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Conserved domains on  [gi|1154134874|ref|WP_078510431|]
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class I SAM-dependent methyltransferase [Streptomyces himastatinicus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 1002172)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; similar to Homo sapiens tRNA wybutosine-synthesizing protein 4

CATH:  3.40.50.150
EC:  2.1.1.-
PubMed:  12826405|12504684
SCOP:  3000118

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RsmC super family cl34491
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
173-332 1.80e-22

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


The actual alignment was detected with superfamily member COG2813:

Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 93.72  E-value: 1.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 173 AHEWREKGVEVPALGGDRIHPYYGVFSPvrgEYVD-----LVAEAPLPASRAAAfDIGTGSGVLAAVLARRG-IERVVAT 246
Cdd:COG2813     4 ASDWPRTITVRLAGRDLTFVTLPGVFSR---DRLDigtrlLLEHLPEPLGGRVL-DLGCGYGVIGLALAKRNpEARVTLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 247 DQDERALACARENVARLGLaERVEVVRADLF---PPGRAPLIVCNPPWvpaRPSSPVEYAVydpgsrmLHGFLNGLTDAL 323
Cdd:COG2813    80 DVNARAVELARANAAANGL-ENVEVLWSDGLsgvPDGSFDLILSNPPF---HAGRAVDKEV-------AHALIADAARHL 148

                  ....*....
gi 1154134874 324 TPDGEGWLI 332
Cdd:COG2813   149 RPGGELWLV 157
 
Name Accession Description Interval E-value
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
173-332 1.80e-22

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: 93.72  E-value: 1.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 173 AHEWREKGVEVPALGGDRIHPYYGVFSPvrgEYVD-----LVAEAPLPASRAAAfDIGTGSGVLAAVLARRG-IERVVAT 246
Cdd:COG2813     4 ASDWPRTITVRLAGRDLTFVTLPGVFSR---DRLDigtrlLLEHLPEPLGGRVL-DLGCGYGVIGLALAKRNpEARVTLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 247 DQDERALACARENVARLGLaERVEVVRADLF---PPGRAPLIVCNPPWvpaRPSSPVEYAVydpgsrmLHGFLNGLTDAL 323
Cdd:COG2813    80 DVNARAVELARANAAANGL-ENVEVLWSDGLsgvPDGSFDLILSNPPF---HAGRAVDKEV-------AHALIADAARHL 148

                  ....*....
gi 1154134874 324 TPDGEGWLI 332
Cdd:COG2813   149 RPGGELWLV 157
PRK14968 PRK14968
putative methyltransferase; Provisional
207-359 4.17e-20

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 87.26  E-value: 4.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 207 DLVAEAPLPASRAAAFDIGTGSGVLAAVLARRGIeRVVATDQDERALACARENVARLGLAER-VEVVRADLFPPGRAP-- 283
Cdd:PRK14968   13 FLLAENAVDKKGDRVLEVGTGSGIVAIVAAKNGK-KVVGVDINPYAVECAKCNAKLNNIRNNgVEVIRSDLFEPFRGDkf 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 284 -LIVCNPPWVPARP----SSPVEYAvYD---PGSRMLHGFLNGLTDALTPDGEGWLILSDLAEhlglrtREELLGAFESA 355
Cdd:PRK14968   92 dVILFNPPYLPTEEeeewDDWLNYA-LSggkDGREVIDRFLDEVGRYLKPGGRILLLQSSLTG------EDEVLEYLEKL 164

                  ....
gi 1154134874 356 GLRV 359
Cdd:PRK14968  165 GFEA 168
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
196-353 1.19e-15

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: 74.16  E-value: 1.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 196 GVFSpvRGEyVD-----LVAEAPLPASRAAAfDIGTGSGVLAAVLARRGIE-RVVATDQDERALACARENVARLGLaERV 269
Cdd:pfam05175   9 GVFS--HGR-LDigsrlLLEHLPKDLSGKVL-DLGCGAGVLGAALAKESPDaELTMVDINARALESARENLAANGL-ENG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 270 EVVRADLF---PPGRAPLIVCNPPWvpaRPSSPVEYAVydpgsrmLHGFLNGLTDALTPDGEGWLILSdlaEHLGLRTR- 345
Cdd:pfam05175  84 EVVASDVYsgvEDGKFDLIISNPPF---HAGLATTYNV-------AQRFIADAKRHLRPGGELWIVAN---RFLGYPPLl 150

