|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09328 |
PRK09328 |
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional |
1-276 |
3.08e-128 |
|
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
Pssm-ID: 236467 [Multi-domain] Cd Length: 275 Bit Score: 365.25 E-value: 3.08e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 1 MLSIKEATKNISQQLttvsKTPRLDAELLLECVLKKSRADLFAYPEIQLNSSQQKTLSAYVKRRLKGEPIAYILGQKEFW 80
Cdd:PRK09328 1 MMTIAEALREATARL----ASPRLDAELLLAHVLGLSRTDLLLNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 81 SLNLKVTPDVLIPRPETEMLVEWILKNLPKDEKLRIADLGTGSGAVALAIAVERPHWTIDATDNSQAALKIAEINAKQHE 160
Cdd:PRK09328 77 GLDFKVSPGVLIPRPETEELVEWALEALLLKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 161 IKNCNFYHGEWCQALPRRDYHAIVGNPPYIPDKDQHLQQ---LKHEPREALAAGSDGLSAIKIIIHEAKSYLVNGGWLLL 237
Cdd:PRK09328 157 GARVEFLQGDWFEPLPGGRFDLIVSNPPYIPEADIHLLQpevRDHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGWLLL 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 499261028 238 EHGYDQAEKIMTLMQADGYREITDRRDLAGLSRMMVARR 276
Cdd:PRK09328 237 EIGYDQGEAVRALLAAAGFADVETRKDLAGRDRVVLGRR 275
|
|
| HemK |
COG2890 |
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
3-276 |
2.94e-125 |
|
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 357.92 E-value: 2.94e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 3 SIKEATKNISQQLTTV-SKTPRLDAELLLECVLKKSRADLFAYPEIQLNSSQQKTLSAYVKRRLKGEPIAYILGQKEFWS 81
Cdd:COG2890 2 TIRELLRWAAARLAAAgVDSARLEAELLLAHVLGLDRADLLLHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 82 LNLKVTPDVLIPRPETEMLVEWILKNLPKDEKLRIADLGTGSGAVALAIAVERPHWTIDATDNSQAALKIAEINAKQHEI 161
Cdd:COG2890 82 LEFKVDPGVLIPRPETEELVELALALLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 162 KN-CNFYHGEWCQALP-RRDYHAIVGNPPYIPDKDQHLQQ---LKHEPREALAAGSDGLSAIKIIIHEAKSYLVNGGWLL 236
Cdd:COG2890 162 EDrVRFLQGDLFEPLPgDGRFDLIVSNPPYIPEDEIALLPpevRDHEPRLALDGGEDGLDFYRRIIAQAPRLLKPGGWLL 241
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 499261028 237 LEHGYDQAEKIMTLMQADGYREITDRRDLAGLSRMMVARR 276
Cdd:COG2890 242 LEIGEDQGEAVRALLEAAGFADVETHKDLAGRDRVVVARR 281
|
|
| RF_mod_PrmC |
TIGR03534 |
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ... |
25-273 |
2.47e-122 |
|
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: 349.08 E-value: 2.47e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 25 DAELLLECVLKKSRADLFAYPEIQLNSSQQKTLSAYVKRRLKGEPIAYILGQKEFWSLNLKVTPDVLIPRPETEMLVEWI 104
Cdd:TIGR03534 1 DAELLLAHVLGKDRAQLLLHPEDELTPEELAAFDALLARRAAGEPVAYILGEREFYGLDFKVSPGVLIPRPETEELVEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 105 LKNLPKDEklRIADLGTGSGAVALAIAVERPHWTIDATDNSQAALKIAEINAKQHEIKNCNFYHGEWCQALPRRDYHAIV 184
Cdd:TIGR03534 81 LERLKKGP--RVLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKNARRLGLENVEFLQGDWFEPLPSGKFDLIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 185 GNPPYIPDKDQHLQQ---LKHEPREALAAGSDGLSAIKIIIHEAKSYLVNGGWLLLEHGYDQAEKIMTLMQADGYREITD 261
Cdd:TIGR03534 159 SNPPYIPEADIHLLDpevRDFEPRLALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFEAAGFADVET 238
|
250
....*....|..
