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Conserved domains on  [gi|489005083|ref|WP_002915684|]
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MULTISPECIES: decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase [Klebsiella]

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 3.58e-129

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


:

Pssm-ID: 181354  Cd Length: 187  Bit Score: 360.47  E-value: 3.58e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083   1 MKDELFLRGAQVPMTKEAVRALALAKLELHRARHLIDIGAGTGSVSIEAALQNPALRVTAIERQADALRLLAENRQRFGC 80
Cdd:PRK08287   1 MKDELFLRGEKVPMTKEEVRALALSKLELHRAKHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKENRQRFGC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083  81 DNIAIVAGVAPLAVADKADAIFMGGSGGHLTALIDWSLAQLHPGGRLVMTFILQENLHSALAHLRQSGIHEVDCQQLAVS 160
Cdd:PRK08287  81 GNIDIIPGEAPIELPGKADAIFIGGSGGNLTAIIDWSLAHLHPGGRLVLTFILLENLHSALAHLEKCGVSELDCVQLQVS 160

                        170       180
                 ....*....|....*....|....*..
gi 489005083 161 TLATLGSGHYFKPHNPVFVIACQKEEN 187
Cdd:PRK08287 161 SLTPLGAGHYFKPNNPTFIISCQKEEN 187
 
Name Accession Description Interval E-value
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
1-187 3.58e-129

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


Pssm-ID: 181354  Cd Length: 187  Bit Score: 360.47  E-value: 3.58e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083   1 MKDELFLRGAQVPMTKEAVRALALAKLELHRARHLIDIGAGTGSVSIEAALQNPALRVTAIERQADALRLLAENRQRFGC 80
Cdd:PRK08287   1 MKDELFLRGEKVPMTKEEVRALALSKLELHRAKHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKENRQRFGC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083  81 DNIAIVAGVAPLAVADKADAIFMGGSGGHLTALIDWSLAQLHPGGRLVMTFILQENLHSALAHLRQSGIHEVDCQQLAVS 160
Cdd:PRK08287  81 GNIDIIPGEAPIELPGKADAIFIGGSGGNLTAIIDWSLAHLHPGGRLVLTFILLENLHSALAHLEKCGVSELDCVQLQVS 160

                        170       180
                 ....*....|....*....|....*..
gi 489005083 161 TLATLGSGHYFKPHNPVFVIACQKEEN 187
Cdd:PRK08287 161 SLTPLGAGHYFKPNNPTFIISCQKEEN 187
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 1-186 4.33e-70

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: 218.11  E-value: 4.33e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083   1 MKDELFLRGaQVPMTKEAVRALALAKLELHRARHLIDIGAGTGSVSIEAALQNPALRVTAIERQADALRLLAENRQRFGC 80
Cdd:COG2242  218 LPDEAFERD-KGPITKREVRALTLAKLALRPGDVLWDIGAGSGSVSIEAARLAPGGRVYAIERDPERAALIRANARRFGV 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083  81 DNIAIVAGVAPLAVAD--KADAIFMGGSGGHLTALIDWSLAQLHPGGRLVMTFILQENLHSALAHLRQSGIhEVDCQQLA 158
Cdd:COG2242  297 PNVEVVEGEAPEALADlpDPDAVFIGGSGGNLPEILEACWARLRPGGRLVANAVTLETLALALEALAELGY-GGELVQVQ 375

                        170       180
                 ....*....|....*....|....*...
gi 489005083 159 VSTLATLGSGHYFKPHNPVFVIACQKEE 186
Cdd:COG2242  376 VSRLKPLGGGTGFRPANPVTIISAEKPE 403
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 13-133 1.55e-49

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: 156.34  E-value: 1.55e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083   13 PMTKEAVRALALAKLELHRARHLIDIGAGTGSVSIEAALQNPALRVTAIERQADALRLLAENRQRFGCDNIAIVAGVAPL 92
Cdd:TIGR02469   1 GMTKREVRALTLAKLRLRPGDVLWDIGAGTGSVTIEAARLVPNGRVYAIERNPEALDLIERNLRRFGVSNIVIVEGDAPE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 489005083   93 AV---ADKADAIFMGGSGGHLTALIDWSLAQLHPGGRLVMTFIL 133
Cdd:TIGR02469  81 APealLPDPDAVFVGGSGGLLQEILEAVERRLRPGGRIVLNAIT 124
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
21-129 2.79e-09

