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Conserved domains on  [gi|16765360|ref|NP_460975|]
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synthesis of vitamin B12 adenosyl cobalamide precursor [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]

Protein Classification

decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase( domain architecture ID 10793077)

decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
1-187 7.50e-134

decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;


:

Pssm-ID: 181354  Cd Length: 187  Bit Score: 372.41  E-value: 7.50e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360    1 MKDELFLRGENVPMTKEAVRALALSKLELHRASHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPAALRLLDENRQRFAC 80
Cdd:PRK08287   1 MKDELFLRGEKVPMTKEEVRALALSKLELHRAKHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKENRQRFGC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360   81 GNIDILPGEAPMTITGKADAVFMGGSGGHLTALIDWAMGHLHPGGRLVMTFILQENLHSALAHLAHIGACRMDCVQLQLS 160
Cdd:PRK08287  81 GNIDIIPGEAPIELPGKADAIFIGGSGGNLTAIIDWSLAHLHPGGRLVLTFILLENLHSALAHLEKCGVSELDCVQLQVS 160

                        170       180
                 ....*....|....*....|....*..
gi 16765360  161 SLTPLGAGHYFKPNNPVFVIACQKEEN 187
Cdd:PRK08287 161 SLTPLGAGHYFKPNNPTFIISCQKEEN 187
 
Name Accession Description Interval E-value
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
1-187 7.50e-134

decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;


Pssm-ID: 181354  Cd Length: 187  Bit Score: 372.41  E-value: 7.50e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360    1 MKDELFLRGENVPMTKEAVRALALSKLELHRASHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPAALRLLDENRQRFAC 80
Cdd:PRK08287   1 MKDELFLRGEKVPMTKEEVRALALSKLELHRAKHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKENRQRFGC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360   81 GNIDILPGEAPMTITGKADAVFMGGSGGHLTALIDWAMGHLHPGGRLVMTFILQENLHSALAHLAHIGACRMDCVQLQLS 160
Cdd:PRK08287  81 GNIDIIPGEAPIELPGKADAIFIGGSGGNLTAIIDWSLAHLHPGGRLVLTFILLENLHSALAHLEKCGVSELDCVQLQVS 160

                        170       180
                 ....*....|....*....|....*..
gi 16765360  161 SLTPLGAGHYFKPNNPVFVIACQKEEN 187
Cdd:PRK08287 161 SLTPLGAGHYFKPNNPTFIISCQKEEN 187
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 1-186 4.36e-73

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: 225.82  E-value: 4.36e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360   1 MKDELFLRGEnVPMTKEAVRALALSKLELHRASHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPAALRLLDENRQRFAC 80
Cdd:COG2242 218 LPDEAFERDK-GPITKREVRALTLAKLALRPGDVLWDIGAGSGSVSIEAARLAPGGRVYAIERDPERAALIRANARRFGV 296

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360  81 GNIDILPGEAPMTITG--KADAVFMGGSGGHLTALIDWAMGHLHPGGRLVMTFILQENLHSALAHLAHIGAcRMDCVQLQ 158
Cdd:COG2242 297 PNVEVVEGEAPEALADlpDPDAVFIGGSGGNLPEILEACWARLRPGGRLVANAVTLETLALALEALAELGY-GGELVQVQ 375

                       170       180
                ....*....|....*....|....*...
gi 16765360 159 LSSLTPLGAGHYFKPNNPVFVIACQKEE 186
Cdd:COG2242 376 VSRLKPLGGGTGFRPANPVTIISAEKPE 403
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 13-133 1.15e-54

