|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09328 |
PRK09328 |
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional |
3-288 |
3.68e-99 |
|
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
Pssm-ID: 236467 [Multi-domain] Cd Length: 275 Bit Score: 291.68 E-value: 3.68e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 3 CISVKEFLLWKKKQLSKggDQQSFEVLLDCLGDISTRDLnlkILNPKGNLhLKKNLEFLESVWEDHLIRsCPIQYLCGLT 82
Cdd:PRK09328 1 MMTIAEALREATARLAS--PRLDAELLLAHVLGLSRTDL---LLNPEEEL-TPEELERFRALVARRAAG-EPLQYILGEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 83 YWRDLKLKVTNKVLIPRPETELIVDIVFNIFRRKsEKLFFAELGTGSGAISIALALAYPFSKGVATDVDQDALEIATKNy 162
Cdd:PRK09328 74 EFWGLDFKVSPGVLIPRPETEELVEWALEALLLK-EPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRN- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 163 INSSKQSNLKFYCGNWWSPLENfkGKLDLAISNPPYIPKDTYEKLPKEVKNFEPKVALLGGEDGLKHIREIIQKAPIFLK 242
Cdd:PRK09328 152 AKHGLGARVEFLQGDWFEPLPG--GRFDLIVSNPPYIPEADIHLLQPEVRDHEPHLALFGGEDGLDFYRRIIEQAPRYLK 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 295421267 243 EKGWLILENHFDQGEKVKQLFIKNKFTSIEIVKDLSGIGRFTIGRY 288
Cdd:PRK09328 230 PGGWLLLEIGYDQGEAVRALLAAAGFADVETRKDLAGRDRVVLGRR 275
|
|
| HemK |
COG2890 |
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
5-289 |
1.88e-88 |
|
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 264.70 E-value: 1.88e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 5 SVKEFLLWKKKQLSKGGdqqSFEVLLDclgdisTRDLNLKILN-PKGNLHLKKNLEFLESVWE--DHLIRS----CPIQY 77
Cdd:COG2890 2 TIRELLRWAAARLAAAG---VDSARLE------AELLLAHVLGlDRADLLLHPDRPLTEEELArlEALVARraagEPLAY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 78 LCGLTYWRDLKLKVTNKVLIPRPETELIVDIVFNIFRrKSEKLFFAELGTGSGAISIALALAYPFSKGVATDVDQDALEI 157
Cdd:COG2890 73 ILGEAEFYGLEFKVDPGVLIPRPETEELVELALALLP-AGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 158 ATKNYINSSKQSNLKFYCGNWWSPLENfKGKLDLAISNPPYIPKDTYEKLPKEVKNFEPKVALLGGEDGLKHIREIIQKA 237
Cdd:COG2890 152 ARRNAERLGLEDRVRFLQGDLFEPLPG-DGRFDLIVSNPPYIPEDEIALLPPEVRDHEPRLALDGGEDGLDFYRRIIAQA 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 295421267 238 PIFLKEKGWLILENHFDQGEKVKQLFIKNKFTSIEIVKDLSGIGRFTIGRYK 289
Cdd:COG2890 231 PRLLKPGGWLLLEIGEDQGEAVRALLEAAGFADVETHKDLAGRDRVVVARRP 282
|
|
| RF_mod_PrmC |
TIGR03534 |
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ... |
39-285 |
2.19e-78 |
|
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: 238.14 E-value: 2.19e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 39 RDLNLKILN-PKGNLHLKKNLEFLESVWE--DHLI----RSCPIQYLCGLTYWRDLKLKVTNKVLIPRPETELIVDIVFN 111
Cdd:TIGR03534 3 ELLLAHVLGkDRAQLLLHPEDELTPEELAafDALLarraAGEPVAYILGEREFYGLDFKVSPGVLIPRPETEELVEAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 112 IFRRKSEklfFAELGTGSGAISIALALAYPFSKGVATDVDQDALEIATKNyINSSKQSNLKFYCGNWWSPLENfkGKLDL 191
Cdd:TIGR03534 83 RLKKGPR---VLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKN-ARRLGLENVEFLQGDWFEPLPS--GKFDL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 192 AISNPPYIPKDTYEKLPKEVKNFEPKVALLGGEDGLKHIREIIQKAPIFLKEKGWLILENHFDQGEKVKQLFIKNKFTSI 271
Cdd:TIGR03534 157 IVSNPPYIPEADIHLLDPEVRDFEPRLALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFEAAGFADV 236
|
250
....*....|....