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 54.30  E-value: 2.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083   21 ALALAKLELHRARHLIDIGAGTG-SVSIEAALQNPALRVTAIERQADALRLLAENRQRFGCDNIAIVAGVAPLAVADKA- 98
Cdd:pfam01135  63 AMMLELLELKPGMRVLEIGSGSGyLTACFARMVGEVGRVVSIEHIPELVEIARRNLEKLGLENVIVVVGDGRQGWPEFAp 142

                          90       100       110
                  ....*....|....*....|....*....|...
gi 489005083   99 -DAIFMGGSGGHL-TALIDwslaQLHPGGRLVM 129
Cdd:pfam01135 143 yDAIHVGAAAPEIpEALID----QLKEGGRLVI 171
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 35-133 6.97e-08

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 48.58  E-value: 6.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083  35 LIDIGAGTGSVSIEAAlQNPALRVTAIERQADALRLLAENRQRFGCDNIAIVAG---VAPLAVADKADAIFMGGSGGHLT 111
Cdd:cd02440    2 VLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAALLADNVEVLKGdaeELPPEADESFDVIISDPPLHHLV 80

                         90       100
                 ....*....|....*....|....*.
gi 489005083 112 ALIDWSLAQLH----PGGRLVMTFIL 133
Cdd:cd02440   81 EDLARFLEEARrllkPGGVLVLTLVL 106
 
Name Accession Description Interval E-value
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
1-187 3.58e-129

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


Pssm-ID: 181354  Cd Length: 187  Bit Score: 360.47  E-value: 3.58e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083   1 MKDELFLRGAQVPMTKEAVRALALAKLELHRARHLIDIGAGTGSVSIEAALQNPALRVTAIERQADALRLLAENRQRFGC 80
Cdd:PRK08287   1 MKDELFLRGEKVPMTKEEVRALALSKLELHRAKHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKENRQRFGC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083  81 DNIAIVAGVAPLAVADKADAIFMGGSGGHLTALIDWSLAQLHPGGRLVMTFILQENLHSALAHLRQSGIHEVDCQQLAVS 160
Cdd:PRK08287  81 GNIDIIPGEAPIELPGKADAIFIGGSGGNLTAIIDWSLAHLHPGGRLVLTFILLENLHSALAHLEKCGVSELDCVQLQVS 160

                        170       180
                 ....*....|....*....|....*..
gi 489005083 161 TLATLGSGHYFKPHNPVFVIACQKEEN 187
Cdd:PRK08287 161 SLTPLGAGHYFKPNNPTFIISCQKEEN 187
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 1-186 4.33e-70

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: 218.11  E-value: 4.33e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083   1 MKDELFLRGaQVPMTKEAVRALALAKLELHRARHLIDIGAGTGSVSIEAALQNPALRVTAIERQADALRLLAENRQRFGC 80
Cdd:COG2242  218 LPDEAFERD-KGPITKREVRALTLAKLALRPGDVLWDIGAGSGSVSIEAARLAPGGRVYAIERDPERAALIRANARRFGV 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083  81 DNIAIVAGVAPLAVAD--KADAIFMGGSGGHLTALIDWSLAQLHPGGRLVMTFILQENLHSALAHLRQSGIhEVDCQQLA 158
Cdd:COG2242  297 PNVEVVEGEAPEALADlpDPDAVFIGGSGGNLPEILEACWARLRPGGRLVANAVTLETLALALEALAELGY-GGELVQVQ 375

                        170       180
                 ....*....|....*....|....*...
gi 489005083 159 VSTLATLGSGHYFKPHNPVFVIACQKEE 186
Cdd:COG2242  376 VSRLKPLGGGTGFRPANPVTIISAEKPE 403
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 13-133 1.55e-49