gi 499261028 262 RRDLAGLSRMMV 273
Cdd:TIGR03534 239 RKDLAGKDRVVL 250
|
|
| MTS |
pfam05175 |
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ... |
105-237 |
2.24e-19 |
|
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: 82.64 E-value: 2.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 105 LKNLPKDEKLRIADLGTGSGAVALAIAVERPHWTIDATDNSQAALKIAEINAKQHEIKNCNFYHGEWCQALPRRDYHAIV 184
Cdd:pfam05175 24 LEHLPKDLSGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGLENGEVVASDVYSGVEDGKFDLII 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 499261028 185 GNPPYipdkdqhlqqlkHEPREalaagsDGLSAIKIIIHEAKSYLVNGGWLLL 237
Cdd:pfam05175 104 SNPPF------------HAGLA------TTYNVAQRFIADAKRHLRPGGELWI 138
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
115-238 |
1.25e-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: 60.14 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 115 RIADLGTGSGAVALAIAvERPHWTIDATDNSQAALKIAEINAKQHEIKNCNFYHGEWCQALPRRD--YHAIVGNPPYipd 192
Cdd:cd02440 1 RVLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADesFDVIISDPPL--- 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 499261028 193 kdQHLQQLKHEprealaagsdglsaikiIIHEAKSYLVNGGWLLLE 238
Cdd:cd02440 77 --HHLVEDLAR-----------------FLEEARRLLKPGGVLVLT 103
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09328 |
PRK09328 |
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional |
1-276 |
3.08e-128 |
|
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
Pssm-ID: 236467 [Multi-domain] Cd Length: 275 Bit Score: 365.25 E-value: 3.08e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 1 MLSIKEATKNISQQLttvsKTPRLDAELLLECVLKKSRADLFAYPEIQLNSSQQKTLSAYVKRRLKGEPIAYILGQKEFW 80
Cdd:PRK09328 1 MMTIAEALREATARL----ASPRLDAELLLAHVLGLSRTDLLLNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 81 SLNLKVTPDVLIPRPETEMLVEWILKNLPKDEKLRIADLGTGSGAVALAIAVERPHWTIDATDNSQAALKIAEINAKQHE 160
Cdd:PRK09328 77 GLDFKVSPGVLIPRPETEELVEWALEALLLKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 161 IKNCNFYHGEWCQALPRRDYHAIVGNPPYIPDKDQHLQQ---LKHEPREALAAGSDGLSAIKIIIHEAKSYLVNGGWLLL 237
Cdd:PRK09328 157 GARVEFLQGDWFEPLPGGRFDLIVSNPPYIPEADIHLLQpevRDHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGWLLL 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 499261028 238 EHGYDQAEKIMTLMQADGYREITDRRDLAGLSRMMVARR 276
Cdd:PRK09328 237 EIGYDQGEAVRALLAAAGFADVETRKDLAGRDRVVLGRR 275
|
|
| HemK |
COG2890 |
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
3-276 |
2.94e-125 |
|
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 357.92 E-value: 2.94e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 3 SIKEATKNISQQLTTV-SKTPRLDAELLLECVLKKSRADLFAYPEIQLNSSQQKTLSAYVKRRLKGEPIAYILGQKEFWS 81
Cdd:COG2890 2 TIRELLRWAAARLAAAgVDSARLEAELLLAHVLGLDRADLLLHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 82 LNLKVTPDVLIPRPETEMLVEWILKNLPKDEKLRIADLGTGSGAVALAIAVERPHWTIDATDNSQAALKIAEINAKQHEI 161
Cdd:COG2890 82 LEFKVDPGVLIPRPETEELVELALALLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 162 KN-CNFYHGEWCQALP-RRDYHAIVGNPPYIPDKDQHLQQ---LKHEPREALAAGSDGLSAIKIIIHEAKSYLVNGGWLL 236
Cdd:COG2890 162 EDrVRFLQGDLFEPLPgDGRFDLIVSNPPYIPEDEIALLPpevRDHEPRLALDGGEDGLDFYRRIIAQAPRLLKPGGWLL 241
