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Conserved domains on  [gi|1085761850|emb|SDS54537|]
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release factor glutamine methyltransferase [Formosa sp. Hel1_31_208]

Protein Classification

N5-glutamine methyltransferase family protein( domain architecture ID 11458394)

N5-glutamine methyltransferase family protein such as peptide chain release factor N(5)-glutamine methyltransferase, which modifies the glutamine residue in the universally conserved glycylglycylglutamine (GGQ) motif of peptide chain release factor, resulting in almost complete loss of release activity

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 1-289 3.81e-103

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


:

Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 302.07  E-value: 3.81e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850   1 MRLKAILHIYHTELDSlYGNNEVDSFFNLVVEHYLGIKRIHLVMDPEYAILKTEEQPIFEALSALKLEQPIQYILGETEF 80
Cdd:COG2890     1 MTIRELLRWAAARLAA-AGVDSARLEAELLLAHVLGLDRADLLLHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850  81 YGLPFKVNSETLIPRPETEELVALILDDVSSitiDTPLKIIDIGTGSGCIAISLAKQLQQAKVSALDVSEAALKVAKRNA 160
Cdd:COG2890    80 YGLEFKVDPGVLIPRPETEELVELALALLPA---GAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 161 EMNTVD--IEFICNDILNPrhntrVFASNSYDIIVSNPPYIRNLEKEEITSNVLDYEPHLALFvEDKNPLQFYKAICEFA 238
Cdd:COG2890   157 ERLGLEdrVRFLQGDLFEP-----LPGDGRFDLIVSNPPYIPEDEIALLPPEVRDHEPRLALD-GGEDGLDFYRRIIAQA 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1085761850 239 LLNLKDSGTLYFEINEYLGAEMIALMKNFGFKDVALKTDIFGKDRIIKGIK 289
Cdd:COG2890   231 PRLLKPGGWLLLEIGEDQGEAVRALLEAAGFADVETHKDLAGRDRVVVARR 281
 
Name Accession Description Interval E-value
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 1-289 3.81e-103

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 302.07  E-value: 3.81e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850   1 MRLKAILHIYHTELDSlYGNNEVDSFFNLVVEHYLGIKRIHLVMDPEYAILKTEEQPIFEALSALKLEQPIQYILGETEF 80
Cdd:COG2890     1 MTIRELLRWAAARLAA-AGVDSARLEAELLLAHVLGLDRADLLLHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850  81 YGLPFKVNSETLIPRPETEELVALILDDVSSitiDTPLKIIDIGTGSGCIAISLAKQLQQAKVSALDVSEAALKVAKRNA 160
Cdd:COG2890    80 YGLEFKVDPGVLIPRPETEELVELALALLPA---GAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 161 EMNTVD--IEFICNDILNPrhntrVFASNSYDIIVSNPPYIRNLEKEEITSNVLDYEPHLALFvEDKNPLQFYKAICEFA 238
Cdd:COG2890   157 ERLGLEdrVRFLQGDLFEP-----LPGDGRFDLIVSNPPYIPEDEIALLPPEVRDHEPRLALD-GGEDGLDFYRRIIAQA 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1085761850 239 LLNLKDSGTLYFEINEYLGAEMIALMKNFGFKDVALKTDIFGKDRIIKGIK 289
Cdd:COG2890   231 PRLLKPGGWLLLEIGEDQGEAVRALLEAAGFADVETHKDLAGRDRVVVARR 281
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 29-289 2.56e-91

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 272.04  E-value: 2.56e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850  29 LVVEHYLGIKRIHLVMDPEYAILKTEEQPIFEALSALKLEQPIQYILGETEFYGLPFKVNSETLIPRPETEELVALILDD 108
Cdd:PRK09328   24 LLLAHVLGLSRTDLLLNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFWGLDFKVSPGVLIPRPETEELVEWALEA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 109 VSSitiDTPLKIIDIGTGSGCIAISLAKQLQQAKVSALDVSEAALKVAKRNAE-MNTVDIEFICNDILNPrhntrvFASN 187
Cdd:PRK09328  104 LLL---KEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKhGLGARVEFLQGDWFEP------LPGG 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 188 SYDIIVSNPPYIRNLEKEEITSNVLDYEPHLALFvEDKNPLQFYKAICEFALLNLKDSGTLYFEINEYLGAEMIALMKNF 267
Cdd:PRK09328  175 RFDLIVSNPPYIPEADIHLLQPEVRDHEPHLALF-GGEDGLDFYRRIIEQAPRYLKPGGWLLLEIGYDQGEAVRALLAAA 253

                         250       260
                  ....*....|....*....|..
gi 1085761850 268 GFKDVALKTDIFGKDRIIKGIK 289
Cdd:PRK09328  254 GFADVETRKDLAGRDRVVLGRR 275
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 29-285 1.58e-87

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: 261.25  E-value: 1.58e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850  29 LVVEHYLGIKRIHLVMDPEYAILKTEEQPIFEALSALKLEQPIQYILGETEFYGLPFKVNSETLIPRPETEELVALILDD 108
Cdd:TIGR03534   4 LLLAHVLGKDRAQLLLHPEDELTPEELAAFDALLARRAAGEPVAYILGEREFYGLDFKVSPGVLIPRPETEELVEAALER 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 109 VSSITidtplKIIDIGTGSGCIAISLAKQLQQAKVSALDVSEAALKVAKRNAEMNTVD-IEFICNDILNPrhntrvFASN 187
Cdd:TIGR03534  84 LKKGP-----RVLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKNARRLGLEnVEFLQGDWFEP------LPSG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 188 SYDIIVSNPPYIRNLEKEEITSNVLDYEPHLALFvEDKNPLQFYKAICEFALLNLKDSGTLYFEINEYLGAEMIALMKNF 267
Cdd:TIGR03534 153 KFDLIVSNPPYIPEADIHLLDPEVRDFEPRLALF-GGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFEAA 231