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: 156.34  E-value: 1.55e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083   13 PMTKEAVRALALAKLELHRARHLIDIGAGTGSVSIEAALQNPALRVTAIERQADALRLLAENRQRFGCDNIAIVAGVAPL 92
Cdd:TIGR02469   1 GMTKREVRALTLAKLRLRPGDVLWDIGAGTGSVTIEAARLVPNGRVYAIERNPEALDLIERNLRRFGVSNIVIVEGDAPE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 489005083   93 AV---ADKADAIFMGGSGGHLTALIDWSLAQLHPGGRLVMTFIL 133
Cdd:TIGR02469  81 APealLPDPDAVFVGGSGGLLQEILEAVERRLRPGGRIVLNAIT 124
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 3-185 6.88e-41

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 136.85  E-value: 6.88e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083   3 DELFLRGAQVPMTKEAVRALALAKLELHRARHLIDIGAGTGSVSIEAAL-QNPALRVTAIERQADALRLLAENRQRFGC- 80
Cdd:PRK00377  12 DEEFERDEEIPMTKEEIRALALSKLRLRKGDMILDIGCGTGSVTVEASLlVGETGKVYAVDKDEKAINLTRRNAEKFGVl 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083  81 DNIAIVAGVAPLAVA---DKADAIFMGGSGGHLTALIDWSLAQLHPGGRLVMTFILQENLHSALAHLRQSGIhEVDCQQL 157
Cdd:PRK00377  92 NNIVLIKGEAPEILFtinEKFDRIFIGGGSEKLKEIISASWEIIKKGGRIVIDAILLETVNNALSALENIGF-NLEITEV 170

                        170       180
                 ....*....|....*....|....*...
gi 489005083 158 AVSTLATLGSGHYFKPHNPVFVIACQKE 185
Cdd:PRK00377 171 IIAKGMKTKVGTAMMTRNPIFIISGEKQ 198
PRK07402 PRK07402
precorrin-6Y C5,15-methyltransferase subunit CbiT;
3-184 2.38e-31

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


Pssm-ID: 180961  Cd Length: 196  Bit Score: 112.40  E-value: 2.38e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083   3 DELFLRGAQVPMTKEAVRALALAKLELHRARHLIDIGAGTGSVSIEAALQNPALRVTAIERQADALRLLAENRQRFGCDN 82
Cdd:PRK07402  12 DELFERLPGIPLTKREVRLLLISQLRLEPDSVLWDIGAGTGTIPVEAGLLCPKGRVIAIERDEEVVNLIRRNCDRFGVKN 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083  83 IAIVAGVAP--LA-VADKADAIFMGGsGGHLTALIDWSLAQLHPGGRLVMTFILQENLHSALAHLRQSGIHEVDCQQLAV 159
Cdd:PRK07402  92 VEVIEGSAPecLAqLAPAPDRVCIEG-GRPIKEILQAVWQYLKPGGRLVATASSLEGLYAISEGLAQLQARNIEVVQAAV 170

                        170       180
                 ....*....|....*....|....*
gi 489005083 160 STLATLGSGHYFKPHNPVFVIACQK 184
Cdd:PRK07402 171 NRLETRGFSQVFAAVDPIFILSGEK 195
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 20-129 8.08e-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: 8.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083  20 RALaLAKLELHRARHLIDIGAGTGSVSIEAALQNPALRVTAIERQADALRLLAENRQRFGCDNIAIVAGVAPLAVAD-KA 98
Cdd:COG2813   39 RLL-LEHLPEPLGGRVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAANGLENVEVLWSDGLSGVPDgSF 117

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489005083  99 DAIFM------GGSGGH--LTALIDWSLAQLHPGGRLVM 129
Cdd:COG2813  118 DLILSnppfhaGRAVDKevAHALIADAARHLRPGGELWL 156
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 19-148 1.37e-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: 53.84  E-value: 1.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083  19 VRALALAKLELHRARHLIDIGAGTGSVSIEAALQNpaLRVTAIERQADALRLLAENRQRFGCDNIAIVAGVAPLAVADKA 98
Cdd:COG2226   10 GREALLAALGLRPGARVLDLGCGTGRLALALAERG--ARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFPDGS 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489005083  99 -DAIFMGGSGGHLTALiDWSLAQLH----PGGRLVMTFILQENLHSALAHLRQSG 148
Cdd:COG2226   88 fDLVISSFVLHHLPDP-ERALAEIArvlkPGGRLVVVDFSPPDLAELEELLAEAG 141
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 22-101 1.99e-09