                  ....*...
gi 1154134874 346 EELLGAFE 353
Cdd:pfam05175 151 EELFGNVE 158
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
223-290 6.11e-10

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: 56.28  E-value: 6.11e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154134874 223 DIGTGSGVLAAVLARRGIERVVATDQDERALACARENVARlGLAERVEVVRADLF-----PPGRAPLIVCNPP 290
Cdd:cd02440     4 DLGCGTGALALALASGPGARVTGVDISPVALELARKAAAA-LLADNVEVLKGDAEelppeADESFDVIISDPP 75
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
223-295 1.34e-09

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 58.52  E-value: 1.34e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154134874 223 DIGTGSGVLAAVLA--RRGIErVVATDQDERALACARENVARLGLAERVEVVRADLFPP---GRAPLIVCNPPWVPAR 295
Cdd:TIGR00536 120 DLGTGSGCIALALAyeFPNAE-VIAVDISPDALAVAEENAEKNQLEHRVEFIQSNLFEPlagQKIDIIVSNPPYIDEE 196
 
Name Accession Description Interval E-value
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
173-332 1.80e-22

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: 93.72  E-value: 1.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 173 AHEWREKGVEVPALGGDRIHPYYGVFSPvrgEYVD-----LVAEAPLPASRAAAfDIGTGSGVLAAVLARRG-IERVVAT 246
Cdd:COG2813     4 ASDWPRTITVRLAGRDLTFVTLPGVFSR---DRLDigtrlLLEHLPEPLGGRVL-DLGCGYGVIGLALAKRNpEARVTLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 247 DQDERALACARENVARLGLaERVEVVRADLF---PPGRAPLIVCNPPWvpaRPSSPVEYAVydpgsrmLHGFLNGLTDAL 323
Cdd:COG2813    80 DVNARAVELARANAAANGL-ENVEVLWSDGLsgvPDGSFDLILSNPPF---HAGRAVDKEV-------AHALIADAARHL 148

                  ....*....
gi 1154134874 324 TPDGEGWLI 332
Cdd:COG2813   149 RPGGELWLV 157
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
206-360 1.57e-20

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 90.59  E-value: 1.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 206 VDLVAEAPLPASRAAAFDIGTGSGVLAAVLARRGIE-RVVATDQDERALACARENVARLGLAERVEVVRADLF----PPG 280
Cdd:COG2890   101 VELALALLPAGAPPRVLDLGTGSGAIALALAKERPDaRVTAVDISPDALAVARRNAERLGLEDRVRFLQGDLFeplpGDG 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 281 RAPLIVCNPPWVPAR--PSSPVEYAVYDPgsRM-LHGFLNGL----------TDALTPDgeGWLILsdlaEHlGLRTREE 347
Cdd:COG2890   181 RFDLIVSNPPYIPEDeiALLPPEVRDHEP--RLaLDGGEDGLdfyrriiaqaPRLLKPG--GWLLL----EI-GEDQGEA 251
                         170
                  ....*....|...
gi 1154134874 348 LLGAFESAGLRVV 360
Cdd:COG2890   252 VRALLEAAGFADV 264
PRK14968 PRK14968
putative methyltransferase; Provisional
207-359 4.17e-20

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 87.26  E-value: 4.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 207 DLVAEAPLPASRAAAFDIGTGSGVLAAVLARRGIeRVVATDQDERALACARENVARLGLAER-VEVVRADLFPPGRAP-- 283
Cdd:PRK14968   13 FLLAENAVDKKGDRVLEVGTGSGIVAIVAAKNGK-KVVGVDINPYAVECAKCNAKLNNIRNNgVEVIRSDLFEPFRGDkf 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 284 -LIVCNPPWVPARP----SSPVEYAvYD---PGSRMLHGFLNGLTDALTPDGEGWLILSDLAEhlglrtREELLGAFESA 355
Cdd:PRK14968   92 dVILFNPPYLPTEEeeewDDWLNYA-LSggkDGREVIDRFLDEVGRYLKPGGRILLLQSSLTG------EDEVLEYLEKL 164

                  ....
gi 1154134874 356 GLRV 359
Cdd:PRK14968  165 GFEA 168
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
223-372 5.29e-18

