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Conserved domains on  [gi|768024643|ref|XP_011528444|]
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tRNA (uracil-5-)-methyltransferase homolog A isoform X2 [Homo sapiens]

Protein Classification

class I SAM-dependent RNA methyltransferase( domain architecture ID 11455144)

class I SAM-dependent RNA methyltransferase catalyzes the methylation of a specific RNA substrate using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0001510|GO:0046872|GO:0008757|GO:1904047
PubMed:  12826405|12504684
SCOP:  3000118

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 48-279 5.25e-64

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: 206.57  E-value: 5.25e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643  48 RKTPSQEGLpLEHV---AGDRCIHEDLLGLTFRISPHAFFQVNTPAAEVLYTVIQDWAQLDAGSMVLDVCCGTGTIGLAL 124
Cdd:COG2265  173 AELGARRGE-LRHLvvrAGRDYLTERLGGLTFRISPGSFFQVNPEQAEALYAAALEWLDLTGGERVLDLYCGVGTFALPL 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643 125 ARgpmysppwvgrhhaflfqKVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDLVPTLVSRLASQhlVAILDPP 204
Cdd:COG2265  252 AR------------------RAKKVIGVEIVPEAVEDARENARLNGLKNVEFVAGDLEEVLPELLWGGRPD--VVVLDPP 311

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768024643 205 RAGLHSKVILAIRRAKnLRRLLYVSCNP----RaamgnfvDLCRAPSNRvkgipFRPVKAVAVDLFPQTPHCEMLILFE 279
Cdd:COG2265  312 RAGAGPEVLEALAALG-PRRIVYVSCNPatlaR-------DLALLVEGG-----YRLEKVQPVDMFPHTHHVESVALLE 377
 
Name Accession Description Interval E-value
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 48-279 5.25e-64

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: 206.57  E-value: 5.25e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643  48 RKTPSQEGLpLEHV---AGDRCIHEDLLGLTFRISPHAFFQVNTPAAEVLYTVIQDWAQLDAGSMVLDVCCGTGTIGLAL 124
Cdd:COG2265  173 AELGARRGE-LRHLvvrAGRDYLTERLGGLTFRISPGSFFQVNPEQAEALYAAALEWLDLTGGERVLDLYCGVGTFALPL 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643 125 ARgpmysppwvgrhhaflfqKVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDLVPTLVSRLASQhlVAILDPP 204
Cdd:COG2265  252 AR------------------RAKKVIGVEIVPEAVEDARENARLNGLKNVEFVAGDLEEVLPELLWGGRPD--VVVLDPP 311

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768024643 205 RAGLHSKVILAIRRAKnLRRLLYVSCNP----RaamgnfvDLCRAPSNRvkgipFRPVKAVAVDLFPQTPHCEMLILFE 279
Cdd:COG2265  312 RAGAGPEVLEALAALG-PRRIVYVSCNPatlaR-------DLALLVEGG-----YRLEKVQPVDMFPHTHHVESVALLE 377
rumA TIGR00479
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ...
 49-273 4.42e-39

23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA methyltransferases by homology to the TrmA family. The member from E. coli has now been shown to act as the 23S RNA methyltransferase for the conserved U1939. The gene is now designated rumA and was previously designated ygcA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 129571 [Multi-domain]  Cd Length: 431  Bit Score: 142.65  E-value: 4.42e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643   49 KTPSQEGLPLEHVAGDRCIHEDLLGLTFRISPHAFFQVNTPAAEVLYTVIQDWAQLDAGSMVLDVCCGTGTIGLALARGp 128
Cdd:TIGR00479 235 KTNVIFGEETEVIAGEMPIYDKSGDLSFTFSARDFIQVNSGQNEKLVDRALEWLELQGEERVLDAYCGMGTFTLPLAKQ- 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643  129 mysppwvgrhhaflfqkVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDLVPTLVSRLASQHLVaILDPPRAGL 208
Cdd:TIGR00479 314 -----------------AKSVVGVEGVPESVEKAQQNAELNGIANVTFYHGTLETVLPKQPWAGNGFDKV-LLDPPRKGC 375

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768024643  209 HSKVILAIRRAKNlRRLLYVSCNPRAAMGNFVDLCRApsnrvkgiPFRPVKAVAVDLFPQTPHCE 273
Cdd:TIGR00479 376 AAGVLRTIIKLKP-ERIVYVSCNPATLARDLEALCKA--------GYTIARVQPVDMFPHTGHVE 431
rumB PRK03522
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
59-280 8.88e-25