                         250
                  ....*....|....*...
gi 1085761850 268 GFKDVALKTDIFGKDRII 285
Cdd:TIGR03534 232 GFADVETRKDLAGKDRVV 249
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 120-195 4.26e-15

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 69.51  E-value: 4.26e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1085761850 120 IIDIGTGSGCIAISLAKQLQqAKVSALDVSEAALKVAKRNAEMNTVDIEFICNDILNPRhntrvFASNSYDIIVSN 195
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG-ARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLP-----FPDGSFDLVVSS 70
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 119-203 4.06e-11

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 58.98  E-value: 4.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 119 KIIDIGTGSGCIAISLAKQLqQAKVSALDVSEAALKVAKRNAEMNTVD-IEFICNDILNPRHntrvFASNSYDIIVSNPP 197
Cdd:cd02440     1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALELARKAAAALLADnVEVLKGDAEELPP----EADESFDVIISDPP 75


                  ....*.
gi 1085761850 198 YIRNLE 203
Cdd:cd02440    76 LHHLVE 81
 
Name Accession Description Interval E-value
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 1-289 3.81e-103

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 302.07  E-value: 3.81e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850   1 MRLKAILHIYHTELDSlYGNNEVDSFFNLVVEHYLGIKRIHLVMDPEYAILKTEEQPIFEALSALKLEQPIQYILGETEF 80
Cdd:COG2890     1 MTIRELLRWAAARLAA-AGVDSARLEAELLLAHVLGLDRADLLLHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850  81 YGLPFKVNSETLIPRPETEELVALILDDVSSitiDTPLKIIDIGTGSGCIAISLAKQLQQAKVSALDVSEAALKVAKRNA 160
Cdd:COG2890    80 YGLEFKVDPGVLIPRPETEELVELALALLPA---GAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 161 EMNTVD--IEFICNDILNPrhntrVFASNSYDIIVSNPPYIRNLEKEEITSNVLDYEPHLALFvEDKNPLQFYKAICEFA 238
Cdd:COG2890   157 ERLGLEdrVRFLQGDLFEP-----LPGDGRFDLIVSNPPYIPEDEIALLPPEVRDHEPRLALD-GGEDGLDFYRRIIAQA 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1085761850 239 LLNLKDSGTLYFEINEYLGAEMIALMKNFGFKDVALKTDIFGKDRIIKGIK 289
Cdd:COG2890   231 PRLLKPGGWLLLEIGEDQGEAVRALLEAAGFADVETHKDLAGRDRVVVARR 281
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 29-289 2.56e-91

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 272.04  E-value: 2.56e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850  29 LVVEHYLGIKRIHLVMDPEYAILKTEEQPIFEALSALKLEQPIQYILGETEFYGLPFKVNSETLIPRPETEELVALILDD 108
Cdd:PRK09328   24 LLLAHVLGLSRTDLLLNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFWGLDFKVSPGVLIPRPETEELVEWALEA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 109 VSSitiDTPLKIIDIGTGSGCIAISLAKQLQQAKVSALDVSEAALKVAKRNAE-MNTVDIEFICNDILNPrhntrvFASN 187
Cdd:PRK09328  104 LLL---KEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKhGLGARVEFLQGDWFEP------LPGG 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 188 SYDIIVSNPPYIRNLEKEEITSNVLDYEPHLALFvEDKNPLQFYKAICEFALLNLKDSGTLYFEINEYLGAEMIALMKNF 267
Cdd:PRK09328  175 RFDLIVSNPPYIPEADIHLLQPEVRDHEPHLALF-GGEDGLDFYRRIIEQAPRYLKPGGWLLLEIGYDQGEAVRALLAAA 253

                         250       260
                  ....*....|....*....|..
gi 1085761850 268 GFKDVALKTDIFGKDRIIKGIK 289
Cdd:PRK09328  254 GFADVETRKDLAGRDRVVLGRR 275
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 29-285 1.58e-87

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: 261.25  E-value: 1.58e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850  29 LVVEHYLGIKRIHLVMDPEYAILKTEEQPIFEALSALKLEQPIQYILGETEFYGLPFKVNSETLIPRPETEELVALILDD 108
Cdd:TIGR03534   4 LLLAHVLGKDRAQLLLHPEDELTPEELAAFDALLARRAAGEPVAYILGEREFYGLDFKVSPGVLIPRPETEELVEAALER 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 109 VSSITidtplKIIDIGTGSGCIAISLAKQLQQAKVSALDVSEAALKVAKRNAEMNTVD-IEFICNDILNPrhntrvFASN 187
Cdd:TIGR03534  84 LKKGP-----RVLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKNARRLGLEnVEFLQGDWFEP------LPSG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 188 SYDIIVSNPPYIRNLEKEEITSNVLDYEPHLALFvEDKNPLQFYKAICEFALLNLKDSGTLYFEINEYLGAEMIALMKNF 267
Cdd:TIGR03534 153 KFDLIVSNPPYIPEADIHLLDPEVRDFEPRLALF-GGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFEAA 231

                         250
                  ....*....|....*...
gi 1085761850 268 GFKDVALKTDIFGKDRII 285
Cdd:TIGR03534 232 GFADVETRKDLAGKDRVV 249
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 29-289 3.21e-56