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 499261028 237 LEHGYDQAEKIMTLMQADGYREITDRRDLAGLSRMMVARR 276
Cdd:COG2890 242 LEIGEDQGEAVRALLEAAGFADVETHKDLAGRDRVVVARR 281
|
|
| RF_mod_PrmC |
TIGR03534 |
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ... |
25-273 |
2.47e-122 |
|
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: 349.08 E-value: 2.47e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 25 DAELLLECVLKKSRADLFAYPEIQLNSSQQKTLSAYVKRRLKGEPIAYILGQKEFWSLNLKVTPDVLIPRPETEMLVEWI 104
Cdd:TIGR03534 1 DAELLLAHVLGKDRAQLLLHPEDELTPEELAAFDALLARRAAGEPVAYILGEREFYGLDFKVSPGVLIPRPETEELVEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 105 LKNLPKDEklRIADLGTGSGAVALAIAVERPHWTIDATDNSQAALKIAEINAKQHEIKNCNFYHGEWCQALPRRDYHAIV 184
Cdd:TIGR03534 81 LERLKKGP--RVLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKNARRLGLENVEFLQGDWFEPLPSGKFDLIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 185 GNPPYIPDKDQHLQQ---LKHEPREALAAGSDGLSAIKIIIHEAKSYLVNGGWLLLEHGYDQAEKIMTLMQADGYREITD 261
Cdd:TIGR03534 159 SNPPYIPEADIHLLDpevRDFEPRLALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFEAAGFADVET 238
|
250
....*....|..
gi 499261028 262 RRDLAGLSRMMV 273
Cdd:TIGR03534 239 RKDLAGKDRVVL 250
|
|
| hemK_fam |
TIGR00536 |
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ... |
3-276 |
2.41e-78 |
|
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: 238.79 E-value: 2.41e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 3 SIKEATKNISQQLT--TVSKTPRLDAELLLECVLKKSRADLFAYPEIQLNSSQQKTLSAYVKRRLKGEPIAYILGQKEFW 80
Cdd:TIGR00536 2 TIQEFLRWASSALSraIARENPWLEALLLLEHDLGRERDLLLAFLTEELTPDEKERIFRLVLRRVKGVPVAYLLGSKEFY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 81 SLNLKVTPDVLIPRPETEMLVEWILKNL-PKDEKLRIADLGTGSGAVALAIAVERPHWTIDATDNSQAALKIAEINAKQH 159
Cdd:TIGR00536 82 GLEFFVNEHVLIPRPETEELVEKALASLiSQPPILHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 160 EIKNC-NFYHGEWCQALPRRDYHAIVGNPPYIPDKDQHLQQ--LKHEPREALAAGSDGLSAIKIIIHEAKSYLVNGGWLL 236
Cdd:TIGR00536 162 QLEHRvEFIQSNLFEPLAGQKIDIIVSNPPYIDEEDLADLPnvVRFEPLLALVGGDDGLNILRQIIELAPDYLKPNGFLV 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 499261028 237 LEHGYDQA-EKIMTLMQADGYREITDRRDLAGLSRMMVARR 276
Cdd:TIGR00536 242 CEIGNWQQkSLKELLRIKFTWYDVENGRDLNGKERVVLGFY 282
|
|
| PRK14966 |
PRK14966 |
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; ... |
18-275 |
1.25e-55 |
|
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; Provisional
Pssm-ID: 184930 [Multi-domain] Cd Length: 423 Bit Score: 184.90 E-value: 1.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 18 VSKTPRLDAELLLECVLKKSRADLFAYPEIQLNSSQQKTLSAYVKRRLKGEPIAYILGQKEFWSLNLKVTPDVLIPRPET 97
Cdd:PRK14966 159 LSKLPKNEARMLLQYASEYTRVQLLTRGGEEMPDEVRQRADRLAQRRLNGEPVAYILGVREFYGRRFAVNPNVLIPRPET 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 98 EMLVEWILKNLPkdEKLRIADLGTGSGAVALAIAVERPHWTIDATDNSQAALKIAEINAKQHEIKnCNFYHGEWCQA-LP 176
Cdd:PRK14966 239 EHLVEAVLARLP--ENGRVWDLGTGSGAVAVTVALERPDAFVRASDISPPALETARKNAADLGAR-VEFAHGSWFDTdMP 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 177 RR-DYHAIVGNPPYIPDKDQHLQQ--LKHEPREALAAGSDGLSAIKIIIHEAKSYLVNGGWLLLEHGYDQAEKIMTLMQA 253
Cdd:PRK14966 316 SEgKWDIIVSNPPYIENGDKHLLQgdLRFEPQIALTDFSDGLSCIRTLAQGAPDRLAEGGFLLLEHGFDQGAAVRGVLAE 395
|
250 260
....*....|....*....|..