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 55.54  E-value: 1.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083  22 LALAKLELHRARHLIDIGAGTGSVSIEAALQNPALRVTAIERQADALRLLAENRQRFGCDN-IAIVAG--VAPLAVADKA 98
Cdd:COG2890  103 LALALLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLGLEDrVRFLQGdlFEPLPGDGRF 182


                 ...
gi 489005083  99 DAI 101
Cdd:COG2890  183 DLI 185
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 28-129 2.07e-09

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: 55.15  E-value: 2.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083  28 ELHRARHLIDIGAGTGSVSIEAALQNPALRVTAIERQADALRLLAENRQRFGCDN-IAIVAG----VAPLAVADKADAI- 101
Cdd:COG4123   34 PVKKGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLEDrITVIHGdlkeFAAELPPGSFDLVv 113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489005083 102 -----FMGGSG--------------GHLT--ALIDWSLAQLHPGGRLVM 129
Cdd:COG4123  114 snppyFKAGSGrkspdearaiarheDALTleDLIRAAARLLKPGGRFAL 162
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
21-129 2.79e-09

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 54.30  E-value: 2.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083   21 ALALAKLELHRARHLIDIGAGTG-SVSIEAALQNPALRVTAIERQADALRLLAENRQRFGCDNIAIVAGVAPLAVADKA- 98
Cdd:pfam01135  63 AMMLELLELKPGMRVLEIGSGSGyLTACFARMVGEVGRVVSIEHIPELVEIARRNLEKLGLENVIVVVGDGRQGWPEFAp 142

                          90       100       110
                  ....*....|....*....|....*....|...
gi 489005083   99 -DAIFMGGSGGHL-TALIDwslaQLHPGGRLVM 129
Cdd:pfam01135 143 yDAIHVGAAAPEIpEALID----QLKEGGRLVI 171
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 22-88 3.84e-08

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 51.70  E-value: 3.84e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489005083  22 LALAKLELHRARHLIDIGAGTGSVSIEAALQNPALRVTAIERQADALRLLAENRQRFGCDNIAIVAG 88
Cdd:PRK09328  99 WALEALLLKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGLGARVEFLQG 165
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
31-131 4.33e-08

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 49.05  E-value: 4.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083  31 RARHLIDIGAGTGSVSIEAALQNPALRVTAIERQADALRLLAEN--RQRFgcdniaIVAGVAPLAVADKADAIFMGGSGG 108
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARlpNVRF------VVADLRDLDPPEPFDLVVSNAALH 74

                         90       100
                 ....*....|....*....|....*.
gi 489005083 109 HLT---ALIDWSLAQLHPGGRLVMTF 131
Cdd:COG4106   75 WLPdhaALLARLAAALAPGGVLAVQV 100
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 35-133 6.97e-08

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 48.58  E-value: 6.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083  35 LIDIGAGTGSVSIEAAlQNPALRVTAIERQADALRLLAENRQRFGCDNIAIVAG---VAPLAVADKADAIFMGGSGGHLT 111
Cdd:cd02440    2 VLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAALLADNVEVLKGdaeELPPEADESFDVIISDPPLHHLV 80

                         90       100
                 ....*....|....*....|....*.
gi 489005083 112 ALIDWSLAQLH----PGGRLVMTFIL 133
Cdd:cd02440   81 EDLARFLEEARrllkPGGVLVLTLVL 106
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 21-129 1.22e-07

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 49.70  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083  21 ALALAKLELHRARHLIDIGAGTG-SVSIEAALqnpALRVTAIERQADALRLLAENRQRFGCDNIAIVAGVAPLAVADKA- 98
Cdd:COG2518   56 ARMLEALDLKPGDRVLEIGTGSGyQAAVLARL---AGRVYSVERDPELAERARERLAALGYDNVTVRVGDGALGWPEHAp 132

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489005083  99 -DAIFMGGSGGHL-TALidwsLAQLHPGGRLVM 129
Cdd:COG2518  133 fDRIIVTAAAPEVpEAL----LEQLAPGGRLVA 161
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
28-90 2.74e-07