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: 169.43  E-value: 1.15e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360    13 PMTKEAVRALALSKLELHRASHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPAALRLLDENRQRFACGNIDILPGEAPM 92
Cdd:TIGR02469   1 GMTKREVRALTLAKLRLRPGDVLWDIGAGTGSVTIEAARLVPNGRVYAIERNPEALDLIERNLRRFGVSNIVIVEGDAPE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 16765360    93 T---ITGKADAVFMGGSGGHLTALIDWAMGHLHPGGRLVMTFIL 133
Cdd:TIGR02469  81 ApeaLLPDPDAVFVGGSGGLLQEILEAVERRLRPGGRIVLNAIT 124
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 35-133 8.67e-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: 53.59  E-value: 8.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360  35 LIDVGAGTGSVSIEAAlQFPSLQVTAIERNPAALRLLDENRQRFACGNIDILPG---EAPMTITGKADAVFMGGSGGHLT 111
Cdd:cd02440   2 VLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAALLADNVEVLKGdaeELPPEADESFDVIISDPPLHHLV 80

                        90       100
                ....*....|....*....|....*.
gi 16765360 112 ----ALIDWAMGHLHPGGRLVMTFIL 133
Cdd:cd02440  81 edlaRFLEEARRLLKPGGVLVLTLVL 106
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 36-127 9.19e-08

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 48.13  E-value: 9.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360    36 IDVGAGTGSVSIEAALQFPSLQVTAIERNPAALRLLDEN---RQRFACGNIDILPGEAPMTITGKADAVFMGGSGGHLTA 112
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERlaaLGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 16765360   113 LIDW---AMGHLHPGGRL 127
Cdd:pfam08242  81 PRAVlrnIRRLLKPGGVL 98
 
Name Accession Description Interval E-value
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
1-187 7.50e-134

decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;


Pssm-ID: 181354  Cd Length: 187  Bit Score: 372.41  E-value: 7.50e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360    1 MKDELFLRGENVPMTKEAVRALALSKLELHRASHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPAALRLLDENRQRFAC 80
Cdd:PRK08287   1 MKDELFLRGEKVPMTKEEVRALALSKLELHRAKHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKENRQRFGC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360   81 GNIDILPGEAPMTITGKADAVFMGGSGGHLTALIDWAMGHLHPGGRLVMTFILQENLHSALAHLAHIGACRMDCVQLQLS 160
Cdd:PRK08287  81 GNIDIIPGEAPIELPGKADAIFIGGSGGNLTAIIDWSLAHLHPGGRLVLTFILLENLHSALAHLEKCGVSELDCVQLQVS 160

                        170       180
                 ....*....|....*....|....*..
gi 16765360  161 SLTPLGAGHYFKPNNPVFVIACQKEEN 187
Cdd:PRK08287 161 SLTPLGAGHYFKPNNPTFIISCQKEEN 187
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 1-186 4.36e-73

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: 225.82  E-value: 4.36e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360   1 MKDELFLRGEnVPMTKEAVRALALSKLELHRASHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPAALRLLDENRQRFAC 80
Cdd:COG2242 218 LPDEAFERDK-GPITKREVRALTLAKLALRPGDVLWDIGAGSGSVSIEAARLAPGGRVYAIERDPERAALIRANARRFGV 296

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360  81 GNIDILPGEAPMTITG--KADAVFMGGSGGHLTALIDWAMGHLHPGGRLVMTFILQENLHSALAHLAHIGAcRMDCVQLQ 158
Cdd:COG2242 297 PNVEVVEGEAPEALADlpDPDAVFIGGSGGNLPEILEACWARLRPGGRLVANAVTLETLALALEALAELGY-GGELVQVQ 375

                       170       180
                ....*....|....*....|....*...
gi 16765360 159 LSSLTPLGAGHYFKPNNPVFVIACQKEE 186
Cdd:COG2242 376 VSRLKPLGGGTGFRPANPVTIISAEKPE 403
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 13-133 1.15e-54

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: 169.43  E-value: 1.15e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360    13 PMTKEAVRALALSKLELHRASHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPAALRLLDENRQRFACGNIDILPGEAPM 92
Cdd:TIGR02469   1 GMTKREVRALTLAKLRLRPGDVLWDIGAGTGSVTIEAARLVPNGRVYAIERNPEALDLIERNLRRFGVSNIVIVEGDAPE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 16765360    93 T---ITGKADAVFMGGSGGHLTALIDWAMGHLHPGGRLVMTFIL 133
Cdd:TIGR02469  81 ApeaLLPDPDAVFVGGSGGLLQEILEAVERRLRPGGRIVLNAIT 124
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 3-185 6.84e-41

