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Conserved domains on  [gi|802115983|ref|WP_046034116|]
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MULTISPECIES: peptide chain release factor N(5)-glutamine methyltransferase [Pseudomonas]

Protein Classification

HemK/PrmC family methyltransferase( domain architecture ID 11483836)

HemK/PrmC family methyltransferase is a class I SAM-dependent methyltransferase that catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; such as peptide chain release factor N(5)-glutamine methyltransferase that methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:0003676|GO:0032259|GO:1904047
PubMed:  12741815|12504684|12826405
SCOP:  3000118

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 32-274 5.28e-114

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


:

Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 329.04  E-value: 5.28e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983  32 GKSRSYLHTWPEKIVSSEDALTFAGYLQRRRGGEPVAYILGQQGFWKLDLEVAPHTLIPRPDT-ELLVEAALELLPATPA 110
Cdd:PRK09328  31 GLSRTDLLLNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFWGLDFKVSPGVLIPRPETeELVEWALEALLLKEPL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 111 KVLDLGTGSGAIALALASERPAWQVTAVDRVLEAVALAERNRQRLHLNNATVLNSHWFSALPGHTYDLIISNPPYIAAND 190
Cdd:PRK09328 111 RVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGLGARVEFLQGDWFEPLPGGRFDLIVSNPPYIPEAD 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 191 PHLVAGDVR-FEPASALVAGHDGLDDLRLIIKEAPAHLNAGGRLLLEHGYDQAPAVRDLLLSEGFEEVHSRIDLGGHERI 269
Cdd:PRK09328 191 IHLLQPEVRdHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGWLLLEIGYDQGEAVRALLAAAGFADVETRKDLAGRDRV 270


                 ....*
gi 802115983 270 TLGRR 274
Cdd:PRK09328 271 VLGRR 275
 
Name Accession Description Interval E-value
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 32-274 5.28e-114

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 329.04  E-value: 5.28e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983  32 GKSRSYLHTWPEKIVSSEDALTFAGYLQRRRGGEPVAYILGQQGFWKLDLEVAPHTLIPRPDT-ELLVEAALELLPATPA 110
Cdd:PRK09328  31 GLSRTDLLLNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFWGLDFKVSPGVLIPRPETeELVEWALEALLLKEPL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 111 KVLDLGTGSGAIALALASERPAWQVTAVDRVLEAVALAERNRQRLHLNNATVLNSHWFSALPGHTYDLIISNPPYIAAND 190
Cdd:PRK09328 111 RVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGLGARVEFLQGDWFEPLPGGRFDLIVSNPPYIPEAD 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 191 PHLVAGDVR-FEPASALVAGHDGLDDLRLIIKEAPAHLNAGGRLLLEHGYDQAPAVRDLLLSEGFEEVHSRIDLGGHERI 269
Cdd:PRK09328 191 IHLLQPEVRdHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGWLLLEIGYDQGEAVRALLAAAGFADVETRKDLAGRDRV 270


                 ....*
gi 802115983 270 TLGRR 274
Cdd:PRK09328 271 VLGRR 275
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 32-271 1.06e-112

protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein family are HemK (PrmC), a protein once thought to be involved in heme biosynthesis but now recognized to be a protein-glutamine methyltransferase that modifies the peptide chain release factors. All members of the seed alignment are encoded next to the release factor 1 gene (prfA) and confirmed by phylogenetic analysis. SIMBAL analysis (manuscript in prep.) shows the motif [LIV]PRx[DE]TE (in Escherichia coli, IPRPDTE) confers specificity for the release factors rather than for ribosomal protein L3. [Protein fate, Protein modification and repair]


Pssm-ID: 274634 [Multi-domain]  Cd Length: 250  Bit Score: 324.81  E-value: 1.06e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983   32 GKSRSYLHTWPEKIVSSEDALTFAGYLQRRRGGEPVAYILGQQGFWKLDLEVAPHTLIPRPDTELLVEAALELLPATPaK 111
Cdd:TIGR03534  11 GKDRAQLLLHPEDELTPEELAAFDALLARRAAGEPVAYILGEREFYGLDFKVSPGVLIPRPETEELVEAALERLKKGP-R 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983  112 VLDLGTGSGAIALALASERPAWQVTAVDRVLEAVALAERNRQRLHLNNATVLNSHWFSALPGHTYDLIISNPPYIAANDP 191
Cdd:TIGR03534  90 VLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKNARRLGLENVEFLQGDWFEPLPSGKFDLIVSNPPYIPEADI 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983  192 HLVAGDVR-FEPASALVAGHDGLDDLRLIIKEAPAHLNAGGRLLLEHGYDQAPAVRDLLLSEGFEEVHSRIDLGGHERIT 270
Cdd:TIGR03534 170 HLLDPEVRdFEPRLALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFEAAGFADVETRKDLAGKDRVV 249


                  .
gi 802115983  271 L 271
Cdd:TIGR03534 250 L 250
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 32-275 5.74e-106

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 309.00  E-value: 5.74e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983  32 GKSRSYLHTWPEKIVSSEDALTFAGYLQRRRGGEPVAYILGQQGFWKLDLEVAPHTLIPRPDTELLVEAALELLPA-TPA 110
Cdd:COG2890   35 GLDRADLLLHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFYGLEFKVDPGVLIPRPETEELVELALALLPAgAPP 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 111 KVLDLGTGSGAIALALASERPAWQVTAVDRVLEAVALAERNRQRLHLNN-ATVLNSHWFSALPGH-TYDLIISNPPYIAA 188
Cdd:COG2890  115 RVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLGLEDrVRFLQGDLFEPLPGDgRFDLIVSNPPYIPE 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 189 NDPHLVAGDVR-FEPASALVAGHDGLDDLRLIIKEAPAHLNAGGRLLLEHGYDQAPAVRDLLLSEGFEEVHSRIDLGGHE 267
Cdd:COG2890  195 DEIALLPPEVRdHEPRLALDGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGEDQGEAVRALLEAAGFADVETHKDLAGRD 274