gi 499261028 254 DGYREITDRRDLAGLSRMMVAR 275
Cdd:PRK14966 396 NGFSGVETLPDLAGLDRVTLGK 417
|
|
| PRK01544 |
PRK01544 |
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ... |
3-272 |
8.44e-48 |
|
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) methyltransferase; Reviewed
Pssm-ID: 234958 [Multi-domain] Cd Length: 506 Bit Score: 166.19 E-value: 8.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 3 SIKEATKNISQQLTTVS-KTPRLDAELLLECVLKKSRADLFAYPEIQLNSSQQKTLSAYVKRRLKGEPIAYILGQKEFWS 81
Cdd:PRK01544 4 SIKQILSDATDKLNKIGiSSPQLEARILLQHVINKPIEYLLINLDEQLNEAEIEAFEKLLERRLKHEPIAYITGVKEFYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 82 LNLKVTPDVLIPRPETEMLVEWIL------------KNLPK------------DEKLRIADLGTGSGAVALAIAVERPHW 137
Cdd:PRK01544 84 REFIVNKHVLIPRSDTEVLVDVVFqchsresgnpekKQLNPcfrgndissncnDKFLNILELGTGSGCIAISLLCELPNA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 138 TIDATDNSQAALKIAEINAKQHEIKN-CNFYHGEWCQALPRRDYHAIVGNPPYIPDKDQ---HLQQLKHEPREALAAGSD 213
Cdd:PRK01544 164 NVIATDISLDAIEVAKSNAIKYEVTDrIQIIHSNWFENIEKQKFDFIVSNPPYISHSEKsemAIETINYEPSIALFAEED 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 499261028 214 GLSAIKIIIHEAKSYLVNGGWLLLEHGYDQAEKIMTLMQADGYREITDRRDLAGLSRMM 272
Cdd:PRK01544 244 GLQAYFIIAENAKQFLKPNGKIILEIGFKQEEAVTQIFLDHGYNIESVYKDLQGHSRVI 302
|
|
| L3_gln_methyl |
TIGR03533 |
protein-(glutamine-N5) methyltransferase, ribosomal protein L3-specific; Members of this ... |
48-240 |
4.87e-38 |
|
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: 134.95 E-value: 4.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 48 QLNSSQQKTLSAYVKRRLKGE-PIAYILGQKEFWSLNLKVTPDVLIPR-PETEMLVE----WILKNLPKdeklRIADLGT 121
Cdd:TIGR03533 55 RLTPSEKERILELIERRIEERiPVAYLTNEAWFAGLEFYVDERVLIPRsPIAELIEDgfapWLEPEPVK----RILDLCT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 122 GSGAVALAIAVERPHWTIDATDNSQAALKIAEINAKQHEIKN-CNFYHGEWCQALPRRDYHAIVGNPPYIPDKD-QHL-Q 198
Cdd:TIGR03533 131 GSGCIAIACAYAFPEAEVDAVDISPDALAVAEINIERHGLEDrVTLIQSDLFAALPGRKYDLIVSNPPYVDAEDmADLpA 210
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499261028 199 QLKHEPREALAAGSDGLSAIKIIIHEAKSYLVNGGWLLLEHG 240
Cdd:TIGR03533 211 EYHHEPELALASGEDGLDLVRRILAEAADHLNENGVLVVEVG 252
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
97-237 |
1.98e-21 |
|
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: 88.71 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 97 TEMLvewiLKNLPKDEKLRIADLGTGSGAVALAIAVERPHWTIDATDNSQAALKIAEINAKQHEIKNCNFYHGEWCQALP 176
Cdd:COG2813 38 TRLL----LEHLPEPLGGRVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAANGLENVEVLWSDGLSGVP 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499261028 177 RRDYHAIVGNPPYipdkdqHlQQLKHEPREALAagsdglsaikiIIHEAKSYLVNGGWLLL 237
Cdd:COG2813 114 DGSFDLILSNPPF------H-AGRAVDKEVAHA-----------LIADAARHLRPGGELWL 156
|
|
| MTS |
pfam05175 |
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ... |
105-237 |
2.24e-19 |
|
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: 82.64 E-value: 2.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 105 LKNLPKDEKLRIADLGTGSGAVALAIAVERPHWTIDATDNSQAALKIAEINAKQHEIKNCNFYHGEWCQALPRRDYHAIV 184
Cdd:pfam05175 24 LEHLPKDLSGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGLENGEVVASDVYSGVEDGKFDLII 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 499261028 185 GNPPYipdkdqhlqqlkHEPREalaagsDGLSAIKIIIHEAKSYLVNGGWLLL 237