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: 182.55  E-value: 3.21e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850  29 LVVEHYLGIKRIHLVMDPEYAILKTEEQPIFEALSALKLEQPIQYILGETEFYGLPFKVNSETLIPRPETEELVALILDD 108
Cdd:TIGR00536  29 LLLEHDLGRERDLLLAFLTEELTPDEKERIFRLVLRRVKGVPVAYLLGSKEFYGLEFFVNEHVLIPRPETEELVEKALAS 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 109 VSSitIDTPLKIIDIGTGSGCIAISLAKQLQQAKVSALDVSEAALKVAKRNAEMNTV--DIEFICNDILNPrhntrvFAS 186
Cdd:TIGR00536 109 LIS--QPPILHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQLehRVEFIQSNLFEP------LAG 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 187 NSYDIIVSNPPYIRNlEKEEITSNVLDYEPHLALFVEDKNpLQFYKAICEFALLNLKDSGTLYFEIneylGAEMIALMKN 266
Cdd:TIGR00536 181 QKIDIIVSNPPYIDE-EDLADLPNVVRFEPLLALVGGDDG-LNILRQIIELAPDYLKPNGFLVCEI----GNWQQKSLKE 254

                         250       260
                  ....*....|....*....|....*...
gi 1085761850 267 FGFK-----DVALKTDIFGKDRIIKGIK 289
Cdd:TIGR00536 255 LLRIkftwyDVENGRDLNGKERVVLGFY 282
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
 41-285 5.29e-34

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


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 129.21  E-value: 5.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850  41 HLVMDP-EYAILKTEEQ------PIFEALSALKLE-QPIQYILGETEFYGLPFKVNSETLIPRPETEELVALIL------ 106
Cdd:PRK01544   34 HVINKPiEYLLINLDEQlneaeiEAFEKLLERRLKhEPIAYITGVKEFYSREFIVNKHVLIPRSDTEVLVDVVFqchsre 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 107 ---------------DDVSSITIDTPLKIIDIGTGSGCIAISLAKQLQQAKVSALDVSEAALKVAKRNAemntvdIEFIC 171
Cdd:PRK01544  114 sgnpekkqlnpcfrgNDISSNCNDKFLNILELGTGSGCIAISLLCELPNANVIATDISLDAIEVAKSNA------IKYEV 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 172 NDILNPRHNT--RVFASNSYDIIVSNPPYIRNLEKEEITSNVLDYEPHLALFVEdKNPLQFYKAICEFALLNLKDSGTLY 249
Cdd:PRK01544  188 TDRIQIIHSNwfENIEKQKFDFIVSNPPYISHSEKSEMAIETINYEPSIALFAE-EDGLQAYFIIAENAKQFLKPNGKII 266

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1085761850 250 FEINEYLGAEMIALMKNFGFKDVALKTDIFGKDRII 285
Cdd:PRK01544  267 LEIGFKQEEAVTQIFLDHGYNIESVYKDLQGHSRVI 302
PRK14966 PRK14966
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; ...
 69-287 1.31e-28

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


Pssm-ID: 184930 [Multi-domain]  Cd Length: 423  Bit Score: 113.25  E-value: 1.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850  69 QPIQYILGETEFYGLPFKVNSETLIPRPETEELVALILDDVSSITidtplKIIDIGTGSGCIAISLAKQLQQAKVSALDV 148
Cdd:PRK14966  209 EPVAYILGVREFYGRRFAVNPNVLIPRPETEHLVEAVLARLPENG-----RVWDLGTGSGAVAVTVALERPDAFVRASDI 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 149 SEAALKVAKRNAEMNTVDIEFICNDILnprhNTRVFASNSYDIIVSNPPYIRNLEKeEITSNVLDYEPHLALfVEDKNPL 228
Cdd:PRK14966  284 SPPALETARKNAADLGARVEFAHGSWF----DTDMPSEGKWDIIVSNPPYIENGDK-HLLQGDLRFEPQIAL-TDFSDGL 357

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1085761850 229 QFYKAICEFALLNLKDSGTLYFEINEYLGAEMIALMKNFGFKDVALKTDIFGKDRIIKG 287
Cdd:PRK14966  358 SCIRTLAQGAPDRLAEGGFLLLEHGFDQGAAVRGVLAENGFSGVETLPDLAGLDRVTLG 416
L3_gln_methyl TIGR03533
protein-(glutamine-N5) methyltransferase, ribosomal protein L3-specific; Members of this ...
 70-267 1.89e-27

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: 107.60  E-value: 1.89e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850  70 PIQYILGETEFYGLPFKVNSETLIPRPETEELVALILDDVssITIDTPLKIIDIGTGSGCIAISLAKQLQQAKVSALDVS 149
Cdd:TIGR03533  77 PVAYLTNEAWFAGLEFYVDERVLIPRSPIAELIEDGFAPW--LEPEPVKRILDLCTGSGCIAIACAYAFPEAEVDAVDIS 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 150 EAALKVAKRNAEMNTVD--IEFICNDILNPRHNTRvfasnsYDIIVSNPPYIrnlEKEEITSNVLDY--EPHLALFVEDk 225
Cdd:TIGR03533 155 PDALAVAEINIERHGLEdrVTLIQSDLFAALPGRK------YDLIVSNPPYV---DAEDMADLPAEYhhEPELALASGE- 224

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1085761850 226 NPLQFYKAICEFALLNLKDSGTLYFEIneylGAEMIALMKNF 267
Cdd:TIGR03533 225 DGLDLVRRILAEAADHLNENGVLVVEV----GNSMEALEEAY 262
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 112-269 2.84e-19

