11-60 1.14e-04

23S rRNA pseudouridine(1911/1915/1917) synthase RluD;


Pssm-ID: 183020 [Multi-domain]  Cd Length: 325  Bit Score: 42.74  E-value: 1.14e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 501038873  11 RLDQLLVELGLFATRSRARDAIQRGTVKVDGKPVTKPGQTVLRTAKIAVD 60
Cdd:PRK11180  19 RLDQALAELFPDYSRSRIKEWILDQRVLVNGKVINKPKEKVLGGEQVAID 68
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 64-173 1.65e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 41.44  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038873  64 SAYVSRAALKLIAALDHFEldvKGRTALDIGASTGGFTQVLLERGASHVLAIDV--GHDQLHETLRADPRVTNKEGLNAR 141
Cdd:COG0500    7 SDELLPGLAALLALLERLP---KGGRVLDLGCGTGRNLLALAARFGGRVIGIDLspEAIALARARAAKAGLGNVEFLVAD 83

                         90       100       110
                 ....*....|....*....|....*....|..
gi 501038873 142 ALELSHLDGREIDCVVSDVSFISLKLALPPAL 173
Cdd:COG0500   84 LAELDPLPAESFDLVVAFGVLHHLPPEEREAL 115
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 60-158 1.87e-04

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: 40.36  E-value: 1.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038873  60 DDPASAYVSRAALklIAALDhfelDVKGRTALDIGASTGGFTQVLLERGAsHVLAIDVGHDQLHETL-RADPRVTNKEGL 138
Cdd:COG2226    2 DRVAARYDGREAL--LAALG----LRPGARVLDLGCGTGRLALALAERGA-RVTGVDISPEMLELAReRAAEAGLNVEFV 74

                         90       100
                 ....*....|....*....|
gi 501038873 139 NARALELShLDGREIDCVVS 158
Cdd:COG2226   75 VGDAEDLP-FPDGSFDLVIS 93
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 91-158 2.41e-04

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 39.08  E-value: 2.41e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501038873   91 LDIGASTGGFTQVLLERGASHVLAIDVGHDQLHET-LRADPRVTNKEGLNARALELSHLDGReIDCVVS 158
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERArERAAEAGLNVEFVQGDAEDLPFPDGS-FDLVVS 69
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 82-158 2.97e-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: 39.62  E-value: 2.97e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501038873  82 ELDVKGRTALDIGASTGGFTQVLLERGAsHVLAIDVGHDQLhETLRADPRVTNKEGLNARALELSHLDGReIDCVVS 158
Cdd:COG2227   20 RLLPAGGRVLDVGCGTGRLALALARRGA-DVTGVDISPEAL-EIARERAAELNVDFVQGDLEDLPLEDGS-FDLVIC 93
YbcJ COG2501
Ribosome-associated protein YbcJ, S4-like RNA-binding protein [Translation, ribosomal ...
 11-61 6.01e-04

Ribosome-associated protein YbcJ, S4-like RNA-binding protein [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441995 [Multi-domain]  Cd Length: 61  Bit Score: 36.92  E-value: 6.01e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501038873  11 RLDQLLVELGLFATRSRARDAIQRGTVKVDGKPVTKpgqtvlRTAKIAVDD 61
Cdd:COG2501    4 TLGQLLKLAGLVESGGEAKALIAEGEVKVNGEVETR------RGRKLRPGD 48
S4_2 pfam13275
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ...
 11-61 2.38e-03

S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was detected in the bacterial ribosomal protein S4.


Pssm-ID: 433078 [Multi-domain]  Cd Length: 65  Bit Score: 35.49  E-value: 2.38e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 501038873   11 RLDQLLVELGLFATRSRARDAIQRGTVKVDGKPVTKpgqtvlRTAKIAVDD 61
Cdd:pfam13275   9 TLGQLLKLAGLVESGGEAKWFIAEGEVLVNGEVETR------RGKKLRAGD 53
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 68-158 9.84e-03

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 35.68  E-value: 9.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038873  68 SRAALKLIAALdhfeLDVK-GRTALDIGASTGGFTQVLLERGASHVLAIDVGHDQLHetlRADPRVtNKEGLNARAlELS 146
Cdd:COG2230   36 QEAKLDLILRK----LGLKpGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLE---YARERA-AEAGLADRV-EVR 106

                         90
                 ....*....|....*...
gi 501038873 147 HLDGREI------DCVVS 158
Cdd:COG2230  107 LADYRDLpadgqfDAIVS 124
 
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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