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: 82.50  E-value: 5.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 223 DIGTGSGVLAAVLARRGIE-RVVATDQDERALACARENVARLGLAERVEVVRADL------FPPGRAPLIVCNPPWVPAR 295
Cdd:COG4123    43 DLGTGTGVIALMLAQRSPGaRITGVEIQPEAAELARRNVALNGLEDRITVIHGDLkefaaeLPPGSFDLVVSNPPYFKAG 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 296 PS--SPVE------YAVYDPgsrmLHGFLNGLTDALTPDGEGWLILSdlAEHLglrtrEELLGAFESAGLRVVDRLDTRP 367
Cdd:COG4123   123 SGrkSPDEaraiarHEDALT----LEDLIRAAARLLKPGGRFALIHP--AERL-----AEILAALRKYGLGPKRLRPVHP 191

                  ....*
gi 1154134874 368 THHRA 372
Cdd:COG4123   192 RPGKP 196
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
222-363 1.97e-17

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 81.76  E-value: 1.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 222 FDIGTGSGVLAAVLARRGIERVVATDQDERALACARENVARLGLAERVEVVRADLFPPGRAPLIVCNppwVPARPsspve 301
Cdd:COG2264   153 LDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVEDRIEVVLGDLLEDGPYDLVVAN---ILANP----- 224
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154134874 302 yavydpgsrmLHGFLNGLTDALTPDgeGWLILSdlaehlGLRTR--EELLGAFESAGLRVVDRL 363
Cdd:COG2264   225 ----------LIELAPDLAALLKPG--GYLILS------GILEEqaDEVLAAYEAAGFELVERR 270
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
206-360 3.85e-17

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 80.59  E-value: 3.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 206 VDLVAEAPLPASRAAAFDIGTGSGVLAAVLA--RRGIeRVVATDQDERALACARENvARLGLAERVEVVRADLF---PPG 280
Cdd:PRK09328   97 VEWALEALLLKEPLRVLDLGTGSGAIALALAkeRPDA-EVTAVDISPEALAVARRN-AKHGLGARVEFLQGDWFeplPGG 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 281 RAPLIVCNPPWVPA--RPSSPVEYAVYDP---------GSRMLHGFLNGLTDALTPDgeGWLILsdlaEHlGLRTREELL 349
Cdd:PRK09328  175 RFDLIVSNPPYIPEadIHLLQPEVRDHEPhlalfggedGLDFYRRIIEQAPRYLKPG--GWLLL----EI-GYDQGEAVR 247
                         170
                  ....*....|.
gi 1154134874 350 GAFESAGLRVV 360
Cdd:PRK09328  248 ALLAAAGFADV 258
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
196-353 1.19e-15

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: 74.16  E-value: 1.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 196 GVFSpvRGEyVD-----LVAEAPLPASRAAAfDIGTGSGVLAAVLARRGIE-RVVATDQDERALACARENVARLGLaERV 269
Cdd:pfam05175   9 GVFS--HGR-LDigsrlLLEHLPKDLSGKVL-DLGCGAGVLGAALAKESPDaELTMVDINARALESARENLAANGL-ENG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 270 EVVRADLF---PPGRAPLIVCNPPWvpaRPSSPVEYAVydpgsrmLHGFLNGLTDALTPDGEGWLILSdlaEHLGLRTR- 345
Cdd:pfam05175  84 EVVASDVYsgvEDGKFDLIISNPPF---HAGLATTYNV-------AQRFIADAKRHLRPGGELWIVAN---RFLGYPPLl 150

                  ....*...
gi 1154134874 346 EELLGAFE 353
Cdd:pfam05175 151 EELFGNVE 158
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
222-287 7.37e-13

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 67.37  E-value: 7.37e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154134874 222 FDIGTGSGVLAAVLARRGIERVVATDQDERALACARENVARLGLAERVEVVRADLF---PPGRAPLIVC 287
Cdd:COG4076    40 LDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATdldLPEKADVIIS 108
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
222-362 2.12e-11

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: 64.21  E-value: 2.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 222 FDIGTGSGVLAAVLARRGIERVVATDQDERALACARENVARLGLAERVEVVRADLFPPGRAPLIVCNppwvparpsspve 301
Cdd:pfam06325 166 LDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEARLEVYLPGDLPKEKADVVVAN------------- 232
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154134874 302 yavydpgsrMLHGFLNGLTD----ALTPdgEGWLILSDLaehlgLRTREELLGAFESAGLRVVDR 362
Cdd:pfam06325 233 ---------ILADPLIELAPdiyaLVKP--GGYLILSGI-----LKEQAQMVAEAYSQGFELITV 281
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
223-288 1.61e-10