                 ....*...
gi 802115983 268 RITLGRRP 275
Cdd:COG2890  275 RVVVARRP 282
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 111-235 1.26e-18

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: 80.71  E-value: 1.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983  111 KVLDLGTGSGAIALALASERPAWQVTAVDRVLEAVALAERNRQRLHLNNATVLNSHWFSALPGHTYDLIISNPPYiaand 190
Cdd:pfam05175  34 KVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGLENGEVVASDVYSGVEDGKFDLIISNPPF----- 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 802115983  191 pHlvagdvrfepasalvAGHDGLDDL-RLIIKEAPAHLNAGGRLLL 235
Cdd:pfam05175 109 -H---------------AGLATTYNVaQRFIADAKRHLRPGGELWI 138
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 111-236 4.33e-14

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: 66.68  E-value: 4.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 111 KVLDLGTGSGAIALALAsERPAWQVTAVDRVLEAVALAERNRQRLHLNNATVLNSHWFSAL--PGHTYDLIISNPPYiaa 188
Cdd:cd02440    1 RVLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPpeADESFDVIISDPPL--- 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 802115983 189 ndphlvagdvrfepasalvagHDGLDDLRLIIKEAPAHLNAGGRLLLE 236
Cdd:cd02440   77 ---------------------HHLVEDLARFLEEARRLLKPGGVLVLT 103
rADc smart00650
Ribosomal RNA adenine dimethylases;
106-185 6.51e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 36.72  E-value: 6.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983   106 PATPAKVLDLGTGSGAIALALAseRPAWQVTAV--DRVLEAVaLAER--NRQRLHLNNATVLNSHwfsaLPGHTYDLIIS 181
Cdd:smart00650  11 LRPGDTVLEIGPGKGALTEELL--ERAKRVTAIeiDPRLAPR-LREKfaAADNLTVIHGDALKFD----LPKLQPYKVVG 83


                   ....
gi 802115983   182 NPPY 185
Cdd:smart00650  84 NLPY 87
 
Name Accession Description Interval E-value
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 32-274 5.28e-114

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 329.04  E-value: 5.28e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983  32 GKSRSYLHTWPEKIVSSEDALTFAGYLQRRRGGEPVAYILGQQGFWKLDLEVAPHTLIPRPDT-ELLVEAALELLPATPA 110
Cdd:PRK09328  31 GLSRTDLLLNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFWGLDFKVSPGVLIPRPETeELVEWALEALLLKEPL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 111 KVLDLGTGSGAIALALASERPAWQVTAVDRVLEAVALAERNRQRLHLNNATVLNSHWFSALPGHTYDLIISNPPYIAAND 190
Cdd:PRK09328 111 RVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGLGARVEFLQGDWFEPLPGGRFDLIVSNPPYIPEAD 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 191 PHLVAGDVR-FEPASALVAGHDGLDDLRLIIKEAPAHLNAGGRLLLEHGYDQAPAVRDLLLSEGFEEVHSRIDLGGHERI 269
Cdd:PRK09328 191 IHLLQPEVRdHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGWLLLEIGYDQGEAVRALLAAAGFADVETRKDLAGRDRV 270


                 ....*
gi 802115983 270 TLGRR 274
Cdd:PRK09328 271 VLGRR 275
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 32-271 1.06e-112

protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein family are HemK (PrmC), a protein once thought to be involved in heme biosynthesis but now recognized to be a protein-glutamine methyltransferase that modifies the peptide chain release factors. All members of the seed alignment are encoded next to the release factor 1 gene (prfA) and confirmed by phylogenetic analysis. SIMBAL analysis (manuscript in prep.) shows the motif [LIV]PRx[DE]TE (in Escherichia coli, IPRPDTE) confers specificity for the release factors rather than for ribosomal protein L3. [Protein fate, Protein modification and repair]


Pssm-ID: 274634 [Multi-domain]  Cd Length: 250  Bit Score: 324.81  E-value: 1.06e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983   32 GKSRSYLHTWPEKIVSSEDALTFAGYLQRRRGGEPVAYILGQQGFWKLDLEVAPHTLIPRPDTELLVEAALELLPATPaK 111
Cdd:TIGR03534  11 GKDRAQLLLHPEDELTPEELAAFDALLARRAAGEPVAYILGEREFYGLDFKVSPGVLIPRPETEELVEAALERLKKGP-R 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983  112 VLDLGTGSGAIALALASERPAWQVTAVDRVLEAVALAERNRQRLHLNNATVLNSHWFSALPGHTYDLIISNPPYIAANDP 191
Cdd:TIGR03534  90 VLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKNARRLGLENVEFLQGDWFEPLPSGKFDLIVSNPPYIPEADI 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983  192 HLVAGDVR-FEPASALVAGHDGLDDLRLIIKEAPAHLNAGGRLLLEHGYDQAPAVRDLLLSEGFEEVHSRIDLGGHERIT 270
Cdd:TIGR03534 170 HLLDPEVRdFEPRLALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFEAAGFADVETRKDLAGKDRVV 249


                  .
gi 802115983  271 L 271
Cdd:TIGR03534 250 L 250
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 32-275 5.74e-106

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 309.00  E-value: 5.74e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983  32 GKSRSYLHTWPEKIVSSEDALTFAGYLQRRRGGEPVAYILGQQGFWKLDLEVAPHTLIPRPDTELLVEAALELLPA-TPA 110
Cdd:COG2890   35 GLDRADLLLHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFYGLEFKVDPGVLIPRPETEELVELALALLPAgAPP 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 111 KVLDLGTGSGAIALALASERPAWQVTAVDRVLEAVALAERNRQRLHLNN-ATVLNSHWFSALPGH-TYDLIISNPPYIAA 188
Cdd:COG2890  115 RVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLGLEDrVRFLQGDLFEPLPGDgRFDLIVSNPPYIPE 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 189 NDPHLVAGDVR-FEPASALVAGHDGLDDLRLIIKEAPAHLNAGGRLLLEHGYDQAPAVRDLLLSEGFEEVHSRIDLGGHE 267
Cdd:COG2890  195 DEIALLPPEVRdHEPRLALDGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGEDQGEAVRALLEAAGFADVETHKDLAGRD 274