gi 295421267 272 EIVKDLSGIGRFTI 285
Cdd:TIGR03534 237 ETRKDLAGKDRVVL 250
|
|
| MTS |
pfam05175 |
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ... |
123-253 |
3.62e-08 |
|
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: 51.82 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 123 AELGTGSGAISIALALAYPFSKGVATDVDQDALEIATKNYiNSSKQSNLKFYCGNWWSPLEnfKGKLDLAISNPPYipkd 202
Cdd:pfam05175 36 LDLGCGAGVLGAALAKESPDAELTMVDINARALESARENL-AANGLENGEVVASDVYSGVE--DGKFDLIISNPPF---- 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 295421267 203 tyeklpkevknfepkvaLLGGEDGLKHIREIIQKAPIFLKEKG-WLILENHF 253
Cdd:pfam05175 109 -----------------HAGLATTYNVAQRFIADAKRHLRPGGeLWIVANRF 143
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
122-200 |
1.33e-07 |
|
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).
Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 48.97 E-value: 1.33e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 295421267 122 FAELGTGSGAISIALAlAYPFSKGVATDVDQDALEIATKNYINsSKQSNLKFYCGNWWSPLENFKGKLDLAISNPPYIP 200
Cdd:cd02440 2 VLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAA-LLADNVEVLKGDAEELPPEADESFDVIISDPPLHH 78
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09328 |
PRK09328 |
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional |
3-288 |
3.68e-99 |
|
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
Pssm-ID: 236467 [Multi-domain] Cd Length: 275 Bit Score: 291.68 E-value: 3.68e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 3 CISVKEFLLWKKKQLSKggDQQSFEVLLDCLGDISTRDLnlkILNPKGNLhLKKNLEFLESVWEDHLIRsCPIQYLCGLT 82
Cdd:PRK09328 1 MMTIAEALREATARLAS--PRLDAELLLAHVLGLSRTDL---LLNPEEEL-TPEELERFRALVARRAAG-EPLQYILGEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 83 YWRDLKLKVTNKVLIPRPETELIVDIVFNIFRRKsEKLFFAELGTGSGAISIALALAYPFSKGVATDVDQDALEIATKNy 162
Cdd:PRK09328 74 EFWGLDFKVSPGVLIPRPETEELVEWALEALLLK-EPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRN- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 163 INSSKQSNLKFYCGNWWSPLENfkGKLDLAISNPPYIPKDTYEKLPKEVKNFEPKVALLGGEDGLKHIREIIQKAPIFLK 242
Cdd:PRK09328 152 AKHGLGARVEFLQGDWFEPLPG--GRFDLIVSNPPYIPEADIHLLQPEVRDHEPHLALFGGEDGLDFYRRIIEQAPRYLK 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 295421267 243 EKGWLILENHFDQGEKVKQLFIKNKFTSIEIVKDLSGIGRFTIGRY 288
Cdd:PRK09328 230 PGGWLLLEIGYDQGEAVRALLAAAGFADVETRKDLAGRDRVVLGRR 275
|
|
| HemK |
COG2890 |
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
5-289 |
1.88e-88 |
|
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 264.70 E-value: 1.88e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 5 SVKEFLLWKKKQLSKGGdqqSFEVLLDclgdisTRDLNLKILN-PKGNLHLKKNLEFLESVWE--DHLIRS----CPIQY 77