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 57.57  E-value: 1.61e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 223 DIGTGSGVLAAVLARRGIERVVATDQDERALACARENVARLGLaeRVEVVRADL----FPPGRAPLIVCN 288
Cdd:pfam13649   3 DLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAedlpFPDGSFDLVVSS 70
PRK14967 PRK14967
putative methyltransferase; Provisional
206-359 1.77e-10

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 60.45  E-value: 1.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 206 VDLVAEAPLPASRAAAfDIGTGSGVLAAVLARRGIERVVATDQDERALACARENVARLGLaeRVEVVRADL---FPPGRA 282
Cdd:PRK14967   26 ADALAAEGLGPGRRVL-DLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNALLAGV--DVDVRRGDWaraVEFRPF 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 283 PLIVCNPPWVPARPSSPVEY-------AVYDpGSRMLHGFLNGLTDALTPDGEGWLILSDLAehlglrTREELLGAFESA 355
Cdd:PRK14967  103 DVVVSNPPYVPAPPDAPPSRgparawdAGPD-GRAVLDRLCDAAPALLAPGGSLLLVQSELS------GVERTLTRLSEA 175

                  ....
gi 1154134874 356 GLRV 359
Cdd:PRK14967  176 GLDA 179
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
221-363 5.14e-10

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 59.40  E-value: 5.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 221 AFDIGTGSGVLAAVLARRGIERVVATDQDERALACARENVARLGLAERVEVVRADLfppgRAPLIVCNppwVPARPsspv 300
Cdd:PRK00517  123 VLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGVELNVYLPQGDL----KADVIVAN---ILANP---- 191
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154134874 301 eyavydpgsrmLHGFLNGLTDALTPDgeGWLILSD-LAEHLglrtrEELLGAFESAGLRVVDRL 363
Cdd:PRK00517  192 -----------LLELAPDLARLLKPG--GRLILSGiLEEQA-----DEVLEAYEEAGFTLDEVL 237
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
223-290 6.11e-10

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: 56.28  E-value: 6.11e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154134874 223 DIGTGSGVLAAVLARRGIERVVATDQDERALACARENVARlGLAERVEVVRADLF-----PPGRAPLIVCNPP 290
Cdd:cd02440     4 DLGCGTGALALALASGPGARVTGVDISPVALELARKAAAA-LLADNVEVLKGDAEelppeADESFDVIISDPP 75
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
222-291 1.28e-09

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 57.61  E-value: 1.28e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154134874 222 FDIGTGSGVLAAVLARRGIERVVATDQDERALACARENVARLGlaERVEVVRADLF---PPGRAPLIVCNPPW 291
Cdd:COG2263    50 LDLGCGTGMLAIGAALLGAKKVVGVDIDPEALEIARENAERLG--VRVDFIRADVTripLGGSVDTVVMNPPF 120
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
223-295 1.34e-09

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 58.52  E-value: 1.34e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154134874 223 DIGTGSGVLAAVLA--RRGIErVVATDQDERALACARENVARLGLAERVEVVRADLFPP---GRAPLIVCNPPWVPAR 295
Cdd:TIGR00536 120 DLGTGSGCIALALAyeFPNAE-VIAVDISPDALAVAEENAEKNQLEHRVEFIQSNLFEPlagQKIDIIVSNPPYIDEE 196
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
242-344 4.26e-09