                 ....*...
gi 802115983 268 RITLGRRP 275
Cdd:COG2890  275 RVVVARRP 282
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 32-276 2.55e-73

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: 226.08  E-value: 2.55e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983   32 GKSRSYLHTWPEKIVSSEDALTFAGYLQRRRGGEPVAYILGQQGFWKLDLEVAPHTLIPRPDTELLVEAALELLPATPA- 110
Cdd:TIGR00536  36 GRERDLLLAFLTEELTPDEKERIFRLVLRRVKGVPVAYLLGSKEFYGLEFFVNEHVLIPRPETEELVEKALASLISQPPi 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983  111 -KVLDLGTGSGAIALALASERPAWQVTAVDRVLEAVALAERNRQRLHLNNAT-VLNSHWFSALPGHTYDLIISNPPYIAA 188
Cdd:TIGR00536 116 lHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQLEHRVeFIQSNLFEPLAGQKIDIIVSNPPYIDE 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983  189 NDPHLVAGDVRFEPASALVAGHDGLDDLRLIIKEAPAHLNAGGRLLLEHGYDQAPAVRDLLLSEG-FEEVHSRIDLGGHE 267
Cdd:TIGR00536 196 EDLADLPNVVRFEPLLALVGGDDGLNILRQIIELAPDYLKPNGFLVCEIGNWQQKSLKELLRIKFtWYDVENGRDLNGKE 275


                  ....*....
gi 802115983  268 RITLGRRPC 276
Cdd:TIGR00536 276 RVVLGFYHS 284
PRK14966 PRK14966
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; ...
 42-273 5.09e-45

unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; Provisional


Pssm-ID: 184930 [Multi-domain]  Cd Length: 423  Bit Score: 156.78  E-value: 5.09e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983  42 PEKIVSSEDALTfagylQRRRGGEPVAYILGQQGFWKLDLEVAPHTLIPRPDTELLVEAALELLPATpAKVLDLGTGSGA 121
Cdd:PRK14966 191 PDEVRQRADRLA-----QRRLNGEPVAYILGVREFYGRRFAVNPNVLIPRPETEHLVEAVLARLPEN-GRVWDLGTGSGA 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 122 IALALASERPAWQVTAVDRVLEAVALAERNRQRLhlnNATVLNSH--WFSA-LPGH-TYDLIISNPPYIAANDPHLVAGD 197
Cdd:PRK14966 265 VAVTVALERPDAFVRASDISPPALETARKNAADL---GARVEFAHgsWFDTdMPSEgKWDIIVSNPPYIENGDKHLLQGD 341

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 802115983 198 VRFEPASALVAGHDGLDDLRLIIKEAPAHLNAGGRLLLEHGYDQAPAVRDLLLSEGFEEVHSRIDLGGHERITLGR 273
Cdd:PRK14966 342 LRFEPQIALTDFSDGLSCIRTLAQGAPDRLAEGGFLLLEHGFDQGAAVRGVLAENGFSGVETLPDLAGLDRVTLGK 417
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
 33-271 3.91e-38

bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) methyltransferase; Reviewed


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 140.00  E-value: 3.91e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983  33 KSRSYLHTWPEKIVSSEDALTFAGYLQRRRGGEPVAYILGQQGFWKLDLEVAPHTLIPRPDT-----------ELLVEAA 101
Cdd:PRK01544  38 KPIEYLLINLDEQLNEAEIEAFEKLLERRLKHEPIAYITGVKEFYSREFIVNKHVLIPRSDTevlvdvvfqchSRESGNP 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 102 LELLPATPAK--------------VLDLGTGSGAIALALASERPAWQVTAVDRVLEAVALAERNRQRLHLNN-ATVLNSH 166
Cdd:PRK01544 118 EKKQLNPCFRgndissncndkflnILELGTGSGCIAISLLCELPNANVIATDISLDAIEVAKSNAIKYEVTDrIQIIHSN 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 167 WFSALPGHTYDLIISNPPYIAAND-PHLVAGDVRFEPASALVAGHDGLDDLRLIIKEAPAHLNAGGRLLLEHGYDQAPAV 245
Cdd:PRK01544 198 WFENIEKQKFDFIVSNPPYISHSEkSEMAIETINYEPSIALFAEEDGLQAYFIIAENAKQFLKPNGKIILEIGFKQEEAV 277

                        250       260
                 ....*....|....*....|....*.
gi 802115983 246 RDLLLSEGFEEVHSRIDLGGHERITL 271
Cdd:PRK01544 278 TQIFLDHGYNIESVYKDLQGHSRVIL 303
L3_gln_methyl TIGR03533
protein-(glutamine-N5) methyltransferase, ribosomal protein L3-specific; Members of this ...
 60-238 3.47e-37

protein-(glutamine-N5) methyltransferase, ribosomal protein L3-specific; Members of this protein family methylate ribosomal protein L3 on a glutamine side chain. This family is related to HemK, a protein-glutamine methyltranferase for peptide chain release factors. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 274633 [Multi-domain]  Cd Length: 284  Bit Score: 132.64  E-value: 3.47e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983   60 RRRGGE--PVAYILGQQGFWKLDLEVAPHTLIPR------------PdtellveaalELLPATPAKVLDLGTGSGAIALA 125
Cdd:TIGR03533  69 ERRIEEriPVAYLTNEAWFAGLEFYVDERVLIPRspiaeliedgfaP----------WLEPEPVKRILDLCTGSGCIAIA 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983  126 LASERPAWQVTAVDRVLEAVALAERNRQRLHL-NNATVLNSHWFSALPGHTYDLIISNPPYIAANDPHLVAGDVRFEPAS 204
Cdd:TIGR03533 139 CAYAFPEAEVDAVDISPDALAVAEINIERHGLeDRVTLIQSDLFAALPGRKYDLIVSNPPYVDAEDMADLPAEYHHEPEL 218