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 137.24  E-value: 6.84e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360    3 DELFLRGENVPMTKEAVRALALSKLELHRASHLIDVGAGTGSVSIEAALQF-PSLQVTAIERNPAALRLLDENRQRFACG 81
Cdd:PRK00377  12 DEEFERDEEIPMTKEEIRALALSKLRLRKGDMILDIGCGTGSVTVEASLLVgETGKVYAVDKDEKAINLTRRNAEKFGVL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360   82 -NIDILPGEAP---MTITGKADAVFMGGSGGHLTALIDWAMGHLHPGGRLVMTFILQENLHSALAHLAHIGAcRMDCVQL 157
Cdd:PRK00377  92 nNIVLIKGEAPeilFTINEKFDRIFIGGGSEKLKEIISASWEIIKKGGRIVIDAILLETVNNALSALENIGF-NLEITEV 170

                        170       180
                 ....*....|....*....|....*...
gi 16765360  158 QLSSLTPLGAGHYFKPNNPVFVIACQKE 185
Cdd:PRK00377 171 IIAKGMKTKVGTAMMTRNPIFIISGEKQ 198
PRK07402 PRK07402
precorrin-6Y C5,15-methyltransferase subunit CbiT;
3-184 1.96e-31

precorrin-6Y C5,15-methyltransferase subunit CbiT;


Pssm-ID: 180961  Cd Length: 196  Bit Score: 112.78  E-value: 1.96e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360    3 DELFLRGENVPMTKEAVRALALSKLELHRASHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPAALRLLDENRQRFACGN 82
Cdd:PRK07402  12 DELFERLPGIPLTKREVRLLLISQLRLEPDSVLWDIGAGTGTIPVEAGLLCPKGRVIAIERDEEVVNLIRRNCDRFGVKN 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360   83 IDILPGEAP---MTITGKADAVFMGGsGGHLTALIDWAMGHLHPGGRLVMTFILQENLHSALAHLAHIGACRMDCVQLQL 159
Cdd:PRK07402  92 VEVIEGSAPeclAQLAPAPDRVCIEG-GRPIKEILQAVWQYLKPGGRLVATASSLEGLYAISEGLAQLQARNIEVVQAAV 170

                        170       180
                 ....*....|....*....|....*
gi 16765360  160 SSLTPLGAGHYFKPNNPVFVIACQK 184
Cdd:PRK07402 171 NRLETRGFSQVFAAVDPIFILSGEK 195
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 20-129 9.52e-12

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: 60.97  E-value: 9.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360  20 RALaLSKLELHRASHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPAALRLLDENRQRFACGNIDILPGEAPMTI-TGKA 98
Cdd:COG2813  39 RLL-LEHLPEPLGGRVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAANGLENVEVLWSDGLSGVpDGSF 117

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 16765360  99 DAVFM------GGSGG-HLT-ALIDWAMGHLHPGGRLVM 129
Cdd:COG2813 118 DLILSnppfhaGRAVDkEVAhALIADAARHLRPGGELWL 156
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
31-131 3.72e-11

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 57.14  E-value: 3.72e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360  31 RASHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPAALRLLdenRQRFAcgNIDILPGEAP-MTITGKADAVFMGGSGGH 109
Cdd:COG4106   1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARA---RARLP--NVRFVVADLRdLDPPEPFDLVVSNAALHW 75

                        90       100
                ....*....|....*....|....*
gi 16765360 110 LT---ALIDWAMGHLHPGGRLVMTF 131
Cdd:COG4106  76 LPdhaALLARLAAALAPGGVLAVQV 100
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 35-133 8.67e-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: 53.59  E-value: 8.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360  35 LIDVGAGTGSVSIEAAlQFPSLQVTAIERNPAALRLLDENRQRFACGNIDILPG---EAPMTITGKADAVFMGGSGGHLT 111
Cdd:cd02440   2 VLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAALLADNVEVLKGdaeELPPEADESFDVIISDPPLHHLV 80