23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;


Pssm-ID: 235128 [Multi-domain]  Cd Length: 315  Bit Score: 101.48  E-value: 8.88e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643  59 EHVA---GDRCIH--------EDLLGLTFRISPHAFFQVNTPAAEVLYTVIQDW-AQLDAGSMVlDVCCGTGTIGLALAR 126
Cdd:PRK03522 115 VHMAileGEEEIFlteqqalpERFNGVPLFIRPQSFFQTNPAVAAQLYATARDWvRELPPRSMW-DLFCGVGGFGLHCAT 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643 127 GPMysppwvgrhhaflfqkvkRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRA------EDLVPTLVsrlasqhlvaI 200
Cdd:PRK03522 194 PGM------------------QLTGIEISAEAIACAKQSAAELGLTNVQFQALDStqfataQGEVPDLV----------L 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643 201 LDPPRAGLhSKVILAIRRAKNLRRLLYVSCNPrAAMGNfvDLCRAPSnrvkgipFRPVKAVAVDLFPQTPHCEMLILFER 280
Cdd:PRK03522 246 VNPPRRGI-GKELCDYLSQMAPRFILYSSCNA-QTMAK--DLAHLPG-------YRIERVQLFDMFPHTAHYEVLTLLVR 314
tRNA_U5-meth_tr pfam05958
tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC: ...
 82-281 5.56e-11

tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC:2.1.1.35 from bacteria, archaea and eukaryotes. A 5-methyluridine (m(5)U) residue at position 54 is a conserved feature of bacterial and eukaryotic tRNAs. The methylation of U54 is catalyzed by the tRNA(m5U54)methyltransferase, which in Saccharomyces cerevisiae is encoded by the nonessential TRM2 gene. It is thought that tRNA modification enzymes might have a role in tRNA maturation not necessarily linked to their known catalytic activity.


Pssm-ID: 428692  Cd Length: 357  Bit Score: 62.84  E-value: 5.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643   82 AFFQVNTPAAEVLYTVIQDWAQLDAGSMvLDVCCGTGTIGLALARgpmysppwvgrhhaflfqKVKRVIGVELCPEAVED 161
Cdd:pfam05958 178 SFTQPNAAVNIKMLEWACDVTQGSKGDL-LELYCGNGNFSLALAR------------------NFRKVLATEIAKPSVAA 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643  162 ARVNAQDNELSNVEFHCGRAEDLVPTLVSRLASQHLVAI-----------LDPPRAGLHSKVIlaiRRAKNLRRLLYVSC 230
Cdd:pfam05958 239 AQYNIAANNIDNVQIIRMSAEEFTQAMNGVREFNRLKGIdlksyncstifVDPPRAGLDPETL---KLVQAYPRILYISC 315

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768024643  231 NPRAAMGNFVDLCRapSNRVKgipfrpvKAVAVDLFPQTPHCEMLILFERV 281
Cdd:pfam05958 316 NPETLCANLEQLSK--THRVE-------RFALFDQFPYTHHMECGVLLEKK 357
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 110-230 9.91e-11

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: 57.83  E-value: 9.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643 110 VLDVCCGTGTIGLALARGPmysppwvgrhhaflfqkVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDLVPTLV 189
Cdd:cd02440    2 VLDLGCGTGALALALASGP-----------------GARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEAD 64

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 768024643 190 SRLAsqhlVAILDPP---RAGLHSKVILAIRRAKNLRRLLYVSC 230
Cdd:cd02440   65 ESFD----VIISDPPlhhLVEDLARFLEEARRLLKPGGVLVLTL 104
 
Name Accession Description Interval E-value
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 48-279 5.25e-64

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: 206.57  E-value: 5.25e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643  48 RKTPSQEGLpLEHV---AGDRCIHEDLLGLTFRISPHAFFQVNTPAAEVLYTVIQDWAQLDAGSMVLDVCCGTGTIGLAL 124
Cdd:COG2265  173 AELGARRGE-LRHLvvrAGRDYLTERLGGLTFRISPGSFFQVNPEQAEALYAAALEWLDLTGGERVLDLYCGVGTFALPL 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643 125 ARgpmysppwvgrhhaflfqKVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDLVPTLVSRLASQhlVAILDPP 204
Cdd:COG2265  252 AR------------------RAKKVIGVEIVPEAVEDARENARLNGLKNVEFVAGDLEEVLPELLWGGRPD--VVVLDPP 311