                         170       180       190
                  ....*....|....*....|....*....|....
gi 802115983  205 ALVAGHDGLDDLRLIIKEAPAHLNAGGRLLLEHG 238
Cdd:TIGR03533 219 ALASGEDGLDLVRRILAEAADHLNENGVLVVEVG 252
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 106-235 8.42e-24

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: 95.26  E-value: 8.42e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 106 PATPAKVLDLGTGSGAIALALASERPAWQVTAVDRVLEAVALAERNRQRLHLNNATVLNSHWFSALPGHTYDLIISNPPY 185
Cdd:COG2813   47 EPLGGRVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAANGLENVEVLWSDGLSGVPDGSFDLILSNPPF 126

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 802115983 186 iaandpHlvagdvrfepasalvAGHDGLDDL-RLIIKEAPAHLNAGGRLLL 235
Cdd:COG2813  127 ------H---------------AGRAVDKEVaHALIADAARHLRPGGELWL 156
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 109-262 5.77e-22

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: 91.36  E-value: 5.77e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 109 PAKVLDLGTGSGAIALALASERPAWQVTAVDRVLEAVALAERNRQRLHLNN-ATVLNS---HWFSALPGHTYDLIISNPP 184
Cdd:COG4123   38 GGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLEDrITVIHGdlkEFAAELPPGSFDLVVSNPP 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 185 YIAANDpHLVAGDVRFepASALVAGHDGLDDLrliIKEAPAHLNAGGRLLLEHGYDQAPAVRDLLLSEGFE-----EVHS 259
Cdd:COG4123  118 YFKAGS-GRKSPDEAR--AIARHEDALTLEDL---IRAAARLLKPGGRFALIHPAERLAEILAALRKYGLGpkrlrPVHP 191


                 ...
gi 802115983 260 RID 262
Cdd:COG4123  192 RPG 194
PRK14967 PRK14967
putative methyltransferase; Provisional
 110-237 3.95e-19

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 83.56  E-value: 3.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 110 AKVLDLGTGSGAIALAlASERPAWQVTAVDRVLEAVALAERNrQRLHLNNATVLNSHWFSALPGHTYDLIISNPPYI-AA 188
Cdd:PRK14967  38 RRVLDLCTGSGALAVA-AAAAGAGSVTAVDISRRAVRSARLN-ALLAGVDVDVRRGDWARAVEFRPFDVVVSNPPYVpAP 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 802115983 189 NDPHLVAGdvrfePASALVAGHDGLDDLRLIIKEAPAHLNAGGRLLLEH 237
Cdd:PRK14967 116 PDAPPSRG-----PARAWDAGPDGRAVLDRLCDAAPALLAPGGSLLLVQ 159
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 111-235 1.26e-18

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: 80.71  E-value: 1.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983  111 KVLDLGTGSGAIALALASERPAWQVTAVDRVLEAVALAERNRQRLHLNNATVLNSHWFSALPGHTYDLIISNPPYiaand 190
Cdd:pfam05175  34 KVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGLENGEVVASDVYSGVEDGKFDLIISNPPF----- 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 802115983  191 pHlvagdvrfepasalvAGHDGLDDL-RLIIKEAPAHLNAGGRLLL 235
Cdd:pfam05175 109 -H---------------AGLATTYNVaQRFIADAKRHLRPGGELWI 138
PRK14968 PRK14968
putative methyltransferase; Provisional
 111-271 3.56e-17

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 77.25  E-value: 3.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 111 KVLDLGTGSGAIALALASErpAWQVTAVDRVLEAVALAERNRQRLHLNNAT--VLNSHWFSALPGHTYDLIISNPPYIAA 188
Cdd:PRK14968  26 RVLEVGTGSGIVAIVAAKN--GKKVVGVDINPYAVECAKCNAKLNNIRNNGveVIRSDLFEPFRGDKFDVILFNPPYLPT 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 189 NDPHLVAGDVRFepasALVAGHDGLDDLRLIIKEAPAHLNAGGRLLLEH----GYDqapAVRDLLLSEGFE-EVHSRIDL 263
Cdd:PRK14968 104 EEEEEWDDWLNY----ALSGGKDGREVIDRFLDEVGRYLKPGGRILLLQssltGED---EVLEYLEKLGFEaEVVAEEKF 176


                 ....*...
gi 802115983 264 GGhERITL 271
Cdd:PRK14968 177 PF-EELIV 183
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 111-236 4.33e-14

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: 66.68  E-value: 4.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 111 KVLDLGTGSGAIALALAsERPAWQVTAVDRVLEAVALAERNRQRLHLNNATVLNSHWFSAL--PGHTYDLIISNPPYiaa 188
Cdd:cd02440    1 RVLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPpeADESFDVIISDPPL--- 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 802115983 189 ndphlvagdvrfepasalvagHDGLDDLRLIIKEAPAHLNAGGRLLLE 236
Cdd:cd02440   77 ---------------------HHLVEDLARFLEEARRLLKPGGVLVLT 103
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
106-233 4.54e-14

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


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 71.12  E-value: 4.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 106 PATPAKVLDLGTGSGAIALALASERPAWQVTAVDrvLEAVALaERNRQRLHLNN--ATVLNSHWFSALPGhTYDLIISNP 183
Cdd:PRK09489 194 PHTKGKVLDVGCGAGVLSAVLARHSPKIRLTLSD--VSAAAL-ESSRATLAANGleGEVFASNVFSDIKG-RFDMIISNP 269