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: 84.43  E-value: 2.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 112 ITIDTPLKIIDIGTGSGCIAISLAKQLQQAKVSALDVSEAALKVAKRNAEMNTVD--IEFICNDILNPRhntRVFASNSY 189
Cdd:COG4123    33 APVKKGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLEdrITVIHGDLKEFA---AELPPGSF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 190 DIIVSNPPYiRNLEKEEITSNvldyePHLAL-FVEDKNPLQfykAICEFALLNLKDSGTLYFEINEYLGAEMIALMKNFG 268
Cdd:COG4123   110 DLVVSNPPY-FKAGSGRKSPD-----EARAIaRHEDALTLE---DLIRAAARLLKPGGRFALIHPAERLAEILAALRKYG 180


                  .
gi 1085761850 269 F 269
Cdd:COG4123   181 L 181
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 113-268 1.30e-17

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: 78.69  E-value: 1.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 113 TIDTPL--KIIDIGTGSGCIAISLAKQLQQAKVSALDVSEAALKVAKRNAEMNTVD-IEFICNDILNPrhntrvFASNSY 189
Cdd:COG2813    44 HLPEPLggRVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAANGLEnVEVLWSDGLSG------VPDGSF 117

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085761850 190 DIIVSNPPyIRnlekeeiTSNVLDYEPHLALFVEdknplqfykaicefALLNLKDSGTLYFEINEYLGAEmIALMKNFG 268
Cdd:COG2813   118 DLILSNPP-FH-------AGRAVDKEVAHALIAD--------------AARHLRPGGELWLVANRHLPYE-RKLEELFG 173
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 120-195 4.26e-15

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 69.51  E-value: 4.26e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1085761850 120 IIDIGTGSGCIAISLAKQLQqAKVSALDVSEAALKVAKRNAEMNTVDIEFICNDILNPRhntrvFASNSYDIIVSN 195
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG-ARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLP-----FPDGSFDLVVSS 70
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 113-279 2.59e-14

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: 69.16  E-value: 2.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 113 TIDTPL--KIIDIGTGSGCIAISLAKQLQQAKVSALDVSEAALKVAKRNAEMNTVD-IEFICNDILNPrhntrvFASNSY 189
Cdd:pfam05175  26 HLPKDLsgKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGLEnGEVVASDVYSG------VEDGKF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 190 DIIVSNPPyIRnlEKEEITSNVLDyephlalfvedknplqfykAICEFALLNLKDSGTLYFEINEYLGAEMIaLMKNFGF 269
Cdd:pfam05175 100 DLIISNPP-FH--AGLATTYNVAQ-------------------RFIADAKRHLRPGGELWIVANRFLGYPPL-LEELFGN 156

                         170
                  ....*....|
gi 1085761850 270 KDVALKTDIF 279
Cdd:pfam05175 157 VEVVAKTNGF 166
PRK14968 PRK14968
putative methyltransferase; Provisional
 119-214 3.72e-13

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 66.46  E-value: 3.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 119 KIIDIGTGSGCIAISLAKqlQQAKVSALDVSEAALKVAKRNAEMNTV---DIEFICNDILNPrhntrvFASNSYDIIVSN 195
Cdd:PRK14968   26 RVLEVGTGSGIVAIVAAK--NGKKVVGVDINPYAVECAKCNAKLNNIrnnGVEVIRSDLFEP------FRGDKFDVILFN 97

                          90
                  ....*....|....*....
gi 1085761850 196 PPYIRNLEKEEITSNvLDY 214
Cdd:PRK14968   98 PPYLPTEEEEEWDDW-LNY 115
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 109-270 4.61e-13

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: 65.02  E-value: 4.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 109 VSSITIDTPLKIIDIGTGSGCIAISLAKQlqQAKVSALDVSEAALKVAKRNAEMNTVDIEFICNDILN-PrhntrvFASN 187
Cdd:COG2226    15 LAALGLRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDlP------FPDG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 188 SYDIIVSNppyirnlekeeitsNVLDYEPHLAlfvedknplqfyKAICEFALLnLKDSGTLYF-EINEYLGAEMIALMKN 266
Cdd:COG2226    87 SFDLVISS--------------FVLHHLPDPE------------RALAEIARV-LKPGGRLVVvDFSPPDLAELEELLAE 139


                  ....
gi 1085761850 267 FGFK 270
Cdd:COG2226   140 AGFE 143
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 114-251 4.75e-12

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: 61.96  E-value: 4.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 114 IDTPLKIIDIGTGSGCIAISLAKqlQQAKVSALDVSEAALKVAKRNAEmnTVDIEFICNDILNPrhntrVFASNSYDIIV 193
Cdd:COG2227    22 LPAGGRVLDVGCGTGRLALALAR--RGADVTGVDISPEALEIARERAA--ELNVDFVQGDLEDL-----PLEDGSFDLVI 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1085761850 194 SNppyirnlekeeitsNVLdyePHLAlfvedkNPLQFYKAICEFallnLKDSGTLYFE 251
Cdd:COG2227    93 CS--------------EVL---EHLP------DPAALLRELARL----LKPGGLLLLS 123
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
119-197 5.72e-12

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 63.38  E-value: 5.72e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085761850 119 KIIDIGTGSGCIAIsLAKQLQQAKVSALDVSEAALKVAKRNAEMNTVDIEFICNDIlnprhnTRVFASNSYDIIVSNPP 197
Cdd:COG2263    48 TVLDLGCGTGMLAI-GAALLGAKKVVGVDIDPEALEIARENAERLGVRVDFIRADV------TRIPLGGSVDTVVMNPP 119
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 119-203 4.06e-11

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 58.98  E-value: 4.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 119 KIIDIGTGSGCIAISLAKQLqQAKVSALDVSEAALKVAKRNAEMNTVD-IEFICNDILNPRHntrvFASNSYDIIVSNPP 197
Cdd:cd02440     1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALELARKAAAALLADnVEVLKGDAEELPP----EADESFDVIISDPP 75