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 48.39  E-value: 2.74e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489005083   28 ELHRARHLiDIGAGTGSVSIEAALQNpALRVTAIERQADALRLLAENRQRFGCDNIAIVAGVA 90
Cdd:pfam03602  39 YIEGARVL-DLFAGSGALGLEALSRG-AKRVTLVEKDKRAVQILKENLQLLGLPGAVLVMDAL 99
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 24-132 6.19e-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: 46.55  E-value: 6.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083  24 LAKLELHRARHLiDIGAGTGSVSIEAALQNpaLRVTAIERQADALRLLAENRQRFGCDniAIVAGVAPLAVAD-KADAIF 102
Cdd:COG2227   18 LARLLPAGGRVL-DVGCGTGRLALALARRG--ADVTGVDISPEALEIARERAAELNVD--FVQGDLEDLPLEDgSFDLVI 92

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489005083 103 MGGSGGHLT---ALIDWSLAQLHPGGRLVMTFI 132
Cdd:COG2227   93 CSEVLEHLPdpaALLRELARLLKPGGLLLLSTP 125
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 17-131 6.60e-07

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 46.85  E-value: 6.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083  17 EAVRALALAKLELHRARHLIDIGAGTGSVSIEAAlQNPALRVTAIERQADALRLLAENRQRFGCDNIA--IVAGVAPLAV 94
Cdd:COG2230   37 EAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLA-RRYGVRVTGVTLSPEQLEYARERAAEAGLADRVevRLADYRDLPA 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489005083  95 ADKADAIFMGGSGGHL-----TALIDWSLAQLHPGGRLVMTF 131
Cdd:COG2230  116 DGQFDAIVSIGMFEHVgpenyPAYFAKVARLLKPGGRLLLHT 157
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 13-79 7.05e-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: 45.04  E-value: 7.05e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489005083   13 PMTKEAVRALALAKLELHRARHLIDIGAGTGSVSIEAALQNPALRVTAIERQADALRLLAENRQRFG 79
Cdd:TIGR00536  96 PETEELVEKALASLISQPPILHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQ 162
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
33-103 1.81e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 43.35  E-value: 1.81e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489005083  33 RHLIDIGAGTGSVSIEAALQNPAlRVTAIERQADALRLLAENRQRFGCDNIAIVAGVAPLAVADKADAIFM 103
Cdd:COG2263   47 KTVLDLGCGTGMLAIGAALLGAK-KVVGVDIDPEALEIARENAERLGVRVDFIRADVTRIPLGGSVDTVVM 116
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 21-127 1.87e-05

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: 42.96  E-value: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083   21 ALALAKLELHRARHLIDIGAGTGSVSIEAALQNPALRVTAIERQADALRLLAENRQRFGCDNIAIVAGVAPLAVAD-KAD 99
Cdd:pfam05175  21 RLLLEHLPKDLSGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGLENGEVVASDVYSGVEDgKFD 100

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 489005083  100 AIFMG---GSGGHLTALIDWSL-----AQLHPGGRL 127
Cdd:pfam05175 101 LIISNppfHAGLATTYNVAQRFiadakRHLRPGGEL 136
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 36-103 1.89e-05

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: 42.68  E-value: 1.89e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489005083   36 IDIGAGTGSVSIEAALQNPALRVTAIERQADALRLLAENRQRFGCDNIAIVagvaPLAVADKADAIFM 103
Cdd:TIGR01444   3 IDVGANIGDTSLYFARKGAEGRVIAFEPLPDAYEILEENVKLNNLPNVVLL----NAAVGDRDGELEF 66
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 36-127 4.20e-05

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 40.81  E-value: 4.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083   36 IDIGAGTGSVSIEAALQNPALRVTAIERQADALRLLAENRQRFG---CDNIAIVAGVAPLAVADKADAIFMGGSGGHLTA 112
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGllnAVRVELFQLDLGELDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*....
gi 489005083  113 LIDWsLAQLH----PGGRL 127
Cdd:pfam08242  81 PRAV-LRNIRrllkPGGVL 98
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 40-103 4.87e-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: 41.99  E-value: 4.87e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489005083  40 AGTGSVSIEaALQNPALRVTAIERQADALRLLAENRQRFGC-DNIAIVAG----VAPLAVADKADAIFM 103
Cdd:COG0742   50 AGSGALGLE-ALSRGAASVVFVEKDRKAAAVIRKNLEKLGLeDRARVIRGdalrFLKRLAGEPFDLVFL 117
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
17-131 7.29e-05