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 802115983 184 PYiaandphlvagdvrfepasalvagHDGLD-DLRL---IIKEAPAHLNAGGRL 233
Cdd:PRK09489 270 PF------------------------HDGIQtSLDAaqtLIRGAVRHLNSGGEL 299
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 109-255 9.42e-11

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: 59.48  E-value: 9.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983  109 PAKVLDLGTGSGAIALALASErpAWQVTAVDRVLEAVALAERNrQRLHLNNATVLNSHWFSALPGhTYDLIISNPPYIAA 188
Cdd:TIGR00537  20 PDDVLEIGAGTGLVAIRLKGK--GKCILTTDINPFAVKELREN-AKLNNVGLDVVMTDLFKGVRG-KFDVILFNPPYLPL 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 802115983  189 NDpHLVAGDVRfepASALVAGHDGLDDLRLIIKEAPAHLNAGGRL-LLEHGYDQAPAVRDLLLSEGFE 255
Cdd:TIGR00537  96 ED-DLRRGDWL---DVAIDGGKDGRKVIDRFLDELPEILKEGGRVqLIQSSLNGEPDTFDKLDERGFR 159
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
109-237 6.66e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 55.21  E-value: 6.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 109 PAKVLDLGTGSGAIALALASERPAWQVTAVDRVLEAVALAERnrqrlHLNNATVLNSHWFSALPGHTYDLIISNppyiaa 188
Cdd:COG4106    2 PRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARA-----RLPNVRFVVADLRDLDPPEPFDLVVSN------ 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 802115983 189 ndphlvagdvrfepaSALvaGHdgLDDLRLIIKEAPAHLNAGGRLLLEH 237
Cdd:COG4106   71 ---------------AAL--HW--LPDHAALLARLAAALAPGGVLAVQV 100
PrmC_N pfam17827
PrmC N-terminal domain; This entry corresponds to the N-terminal alpha helical domain of the ...
 32-72 1.33e-09

PrmC N-terminal domain; This entry corresponds to the N-terminal alpha helical domain of the HemK protein. HemK is a methyltransferase enzyme that carries out the methylation of the N5 nitrogen of the glutamine found in the conserved GGQ motif of class-1 release factors.


Pssm-ID: 436073 [Multi-domain]  Cd Length: 71  Bit Score: 53.25  E-value: 1.33e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 802115983   32 GKSRSYLHTWPEKIVSSEDALTFAGYLQRRRGGEPVAYILG 72
Cdd:pfam17827  31 GLDRTDLLLHPEEELSEEELERFEELLERRAAGEPLQYILG 71
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 109-236 1.46e-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: 55.02  E-value: 1.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 109 PAKVLDLGTGSGAIALALASErpAWQVTAVDRVLEAVALAernRQRLHLNNATVLNSHWFS-ALPGHTYDLIISNppyia 187
Cdd:COG2227   25 GGRVLDVGCGTGRLALALARR--GADVTGVDISPEALEIA---RERAAELNVDFVQGDLEDlPLEDGSFDLVICS----- 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 802115983 188 andphlvagdvrfepasaLVAGHdgLDDLRLIIKEAPAHLNAGGRLLLE 236
Cdd:COG2227   95 ------------------EVLEH--LPDPAALLRELARLLKPGGLLLLS 123
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 106-184 1.73e-09

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


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 57.49  E-value: 1.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 106 PATPAKVLDLGTGSGAIALALAseRPAWQVTAVDRVLEAVALAERNRQRLHLNNATVLNSHWFSALP----GHTYDLIIS 181
Cdd:COG2265  231 LTGGERVLDLYCGVGTFALPLA--RRAKKVIGVEIVPEAVEDARENARLNGLKNVEFVAGDLEEVLPellwGGRPDVVVL 308


                 ...
gi 802115983 182 NPP 184
Cdd:COG2265  309 DPP 311
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 109-255 2.99e-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: 54.23  E-value: 2.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 109 PAKVLDLGTGSGAIALALAseRPAWQVTAVDRVLEAVALAERNRQRLHLN------NATVLnshwfsALPGHTYDLIISN 182
Cdd:COG2226   23 GARVLDLGCGTGRLALALA--ERGARVTGVDISPEMLELARERAAEAGLNvefvvgDAEDL------PFPDGSFDLVISS 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 802115983 183 ppyiaandphlvagdvrfepasaLVAGHdgLDDLRLIIKEAPAHLNAGGRLLL-EHGYDQAPAVRDLLLSEGFE 255
Cdd:COG2226   95 -----------------------FVLHH--LPDPERALAEIARVLKPGGRLVVvDFSPPDLAELEELLAEAGFE 143
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 110-260 4.62e-09

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: 54.70  E-value: 4.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 110 AKVLDLGTGSGAIALALASeRPAWQVTAVDRVLEAVALAERNRQRLHL-NNATVLNS---HWFSALPGHTYDLIISNPPY 185
Cdd:COG0742   43 ARVLDLFAGSGALGLEALS-RGAASVVFVEKDRKAAAVIRKNLEKLGLeDRARVIRGdalRFLKRLAGEPFDLVFLDPPY 121

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 802115983 186 iaandphlvagdvrfepASALVAghdglDDLRLIikEAPAHLNAGGRLLLEHGYDQAPAVrdllLSEGFEEVHSR 260
Cdd:COG0742  122 -----------------AKGLLE-----KALELL--AENGLLAPGGLIVVEHSKREELPE----LPAGLELLKER 168
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 112-195 7.30e-09

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 52.18  E-value: 7.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983  112 VLDLGTGSGAIALALAsERPAWQVTAVDRVLEAVALAERNRQRLHLNNATVLNShwFSALP--GHTYDLIISNPPYIAAN 189
Cdd:pfam13649   1 VLDLGCGTGRLTLALA-RRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGD--AEDLPfpDGSFDLVVSSGVLHHLP 77