                  ....*.
gi 1085761850 198 YIRNLE 203
Cdd:cd02440    76 LHHLVE 81
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
117-195 5.50e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 55.21  E-value: 5.50e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085761850 117 PLKIIDIGTGSGCIAISLAKQLQQAKVSALDVSEAALKVAKRNAEmntvDIEFICNDILNPRhntrvfASNSYDIIVSN 195
Cdd:COG4106     2 PRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLP----NVRFVVADLRDLD------PPEPFDLVVSN 70
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
119-219 5.25e-09

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 55.95  E-value: 5.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 119 KIIDIGTGSGCIAIsLAKQLQQAKVSALDVSEAALKVAKRNAEMNTVD--IEFICNDILNPRHntrvfasnsYDIIVSNp 196
Cdd:COG2264   151 TVLDVGCGSGILAI-AAAKLGAKRVLAVDIDPVAVEAARENAELNGVEdrIEVVLGDLLEDGP---------YDLVVAN- 219

                          90       100
                  ....*....|....*....|....*...
gi 1085761850 197 pyirnlekeeITSNVL-----DYEPHLA 219
Cdd:COG2264   220 ----------ILANPLielapDLAALLK 237
PRK14967 PRK14967
putative methyltransferase; Provisional
 95-199 7.91e-09

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 54.67  E-value: 7.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850  95 RPETEELvaLILDDVSSITIDTPLKIIDIGTGSGCIAISlAKQLQQAKVSALDVSEAALKVAKRNAEMNTVDIEFICNDI 174
Cdd:PRK14967   17 RPQEDTQ--LLADALAAEGLGPGRRVLDLCTGSGALAVA-AAAAGAGSVTAVDISRRAVRSARLNALLAGVDVDVRRGDW 93

                          90       100
                  ....*....|....*....|....*
gi 1085761850 175 lnprhnTRVFASNSYDIIVSNPPYI 199
Cdd:PRK14967   94 ------ARAVEFRPFDVVVSNPPYV 112
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
113-198 8.22e-09

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


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 55.71  E-value: 8.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 113 TIDTPL--KIIDIGTGSGCIAISLAKQLQQAKVSALDVSEAALKVAKRNAEMNTVDIEficndilnprhntrVFASNSY- 189
Cdd:PRK09489  191 TLTPHTkgKVLDVGCGAGVLSAVLARHSPKIRLTLSDVSAAALESSRATLAANGLEGE--------------VFASNVFs 256

                          90
                  ....*....|....*
gi 1085761850 190 ------DIIVSNPPY 198
Cdd:PRK09489  257 dikgrfDMIISNPPF 271
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 114-195 5.60e-08

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 50.88  E-value: 5.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 114 IDTPLKIIDIGTGSGCIAISLAKQL-QQAKVSALDVSEAALKVAKRNAEMNTVD-IEFICNDILnprHNTRVFASNSYDI 191
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEELgPNAEVVGIDISEEAIEKARENAQKLGFDnVEFEQGDIE---ELPELLEDDKFDV 77


                  ....
gi 1085761850 192 IVSN 195
Cdd:pfam13847  78 VISN 81
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 68-197 6.49e-08

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


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 52.87  E-value: 6.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850  68 EQPIQYILGETEFYGLP---FKVNSETliprpeTEELVALILDDVSSITIDTplkIIDIGTGSGCIAISLAKqlQQAKVS 144
Cdd:COG2265   191 RDYLTERLGGLTFRISPgsfFQVNPEQ------AEALYAAALEWLDLTGGER---VLDLYCGVGTFALPLAR--RAKKVI 259

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1085761850 145 ALDVSEAALKVAKRNAEMNTVD-IEFICND---ILnprhnTRVFASNSYDIIVSNPP 197
Cdd:COG2265   260 GVEIVPEAVEDARENARLNGLKnVEFVAGDleeVL-----PELLWGGRPDVVVLDPP 311
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 121-195 2.03e-07

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 48.04  E-value: 2.03e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1085761850 121 IDIGTGSGCIAISLAKQLqqAKVSALDVSEAALKVAKRNAemNTVDIEFICNDILN-PrhntrvFASNSYDIIVSN 195
Cdd:pfam08241   1 LDVGCGTGLLTELLARLG--ARVTGVDISPEMLELAREKA--PREGLTFVVGDAEDlP------FPDNSFDLVLSS 66
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 119-195 2.36e-07

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: 51.11  E-value: 2.36e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1085761850 119 KIIDIGTGSGCIAISLAKqLQQAKVSALDVSEAALKVAKRNAEMNTVdieficNDILNPRHNTRVFASNsYDIIVSN 195
Cdd:pfam06325 164 SVLDVGCGSGILAIAALK-LGAKKVVGVDIDPVAVRAAKENAELNGV------EARLEVYLPGDLPKEK-ADVVVAN 232
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 119-192 2.93e-07

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 50.15  E-value: 2.93e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085761850 119 KIIDIGTGSGCIAISLAKQLQ-QAKVSALDVSEAALKVAKRNAEMNTVD--IEFICNDILN-PrhntrvFASNSYDII 192
Cdd:PRK00216   54 KVLDLACGTGDLAIALAKAVGkTGEVVGLDFSEGMLAVGREKLRDLGLSgnVEFVQGDAEAlP------FPDNSFDAV 125
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 115-264 4.91e-07