23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA G2445 N2-methylase RlmL is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 439886 [Multi-domain]  Cd Length: 369  Bit Score: 57.80  E-value: 4.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 242 RVVATDQDERALACARENVARLGLAERVEVVRADLF---PPGRAPLIVCNPPwvparpsspveYavydpGSRM-----LH 313
Cdd:COG0116   252 PIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRdlePPAEPGLIITNPP-----------Y-----GERLgeeeeLE 315
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1154134874 314 GFLNGLTDALTPDGEGW---LILSD--LAEHLGLRT 344
Cdd:COG0116   316 ALYRELGDVLKQRFKGWsayILTSDpeLEKAIGLKA 351
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
202-335 5.21e-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: 53.87  E-value: 5.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 202 RGEYVDLVAEAPLPASRAaaFDIGTGSGVLAAVLARRGIeRVVATDQDERALACARENVARLglaeRVEVVRADL----F 277
Cdd:COG2227    11 DRRLAALLARLLPAGGRV--LDVGCGTGRLALALARRGA-DVTGVDISPEALEIARERAAEL----NVDFVQGDLedlpL 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1154134874 278 PPGRAPLIVCNppwvparpsSPVEYaVYDPgsrmlHGFLNGLTDALTPDgeGWLILSD 335
Cdd:COG2227    84 EDGSFDLVICS---------EVLEH-LPDP-----AALLRELARLLKPG--GLLLLST 124
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
223-287 7.97e-08

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 51.47  E-value: 7.97e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154134874 223 DIGTGSGVLAAVLARRGIERVVATDQDERALACARENVARLGLAERVEVVRAD---LFPPGRAPLIVC 287
Cdd:COG2230    57 DIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADyrdLPADGQFDAIVS 124
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
232-291 8.92e-08

bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2))-methyltransferase RlmL;


Pssm-ID: 236981 [Multi-domain]  Cd Length: 702  Bit Score: 54.04  E-value: 8.92e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 232 AAVLARRGIERV----VATDQDERALACARENVARLGLAERVEVVRADL------FPPGRAPLIVCNPPW 291
Cdd:PRK11783  244 AQERARAGLAELpskfYGSDIDPRVIQAARKNARRAGVAELITFEVKDVadlknpLPKGPTGLVISNPPY 313
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
164-290 2.25e-07

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 52.49  E-value: 2.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 164 LRELLGLIGAHEWREKGVEVPA--------LGGDRIHPYYGVFSPV--RGEY--VDLVAEA--PLPASRAAafDIGTGSG 229
Cdd:COG2265   168 LRELLAELGARRGELRHLVVRAgrdylterLGGLTFRISPGSFFQVnpEQAEalYAAALEWldLTGGERVL--DLYCGVG 245
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154134874 230 VLAAVLARRGiERVVATDQDERALACARENVARLGLaERVEVVRADLF-------PPGRAPLIVCNPP 290
Cdd:COG2265   246 TFALPLARRA-KKVIGVEIVPEAVEDARENARLNGL-KNVEFVAGDLEevlpellWGGRPDVVVLDPP 311
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
222-286 3.14e-07

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 50.93  E-value: 3.14e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154134874 222 FDIGTGSGVLAAVLAR----RGieRVVATDQDERALACARENVARLGLAERVEVVRADL---FPPGRAPLIV 286
Cdd:COG2519    96 LEAGTGSGALTLALARavgpEG--KVYSYERREDFAEIARKNLERFGLPDNVELKLGDIregIDEGDVDAVF 165
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
194-288 3.69e-07

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 50.30  E-value: 3.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 194 YYGVFSPVRGEYVDLVAEAPLPASraaAFDIGTGSGVLAAVLARRGIERVVATDQDERALACARENVARLGLAeRVEVVR 273
Cdd:COG0500     6 YSDELLPGLAALLALLERLPKGGR---VLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLG-NVEFLV 81
                          90       100
                  ....*....|....*....|
gi 1154134874 274 ADL-----FPPGRAPLIVCN 288
Cdd:COG0500    82 ADLaeldpLPAESFDLVVAF 101
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
223-283 5.45e-07

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 49.70  E-value: 5.45e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154134874 223 DIGTGSGVLAAVLARRGiERVVATDQDERALACARENVARLGLAeRVEVVRADLF--PPGRAP 283
Cdd:COG2518    72 EIGTGSGYQAAVLARLA-GRVYSVERDPELAERARERLAALGYD-NVTVRVGDGAlgWPEHAP 132
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
223-288 1.31e-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: 47.68  E-value: 1.31e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 223 DIGTGSGVLAAVLARRGiERVVATDQDERALACARENVARLGLaeRVEVVRADL----FPPGRAPLIVCN 288
Cdd:COG2226    28 DLGCGTGRLALALAERG-ARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAedlpFPDGSFDLVISS 94
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
223-287 1.38e-06