                  ....*.
gi 802115983  190 DPHLVA 195
Cdd:pfam13649  78 DPDLEA 83
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 111-235 1.39e-08

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: 51.95  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983  111 KVLDLGTGSGAIALALASERPAWQVTAVDRVLEAVALAERNRQRLHLNNatvlnshwfsalpghtYDLIISNPPYIAAND 190
Cdd:TIGR02469  22 VLWDIGAGTGSVTIEAARLVPNGRVYAIERNPEALDLIERNLRRFGVSN----------------IVIVEGDAPEAPEAL 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 802115983  191 PHlvagdvrfEPASALVAGHDGLddLRLIIKEAPAHLNAGGRLLL 235
Cdd:TIGR02469  86 LP--------DPDAVFVGGSGGL--LQEILEAVERRLRPGGRIVL 120
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 111-191 1.70e-08

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 52.42  E-value: 1.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983  111 KVLDLGTGSGAIALALASE-RPAWQVTAVDRVLEAVALAERNRQRLHLNNATVLNSHWFS---ALPGHTYDLIISNPPYI 186
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAEElGPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEElpeLLEDDKFDVVISNCVLN 85


                  ....*
gi 802115983  187 AANDP 191
Cdd:pfam13847  86 HIPDP 90
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
111-235 1.92e-08

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


Pssm-ID: 181354  Cd Length: 187  Bit Score: 53.08  E-value: 1.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 111 KVLDLGTGSGAIALALASERPAWQVTAVDRVLEAVALAERNRQRLHLNNATVlnshwfsalpghtydliisnppyIAAND 190
Cdd:PRK08287  34 HLIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKENRQRFGCGNIDI-----------------------IPGEA 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 802115983 191 PHLVAgdvrfEPASALVAGHDG--LDDlrlIIKEAPAHLNAGGRLLL 235
Cdd:PRK08287  91 PIELP-----GKADAIFIGGSGgnLTA---IIDWSLAHLHPGGRLVL 129
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 109-182 3.49e-08

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 52.61  E-value: 3.49e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 802115983 109 PAKVLDLGTGSGAIALALAsERPAWQVTAVDRVLEAVALAERNRQRLHLNNATVLNSHW--FSALPGHTYDLIISN 182
Cdd:COG0500   27 GGRVLDLGCGTGRNLLALA-ARFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLaeLDPLPAESFDLVVAF 101
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 110-235 2.71e-07

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 49.16  E-value: 2.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 110 AKVLDLGTGSGAIALALAsERPAWQVTAVDRVLEAVALAERNRQRLHL-NNATVLNSHWFSALPGHTYDLIISnppyIAA 188
Cdd:COG2230   53 MRVLDIGCGWGGLALYLA-RRYGVRVTGVTLSPEQLEYARERAAEAGLaDRVEVRLADYRDLPADGQFDAIVS----IGM 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 802115983 189 ndphlvagdvrFEpasalvagHDGLDDLRLIIKEAPAHLNAGGRLLL 235
Cdd:COG2230  128 -----------FE--------HVGPENYPAYFAKVARLLKPGGRLLL 155
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
109-255 3.90e-07

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 49.77  E-value: 3.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 109 PAKVLDLGTGSG--AIALALaseRPAWQVTAVDrvLEAVAL--AERNRQRlhlNNATVLNSHWFSALPghtYDLIISNpp 184
Cdd:PRK00517 120 GKTVLDVGCGSGilAIAAAK---LGAKKVLAVD--IDPQAVeaARENAEL---NGVELNVYLPQGDLK---ADVIVAN-- 186

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 802115983 185 yIAANdPhlvagdvrfepasalvaghdglddLRLIIKEAPAHLNAGGRLLLEhG--YDQAPAVRDLLLSEGFE 255
Cdd:PRK00517 187 -ILAN-P------------------------LLELAPDLARLLKPGGRLILS-GilEEQADEVLEAYEEAGFT 232
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
110-275 3.93e-07

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 50.17  E-value: 3.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 110 AKVLDLGTGSG--AIALALaseRPAWQVTAVDrvLEAVAL------AERNrqrlHL-NNATVLNShwfSALPGHTYDLII 180
Cdd:COG2264  150 KTVLDVGCGSGilAIAAAK---LGAKRVLAVD--IDPVAVeaarenAELN----GVeDRIEVVLG---DLLEDGPYDLVV 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 181 SNppyIAANdPhlvagdvrfepasalvaghdglddLRLIIKEAPAHLNAGGRL----LLEHgydQAPAVRDLLLSEGFeE 256
Cdd:COG2264  218 AN---ILAN-P------------------------LIELAPDLAALLKPGGYLilsgILEE---QADEVLAAYEAAGF-E 265

                        170
                 ....*....|....*....
gi 802115983 257 VHSRIDLGGHERITLGRRP 275
Cdd:COG2264  266 LVERRERGEWVALVLRKKA 284
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
106-256 6.69e-07

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 48.46  E-value: 6.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 106 PATPAKVLDLGTGSGAIALALASErpAWQVTAVDRVLEAVALAERNR--QRLHLNNATVLnshwfsALPGHTYDLIIsnp 183
Cdd:COG4976   44 PGPFGRVLDLGCGTGLLGEALRPR--GYRLTGVDLSEEMLAKAREKGvyDRLLVADLADL------AEPDGRFDLIV--- 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 184 pyiaandphlvagdvrfepaSALVAGHdgLDDLRLIIKEAPAHLNAGGRLLL-------EHGYDQAPA-VRDLLLSEGFE 255
Cdd:COG4976  113 --------------------AADVLTY--LGDLAAVFAGVARALKPGGLFIFsvedadgSGRYAHSLDyVRDLLAAAGFE 170