                        90       100
                ....*....|....*....|....*.
gi 16765360 112 ----ALIDWAMGHLHPGGRLVMTFIL 133
Cdd:cd02440  81 edlaRFLEEARRLLKPGGVLVLTLVL 106
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 29-132 1.29e-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: 1.29e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360  29 LHRASHLIDVGAGTGSVSIEAALQFpsLQVTAIERNPAAL----RLLDENRQRFACGNIDILPGEApmtitGKADAVFMG 104
Cdd:COG2227  22 LPAGGRVLDVGCGTGRLALALARRG--ADVTGVDISPEALeiarERAAELNVDFVQGDLEDLPLED-----GSFDLVICS 94

                        90       100       110
                ....*....|....*....|....*....|.
gi 16765360 105 GSGGHLT---ALIDWAMGHLHPGGRLVMTFI 132
Cdd:COG2227  95 EVLEHLPdpaALLRELARLLKPGGLLLLSTP 125
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 22-129 2.17e-09

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 55.16  E-value: 2.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360  22 LALSKLELHRASHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPAALRLLDENRQRFACGN-IDILPGE--APMTITGKA 98
Cdd:COG2890 103 LALALLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLGLEDrVRFLQGDlfEPLPGDGRF 182

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16765360  99 D----------------------------AVFmGGSGG--HLTALIDWAMGHLHPGGRLVM 129
Cdd:COG2890 183 DlivsnppyipedeiallppevrdheprlALD-GGEDGldFYRRIIAQAPRLLKPGGWLLL 242
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 19-148 5.94e-09

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: 52.30  E-value: 5.94e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360  19 VRALALSKLELHRASHLIDVGAGTGSVSIEAALQfpSLQVTAIERNPAALRLLDENRQ------RFACGNIDILPGEApm 92
Cdd:COG2226  10 GREALLAALGLRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAeaglnvEFVVGDAEDLPFPD-- 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360  93 titGKADAVFMGGSGGHLTALiDWAMGHLH----PGGRLVMTFILQENLHSALAHLAHIG 148
Cdd:COG2226  86 ---GSFDLVISSFVLHHLPDP-ERALAEIArvlkPGGRLVVVDFSPPDLAELEELLAEAG 141
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 17-131 9.13e-08

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 49.54  E-value: 9.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360  17 EAVRALALSKLELHRASHLIDVGAGTGSVSIEAALQFpSLQVTAIERNPAALRLLDENRQRFAC-GNIDILPGEA-PMTI 94
Cdd:COG2230  37 EAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAEAGLaDRVEVRLADYrDLPA 115

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 16765360  95 TGKADAVFMGGSGGHL-----TALIDWAMGHLHPGGRLVMTF 131
Cdd:COG2230 116 DGQFDAIVSIGMFEHVgpenyPAYFAKVARLLKPGGRLLLHT 157
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 36-127 9.19e-08

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 48.13  E-value: 9.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360    36 IDVGAGTGSVSIEAALQFPSLQVTAIERNPAALRLLDEN---RQRFACGNIDILPGEAPMTITGKADAVFMGGSGGHLTA 112
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERlaaLGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 16765360   113 LIDW---AMGHLHPGGRL 127
Cdd:pfam08242  81 PRAVlrnIRRLLKPGGVL 98
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 22-88 1.34e-07

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 50.16  E-value: 1.34e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16765360   22 LALSKLELHRASHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPAALRLLDENRQRFACGNIDILPG 88
Cdd:PRK09328  99 WALEALLLKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGLGARVEFLQG 165
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 37-125 3.50e-07

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 46.40  E-value: 3.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360    37 DVGAGTGSVSIEAALQFPSlQVTAIERNPAALRLLDEN------RQRFACGNIDILPGEApmtitGKADAVFMGGSGGHL 110
Cdd:pfam13649   3 DLGCGTGRLTLALARRGGA-RVTGVDLSPEMLERARERaaeaglNVEFVQGDAEDLPFPD-----GSFDLVVSSGVLHHL 76

                          90       100
                  ....*....|....*....|
gi 16765360   111 T-----ALIDWAMGHLHPGG 125
Cdd:pfam13649  77 PdpdleAALREIARVLKPGG 96
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 12-70 1.27e-06

Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal structure and biogenesis]; Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) is part of the Pathway/BioSystem: Archaeal ribosomal proteins


Pssm-ID: 444210 [Multi-domain]  Cd Length: 306  Bit Score: 47.26  E-value: 1.27e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16765360  12 VPMTKEAVRAlALSKLELHRAS----HLIDVGAGTGSVSIEAALQFPSL-QVTAIERNPAALRL 70
Cdd:COG5459  58 LPATYAAVRA-ALAELAEAGPDfaplTVLDVGAGPGTAAWAAADAWPSLlDATLLERSAAALAL 120
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 13-82 1.29e-06

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: 47.35  E-value: 1.29e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360    13 PMTKEAVRALALSKLELHRASHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPAALRLLDENRQRFACGN 82
Cdd:TIGR00536  96 PETEELVEKALASLISQPPILHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQLEH 165
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 21-127 1.47e-06

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: 46.04  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360    21 ALALSKLELHRASHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPAALRLLDENRQRFACGNIDILPGEAPMTIT-GKAD 99
Cdd:pfam05175  21 RLLLEHLPKDLSGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGLENGEVVASDVYSGVEdGKFD 100

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 16765360   100 AVFMG---GSGGHLTALIDWAM-----GHLHPGGRL 127
Cdd:pfam05175 101 LIISNppfHAGLATTYNVAQRFiadakRHLRPGGEL 136
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
17-150 2.06e-06

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 46.14  E-value: 2.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360  17 EAVRALALSKLELHRASHLIDVGAGTGSVSieAALQFPSLQVTAIERNPAALRLLDENR--QRFACGNIDILPGEApmti 94
Cdd:COG4976  32 ALLAEELLARLPPGPFGRVLDLGCGTGLLG--EALRPRGYRLTGVDLSEEMLAKAREKGvyDRLLVADLADLAEPD---- 105

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16765360  95 tGKADAVFMGGS---GGHLTALIDWAMGHLHPGGRLVMTFILQENLHSALAHLAHIGAC 150
Cdd:COG4976 106 -GRFDLIVAADVltyLGDLAAVFAGVARALKPGGLFIFSVEDADGSGRYAHSLDYVRDL 163
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 28-129 2.28e-06

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 46.29  E-value: 2.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360  28 ELHRASHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPAALRLLDENRQ--------RFACGNIDILPGEAPmtiTGKAD 99
Cdd:COG4123  34 PVKKGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVAlngledriTVIHGDLKEFAAELP---PGSFD 110

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 16765360 100 AV------FMGGSG--------------GHLT--ALIDWAMGHLHPGGRLVM 129
Cdd:COG4123 111 LVvsnppyFKAGSGrkspdearaiarheDALTleDLIRAAARLLKPGGRFAL 162
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 36-96 3.12e-06

methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.


Pssm-ID: 273628  Cd Length: 143  Bit Score: 44.99  E-value: 3.12e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16765360    36 IDVGAGTGSVSIEAALQFPSLQVTAIERNPAALRLLDENRQRFACGNIDILP-------GEAPMTITG 96
Cdd:TIGR01444   3 IDVGANIGDTSLYFARKGAEGRVIAFEPLPDAYEILEENVKLNNLPNVVLLNaavgdrdGELEFNVSD 70
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 21-145 3.95e-06

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 45.29  E-value: 3.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360  21 ALALSKLELHRASHLIDVGAGTGSVSIEAALQFPSlQVTAIERNPAALRLLDENRQRFACGNIDIL------PGEAPmti 94
Cdd:COG0500  16 ALLALLERLPKGGRVLDLGCGTGRNLLALAARFGG-RVIGIDLSPEAIALARARAAKAGLGNVEFLvadlaeLDPLP--- 91