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768024643 205 RAGLHSKVILAIRRAKnLRRLLYVSCNP----RaamgnfvDLCRAPSNRvkgipFRPVKAVAVDLFPQTPHCEMLILFE 279
Cdd:COG2265  312 RAGAGPEVLEALAALG-PRRIVYVSCNPatlaR-------DLALLVEGG-----YRLEKVQPVDMFPHTHHVESVALLE 377
rumA TIGR00479
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ...
 49-273 4.42e-39

23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA methyltransferases by homology to the TrmA family. The member from E. coli has now been shown to act as the 23S RNA methyltransferase for the conserved U1939. The gene is now designated rumA and was previously designated ygcA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 129571 [Multi-domain]  Cd Length: 431  Bit Score: 142.65  E-value: 4.42e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643   49 KTPSQEGLPLEHVAGDRCIHEDLLGLTFRISPHAFFQVNTPAAEVLYTVIQDWAQLDAGSMVLDVCCGTGTIGLALARGp 128
Cdd:TIGR00479 235 KTNVIFGEETEVIAGEMPIYDKSGDLSFTFSARDFIQVNSGQNEKLVDRALEWLELQGEERVLDAYCGMGTFTLPLAKQ- 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643  129 mysppwvgrhhaflfqkVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDLVPTLVSRLASQHLVaILDPPRAGL 208
Cdd:TIGR00479 314 -----------------AKSVVGVEGVPESVEKAQQNAELNGIANVTFYHGTLETVLPKQPWAGNGFDKV-LLDPPRKGC 375

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768024643  209 HSKVILAIRRAKNlRRLLYVSCNPRAAMGNFVDLCRApsnrvkgiPFRPVKAVAVDLFPQTPHCE 273
Cdd:TIGR00479 376 AAGVLRTIIKLKP-ERIVYVSCNPATLARDLEALCKA--------GYTIARVQPVDMFPHTGHVE 431
rumB PRK03522
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
59-280 8.88e-25

23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;


Pssm-ID: 235128 [Multi-domain]  Cd Length: 315  Bit Score: 101.48  E-value: 8.88e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643  59 EHVA---GDRCIH--------EDLLGLTFRISPHAFFQVNTPAAEVLYTVIQDW-AQLDAGSMVlDVCCGTGTIGLALAR 126
Cdd:PRK03522 115 VHMAileGEEEIFlteqqalpERFNGVPLFIRPQSFFQTNPAVAAQLYATARDWvRELPPRSMW-DLFCGVGGFGLHCAT 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643 127 GPMysppwvgrhhaflfqkvkRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRA------EDLVPTLVsrlasqhlvaI 200
Cdd:PRK03522 194 PGM------------------QLTGIEISAEAIACAKQSAAELGLTNVQFQALDStqfataQGEVPDLV----------L 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643 201 LDPPRAGLhSKVILAIRRAKNLRRLLYVSCNPrAAMGNfvDLCRAPSnrvkgipFRPVKAVAVDLFPQTPHCEMLILFER 280
Cdd:PRK03522 246 VNPPRRGI-GKELCDYLSQMAPRFILYSSCNA-QTMAK--DLAHLPG-------YRIERVQLFDMFPHTAHYEVLTLLVR 314
rumA PRK13168
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;
73-280 1.15e-22

23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;


Pssm-ID: 237291 [Multi-domain]  Cd Length: 443  Bit Score: 97.53  E-value: 1.15e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643  73 GLTFRISPHAFFQVNTPAAEVLytVIQ--DWAQLDAGSMVLDVCCGTGTIGLALARgpmysppwvgrhhaflfqKVKRVI 150
Cdd:PRK13168 264 GLRLAFSPRDFIQVNAQVNQKM--VARalEWLDPQPGDRVLDLFCGLGNFTLPLAR------------------QAAEVV 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643 151 GVELCPEAVEDARVNAQDNELSNVEFHCgraEDLVPTLVSRL-ASQHLVAIL-DPPRAGlhskvilAIRRAKNL-----R 223
Cdd:PRK13168 324 GVEGVEAMVERARENARRNGLDNVTFYH---ANLEEDFTDQPwALGGFDKVLlDPPRAG-------AAEVMQALaklgpK 393

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 768024643 224 RLLYVSCNPraamgnfVDLCRAPSNRVKGiPFRPVKAVAVDLFPQTPHCEMLILFER 280
Cdd:PRK13168 394 RIVYVSCNP-------ATLARDAGVLVEA-GYRLKRAGMLDMFPHTGHVESMALFER 442
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 53-179 8.59e-12