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 41.52  E-value: 7.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083  17 EAVRALALAKLELHRARHLIDIGAGTGSVSieAALQNPALRVTAIERQADALRLLAENR--QRFGCDNIAIVAgvaplAV 94
Cdd:COG4976   32 ALLAEELLARLPPGPFGRVLDLGCGTGLLG--EALRPRGYRLTGVDLSEEMLAKAREKGvyDRLLVADLADLA-----EP 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489005083  95 ADKADAIFMGGS---GGHLTALIDWSLAQLHPGGRLVMTF 131
Cdd:COG4976  105 DGRFDLIVAADVltyLGDLAAVFAGVARALKPGGLFIFSV 144
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 29-130 7.90e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 40.86  E-value: 7.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083   29 LHRARHLIDIGAGTGSVSIEAA-LQNPALRVTAIERQADALRLLAENRQRFGCDNIAIVAGVA---PLAVAD-KADAIFM 103
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAeELGPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIeelPELLEDdKFDVVIS 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 489005083  104 GGSGGHLTALIDW---SLAQLHPGGRLVMT 130
Cdd:pfam13847  81 NCVLNHIPDPDKVlqeILRVLKPGGRLIIS 110
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 1-128 8.06e-05

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: 41.86  E-value: 8.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083   1 MKDELFLRG---AQVPMTKEAVRAlALAKLELH----RARHLIDIGAGTGSVSIEAALQNPAL-RVTAIERQADALRL-- 70
Cdd:COG5459   44 LADEADALAyaaYRLPATYAAVRA-ALAELAEAgpdfAPLTVLDVGAGPGTAAWAAADAWPSLlDATLLERSAAALALgr 122

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489005083  71 -LAENRQRFGCDN-IAIVAGVAPLAVADKADAIFMGGS-----GGHLTALIDWslAQLHPGGRLV 128
Cdd:COG5459  123 rLARAAANPALETaEWRLADLAAALPAPPADLVVASYVlnelaDAARAALVDR--LWLAPDGALL 185
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 37-125 1.05e-04

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 39.47  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083   37 DIGAGTGSVSIEAAlQNPALRVTAIERQADALRLLAENRQRFGCDNIAIVAGVAPLAVAD-KADAIFMGGSGGHLT-ALI 114
Cdd:pfam13649   3 DLGCGTGRLTLALA-RRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDgSFDLVVSSGVLHHLPdPDL 81

                          90
                  ....*....|....*
gi 489005083  115 DWSLAQLH----PGG 125
Cdd:pfam13649  82 EAALREIArvlkPGG 96
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 21-148 2.90e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 39.90  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083  21 ALALAKLELHRARHLIDIGAGTGSVSIEAALQNPAlRVTAIERQADALRLLAENRQRFGCDNIAI----VAGVAPLAvAD 96
Cdd:COG0500   16 ALLALLERLPKGGRVLDLGCGTGRNLLALAARFGG-RVIGIDLSPEAIALARARAAKAGLGNVEFlvadLAELDPLP-AE 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489005083  97 KADAIFMGGSGGHL-----TALIDWSLAQLHPGGRLVMT--FILQENLHSALAHLRQSG 148
Cdd:COG0500   94 SFDLVVAFGVLHHLppeerEALLRELARALKPGGVLLLSasDAAAALSLARLLLLATAS 152
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
37-90 2.97e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 40.02  E-value: 2.97e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489005083  37 DIGAGTGSVSIEAAlQNPALRVTAIERQADALRLLAENRQRFGC-DNIAIVAGVA 90
Cdd:COG4076   41 DIGTGSGLLSMLAA-RAGAKKVYAVEVNPDIAAVARRIIAANGLsDRITVINADA 94
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 35-132 4.01e-04

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 39.16  E-value: 4.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083  35 LIDIGAGTGSVSIEAALQNpaLRVTAIERQADALRLLAENRQRFGCDNIAIVAGVA---PLAvADKADAIFM-------- 103
Cdd:COG1041   30 VLDPFCGTGTILIEAGLLG--RRVIGSDIDPKMVEGARENLEHYGYEDADVIRGDArdlPLA-DESVDAIVTdppygrss 106