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16765360  95 TGKADAVFMGGSGGHL-----TALIDWAMGHLHPGGRLVMT--FILQENLHSALAHLA 145
Cdd:COG0500  92 AESFDLVVAFGVLHHLppeerEALLRELARALKPGGVLLLSasDAAAALSLARLLLLA 149
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 40-129 9.71e-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: 43.92  E-value: 9.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360  40 AGTGSVSIEAAlqfpS---LQVTAIERNPAALRLLDENRQRF-ACGNIDILPGEA----PMTITGKADAVFMG-----GS 106
Cdd:COG0742  50 AGSGALGLEAL----SrgaASVVFVEKDRKAAAVIRKNLEKLgLEDRARVIRGDAlrflKRLAGEPFDLVFLDppyakGL 125

                        90       100
                ....*....|....*....|...
gi 16765360 107 GGHLTALIDWAmGHLHPGGRLVM 129
Cdd:COG0742 126 LEKALELLAEN-GLLAPGGLIVV 147
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 36-145 2.08e-05

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: 43.79  E-value: 2.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360    36 IDVGAGTGSVSIeAALQFPSLQVTAIERNPAALRLLDENRQRFACGNID--ILPGEAPmtiTGKADAVFMGGSGGHLTAL 113
Cdd:pfam06325 166 LDVGCGSGILAI-AALKLGAKKVVGVDIDPVAVRAAKENAELNGVEARLevYLPGDLP---KEKADVVVANILADPLIEL 241

                          90       100       110
                  ....*....|....*....|....*....|..
gi 16765360   114 IDWAMGHLHPGGRLVMTFILQENLHSALAHLA 145
Cdd:pfam06325 242 APDIYALVKPGGYLILSGILKEQAQMVAEAYS 273
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
28-82 4.07e-05

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 42.23  E-value: 4.07e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 16765360    28 ELHRAsHLIDVGAGTGSVSIEAAlqfpS---LQVTAIERNPAALRLLDENRQRFACGN 82
Cdd:pfam03602  39 YIEGA-RVLDLFAGSGALGLEAL----SrgaKRVTLVEKDKRAVQILKENLQLLGLPG 91
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 40-127 8.00e-05

tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442010 [Multi-domain]  Cd Length: 333  Bit Score: 42.16  E-value: 8.00e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360  40 AGTGSVSIEAALQFPSlQVTAIERNPAALRLLDEN--RQRFAcGNIDILPG---EAPMTITGKADAVFMG---GSGGHLt 111
Cdd:COG2520 189 AGVGPFSIPIAKRSGA-KVVAIDINPDAVEYLKENirLNKVE-DRVTPILGdarEVAPELEGKADRIIMNlphSADEFL- 265

                        90
                ....*....|....*.
gi 16765360 112 aliDWAMGHLHPGGRL 127
Cdd:COG2520 266 ---DAALRALKPGGVI 278
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 29-125 2.15e-04

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: 40.17  E-value: 2.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360  29 LHRASHLIDVGAGTG--SVSIEAALQfPSLQVTAIERNPAALRLLDENRQRFACGN-IDILPGEA----PMTITGKADAV 101
Cdd:COG4122  14 LLGAKRILEIGTGTGysTLWLARALP-DDGRLTTIEIDPERAAIARENFARAGLADrIRLILGDAlevlPRLADGPFDLV 92

                        90       100
                ....*....|....*....|....
gi 16765360 102 FMGGSGGHLTALIDWAMGHLHPGG 125
Cdd:COG4122  93 FIDADKSNYPDYLELALPLLRPGG 116
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
36-103 4.93e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 39.50  E-value: 4.93e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16765360  36 IDVGAGTGSVSIEAALQFPSlQVTAIERNPAALRLLDENRQRFACgNIDILPGEAP-MTITGKADAVFM 103
Cdd:COG2263  50 LDLGCGTGMLAIGAALLGAK-KVVGVDIDPEALEIARENAERLGV-RVDFIRADVTrIPLGGSVDTVVM 116
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 29-130 4.98e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 38.94  E-value: 4.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360    29 LHRASHLIDVGAGTGSVSIEAA-LQFPSLQVTAIERNPAALRLLDENRQRFACGNI-----DILpgEAPMTIT-GKADAV 101
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAeELGPNAEVVGIDISEEAIEKARENAQKLGFDNVefeqgDIE--ELPELLEdDKFDVV 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 16765360   102 FMGGSGGHLTALIDwAMGH----LHPGGRLVMT 130
Cdd:pfam13847  79 ISNCVLNHIPDPDK-VLQEilrvLKPGGRLIIS 110
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 36-129 5.12e-04