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 64.40  E-value: 8.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643  53 QEGLPLEHVAGdrciHEDLLGLTFRISPHAFfqV---NTpaaEVLYTVIQDWAQLDAGSMVLDVCCGTGTIGLALARgpm 129
Cdd:COG2890   65 AAGEPLAYILG----EAEFYGLEFKVDPGVL--IprpET---EELVELALALLPAGAPPRVLDLGTGSGAIALALAK--- 132

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 768024643 130 YSPPWvgrhhaflfqkvkRVIGVELCPEAVEDARVNAQDNELSN-VEFHCG 179
Cdd:COG2890  133 ERPDA-------------RVTAVDISPDALAVARRNAERLGLEDrVRFLQG 170
tRNA_U5-meth_tr pfam05958
tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC: ...
 82-281 5.56e-11

tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC:2.1.1.35 from bacteria, archaea and eukaryotes. A 5-methyluridine (m(5)U) residue at position 54 is a conserved feature of bacterial and eukaryotic tRNAs. The methylation of U54 is catalyzed by the tRNA(m5U54)methyltransferase, which in Saccharomyces cerevisiae is encoded by the nonessential TRM2 gene. It is thought that tRNA modification enzymes might have a role in tRNA maturation not necessarily linked to their known catalytic activity.


Pssm-ID: 428692  Cd Length: 357  Bit Score: 62.84  E-value: 5.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643   82 AFFQVNTPAAEVLYTVIQDWAQLDAGSMvLDVCCGTGTIGLALARgpmysppwvgrhhaflfqKVKRVIGVELCPEAVED 161
Cdd:pfam05958 178 SFTQPNAAVNIKMLEWACDVTQGSKGDL-LELYCGNGNFSLALAR------------------NFRKVLATEIAKPSVAA 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643  162 ARVNAQDNELSNVEFHCGRAEDLVPTLVSRLASQHLVAI-----------LDPPRAGLHSKVIlaiRRAKNLRRLLYVSC 230
Cdd:pfam05958 239 AQYNIAANNIDNVQIIRMSAEEFTQAMNGVREFNRLKGIdlksyncstifVDPPRAGLDPETL---KLVQAYPRILYISC 315

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768024643  231 NPRAAMGNFVDLCRapSNRVKgipfrpvKAVAVDLFPQTPHCEMLILFERV 281
Cdd:pfam05958 316 NPETLCANLEQLSK--THRVE-------RFALFDQFPYTHHMECGVLLEKK 357
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 54-179 6.09e-11

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 61.72  E-value: 6.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643  54 EGLPLEHVAGdrciHEDLLGLTFRISPHAFfqVNTPAAEVLYTVIQDWAQLDAGSMVLDVCCGTGTIGLALARgpmYSPP 133
Cdd:PRK09328  62 AGEPLQYILG----EAEFWGLDFKVSPGVL--IPRPETEELVEWALEALLLKEPLRVLDLGTGSGAIALALAK---ERPD 132

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 768024643 134 WvgrhhaflfqkvkRVIGVELCPEAVEDARVNAQDNELSNVEFHCG 179
Cdd:PRK09328 133 A-------------EVTAVDISPEALAVARRNAKHGLGARVEFLQG 165
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 110-230 9.91e-11

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: 57.83  E-value: 9.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643 110 VLDVCCGTGTIGLALARGPmysppwvgrhhaflfqkVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDLVPTLV 189
Cdd:cd02440    2 VLDLGCGTGALALALASGP-----------------GARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEAD 64

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 768024643 190 SRLAsqhlVAILDPP---RAGLHSKVILAIRRAKNLRRLLYVSC 230
Cdd:cd02440   65 ESFD----VIISDPPlhhLVEDLARFLEEARRLLKPGGVLVLTL 104
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 110-184 1.14e-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: 1.14e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768024643  110 VLDVCCGTGTIGLALARgpmysppwvgRHHAflfqkvkRVIGVELCPEAVEDARVNAQDNELsNVEFHCGRAEDL 184
Cdd:pfam13649   1 VLDLGCGTGRLTLALAR----------RGGA-------RVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDL 57
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 100-188 4.26e-10

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: 59.00  E-value: 4.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643 100 DWAQLDAGSMVLDVCCGTGTIGLALARgpmysppwvgRHHAflfqkvKRVIGVELCPEAVEDARVNAQDNELSN-VEFHC 178
Cdd:COG4123   31 AFAPVKKGGRVLDLGTGTGVIALMLAQ----------RSPG------ARITGVEIQPEAAELARRNVALNGLEDrITVIH 94