Cdd:pfam05175 104 SNPPF------------HAGLA------TTYNVAQRFIADAKRHLRPGGELWI 138
|
|
| PrmC_N |
pfam17827 |
PrmC N-terminal domain; This entry corresponds to the N-terminal alpha helical domain of the ... |
6-75 |
7.03e-18 |
|
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: 75.98 E-value: 7.03e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499261028 6 EATKNISQQLTTV-SKTPRLDAELLLECVLKKSRADLFAYPEIQLNSSQQKTLSAYVKRRLKGEPIAYILG 75
Cdd:pfam17827 1 EALRWASSRLKEAgIESPRLDAELLLAHVLGLDRTDLLLHPEEELSEEELERFEELLERRAAGEPLQYILG 71
|
|
| PRK14967 |
PRK14967 |
putative methyltransferase; Provisional |
84-277 |
1.57e-14 |
|
putative methyltransferase; Provisional
Pssm-ID: 184931 [Multi-domain] Cd Length: 223 Bit Score: 70.85 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 84 LKVTPDVLIPRPETEMLVEwILKNLPKDEKLRIADLGTGSGAVALAIAVERPHWtIDATDNSQAALKIAEINA--KQHEI 161
Cdd:PRK14967 9 LLRAPGVYRPQEDTQLLAD-ALAAEGLGPGRRVLDLCTGSGALAVAAAAAGAGS-VTAVDISRRAVRSARLNAllAGVDV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 162 KncnFYHGEWCQALPRRDYHAIVGNPPYIPDKDQHLQqlKHEPREALAAGSDGLSAIKIIIHEAKSYLVNGGWLLLEH-G 240
Cdd:PRK14967 87 D---VRRGDWARAVEFRPFDVVVSNPPYVPAPPDAPP--SRGPARAWDAGPDGRAVLDRLCDAAPALLAPGGSLLLVQsE 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 499261028 241 YDQAEKIMTLMQADGYR-EITDRRDLaGLSRMMVARRG 277
Cdd:PRK14967 162 LSGVERTLTRLSEAGLDaEVVASQWI-PFGPVLRARAA 198
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
115-255 |
2.93e-13 |
|
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: 67.48 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 115 RIADLGTGSGAVALAIAVERPHWTIDATDNSQAALKIAEINAKQHEIKN-CNFYHG---EWCQALPRRDYHAIVGNPPYI 190
Cdd:COG4123 40 RVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLEDrITVIHGdlkEFAAELPPGSFDLVVSNPPYF 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499261028 191 PD------KDQHLQQLKHEPREALAAgsdglsaikiIIHEAKSYLVNGGWLLLEHGYDQAEKIMTLMQADG 255
Cdd:COG4123 120 KAgsgrksPDEARAIARHEDALTLED----------LIRAAARLLKPGGRFALIHPAERLAEILAALRKYG 180
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
115-238 |
1.25e-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: 60.14 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 115 RIADLGTGSGAVALAIAvERPHWTIDATDNSQAALKIAEINAKQHEIKNCNFYHGEWCQALPRRD--YHAIVGNPPYipd 192
Cdd:cd02440 1 RVLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADesFDVIISDPPL--- 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 499261028 193 kdQHLQQLKHEprealaagsdglsaikiIIHEAKSYLVNGGWLLLE 238
Cdd:cd02440 77 --HHLVEDLAR-----------------FLEEARRLLKPGGVLVLT 103
|
|
| PRK14968 |
PRK14968 |
putative methyltransferase; Provisional |
88-263 |
1.73e-09 |
|
putative methyltransferase; Provisional
Pssm-ID: 237872 [Multi-domain] Cd Length: 188 Bit Score: 56.06 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 88 PDVLIPRPETEMLVEwilkNLPKDEKLRIADLGTGSGAVALAIAvERPHWTIdATDNSQAALKIAEINAKQHEIKNC--N 165
Cdd:PRK14968 3 DEVYEPAEDSFLLAE----NAVDKKGDRVLEVGTGSGIVAIVAA-KNGKKVV-GVDINPYAVECAKCNAKLNNIRNNgvE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 166 FYHGEWCQALPRRDYHAIVGNPPYIPDKDQhlqqlkHEPRE----ALAAGSDGLSAIKIIIHEAKSYLVNGG-WLLLEHG 240
Cdd:PRK14968 77 VIRSDLFEPFRGDKFDVILFNPPYLPTEEE------EEWDDwlnyALSGGKDGREVIDRFLDEVGRYLKPGGrILLLQSS 150
|
170 180
....*....|....*....|....