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 37.64  E-value: 5.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360    36 IDVGAGTGSVSIEAALQFPslQVTAIERNPAALRLLDENRQR----FACGNIDILPGEApmtitGKADAVFMGGSGGHLT 111
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMLELAREKAPRegltFVVGDAEDLPFPD-----NSFDLVLSSEVLHHVE 73

                          90       100
                  ....*....|....*....|.
gi 16765360   112 ---ALIDWAMGHLHPGGRLVM 129
Cdd:pfam08241  74 dpeRALREIARVLKPGGILII 94
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 22-137 6.39e-04

HemK-related putative methylase; 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. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 38.68  E-value: 6.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360    22 LALSKLELHRASHLIDVGAGTGSVSIEAALQfpSLQVTAIERNPAALRLLDENrQRFACGNIDILPGEAPMTITGKADAV 101
Cdd:TIGR00537  10 LLEANLRELKPDDVLEIGAGTGLVAIRLKGK--GKCILTTDINPFAVKELREN-AKLNNVGLDVVMTDLFKGVRGKFDVI 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360   102 ----------------------FMGGSGGH--LTALIDWAMGHLHPGGRLVmtfILQENL 137
Cdd:TIGR00537  87 lfnppylpleddlrrgdwldvaIDGGKDGRkvIDRFLDELPEILKEGGRVQ---LIQSSL 143
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
21-129 9.95e-04

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 38.50  E-value: 9.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360    21 ALALSKLELHRASHLIDVGAGTG-SVSIEAALQFPSLQVTAIERNPAALRLLDENRQRFACGNIDILPGEAPMTITGKA- 98
Cdd:pfam01135  63 AMMLELLELKPGMRVLEIGSGSGyLTACFARMVGEVGRVVSIEHIPELVEIARRNLEKLGLENVIVVVGDGRQGWPEFAp 142

                          90       100       110
                  ....*....|....*....|....*....|...
gi 16765360    99 -DAVFMGGSGGHL-TALIDwamgHLHPGGRLVM 129
Cdd:pfam01135 143 yDAIHVGAAAPEIpEALID----QLKEGGRLVI 171
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
22-127 1.25e-03

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


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 38.77  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360   22 LALSKLELHRASHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPAAL----RLLDENRQRfacGniDILPGEAPMTITGK 97
Cdd:PRK09489 187 LLLSTLTPHTKGKVLDVGCGAGVLSAVLARHSPKIRLTLSDVSAAALessrATLAANGLE---G--EVFASNVFSDIKGR 261

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 16765360   98 ADAV-----FMGGSGGHLTA---LIDWAMGHLHPGGRL 127
Cdd:PRK09489 262 FDMIisnppFHDGIQTSLDAaqtLIRGAVRHLNSGGEL 299
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 21-129 1.65e-03

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 37.76  E-value: 1.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360  21 ALALSKLELHRASHLIDVGAGTG-SVSIEAALqfpSLQVTAIERNPAalrLLDENRQRFA---CGNIDI--------LPG 88
Cdd:COG2518  56 ARMLEALDLKPGDRVLEIGTGSGyQAAVLARL---AGRVYSVERDPE---LAERARERLAalgYDNVTVrvgdgalgWPE 129