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489005083 104 GGSGGHLTALIDWSLA----QLHPGGRLVMTFI 132
Cdd:COG1041  107 KISGEELLELYEKALEeaarVLKPGGRVVIVTP 139
PRK08317 PRK08317
hypothetical protein; Provisional
 17-129 7.15e-04

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 39.15  E-value: 7.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083  17 EAVRALALAKLELHRARHLIDIGAGTGSVSIE-AALQNPALRVTAIERQADALrLLAENRQRFGCDNIAIVAGVA-PLAV 94
Cdd:PRK08317   5 RRYRARTFELLAVQPGDRVLDVGCGPGNDARElARRVGPEGRVVGIDRSEAML-ALAKERAAGLGPNVEFVRGDAdGLPF 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489005083  95 ADKA-DAIFMGGSGGHLTAlIDWSLAQLH----PGGRLVM 129
Cdd:PRK08317  84 PDGSfDAVRSDRVLQHLED-PARALAEIArvlrPGGRVVV 122
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 29-125 9.88e-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: 38.24  E-value: 9.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083  29 LHRARHLIDIGAGTG--SVSIEAALQNPAlRVTAIERQADALRLLAENRQRFGC-DNIAIVAGVA----PLAVADKADAI 101
Cdd:COG4122   14 LLGAKRILEIGTGTGysTLWLARALPDDG-RLTTIEIDPERAAIARENFARAGLaDRIRLILGDAlevlPRLADGPFDLV 92

                         90       100
                 ....*....|....*....|....
gi 489005083 102 FMGGSGGHLTALIDWSLAQLHPGG 125
Cdd:COG4122   93 FIDADKSNYPDYLELALPLLRPGG 116
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 36-146 1.06e-03

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 38.79  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083   36 IDIGAGTGSVSIEAALQNPAlRVTAIERQADALRLLAENRQRFGCDNIAIVAGVAPLaVADKADAIFMGGSGGHLTALID 115
Cdd:pfam06325 166 LDVGCGSGILAIAALKLGAK-KVVGVDIDPVAVRAAKENAELNGVEARLEVYLPGDL-PKEKADVVVANILADPLIELAP 243

                          90       100       110
                  ....*....|....*....|....*....|.
gi 489005083  116 WSLAQLHPGGRLVMTFILQENLHSALAHLRQ 146
Cdd:pfam06325 244 DIYALVKPGGYLILSGILKEQAQMVAEAYSQ 274
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 24-127 2.09e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 37.62  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083  24 LAKLELHRARHLIDIGAGTGSvSIEAALQN-PALRVTAIERQADalrLLAENRQRF-GCDNIAivAGVAPLAVADKADAI 101
Cdd:PRK01683  24 LARVPLENPRYVVDLGCGPGN-STELLVERwPAARITGIDSSPA---MLAEARSRLpDCQFVE--ADIASWQPPQALDLI 97

                         90       100       110
                 ....*....|....*....|....*....|
gi 489005083 102 FMGGS----GGHLTaLIDWSLAQLHPGGRL 127
Cdd:PRK01683  98 FANASlqwlPDHLE-LFPRLVSLLAPGGVL 126
GidB pfam02527
rRNA small subunit methyltransferase G; This is a family of bacterial glucose inhibited ...
 33-128 3.82e-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: 36.49  E-value: 3.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005083   33 RHLIDIGAGTGSVSIEAALQNPALRVTAIERQADALRLLAENRQRFGCDNIAIVAG-VAPLAVADKADAI----Fmggsg 107
Cdd:pfam02527  50 DHVLDVGSGAGFPGIPLAIARPDKKVTLLESLLKKINFLEEVKSELGLDNVTIVHArAEEYQPEEQYDVItsraV----- 124

                          90       100
                  ....*....|....*....|.
gi 489005083  108 GHLTALIDWSLAQLHPGGRLV 128
Cdd:pfam02527 125 ASLNELTEWTLPLLKPGGYFL 145
TIGR00095 TIGR00095
16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of ...
 34-82 7.43e-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: 35.85  E-value: 7.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 489005083   34 HLIDIGAGTGSVSIEaALQNPALRVTAIERQADALRLLAENRQRFGCDN 82
Cdd:TIGR00095  53 HFLDLFAGSGALGLE-ALSRGAASAVFVEQDRKVAQTLKENLSTLKKSG 100
 
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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