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: 48.73  E-value: 1.38e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154134874 223 DIGTGSGVLAAVLARRGIERVVATDQDERALACARENVARLGLAerVEVVRADLF---PPGRAPLIVC 287
Cdd:COG3897    76 ELGCGLGLVGIAAAKAGAADVTATDYDPEALAALRLNAALNGVA--ITTRLGDWRdppAAGGFDLILG 141
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
227-290 4.46e-06

16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA G966 N2-methylase RsmD is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440505 [Multi-domain]  Cd Length: 183  Bit Score: 46.61  E-value: 4.46e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 227 GSGVLAAVLARRGIERVVATDQDERALACARENVARLGLAERVEVVRADLF------PPGRAPLIVCNPP 290
Cdd:COG0742    51 GSGALGLEALSRGAASVVFVEKDRKAAAVIRKNLEKLGLEDRARVIRGDALrflkrlAGEPFDLVFLDPP 120
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
221-288 9.09e-06

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 44.04  E-value: 9.09e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154134874 221 AFDIGTGSGVLAAVLARRGIE-RVVATDQDERALACARENVArlglaeRVEVVRADLF---PPGRAPLIVCN 288
Cdd:COG4106     5 VLDLGCGTGRLTALLAERFPGaRVTGVDLSPEMLARARARLP------NVRFVVADLRdldPPEPFDLVVSN 70
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
226-290 1.74e-05

23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 46.33  E-value: 1.74e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154134874 226 TGS-GVLAAvlaRRGIERVVATDQDERALACARENVARLGLAERVEVVRADLFP--------PGRAPLIVCNPP 290
Cdd:COG1092   227 TGGfSVHAA---AGGAKSVTSVDLSATALEWAKENAALNGLDDRHEFVQADAFDwlrelareGERFDLIILDPP 297
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
223-288 2.31e-05

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 42.65  E-value: 2.31e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154134874 223 DIGTGSGVLAAVLARRGiERVVATDQDERALACARENVARLGLAERVEVVRADLFPPGRAPLIVCN 288
Cdd:pfam08241   2 DVGCGTGLLTELLARLG-ARVTGVDISPEMLELAREKAPREGLTFVVGDAEDLPFPDNSFDLVLSS 66
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
224-275 2.35e-05

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: 44.40  E-value: 2.35e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1154134874 224 IGTGSGV----LAAVLARRGieRVVATDQDERALACARENVARLGLAERVEVVRAD 275
Cdd:COG4122    23 IGTGTGYstlwLARALPDDG--RLTTIEIDPERAAIARENFARAGLADRIRLILGD 76
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
223-335 3.54e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 43.56  E-value: 3.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 223 DIGTGSGVLAAVLARRGIE--RVVATDQDERALACARENVARLGLaERVEVVRAD------LFPPGRAPLIVCNppwvpa 294
Cdd:pfam13847   9 DLGCGTGHLSFELAEELGPnaEVVGIDISEEAIEKARENAQKLGF-DNVEFEQGDieelpeLLEDDKFDVVISN------ 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1154134874 295 rpssPVEYAVYDPGSrmlhgFLNGLTDALTPDGEgwLILSD 335
Cdd:pfam13847  82 ----CVLNHIPDPDK-----VLQEILRVLKPGGR--LIISD 111
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
223-290 4.05e-05

16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 45.31  E-value: 4.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154134874 223 DIGTGSGVLAAVLARRGIE-RVVATDQDERALACARENVARLGLAErvEVVRADLFP--PGRAPLIVCNPP 290
Cdd:PRK09489  202 DVGCGAGVLSAVLARHSPKiRLTLSDVSAAALESSRATLAANGLEG--EVFASNVFSdiKGRFDMIISNPP 270
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
204-359 5.10e-05

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 43.45  E-value: 5.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 204 EYVDLVAEAPLPASRAAAFDIGTGSGVLAAVLARRGIeRVVATDQDERALACARENvarlglAERVEVVRADL----FPP 279
Cdd:COG4976    33 LLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGY-RLTGVDLSEEMLAKAREK------GVYDRLLVADLadlaEPD 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 280 GRAPLIVCNppwvparpsspveyAVYDPGsRMLHGFLNGLTDALTPDgeGWLILS---DLAEHLGLRTREELLGAFESAG 356
Cdd:COG4976   106 GRFDLIVAA--------------DVLTYL-GDLAAVFAGVARALKPG--GLFIFSvedADGSGRYAHSLDYVRDLLAAAG 168