Cdd:COG2890 2 TIRELLRWAAARLAAAG---VDSARLE------AELLLAHVLGlDRADLLLHPDRPLTEEELArlEALVARraagEPLAY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 78 LCGLTYWRDLKLKVTNKVLIPRPETELIVDIVFNIFRrKSEKLFFAELGTGSGAISIALALAYPFSKGVATDVDQDALEI 157
Cdd:COG2890 73 ILGEAEFYGLEFKVDPGVLIPRPETEELVELALALLP-AGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 158 ATKNYINSSKQSNLKFYCGNWWSPLENfKGKLDLAISNPPYIPKDTYEKLPKEVKNFEPKVALLGGEDGLKHIREIIQKA 237
Cdd:COG2890 152 ARRNAERLGLEDRVRFLQGDLFEPLPG-DGRFDLIVSNPPYIPEDEIALLPPEVRDHEPRLALDGGEDGLDFYRRIIAQA 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 295421267 238 PIFLKEKGWLILENHFDQGEKVKQLFIKNKFTSIEIVKDLSGIGRFTIGRYK 289
Cdd:COG2890 231 PRLLKPGGWLLLEIGEDQGEAVRALLEAAGFADVETHKDLAGRDRVVVARRP 282
|
|
| RF_mod_PrmC |
TIGR03534 |
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ... |
39-285 |
2.19e-78 |
|
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: 238.14 E-value: 2.19e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 39 RDLNLKILN-PKGNLHLKKNLEFLESVWE--DHLI----RSCPIQYLCGLTYWRDLKLKVTNKVLIPRPETELIVDIVFN 111
Cdd:TIGR03534 3 ELLLAHVLGkDRAQLLLHPEDELTPEELAafDALLarraAGEPVAYILGEREFYGLDFKVSPGVLIPRPETEELVEAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 112 IFRRKSEklfFAELGTGSGAISIALALAYPFSKGVATDVDQDALEIATKNyINSSKQSNLKFYCGNWWSPLENfkGKLDL 191
Cdd:TIGR03534 83 RLKKGPR---VLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKN-ARRLGLENVEFLQGDWFEPLPS--GKFDL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 192 AISNPPYIPKDTYEKLPKEVKNFEPKVALLGGEDGLKHIREIIQKAPIFLKEKGWLILENHFDQGEKVKQLFIKNKFTSI 271
Cdd:TIGR03534 157 IVSNPPYIPEADIHLLDPEVRDFEPRLALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFEAAGFADV 236
|
250
....*....|....
gi 295421267 272 EIVKDLSGIGRFTI 285
Cdd:TIGR03534 237 ETRKDLAGKDRVVL 250
|
|
| hemK_fam |
TIGR00536 |
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ... |
5-289 |
1.21e-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: 183.71 E-value: 1.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 5 SVKEFLLWKKKQLSKGGDQQSF----EVLLDClgdistrDLNLKILNPKGNLHLKKNLEFLESVWE--DHLIRSCPIQYL 78
Cdd:TIGR00536 2 TIQEFLRWASSALSRAIARENPwleaLLLLEH-------DLGRERDLLLAFLTEELTPDEKERIFRlvLRRVKGVPVAYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 79 CGLTYWRDLKLKVTNKVLIPRPETELIVDIVFNIFRRKSEKLFFAELGTGSGAISIALALAYPFSKGVATDVDQDALEIA 158
Cdd:TIGR00536 75 LGSKEFYGLEFFVNEHVLIPRPETEELVEKALASLISQPPILHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 159 TKNYINSSKQSNLKFYCGNWWSPLEnfKGKLDLAISNPPYIPKDTYEKLPKEVKnFEPKVALLGGEDGLKHIREIIQKAP 238
Cdd:TIGR00536 155 EENAEKNQLEHRVEFIQSNLFEPLA--GQKIDIIVSNPPYIDEEDLADLPNVVR-FEPLLALVGGDDGLNILRQIIELAP 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 295421267 239 IFLKEKGWLILENHFDQ-GEKVKQLFIKNKFTSIEIVKDLSGIGRFTIGRYK 289