                 .
gi 802115983 256 E 256
Cdd:COG4976  171 V 171
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 106-181 8.98e-07

16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ribosomal structure and biogenesis]; 16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440126  Cd Length: 211  Bit Score: 48.61  E-value: 8.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 106 PATPAKVLDLGTGSG--AIALALAseRPAWQVTAVD------RVLEAVAlaernrQRLHLNNATVLNSHWFSALPGHTYD 177
Cdd:COG0357   65 PKEGARVLDVGSGAGfpGIPLAIA--RPDLQVTLVDslgkkiAFLREVV------RELGLKNVTVVHGRAEELAPREKFD 136


                 ....
gi 802115983 178 LIIS 181
Cdd:COG0357  137 VVTA 140
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 111-260 1.91e-06

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 47.57  E-value: 1.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 111 KVLDLGTGSGAIALALASeRPAWQVTAVDRVLEAVALAERNRQRLHLnNATVLNSHWFSALPGHTYDLIIsnppyiaand 190
Cdd:COG3897   73 RVLELGCGLGLVGIAAAK-AGAADVTATDYDPEALAALRLNAALNGV-AITTRLGDWRDPPAAGGFDLIL---------- 140

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 802115983 191 phlvAGDVRFEPASAlvaghdglDDLRLIIKeapAHLNAGGRLLLEH-GYDQAPAVRDLLLSEGFEEVHSR 260
Cdd:COG3897  141 ----GGDVLYERDLA--------EPLLPFLD---RLAAPGGEVLIGDpGRGYLPAFRERLEALAGYEVVTR 196
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
109-185 1.94e-06

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 47.23  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983  109 PAKVLDLGTGSGAIALALASeRPAWQVTAVDRVLEAVALAERNRQRLHLNNATVLNSHwFSALP-----GHTYDLIISNP 183
Cdd:pfam03602  42 GARVLDLFAGSGALGLEALS-RGAKRVTLVEKDKRAVQILKENLQLLGLPGAVLVMDA-LLALLrlagkGPVFDIVFLDP 119


                  ..
gi 802115983  184 PY 185
Cdd:pfam03602 120 PY 121
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
111-184 3.61e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 46.44  E-value: 3.61e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 802115983 111 KVLDLGTGSG--AIALALASerpAWQVTAVDRVLEAVALAERNRQRLHlNNATVLNSHWFSALPGHTYDLIISNPP 184
Cdd:COG2263   48 TVLDLGCGTGmlAIGAALLG---AKKVVGVDIDPEALEIARENAERLG-VRVDFIRADVTRIPLGGSVDTVVMNPP 119
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 112-162 7.94e-06

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: 46.70  E-value: 7.94e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 802115983 112 VLDLGTGSGAIALALASERPAWQVTAVDRVLEAVALAERNRQRLHLNNATV 162
Cdd:COG2242  251 LWDIGAGSGSVSIEAARLAPGGRVYAIERDPERAALIRANARRFGVPNVEV 301
GidB pfam02527
rRNA small subunit methyltransferase G; This is a family of bacterial glucose inhibited ...
 110-181 1.97e-05

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: 44.19  E-value: 1.97e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 802115983  110 AKVLDLGTGSGAIALALASERPAWQVTAVDRVLEAVALAERNRQRLHLNNATVLNSHWFSALPGHTYDLIIS 181
Cdd:pfam02527  50 DHVLDVGSGAGFPGIPLAIARPDKKVTLLESLLKKINFLEEVKSELGLDNVTIVHARAEEYQPEEQYDVITS 121
PRK07402 PRK07402
precorrin-6Y C5,15-methyltransferase subunit CbiT;
114-260 3.18e-05

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


Pssm-ID: 180961  Cd Length: 196  Bit Score: 43.83  E-value: 3.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 114 DLGTGSGAIALALASERPAWQVTAVDRVLEAVALAERNRQRLHLNNATVLNShwfSAlPGHTYDLiisnppyiaANDPHL 193
Cdd:PRK07402  46 DIGAGTGTIPVEAGLLCPKGRVIAIERDEEVVNLIRRNCDRFGVKNVEVIEG---SA-PECLAQL---------APAPDR 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 802115983 194 VagdvrfepasALVAGHdgldDLRLIIKEAPAHLNAGGRLL-----LEHGYDqapavrdllLSEGFEEVHSR 260
Cdd:PRK07402 113 V----------CIEGGR----PIKEILQAVWQYLKPGGRLVatassLEGLYA---------ISEGLAQLQAR 161
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 111-180 1.43e-04

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 41.61  E-value: 1.43e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 802115983 111 KVLDLGTGSG---AIALALASErpawqVTAVDRVLEAVALAERNRQRLHLNNATVLNSHWFSALPGH-TYDLII 180
Cdd:COG2518   69 RVLEIGTGSGyqaAVLARLAGR-----VYSVERDPELAERARERLAALGYDNVTVRVGDGALGWPEHaPFDRII 137
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 113-182 2.68e-04

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 39.19  E-value: 2.68e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 802115983  113 LDLGTGSGAIALALASERPawQVTAVDRVLEAVALAERNRQRLHLN----NATVLnshwfsALPGHTYDLIISN 182
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMLELAREKAPREGLTfvvgDAEDL------PFPDNSFDLVLSS 66
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 113-182 3.74e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 38.89  E-value: 3.74e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 802115983  113 LDLGTGSGAIALALASERPAWQVTAVDRVLEAVALAERNRQRLHLNNATVLNshWF----SALPGHTYDLIISN 182
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVRVE--LFqldlGELDPGSFDVVVAS 72
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 108-180 5.38e-04

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 39.62  E-value: 5.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983  108 TPAKVLDLGTGSGAIALALASERPAWQVTAVDRVlEAVALAERNRQRLHLNN---ATVLNshWFSALP-----GHTYDLI 179
Cdd:pfam10294  46 SGLNVLELGSGTGLVGIAVALLLPGASVTITDLE-EALELLKKNIELNALSSkvvVKVLD--WGENLPpdlfdGHPVDLI 122