                         90
                 ....*....|
gi 768024643 179 GRAEDLVPTL 188
Cdd:COG4123   95 GDLKEFAAEL 104
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 104-231 7.34e-10

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 56.66  E-value: 7.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643  104 LDAGSMVLDVCCGTGTIGLALAR--GPMysppwvgrhhaflfqkvKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRA 181
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEelGPN-----------------AEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDI 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768024643  182 EDLvPTLVSR------LASQHLVAILDPPRA------GLHSKVILAIRRAKNLRRLLYVSCN 231
Cdd:pfam13847  64 EEL-PELLEDdkfdvvISNCVLNHIPDPDKVlqeilrVLKPGGRLIISDPDSLAELPAHVKE 124
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 89-186 8.50e-10

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 57.62  E-value: 8.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643  89 PAAEVLYTVIQDwaqLDAGSMVLDVCCGTGTIGLALARgpmysppwvgRHHAflfqkvkRVIGVELCPEAVEDARVNAQD 168
Cdd:COG0500   12 PGLAALLALLER---LPKGGRVLDLGCGTGRNLLALAA----------RFGG-------RVIGIDLSPEAIALARARAAK 71

                         90
                 ....*....|....*...
gi 768024643 169 NELSNVEFHCGRAEDLVP 186
Cdd:COG0500   72 AGLGNVEFLVADLAELDP 89
PRK05031 PRK05031
tRNA (uracil-5-)-methyltransferase; Validated
 115-280 4.64e-09

tRNA (uracil-5-)-methyltransferase; Validated


Pssm-ID: 235332  Cd Length: 362  Bit Score: 56.76  E-value: 4.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643 115 CGTGTIGLALArgpmysppwvgrhhaflfQKVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDLVPTL-----V 189
Cdd:PRK05031 215 CGNGNFTLALA------------------RNFRRVLATEISKPSVAAAQYNIAANGIDNVQIIRMSAEEFTQAMngvreF 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643 190 SRLASQHLVA-----IL-DPPRAGLHSKVIlaiRRAKNLRRLLYVSCNPRAAMGNFVDLCRapSNRVKgipfrpvKAVAV 263
Cdd:PRK05031 277 NRLKGIDLKSynfstIFvDPPRAGLDDETL---KLVQAYERILYISCNPETLCENLETLSQ--THKVE-------RFALF 344

                        170
                 ....*....|....*..
gi 768024643 264 DLFPQTPHCEMLILFER 280
Cdd:PRK05031 345 DQFPYTHHMECGVLLEK 361
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 100-184 1.14e-08

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: 53.07  E-value: 1.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643 100 DWAQLDAGSMVLDVCCGTGTIGLALARgpmysppwvgrhhaflfqKVKRVIGVELCPEAVEDARVNAQDNELsNVEFHCG 179
Cdd:COG2226   16 AALGLRPGARVLDLGCGTGRLALALAE------------------RGARVTGVDISPEMLELARERAAEAGL-NVEFVVG 76


                 ....*
gi 768024643 180 RAEDL 184
Cdd:COG2226   77 DAEDL 81
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 101-177 2.76e-08

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: 52.88  E-value: 2.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643 101 WAQLDAGSM-------------VLDVCCGTGTIGLALARgpmysppwvgrhhaflFQKVKRVIGVELCPEAVEDARVNAQ 167
Cdd:COG2813   31 RDRLDIGTRlllehlpeplggrVLDLGCGYGVIGLALAK----------------RNPEARVTLVDVNARAVELARANAA 94

                         90
                 ....*....|
gi 768024643 168 DNELSNVEFH 177
Cdd:COG2813   95 ANGLENVEVL 104
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
100-179 2.09e-07

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 50.44  E-value: 2.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643  100 DWAQLDAGSMVLDVCCGTGTIGLALARgpmysppwvgrhhafLFQKVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCG 179
Cdd:pfam01135  67 ELLELKPGMRVLEIGSGSGYLTACFAR---------------MVGEVGRVVSIEHIPELVEIARRNLEKLGLENVIVVVG 131
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
110-197 3.97e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 47.51  E-value: 3.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643 110 VLDVCCGTGTIGLALARgpmysppwvgRHHAFlfqkvkRVIGVELCPEAVEDARvnaqdNELSNVEFHCGRAEDLVPT-- 187
Cdd:COG4106    5 VLDLGCGTGRLTALLAE----------RFPGA------RVTGVDLSPEMLARAR-----ARLPNVRFVVADLRDLDPPep 63