gi 499261028 241 YDQAEKIMTLMQADGYR-EITDRR 263
Cdd:PRK14968 151 LTGEDEVLEYLEKLGFEaEVVAEE 174
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
115-211 |
2.24e-09 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 53.67 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 115 RIADLGTGSGAVALAIAVERPHWTIDATDNSQAALKIAeinakQHEIKNCNFYHGEWCQALPRRDYHAIVGNP--PYIPD 192
Cdd:COG4106 4 RVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARA-----RARLPNVRFVVADLRDLDPPEPFDLVVSNAalHWLPD 78
|
90
....*....|....*....
gi 499261028 193 KDQHLQQLkhepREALAAG 211
Cdd:COG4106 79 HAALLARL----AAALAPG 93
|
|
| hemK_rel_arch |
TIGR00537 |
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ... |
104-265 |
8.89e-08 |
|
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: 51.01 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 104 ILKNLPKDEKLRIADLGTGSGAVAlaIAVERPHWTIDATDNSQAALKIAEINAKQHEiKNCNFYHGEWCQALpRRDYHAI 183
Cdd:TIGR00537 11 LEANLRELKPDDVLEIGAGTGLVA--IRLKGKGKCILTTDINPFAVKELRENAKLNN-VGLDVVMTDLFKGV-RGKFDVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 184 VGNPPYIPDKDQhlqqlkhEPRE-----ALAAGSDGLSAIKIIIHEAKSYLVNGGWL-LLEHGYDQAEKIMTLMQADGYR 257
Cdd:TIGR00537 87 LFNPPYLPLEDD-------LRRGdwldvAIDGGKDGRKVIDRFLDELPEILKEGGRVqLIQSSLNGEPDTFDKLDERGFR 159
|
....*....
gi 499261028 258 -EITDRRDL 265
Cdd:TIGR00537 160 yEIVAERGL 168
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
92-276 |
1.05e-07 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 51.07 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 92 IPRPETEMLVEwILKNLPKDekLRIADLGTGSGAVALAIAvERPHWTIDATDNSQAALKIAEINAKQHEIKNCNFYHGEW 171
Cdd:COG0500 9 ELLPGLAALLA-LLERLPKG--GRVLDLGCGTGRNLLALA-ARFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 172 CQ--ALPRRDYHAIV--GNppyipdkdqhLQQLKHEPREAlaagsdglsaikiIIHEAKSYLVNGGWLLLE-HGYDQAEK 246
Cdd:COG0500 85 AEldPLPAESFDLVVafGV----------LHHLPPEEREA-------------LLRELARALKPGGVLLLSaSDAAAALS 141
|
170 180 190
....*....|....*....|....*....|
gi 499261028 247 IMTLMQADGYREITDRRDLAGLSRMMVARR 276
Cdd:COG0500 142 LARLLLLATASLLELLLLLRLLALELYLRA 171
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
102-257 |
2.31e-07 |
|
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: 49.22 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 102 EWILKNLPKDEKLRIADLGTGSGAVALAIAveRPHWTIDATDNSQAALKIAEINAKQHEIkNCNFYHGEWcQALPRRD-- 179
Cdd:COG2226 12 EALLAALGLRPGARVLDLGCGTGRLALALA--ERGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDA-EDLPFPDgs 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 180 YHAIVGNP--PYIPDKDQHLQqlkheprealaagsdglsaikiiihEAKSYLVNGGWLLL-EHGYDQAEKIMTLMQADGY 256
Cdd:COG2226 88 FDLVISSFvlHHLPDPERALA-------------------------EIARVLKPGGRLVVvDFSPPDLAELEELLAEAGF 142
|
.