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 49.14  E-value: 4.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 115 DTPLKIIDIGTGSGCIAISLAKQLqQAKVSALDVSEAALKVAKRNAEMNTVD-IEFICNDILNPRHntrvFASNSYDIIV 193
Cdd:COG0500    25 PKGGRVLDLGCGTGRNLLALAARF-GGRVIGIDLSPEAIALARARAAKAGLGnVEFLVADLAELDP----LPAESFDLVV 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1085761850 194 SNppyirnlekeeitsNVLDYEPHLALfvedknplqfyKAICEFALLNLKDSGTLYFEINEYLGAEMIALM 264
Cdd:COG0500   100 AF--------------GVLHHLPPEER-----------EALLRELARALKPGGVLLLSASDAAAALSLARL 145
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 100-195 8.10e-07

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: 49.21  E-value: 8.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 100 ELVALILDdvssITIDTPLKIIDIGTGSGCIAISLAKQLQQAKVSALDVSEAALKVAKRNaemNTVDIEFICNDIlnprh 179
Cdd:TIGR02072  22 RLLALLKE----KGIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTK---LSENVQFICGDA----- 89

                          90
                  ....*....|....*.
gi 1085761850 180 NTRVFASNSYDIIVSN 195
Cdd:TIGR02072  90 EKLPLEDSSFDLIVSN 105
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
117-195 9.51e-07

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 48.99  E-value: 9.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 117 PLKIIDIGTGSGCIAIsLAKQLQQAKVSALDVSEAALKVAKRNAEMNTVDieficndilnprHNTRVFASN-SYDIIVSN 195
Cdd:PRK00517  120 GKTVLDVGCGSGILAI-AAAKLGAKKVLAVDIDPQAVEAARENAELNGVE------------LNVYLPQGDlKADVIVAN 186
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 119-194 1.30e-06

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 47.23  E-value: 1.30e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085761850 119 KIIDIGTGSGCIAISLAKQLqQAKVSALDVSEAALKVAKRNAEMNTVD--IEFICNDILNprhntrVFASNSYDIIVS 194
Cdd:COG2230    54 RVLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAEAGLAdrVEVRLADYRD------LPADGQFDAIVS 124
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 121-195 3.63e-06

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 44.67  E-value: 3.63e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085761850 121 IDIGTGSGCIAISLAKQLQQAKVSALDVSEAALKVAK----RNAEMNTVDIEFICNDILNPrhntrvfASNSYDIIVSN 195
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARerlaALGLLNAVRVELFQLDLGEL-------DPGSFDVVVAS 72
PrmC_N pfam17827
PrmC N-terminal domain; This entry corresponds to the N-terminal alpha helical domain of the ...
 29-76 4.99e-06

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: 43.62  E-value: 4.99e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1085761850  29 LVVEHYLGIKRIHLVMDPEYAILKTEEQPIFEALSALKLEQPIQYILG 76
Cdd:pfam17827  24 LLLAHVLGLDRTDLLLHPEEELSEEELERFEELLERRAAGEPLQYILG 71
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 120-239 1.41e-05

Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 44.65  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 120 IIDIGTGSGCIAISLA-----------KQLQQAKVSALDVSEAALKVAKRNAEMNTVD--IEFICNDILNPRhntrvFAS 186
Cdd:pfam01170  32 LLDPMCGSGTILIEAAlmganiapgkfDARVRAPLYGSDIDRRMVQGARLNAENAGVGdlIEFVQADAADLP-----LLE 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1085761850 187 NSYDIIVSNPPYIRNL----EKEEITSNVLD-YEPHL-------ALFVEDKNplqFYKAICEFAL 239
Cdd:pfam01170 107 GSVDVIVTNPPYGIRLgskgALEALYPEFLReAKRVLrgggwlvLLTAENKD---FEKAARERAW 168
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
119-194 1.54e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 45.03  E-value: 1.54e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085761850 119 KIIDIGTGSGCIAIsLAKQLQQAKVSALDVSEAALKVAKRNAEMNTVD--IEFICNDILNPRHNTRVfasnsyDIIVS 194
Cdd:COG4076    38 VVLDIGTGSGLLSM-LAARAGAKKVYAVEVNPDIAAVARRIIAANGLSdrITVINADATDLDLPEKA------DVIIS 108
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 119-166 3.16e-05

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: 42.70  E-value: 3.16e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1085761850 119 KIIDIGTGSGCIAISLAKQLQQAKVSALDVSEAALKVAKRNAEMNTVD 166
Cdd:TIGR02469  22 VLWDIGAGTGSVTIEAARLVPNGRVYAIERNPEALDLIERNLRRFGVS 69
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 120-161 3.44e-05

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: 44.77  E-value: 3.44e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1085761850 120 IIDIGTGSGCIAISLAKQLQQAKVSALDVSEAALKVAKRNAE 161
Cdd:COG2242   251 LWDIGAGSGSVSIEAARLAPGGRVYAIERDPERAALIRANAR 292
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
109-200 3.95e-05

Adenine-specific DNA N6-methylase [Replication, recombination and repair];


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 44.55  E-value: 3.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 109 VSSITIDTPLKIIDIGTGSGCIAISLAKQLQ-QAKVSALDVSEAALKVAKRNAEMNTVDIEFICNDILNPRHNtrvfasN 187
Cdd:COG0827   108 VEKFTKKEGLRILDPAVGTGNLLTTVLNQLKkKVNAYGVEVDDLLIRLAAVLANLQGHPVELFHQDALQPLLI------D 181

                          90
                  ....*....|...
gi 1085761850 188 SYDIIVSNPPYIR 200
Cdd:COG0827   182 PVDVVISDLPVGY 194
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
99-269 5.09e-05