                         90
                 ....*....|...
gi 768024643 188 ---LVSRLASQHL 197
Cdd:COG4106   64 fdlVVSNAALHWL 76
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 94-184 5.05e-07

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: 48.09  E-value: 5.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643  94 LYTVIQDWaqLDAGSMVLDVCCGTGTIGLALARgpmysppwvgrhhaflfqKVKRVIGVELCPEAVEDARVNAQDnelSN 173
Cdd:COG2227   14 LAALLARL--LPAGGRVLDVGCGTGRLALALAR------------------RGADVTGVDISPEALEIARERAAE---LN 70

                         90
                 ....*....|.
gi 768024643 174 VEFHCGRAEDL 184
Cdd:COG2227   71 VDFVQGDLEDL 81
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 102-204 4.11e-06

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: 46.10  E-value: 4.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643 102 AQLDAGSMVLDVCCGTGTIglALARGpmysppWVGRhhaflfqkvkRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRA 181
Cdd:COG1041   22 AGAKEGDTVLDPFCGTGTI--LIEAG------LLGR----------RVIGSDIDPKMVEGARENLEHYGYEDADVIRGDA 83

                         90       100
                 ....*....|....*....|....
gi 768024643 182 EDLvptlvsRLASQHL-VAILDPP 204
Cdd:COG1041   84 RDL------PLADESVdAIVTDPP 101
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 110-204 1.19e-05

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: 46.19  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643  110 VLDVCCGTGTIGLALArgpMYSPPwvgrhhaflfqkvKRVIGVELCPEAVEDARVNAQDNELS-NVEFHCGRaedlvptL 188
Cdd:TIGR00536 118 ILDLGTGSGCIALALA---YEFPN-------------AEVIAVDISPDALAVAEENAEKNQLEhRVEFIQSN-------L 174

                          90
                  ....*....|....*..
gi 768024643  189 VSRLASQHLVAIL-DPP 204
Cdd:TIGR00536 175 FEPLAGQKIDIIVsNPP 191
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 100-184 1.68e-05

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 45.33  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643  100 DWAQLDAGSMVLDVCCGTGTIGLALARgpmySPPwvgrhhaflfqKVKRVIGVELCPEAVEDARvnAQDNELSNVEFHCG 179
Cdd:TIGR01934  33 KLIGVFKGQKVLDVACGTGDLAIELAK----SAP-----------DRGKVTGVDFSSEMLEVAK--KKSELPLNIEFIQA 95


                  ....*
gi 768024643  180 RAEDL 184
Cdd:TIGR01934  96 DAEAL 100
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 89-187 1.70e-05

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 44.15  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643  89 PAAEVLYTVIQDWAQLDAGSMVLDVCCGTGTIGLALARgpmysppwvgRHHAflfqkvkRVIGVELCPEAVEDARVNAQD 168
Cdd:COG2230   34 EAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLAR----------RYGV-------RVTGVTLSPEQLEYARERAAE 96

                         90       100
                 ....*....|....*....|
gi 768024643 169 NELSN-VEFHCGRAEDLVPT 187
Cdd:COG2230   97 AGLADrVEVRLADYRDLPAD 116
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
85-184 1.72e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 44.89  E-value: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643  85 QVNTP---AAEVLYTVIqdwAQLD-AGSMVLDVCCGTGTIGLALA-RGPmysppwvgrhhaflfqkvKRVIGVELCPEAV 159
Cdd:COG2263   23 QYPTPaelAAELLHLAY---LRGDiEGKTVLDLGCGTGMLAIGAAlLGA------------------KKVVGVDIDPEAL 81

                         90       100
                 ....*....|....*....|....*
gi 768024643 160 EDARVNAqDNELSNVEFHCGRAEDL 184
Cdd:COG2263   82 EIARENA-ERLGVRVDFIRADVTRI 105
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 106-228 7.88e-05

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: 42.76  E-value: 7.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643 106 AGSMVLDVCCGTGTIGL-ALARGpmysppwvgrhhaflfqkVKRVIGVELCPEAVEDARVNAQD-NELSNVEFHCGRAED 183
Cdd:COG0742   41 EGARVLDLFAGSGALGLeALSRG------------------AASVVFVEKDRKAAAVIRKNLEKlGLEDRARVIRGDALR 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 768024643 184 LVPTLVSRlaSQHLVaILDPP-RAGLHSKVILAIRRAKNLRR--LLYV 228
Cdd:COG0742  103 FLKRLAGE--PFDLV-FLDPPyAKGLLEKALELLAENGLLAPggLIVV 147
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 53-204 1.01e-04