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 16765360  89 EAPmtitgkADAVFMGGSGGHL-TALIDWamghLHPGGRLVM 129
Cdd:COG2518 130 HAP------FDRIIVTAAAPEVpEALLEQ----LAPGGRLVA 161
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
16-90 2.60e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 37.32  E-value: 2.60e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16765360  16 KEAVRALALSKlelhraSHLIDVGAGTGSVSIEAALQFPSlQVTAIERNPAALRLLDENRQRFACG-NIDILPGEA 90
Cdd:COG4076  26 KAAIERVVKPG------DVVLDIGTGSGLLSMLAARAGAK-KVYAVEVNPDIAAVARRIIAANGLSdRITVINADA 94
GidB pfam02527
rRNA small subunit methyltransferase G; This is a family of bacterial glucose inhibited ...
 33-128 5.55e-03

rRNA small subunit methyltransferase G; This is a family of bacterial glucose inhibited division proteins these are probably involved in the regulation of cell devision. GidB has been shown to be a methyltransferase G specific to the rRNA small subunit. Previously identified as a glucose-inhibited division protein B that appears to be present and in a single copy in all complete eubacterial genomes so far sequenced. GidB specifically methylates the N7 position of a guanosine in 16S rRNA.


Pssm-ID: 396880  Cd Length: 184  Bit Score: 36.10  E-value: 5.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360    33 SHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPAALRLLDENRQRFACGNIDILPGEA-PMTITGKADAV----Fmggsg 107
Cdd:pfam02527  50 DHVLDVGSGAGFPGIPLAIARPDKKVTLLESLLKKINFLEEVKSELGLDNVTIVHARAeEYQPEEQYDVItsraV----- 124

                          90       100
                  ....*....|....*....|.
gi 16765360   108 GHLTALIDWAMGHLHPGGRLV 128
Cdd:pfam02527 125 ASLNELTEWTLPLLKPGGYFL 145
TIGR00095 TIGR00095
16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of ...
 33-82 5.67e-03

16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of uncharacterized bacterial proteins. Members are present in nearly every complete bacterial genome, always in a single copy. PSI-BLAST analysis shows homology to several families of SAM-dependent methyltransferases, including ribosomal RNA adenine dimethylases. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 188022 [Multi-domain]  Cd Length: 190  Bit Score: 36.23  E-value: 5.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 16765360    33 SHLIDVGAGTGSVSIEaALQFPSLQVTAIERNPAALRLLDENRQRFACGN 82
Cdd:TIGR00095  52 AHFLDLFAGSGALGLE-ALSRGAASAVFVEQDRKVAQTLKENLSTLKKSG 100
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 35-128 6.56e-03

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 35.87  E-value: 6.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765360    35 LIDVGAGTGSVSIEAALQFPSlqVTAIERNPAALRLLDENRQRFACGNIDILPGEapmtitGKADAVFMGGSGGHL---T 111
Cdd:pfam13489  26 VLDFGCGTGIFLRLLRAQGFS--VTGVDPSPIAIERALLNVRFDQFDEQEAAVPA------GKFDVIVAREVLEHVpdpP 97

                          90
                  ....*....|....*..
gi 16765360   112 ALIDWAMGHLHPGGRLV 128
Cdd:pfam13489  98 ALLRQIAALLKPGGLLL 114
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
27-90 7.55e-03

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 36.03  E-value: 7.55e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16765360   27 LELHRASHLIDVGAGTGSVSIEAALQfpSLQVTAIERNPaalRLLDENRQRFAC-GNIDILPGEA 90
Cdd:PRK14896  25 AEDTDGDPVLEIGPGKGALTDELAKR--AKKVYAIELDP---RLAEFLRDDEIAaGNVEIIEGDA 84
PRK14968 PRK14968
putative methyltransferase; Provisional
 36-85 7.87e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 35.64  E-value: 7.87e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 16765360   36 IDVGAGTGSVSIEAALQfpSLQVTAIERNPAALRLLDENRQRFACGNIDI 85
Cdd:PRK14968  28 LEVGTGSGIVAIVAAKN--GKKVVGVDINPYAVECAKCNAKLNNIRNNGV 75
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 34-101 9.30e-03

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 33.72  E-value: 9.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16765360    34 HLIDVGAGTgsVSIEAALQFPSL--QVTAIERNPAALRLLDEN-----RQRFACGNIDILPGEAPMTITGKADAV 101
Cdd:pfam00070   1 RVVVVGGGY--IGLELAGALARLgsKVTVVERRDRLLPGFDPEiakilQEKLEKNGIEFLLNTTVEAIEGNGDGV 73
 
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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