                  ...
gi 1154134874 357 LRV 359
Cdd:COG4976   169 FEV 171
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
223-275 6.67e-04

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 40.91  E-value: 6.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1154134874 223 DIGTGSGVLAAVLARRG--IERVVATDQDERALACARENVARLGLAERVEVVRAD 275
Cdd:PRK00216   57 DLACGTGDLAIALAKAVgkTGEVVGLDFSEGMLAVGREKLRDLGLSGNVEFVQGD 111
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
204-275 9.65e-04

Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 40.04  E-value: 9.65e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154134874 204 EYVDLVaeaplPASRAaaFDIGTGSGVLAAVLAR--RGIERVVATDQDERALACARENVARLGLaERVEVVRAD 275
Cdd:pfam01135  67 ELLELK-----PGMRV--LEIGSGSGYLTACFARmvGEVGRVVSIEHIPELVEIARRNLEKLGL-ENVIVVVGD 132
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
200-275 1.03e-03

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 39.78  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 200 PVRGEYVDLVAEAPLPASRAAAF-DIGTGSG---VLAAVLARRGiERVVATDQDERALACARENVARLGLAERVEVVRAD 275
Cdd:PRK00377   22 PMTKEEIRALALSKLRLRKGDMIlDIGCGTGsvtVEASLLVGET-GKVYAVDKDEKAINLTRRNAEKFGVLNNIVLIKGE 100
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
201-360 1.74e-03

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 38.95  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 201 VRGEYVDLVAE-APLPASRAAAFDIGTGSGVLAAVLARRGIErVVATDQDERALACARENVARLGLAERVEvvradLFPP 279
Cdd:pfam13489   5 RERLLADLLLRlLPKLPSPGRVLDFGCGTGIFLRLLRAQGFS-VTGVDPSPIAIERALLNVRFDQFDEQEA-----AVPA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 280 GRAPLIVCNPpwvparpsspVEYAVYDPgsrmlHGFLNGLTDALTPDGegWLILSDLA-------------------EHL 340
Cdd:pfam13489  79 GKFDVIVARE----------VLEHVPDP-----PALLRQIAALLKPGG--LLLLSTPLasdeadrlllewpylrprnGHI 141
                         170       180
                  ....*....|....*....|
gi 1154134874 341 GLRTREELLGAFESAGLRVV 360
Cdd:pfam13489 142 SLFSARSLKRLLEEAGFEVV 161
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
215-327 1.99e-03

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 38.08  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 215 PASRAAAFDIGTGSGVLAAVLARR-GIERVVATDQDERALACARENVARLGLAeRVEVVRADlfppgrAPLIVCNPPWVP 293
Cdd:TIGR02469  17 LRPGDVLWDIGAGTGSVTIEAARLvPNGRVYAIERNPEALDLIERNLRRFGVS-NIVIVEGD------APEAPEALLPDP 89
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1154134874 294 ARpsspveyAVYDPGSRMLHGFLNGLTDALTPDG 327
Cdd:TIGR02469  90 DA-------VFVGGSGGLLQEILEAVERRLRPGG 116
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
222-288 2.04e-03

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 37.35  E-value: 2.04e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154134874 222 FDIGTGSG-VLAAVLARRGIERVVATDQDERALACARENVARLGL--AERVEVVRADLF--PPGRAPLIVCN 288
Cdd:pfam08242   1 LEIGCGTGtLLRALLEALPGLEYTGLDISPAALEAARERLAALGLlnAVRVELFQLDLGelDPGSFDVVVAS 72
PRK06202 PRK06202
hypothetical protein; Provisional
196-288 5.19e-03

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 38.06  E-value: 5.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154134874 196 GVFSPVRGEYVDLVAEAPLPASRAAAFDIGTGSGVLAAVLA----RRGIE-RVVATDQDERALACARENVARLGLAERVe 270
Cdd:PRK06202   39 RIVAGWRGLYRRLLRPALSADRPLTLLDIGCGGGDLAIDLArwarRDGLRlEVTAIDPDPRAVAFARANPRRPGVTFRQ- 117
                          90
                  ....*....|....*....
gi 1154134874 271 VVRADLFPPGRA-PLIVCN 288
Cdd:PRK06202  118 AVSDELVAEGERfDVVTSN 136
 
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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