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: 43.63  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643  53 QEGLPLE--HVAGDRC----IHEDllGLTFRISPHA-----FF--QVNTPAAevlytvIQDWAqldAGSMVLDVCCGTGT 119
Cdd:COG1092  161 LEGLPQYegVLYGEAPeeveVEEN--GLKFLVDLTDgqktgLFldQRENRAR------VAELA---KGKRVLNLFSYTGG 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643 120 IGLALARGpmysppwvGrhhAflfqkvKRVIGVELCPEAVEDARVNAQDNELS-NVEFHCGRAEDLVPTLVSRLASQHLV 198
Cdd:COG1092  230 FSVHAAAG--------G---A------KSVTSVDLSATALEWAKENAALNGLDdRHEFVQADAFDWLRELAREGERFDLI 292


                 ....*.
gi 768024643 199 aILDPP 204
Cdd:COG1092  293 -ILDPP 297
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 100-184 1.16e-04

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 42.83  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643 100 DWAQLDAGSMVLDVCCGTGTIGLALARGpmysppwVGrhhaflfqKVKRVIGVELCPEAVEDARVNAQDNELS-NVEFHC 178
Cdd:PRK00216  45 KWLGVRPGDKVLDLACGTGDLAIALAKA-------VG--------KTGEVVGLDFSEGMLAVGREKLRDLGLSgNVEFVQ 109


                 ....*.
gi 768024643 179 GRAEDL 184
Cdd:PRK00216 110 GDAEAL 115
PRK14968 PRK14968
putative methyltransferase; Provisional
 102-176 1.29e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 42.19  E-value: 1.29e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768024643 102 AQLDAGSMVLDVCCGTGTIGLALARgpmysppwvgrhhaflfqKVKRVIGVELCPEAVEDARVNAQDNELSN--VEF 176
Cdd:PRK14968  19 AVDKKGDRVLEVGTGSGIVAIVAAK------------------NGKKVVGVDINPYAVECAKCNAKLNNIRNngVEV 77
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
101-223 2.46e-04

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 41.07  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643  101 WAQLDAGSMVLDVCCGTGTIGL-ALARGpmysppwvgrhhaflfqkVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCG 179
Cdd:pfam03602  36 LAPYIEGARVLDLFAGSGALGLeALSRG------------------AKRVTLVEKDKRAVQILKENLQLLGLPGAVLVMD 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 768024643  180 RAEDLvPTLVSRLASQHLVaILDPP-RAGLHSKVILAIRRAKNLR 223
Cdd:pfam03602  98 ALLAL-LRLAGKGPVFDIV-FLDPPyAKGLIEEVLDLLAEKGWLK 140
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
110-184 2.92e-04

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 41.14  E-value: 2.92e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768024643 110 VLDVCCGTGTIGLALArgpmysppwvgrhhaflfQKVKRVIGVELCPEAVEDARVNAQDnelsnVEFHCGRAEDL 184
Cdd:COG4976   50 VLDLGCGTGLLGEALR------------------PRGYRLTGVDLSEEMLAKAREKGVY-----DRLLVADLADL 101
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 111-184 2.92e-04

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 39.19  E-value: 2.92e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768024643  111 LDVCCGTgtiglalargpmysppwvGRHHAFLFQKVKRVIGVELCPEAVEDARVNAQDNelsNVEFHCGRAEDL 184
Cdd:pfam08241   1 LDVGCGT------------------GLLTELLARLGARVTGVDISPEMLELAREKAPRE---GLTFVVGDAEDL 53
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
107-208 5.14e-04

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 41.05  E-value: 5.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643 107 GSMVLDVCCGTG--TIGlALARGpmysppwvgrhhaflfqkVKRVIGVELCPEAVEDARVNAQDNELSN--VEFHCGRAE 182
Cdd:COG2521  133 GDRVLDTCTGLGytAIE-ALKRG------------------AREVITVEKDPNVLELAELNPWSRELANerIKIILGDAS 193

                         90       100
                 ....*....|....*....|....*..
gi 768024643 183 DLVPtlvsRLASQHLVAIL-DPPRAGL 208
Cdd:COG2521  194 EVIK----TFPDESFDAIIhDPPRFSL 216
arsM PRK11873
arsenite methyltransferase;
102-184 6.49e-04