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 43.06  E-value: 5.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850  99 EELVALILDDVSsitIDTPLKIIDIGTGSGCIAISLAKQlqQAKVSALDVSEAALKVAKRNAemntVDIEFICNDILNPR 178
Cdd:COG4976    32 ALLAEELLARLP---PGPFGRVLDLGCGTGLLGEALRPR--GYRLTGVDLSEEMLAKAREKG----VYDRLLVADLADLA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 179 hntrvFASNSYDIIVSnppyirnlekeeitSNVLDYEPHLALFvedknplqfykaiceFALL--NLKDSGTLYFEINE-- 254
Cdd:COG4976   103 -----EPDGRFDLIVA--------------ADVLTYLGDLAAV---------------FAGVarALKPGGLFIFSVEDad 148

                         170       180
                  ....*....|....*....|.
gi 1085761850 255 ------YLGAEMIALMKNFGF 269
Cdd:COG4976   149 gsgryaHSLDYVRDLLAAAGF 169
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 141-250 5.58e-05

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


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 44.02  E-value: 5.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 141 AKVSALDVSEAALKVAKRNAEMNTVD--IEFICNDilnprhntrVFA--------SNSYDIIVSNPP-YIRNleKEEIts 209
Cdd:COG1092   240 KSVTSVDLSATALEWAKENAALNGLDdrHEFVQAD---------AFDwlrelareGERFDLIILDPPaFAKS--KKDL-- 306

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1085761850 210 nvldyephlalfvedKNPLQFYKAICEFALLNLKDSGTLYF 250
Cdd:COG1092   307 ---------------FDAQRDYKDLNRLALKLLAPGGILVT 332
PRK06202 PRK06202
hypothetical protein; Provisional
 115-195 5.71e-05

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 43.45  E-value: 5.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 115 DTPLKIIDIGTGSGCIAISLAKQLQ----QAKVSALDVSEAALKVAKRNAEMNTVDIEFICNDILnprhntrVFASNSYD 190
Cdd:PRK06202   59 DRPLTLLDIGCGGGDLAIDLARWARrdglRLEVTAIDPDPRAVAFARANPRRPGVTFRQAVSDEL-------VAEGERFD 131


                  ....*
gi 1085761850 191 IIVSN 195
Cdd:PRK06202  132 VVTSN 136
PRK15001 PRK15001
23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;
119-211 1.29e-04

23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;


Pssm-ID: 184963 [Multi-domain]  Cd Length: 378  Bit Score: 43.09  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 119 KIIDIGTGSGCIAISLAKQLQQAKVSALDVSEAALKVAKRNAEMNTVDI----EFICNDILNPRHNTRvfasnsYDIIVS 194
Cdd:PRK15001  231 EIVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNMPEAldrcEFMINNALSGVEPFR------FNAVLC 304

                          90
                  ....*....|....*..
gi 1085761850 195 NPPYirnLEKEEITSNV 211
Cdd:PRK15001  305 NPPF---HQQHALTDNV 318
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 131-207 2.13e-04

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


Pssm-ID: 439886 [Multi-domain]  Cd Length: 369  Bit Score: 42.40  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 131 AISLAKQLQQAKVSALDVSEAALKVAKRNAEMNTVD--IEFICNDILNPRhntrvfASNSYDIIVSNPPY-IRNLEKEEI 207
Cdd:COG0116   241 AEARIKRDPPLPIFGSDIDPRAIEAARENAERAGVAdlIEFEQADFRDLE------PPAEPGLIITNPPYgERLGEEEEL 314
PRK08317 PRK08317
hypothetical protein; Provisional
 119-194 2.58e-04

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 41.46  E-value: 2.58e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085761850 119 KIIDIGTGSGCIAISLAKQL-QQAKVSALDVSEAALKVAKRNAEMNTVDIEFICNDILN-PrhntrvFASNSYDIIVS 194
Cdd:PRK08317   22 RVLDVGCGPGNDARELARRVgPEGRVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGlP------FPDGSFDAVRS 93
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 74-161 2.71e-04

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 41.77  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850  74 ILGETEfyglpfKVNSETLIPR---PETEELVALILDDVSSITIDTplkIIDIGTGSGCIAISLAkqLQQAKVSALDVSE 150
Cdd:PLN02585  108 IYGETD------EVNKVQLDIRlghAQTVEKVLLWLAEDGSLAGVT---VCDAGCGTGSLAIPLA--LEGAIVSASDISA 176

                          90
                  ....*....|.
gi 1085761850 151 AALKVAKRNAE 161
Cdd:PLN02585  177 AMVAEAERRAK 187
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 118-171 6.17e-04

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 40.87  E-value: 6.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1085761850 118 LKIIDIGTGSGCIAISLAKqlQQAKVSALDVSEAALKVAKRNAEMN--TVDIEFIC 171
Cdd:PLN02396  133 LKFIDIGCGGGLLSEPLAR--MGATVTGVDAVDKNVKIARLHADMDpvTSTIEYLC 186
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
 120-159 1.04e-03

D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related alcohol dehydrogenases. AraDH is a member of the medium chain dehydrogenase/reductase family and catalyzes the NAD(P)-dependent oxidation of D-arabinose and other pentoses, the initial step in the metabolism of d-arabinose into 2-oxoglutarate. Like the alcohol dehydrogenases, AraDH binds a zinc in the catalytic cleft as well as a distal structural zinc. AraDH forms homotetramers as a dimer of dimers. AraDH replaces a conserved catalytic His with replace with Arg, compared to the canonical ADH site. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176187 [Multi-domain]  Cd Length: 340  Bit Score: 40.24  E-value: 1.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1085761850 120 IIDIGtGSGCIAISLAKQLQQAKVSALDVSEAALKVAKRN 159
Cdd:cd05284   173 VIGVG-GLGHIAVQILRALTPATVIAVDRSEEALKLAERL 211
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
 115-166 1.09e-03