Cdd:TIGR00536 232 DYLKPNGFLVCEIGNWQqKSLKELLRIKFTWYDVENGRDLNGKERVVLGFYH 283
|
|
| PRK14966 |
PRK14966 |
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; ... |
74-288 |
1.42e-38 |
|
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; Provisional
Pssm-ID: 184930 [Multi-domain] Cd Length: 423 Bit Score: 140.22 E-value: 1.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 74 PIQYLCGltyWRDL---KLKVTNKVLIPRPETELIVDIVFnifRRKSEKLFFAELGTGSGAISIALALAYPFSKGVATDV 150
Cdd:PRK14966 210 PVAYILG---VREFygrRFAVNPNVLIPRPETEHLVEAVL---ARLPENGRVWDLGTGSGAVAVTVALERPDAFVRASDI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 151 DQDALEIATKNYINSSkqSNLKFYCGNWWSPLENFKGKLDLAISNPPYIpKDTYEKLPKEVKNFEPKVALLGGEDGLKHI 230
Cdd:PRK14966 284 SPPALETARKNAADLG--ARVEFAHGSWFDTDMPSEGKWDIIVSNPPYI-ENGDKHLLQGDLRFEPQIALTDFSDGLSCI 360
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 295421267 231 REIIQKAPIFLKEKGWLILENHFDQGEKVKQLFIKNKFTSIEIVKDLSGIGRFTIGRY 288
Cdd:PRK14966 361 RTLAQGAPDRLAEGGFLLLEHGFDQGAAVRGVLAENGFSGVETLPDLAGLDRVTLGKY 418
|
|
| PRK01544 |
PRK01544 |
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ... |
74-282 |
1.60e-34 |
|
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) methyltransferase; Reviewed
Pssm-ID: 234958 [Multi-domain] Cd Length: 506 Bit Score: 130.76 E-value: 1.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 74 PIQYLCGLTYWRDLKLKVTNKVLIPRPETELIVDIVFNIFRRKS-----------------------EKLFFAELGTGSG 130
Cdd:PRK01544 71 PIAYITGVKEFYSREFIVNKHVLIPRSDTEVLVDVVFQCHSRESgnpekkqlnpcfrgndissncndKFLNILELGTGSG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 131 AISIALALAYPFSKGVATDVDQDALEIATKNYINSSKQSNLKFYCGNWWSPLEnfKGKLDLAISNPPYIPKDTYEKLPKE 210
Cdd:PRK01544 151 CIAISLLCELPNANVIATDISLDAIEVAKSNAIKYEVTDRIQIIHSNWFENIE--KQKFDFIVSNPPYISHSEKSEMAIE 228
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 295421267 211 VKNFEPKVALLGGEDGLKHIREIIQKAPIFLKEKGWLILENHFDQGEKVKQLFIKNKFTSIEIVKDLSGIGR 282
Cdd:PRK01544 229 TINYEPSIALFAEEDGLQAYFIIAENAKQFLKPNGKIILEIGFKQEEAVTQIFLDHGYNIESVYKDLQGHSR 300
|
|
| PRK14968 |
PRK14968 |
putative methyltransferase; Provisional |
94-278 |
6.10e-19 |
|
putative methyltransferase; Provisional
Pssm-ID: 237872 [Multi-domain] Cd Length: 188 Bit Score: 82.25 E-value: 6.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 94 KVLIPRPETELIVDivfNIFRRKSEKLFfaELGTGSGAISIALALAYpfSKGVATDVDQDALEIATKNY-INSSKQSNLK 172
Cdd:PRK14968 4 EVYEPAEDSFLLAE---NAVDKKGDRVL--EVGTGSGIVAIVAAKNG--KKVVGVDINPYAVECAKCNAkLNNIRNNGVE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 173 FYCGNWwspLENFKG-KLDLAISNPPYIPKDTYEKLPKEVknfepKVALLGGEDGLKHIREIIQKAPIFLKEKG-WLILE 250
Cdd:PRK14968 77 VIRSDL---FEPFRGdKFDVILFNPPYLPTEEEEEWDDWL-----NYALSGGKDGREVIDRFLDEVGRYLKPGGrILLLQ 148
|
170 180
....*....|....*....|....*...