                  .
gi 802115983  180 I 180
Cdd:pfam10294 123 L 123
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
110-181 6.03e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 40.40  E-value: 6.03e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 802115983 110 AKVLDLGTGSGAIALaLASERPAWQVTAVDRVLEAVALAERNRQRLHLN-NATVLNSHWFSALPGHTYDLIIS 181
Cdd:COG4076   37 DVVLDIGTGSGLLSM-LAARAGAKKVYAVEVNPDIAAVARRIIAANGLSdRITVINADATDLDLPEKADVIIS 108
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 108-255 6.87e-04

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: 40.33  E-value: 6.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983  108 TPAKVLDLGTGSGAIALAlASERPAWQVTAVDRVLEAVALAERNRQRLHLNNATVLNSHWfsALPGHTYDLIISNppyIA 187
Cdd:pfam06325 161 PGESVLDVGCGSGILAIA-ALKLGAKKVVGVDIDPVAVRAAKENAELNGVEARLEVYLPG--DLPKEKADVVVAN---IL 234

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983  188 AndphlvagdvrfepasalvaghdglDDLRLIIKEAPAHLNAGGRLLLEhGY--DQAPAVRDlLLSEGFE 255
Cdd:pfam06325 235 A-------------------------DPLIELAPDIYALVKPGGYLILS-GIlkEQAQMVAE-AYSQGFE 277
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 108-181 6.94e-04

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 40.31  E-value: 6.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 108 TPAKVLDLGTGSGAIALALASErpAWQVTAVD------RVLEAVALAErnrqRLHLNNATV-LNSHwfsALPGHtYDLII 180
Cdd:PRK12335 120 KPGKALDLGCGQGRNSLYLALL--GFDVTAVDinqqslENLQEIAEKE----NLNIRTGLYdINSA---SIQEE-YDFIL 189


                 .
gi 802115983 181 S 181
Cdd:PRK12335 190 S 190
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 108-182 1.42e-03

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 39.19  E-value: 1.42e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 802115983  108 TPAKVLDLGTGSGAIALALASERPAWQVTAVDRVLEAVALA-ERNRQRLH--LNNATVLNshwfsaLPGHTYDLIISN 182
Cdd:TIGR02072  34 IPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAkTKLSENVQfiCGDAEKLP------LEDSSFDLIVSN 105
arsM PRK11873
arsenite methyltransferase;
112-182 3.32e-03

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 38.01  E-value: 3.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 802115983 112 VLDLGTGSGAIALaLASER--PAWQVTAVDRVLEAVALAERNRQRLHLNNATVLNSHwFSALP--GHTYDLIISN 182
Cdd:PRK11873  81 VLDLGSGGGFDCF-LAARRvgPTGKVIGVDMTPEMLAKARANARKAGYTNVEFRLGE-IEALPvaDNSVDVIISN 153
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
110-162 3.62e-03

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 37.73  E-value: 3.62e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 802115983  110 AKVLDLGTGSGAIALALASE-RPAWQVTAVDRVLEAVALAERNRQRLHLNNATV 162
Cdd:pfam01135  75 MRVLEIGSGSGYLTACFARMvGEVGRVVSIEHIPELVEIARRNLEKLGLENVIV 128
PRK06202 PRK06202
hypothetical protein; Provisional
 106-182 5.14e-03

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 37.29  E-value: 5.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983 106 PATPAKVLDLGTGSGAIALALAserpAW--------QVTAVDRVLEAVALAERNRQRLHLNNATVLNSHWFSAlpGHTYD 177
Cdd:PRK06202  58 ADRPLTLLDIGCGGGDLAIDLA----RWarrdglrlEVTAIDPDPRAVAFARANPRRPGVTFRQAVSDELVAE--GERFD 131


                 ....*
gi 802115983 178 LIISN 182
Cdd:PRK06202 132 VVTSN 136
rADc smart00650
Ribosomal RNA adenine dimethylases;
106-185 6.51e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 36.72  E-value: 6.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802115983   106 PATPAKVLDLGTGSGAIALALAseRPAWQVTAV--DRVLEAVaLAER--NRQRLHLNNATVLNSHwfsaLPGHTYDLIIS 181
Cdd:smart00650  11 LRPGDTVLEIGPGKGALTEELL--ERAKRVTAIeiDPRLAPR-LREKfaAADNLTVIHGDALKFD----LPKLQPYKVVG 83


                   ....
gi 802115983   182 NPPY 185
Cdd:smart00650  84 NLPY 87
rumB PRK03522
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
109-184 6.80e-03

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


Pssm-ID: 235128 [Multi-domain]  Cd Length: 315  Bit Score: 37.54  E-value: 6.80e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 802115983 109 PAKVLDLGTGSGAIALALASerPAWQVTAVDRVLEAVALAERNRQRLHLNNAT--VLNSHWFSALPGHTYDLIISNPP 184
Cdd:PRK03522 174 PRSMWDLFCGVGGFGLHCAT--PGMQLTGIEISAEAIACAKQSAAELGLTNVQfqALDSTQFATAQGEVPDLVLVNPP 249
TehB pfam03848
Tellurite resistance protein TehB;
108-181 9.97e-03

Tellurite resistance protein TehB;


Pssm-ID: 397776  Cd Length: 193  Bit Score: 36.37  E-value: 9.97e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 802115983  108 TPAKVLDLGTGSGAIALALASErpAWQVTAVDRVLEAVALAERNRQRLHLNNATVLNSHWFSALPGHTYDLIIS 181
Cdd:pfam03848  30 KPGKVLDLGCGQGRNSLYLSLL--GYDVTAWDKNENSIANLQRIKEKENLDNIHTALYDINNATIDENYDFILS 101
 
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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