6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the zinc-dependent alcohol dehydrogenase-like family of medium chain dehydrogenases/reductases catalyzes the conversion of 6-hydroxyhexanoate and NAD(+) to 6-oxohexanoate + NADH and H+. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176202 [Multi-domain]  Cd Length: 350  Bit Score: 39.91  E-value: 1.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1085761850 115 DTPLKIIDIGtGSGCIAISLAKQLQQAKVSALDVSEAALKVAKRNAEMNTVD 166
Cdd:cd08240   176 DEPVVIIGAG-GLGLMALALLKALGPANIIVVDIDEAKLEAAKAAGADVVVN 226
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 109-194 1.90e-03

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 39.18  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 109 VSSITIDTPLKIIDIGT--GSGCIAISlakQLQQAKVSALDVSEAALKVAK-RNAEMNTvdIEFICNDILnprhnTRVFA 185
Cdd:PTZ00098   45 LSDIELNENSKVLDIGSglGGGCKYIN---EKYGAHVHGVDICEKMVNIAKlRNSDKNK--IEFEANDIL-----KKDFP 114


                  ....*....
gi 1085761850 186 SNSYDIIVS 194
Cdd:PTZ00098  115 ENTFDMIYS 123
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 116-174 2.27e-03

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 38.66  E-value: 2.27e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1085761850 116 TPLKIIDIGTGSGCIAISLAKQlqQAKVSALDVSEAALKVAKRNAEMNTVD--IEFICNDI 174
Cdd:PRK07580   63 TGLRILDAGCGVGSLSIPLARR--GAKVVASDISPQMVEEARERAPEAGLAgnITFEVGDL 121
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 120-213 3.91e-03

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: 37.24  E-value: 3.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 120 IIDIGTGSGCIAISLAkqLQQAKVSALDVSEAALKVAKRNAE-MNTVDIEFICNDILNPRhntrvFASNSYDIIVSNPPY 198
Cdd:COG1041    30 VLDPFCGTGTILIEAG--LLGRRVIGSDIDPKMVEGARENLEhYGYEDADVIRGDARDLP-----LADESVDAIVTDPPY 102

                          90       100
                  ....*....|....*....|
gi 1085761850 199 -----IRNLEKEEITSNVLD 213
Cdd:COG1041   103 grsskISGEELLELYEKALE 122
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
115-171 5.29e-03

tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;


Pssm-ID: 182918  Cd Length: 255  Bit Score: 37.64  E-value: 5.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1085761850 115 DTPLKIIDIGTGSGCIAISLAKQLQQakVSALDVSEAALKVAKRNAEMNTV--DIEFIC 171
Cdd:PRK11036   43 PRPLRVLDAGGGEGQTAIKLAELGHQ--VILCDLSAEMIQRAKQAAEAKGVsdNMQFIH 99
Methyltransf_10 pfam05971
RNA methyltransferase; This family includes ribosomal RNA large subunit methyltransferase F, ...
 110-202 5.43e-03

RNA methyltransferase; This family includes ribosomal RNA large subunit methyltransferase F, and related proteins, including methyltransferase-like protein 16 (METTL16). METTL16 is a conserved RNA methyltransferase which interacts specifically with the MALAT1 triple helix. METTL16 shows nuclear localization. Another functional study indicates that METTL16 regulates expression of human MAT2A, which encodes the SAM synthetase expressed in most cells. Furthermore, results indicate that METTL16 is the long-unknown methyltransferase for the U6 spliceosomal small nuclear RNA (snRNA) and it has evolved an additional function in vertebrates to control SAM homeostasis by post-transcriptionally regulating SAM synthetase gene expression.


Pssm-ID: 399160 [Multi-domain]  Cd Length: 291  Bit Score: 37.88  E-value: 5.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085761850 110 SSITIDTPLKIIDIGTGSGCIAISLAKQLQQAKVSALDVSEAALKVAKRNAEMNTVDIEFI-CNDILNPRH--NTRVFAS 186
Cdd:pfam05971  96 QDSDIPTLRRALDIGTGANCIYPLLGVTEYGWRFVGSEVDPQSLNSAKAIVESNPNLSDAIeLRRQPQSTLifNGLIGEN 175

                          90
                  ....*....|....*.
gi 1085761850 187 NSYDIIVSNPPYIRNL 202
Cdd:pfam05971 176 ERYDFTLCNPPFHASL 191
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
96-159 8.23e-03

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


Pssm-ID: 181354  Cd Length: 187  Bit Score: 36.52  E-value: 8.23e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1085761850  96 PETEELV-ALILDDVSsitIDTPLKIIDIGTGSGCIAISLAKQLQQAKVSALDVSEAALKVAKRN 159
Cdd:PRK08287   13 PMTKEEVrALALSKLE---LHRAKHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKEN 74
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 119-162 8.48e-03

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


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 37.06  E-value: 8.48e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1085761850 119 KIIDIGTGSGCIAISLAKQL-QQAKVSALDVSEAALKVAKRNAEM 162
Cdd:COG2519    94 RVLEAGTGSGALTLALARAVgPEGKVYSYERREDFAEIARKNLER 138
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 116-166 9.11e-03

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: 36.16  E-value: 9.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1085761850 116 TPLKIIDIGTGSGCIAISLAKQLQQAKVSALDVSEaALKVAKRNAEMNTVD 166
Cdd:pfam10294  46 SGLNVLELGSGTGLVGIAVALLLPGASVTITDLEE-ALELLKKNIELNALS 95
 
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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