gi 295421267 251 NHFDQGEKVKQLFIKNKFtSIEIVKDLS 278
Cdd:PRK14968 149 SSLTGEDEVLEYLEKLGF-EAEVVAEEK 175
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
124-273 |
1.21e-14 |
|
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: 71.71 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 124 ELGTGSGAISIALALAYPFSKGVATDVDQDALEIATKNYINSSKQSNLKFYCG---NWWSPLENfkGKLDLAISNPPYIP 200
Cdd:COG4123 43 DLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGdlkEFAAELPP--GSFDLVVSNPPYFK 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295421267 201 KDTYEKLPKEVKNfepkVALlgGEDGLKHiREIIQKAPIFLKEKGWLILENHFDQGEKVKQLFIKNKFTSIEI 273
Cdd:COG4123 121 AGSGRKSPDEARA----IAR--HEDALTL-EDLIRAAARLLKPGGRFALIHPAERLAEILAALRKYGLGPKRL 186
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
122-275 |
1.60e-10 |
|
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: 59.05 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 122 FAELGTGSGAISIALALAYPFSKGVATDVDQDALEIATKNYINsSKQSNLKFYCGNWWSPLENfkGKLDLAISNPPYipk 201
Cdd:COG2813 53 VLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAA-NGLENVEVLWSDGLSGVPD--GSFDLILSNPPF--- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 202 dtyeklpkevknfepKVallgGEDGLKHI-REIIQKAPIFLKEKGWL------------ILENHFDQGEKVKQlfiKNKF 268
Cdd:COG2813 127 ---------------HA----GRAVDKEVaHALIADAARHLRPGGELwlvanrhlpyerKLEELFGNVEVLAR---NKGF 184
|
....*..
gi 295421267 269 TSIEIVK 275
Cdd:COG2813 185 KVLRAVK 191
|
|
| hemK_rel_arch |
TIGR00537 |
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ... |
124-249 |
4.65e-10 |
|
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: 57.56 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 124 ELGTGSGAISIALAlaypfSKG---VATDVDQDALEIATKNYINSSKqsNLKFYCGNWWSPLEnfkGKLDLAISNPPYIP 200
Cdd:TIGR00537 25 EIGAGTGLVAIRLK-----GKGkciLTTDINPFAVKELRENAKLNNV--GLDVVMTDLFKGVR---GKFDVILFNPPYLP 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 295421267 201 KDTYEKLpKEVKNFepkvALLGGEDGLKHIREIIQKAPIFLKEKGWLIL 249
Cdd:TIGR00537 95 LEDDLRR-GDWLDV----AIDGGKDGRKVIDRFLDELPEILKEGGRVQL 138
|
|
| MTS |
pfam05175 |
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ... |
123-253 |
3.62e-08 |
|
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: 51.82 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 123 AELGTGSGAISIALALAYPFSKGVATDVDQDALEIATKNYiNSSKQSNLKFYCGNWWSPLEnfKGKLDLAISNPPYipkd 202
Cdd:pfam05175 36 LDLGCGAGVLGAALAKESPDAELTMVDINARALESARENL-AANGLENGEVVASDVYSGVE--DGKFDLIISNPPF---- 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 295421267 203 tyeklpkevknfepkvaLLGGEDGLKHIREIIQKAPIFLKEKG-WLILENHF 253
Cdd:pfam05175 109 -----------------HAGLATTYNVAQRFIADAKRHLRPGGeLWIVANRF 143
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
122-200 |
1.33e-07 |
|
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).
Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 48.97 E-value: 1.33e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 295421267 122 FAELGTGSGAISIALAlAYPFSKGVATDVDQDALEIATKNYINsSKQSNLKFYCGNWWSPLENFKGKLDLAISNPPYIP 200
Cdd:cd02440 2 VLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAA-LLADNVEVLKGDAEELPPEADESFDVIISDPPLHH 78
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
106-255 |
9.12e-06 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 45.68 E-value: 9.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 106 VDIVFNIFRRKSEKLFFAELGTGSGAISIALALAYpFSKGVATDVDQDALEIATKNYiNSSKQSNLKFYCGNWWSPLENF 185
Cdd:COG0500 14 LAALLALLERLPKGGRVLDLGCGTGRNLLALAARF-GGRVIGIDLSPEAIALARARA-AKAGLGNVEFLVADLAELDPLP 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295421267 186 KGKLDLAISNppyipkDTYEKLPKEVknfepkvallgGEDGLKHIREIiqkapifLKEKGWLILENHFDQ 255
Cdd:COG0500 92 AESFDLVVAF------GVLHHLPPEE-----------REALLRELARA-------LKPGGVLLLSASDAA 137
|
|
| COG2263 |
COG2263 |
Predicted RNA methylase [General function prediction only]; |
123-197 |
1.14e-05 |
|
Predicted RNA methylase [General function prediction only];
Pssm-ID: 441864 [Multi-domain] Cd Length: 199 Bit Score: 45.28 E-value: 1.14e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 295421267 123 AELGTGSGAISIALALAYPfSKGVATDVDQDALEIATKNYinSSKQSNLKFYCGNWWSPleNFKGKLDLAISNPP 197
Cdd:COG2263 50 LDLGCGTGMLAIGAALLGA-KKVVGVDIDPEALEIARENA--ERLGVRVDFIRADVTRI--PLGGSVDTVVMNPP 119
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
124-195 |
1.45e-05 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 42.89 E-value: 1.45e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 295421267 124 ELGTGSGAISIALALAYPFSKGVATDVDQDALEIATKNYinsskqSNLKFYCGNW--WSPLENFkgklDLAISN 195
Cdd:COG4106 7 DLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARL------PNVRFVVADLrdLDPPEPF----DLVVSN 70
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
124-195 |
3.97e-04 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 38.70 E-value: 3.97e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295421267 124 ELGTGSGAISIALALAYPFsKGVATDVDQDALEIATKNYinSSKQSNLKFYCGNWWS-PLENfkGKLDLAISN 195
Cdd:pfam13649 3 DLGCGTGRLTLALARRGGA-RVTGVDLSPEMLERARERA--AEAGLNVEFVQGDAEDlPFPD--GSFDLVVSS 70
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
124-195 |
9.37e-04 |
|
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: 38.82 E-value: 9.37e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295421267 124 ELGTGSGAISIALALAypFSKGVATDVDQDALEIATKNYinSSKQSNLKFYCGNWWS-PLENfkGKLDLAISN 195
Cdd:COG2226 28 DLGCGTGRLALALAER--GARVTGVDISPEMLELARERA--AEAGLNVEFVVGDAEDlPFPD--GSFDLVISS 94
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
124-195 |
4.85e-03 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 35.81 E-value: 4.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 295421267 124 ELGTGSGAISIALALAYPFSKGVATDVDQDALEIAtKNYINSSKQSNLKFYCGNWWSPLENFKGKLDLAISN 195
Cdd:pfam08242 2 EIGCGTGTLLRALLEALPGLEYTGLDISPAALEAA-RERLAALGLLNAVRVELFQLDLGELDPGSFDVVVAS 72
|
|
| GlyDH-like |
cd08171 |
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
196-239 |
5.11e-03 |
|
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341450 Cd Length: 345 Bit Score: 37.89 E-value: 5.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 295421267 196 PPY-IPKDTYEKLPKEVKNFEPKVALLGGEDGL----KHIREIIQKAPI 239
Cdd:cd08171 2 PSYtIGEDAYDAIPKICSPYGKKVVVIGGKKALaaakPKLRAALEGSGL 50
|
|
| Gcd14 |
COG2519 |
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ... |
124-161 |
7.61e-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: 7.61e-03
10 20 30
....*....|....*....|....*....|....*....
gi 295421267 124 ELGTGSGAISIALALA-YPFSKGVATDVDQDALEIATKN 161
Cdd:COG2519 97 EAGTGSGALTLALARAvGPEGKVYSYERREDFAEIARKN 135
|
|
| |