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 40.70  E-value: 6.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643 102 AQLDAGSMVLDVCCGTGtIGLALARgpmyspPWVGrhhaflfqKVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRA 181
Cdd:PRK11873  73 AELKPGETVLDLGSGGG-FDCFLAA------RRVG--------PTGKVIGVDMTPEMLAKARANARKAGYTNVEFRLGEI 137


                 ...
gi 768024643 182 EDL 184
Cdd:PRK11873 138 EAL 140
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
107-184 6.65e-04

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 40.50  E-value: 6.65e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768024643  107 GSMVLDVCCGTGTIGLALARgpmysppwvgrhhafLFQKVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDL 184
Cdd:pfam01209  43 GNKFLDVAGGTGDWTFGLSD---------------SAGSSGKVVGLDINENMLKEGEKKAKEEGKYNIEFLQGNAEEL 105
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 101-177 7.04e-04

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


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 39.50  E-value: 7.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643  101 WAQLDAGS-------------MVLDVCCGTGTIGLALARgpmysppwvgrhhaflFQKVKRVIGVELCPEAVEDARVNAQ 167
Cdd:pfam05175  13 HGRLDIGSrlllehlpkdlsgKVLDLGCGAGVLGAALAK----------------ESPDAELTMVDINARALESARENLA 76

                          90
                  ....*....|
gi 768024643  168 DNELSNVEFH 177
Cdd:pfam05175  77 ANGLENGEVV 86
PRK08317 PRK08317
hypothetical protein; Provisional
 88-206 7.94e-04

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 40.31  E-value: 7.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643  88 TPAAEVLYTVIQDWAQLDAGSMVLDVCCGTGTIGLALARgpmysppwvgrhhafLFQKVKRVIGVELCPEAVEDARvNAQ 167
Cdd:PRK08317   1 LPDFRRYRARTFELLAVQPGDRVLDVGCGPGNDARELAR---------------RVGPEGRVVGIDRSEAMLALAK-ERA 64

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 768024643 168 DNELSNVEFHCGRAEDL------VPTLVSRLASQHlvaILDPPRA 206
Cdd:PRK08317  65 AGLGPNVEFVRGDADGLpfpdgsFDAVRSDRVLQH---LEDPARA 106
PRK14967 PRK14967
putative methyltransferase; Provisional
 104-166 1.69e-03

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 39.27  E-value: 1.69e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768024643 104 LDAGSMVLDVCCGTGTIGLALARgpmysppwvgrhhaflfQKVKRVIGVELCPEAVEDARVNA 166
Cdd:PRK14967  34 LGPGRRVLDLCTGSGALAVAAAA-----------------AGAGSVTAVDISRRAVRSARLNA 79
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
102-185 1.89e-03

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 39.39  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643 102 AQLDAGSMVLDVCCGTGtIgLALA---RGPmysppwvgrhhaflfqkvKRVIGVELCPEAVEDARVNAQDNELSN-VEFH 177
Cdd:COG2264  144 KLLKPGKTVLDVGCGSG-I-LAIAaakLGA------------------KRVLAVDIDPVAVEAARENAELNGVEDrIEVV 203

                         90
                 ....*....|...
gi 768024643 178 CGRAE-----DLV 185
Cdd:COG2264  204 LGDLLedgpyDLV 216
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 103-183 3.07e-03

Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 38.99  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643 103 QLDAGSMVLDVCCGTGTIGLALARgpmysppwvgrhhaflFQKVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAE 182
Cdd:COG2242  244 ALRPGDVLWDIGAGSGSVSIEAAR----------------LAPGGRVYAIERDPERAALIRANARRFGVPNVEVVEGEAP 307


                 .
gi 768024643 183 D 183
Cdd:COG2242  308 E 308
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 102-192 5.57e-03

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 37.47  E-value: 5.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768024643 102 AQLDAGSMVLDVCCGTGTIGLalargpmysppwvgrHHAFLFQKVKRVIGVELCPEAVEDARVNAQD-NELSNVEFHCGR 180
Cdd:PRK00377  36 LRLRKGDMILDIGCGTGSVTV---------------EASLLVGETGKVYAVDKDEKAINLTRRNAEKfGVLNNIVLIKGE 100

                         90
                 ....*....|..
gi 768024643 181 AEDLVPTLVSRL 192
Cdd:PRK00377 101 APEILFTINEKF 112
 
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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