gi 499261028 257 R 257
Cdd:COG2226 143 E 143
|
|
| TrmA |
COG2265 |
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ... |
97-188 |
2.85e-07 |
|
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: 50.95 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 97 TEMLVEWILKNLPKDEKLRIADLGTGSGAVALAIAveRPHWTIDATDNSQAALKIAEINAKQHEIKNCNFYHGEWCQALP 176
Cdd:COG2265 218 AEALYAAALEWLDLTGGERVLDLYCGVGTFALPLA--RRAKKVIGVEIVPEAVEDARENARLNGLKNVEFVAGDLEEVLP 295
|
90
....*....|....*.
gi 499261028 177 RRDYH----AIVGNPP 188
Cdd:COG2265 296 ELLWGgrpdVVVLDPP 311
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
110-171 |
1.63e-06 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 46.64 E-value: 1.63e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499261028 110 KDEKLRIADLGTGSGAVALAIAVE-RPHWTIDATDNSQAALKIAEINAKQHEIKNCNFYHGEW 171
Cdd:pfam13847 1 IDKGMRVLDLGCGTGHLSFELAEElGPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDI 63
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
116-195 |
2.36e-06 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 44.86 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 116 IADLGTGSGAVALAIAvERPHWTIDATDNSQAALKIAEINAKQHEIkNCNFYHGEwCQALPRRD--YHAIVGNPP--YIP 191
Cdd:pfam13649 1 VLDLGCGTGRLTLALA-RRGGARVTGVDLSPEMLERARERAAEAGL-NVEFVQGD-AEDLPFPDgsFDLVVSSGVlhHLP 77
|
....
gi 499261028 192 DKDQ 195
Cdd:pfam13649 78 DPDL 81
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
100-211 |
1.42e-05 |
|
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: 43.47 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 100 LVEWILKNLPKDekLRIADLGTGSGAVALAIAveRPHWTIDATDNSQAALKIAEINAKQHEIkncNFYHGEWCQ-ALPRR 178
Cdd:COG2227 14 LAALLARLLPAG--GRVLDVGCGTGRLALALA--RRGADVTGVDISPEALEIARERAAELNV---DFVQGDLEDlPLEDG 86
|
90 100 110
....*....|....*....|....*....|....*
gi 499261028 179 DYHAIVGN--PPYIPDKDQHLQQLkhepREALAAG 211
Cdd:COG2227 87 SFDLVICSevLEHLPDPAALLREL----ARLLKPG 117
|
|
| PrmA |
COG2264 |
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis]; |
97-257 |
7.21e-05 |
|
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441865 [Multi-domain] Cd Length: 284 Bit Score: 43.24 E-value: 7.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 97 TEMLVEWILKNLPKDEklRIADLGTGSGavALAIAVER-PHWTIDATDNSQAALKIAEINAKQHEIKNC-NFYHGEwcqA 174
Cdd:COG2264 135 TRLCLEALEKLLKPGK--TVLDVGCGSG--ILAIAAAKlGAKRVLAVDIDPVAVEAARENAELNGVEDRiEVVLGD---L 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 175 LPRRDYHAIVGNppyIpdkdqhlqqlkhepreaLAagsdglSAIKIIIHEAKSYLVNGGWL----LLEHgydQAEKIMTL 250
Cdd:COG2264 208 LEDGPYDLVVAN---I-----------------LA------NPLIELAPDLAALLKPGGYLilsgILEE---QADEVLAA 258
|
....*..
gi 499261028 251 MQADGYR 257
Cdd:COG2264 259 YEAAGFE 265
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
98-211 |
1.66e-04 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 41.52 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 98 EMLVEWILKNLPKDEKLRIADLGTGSGAVALAIaveRPH-WTIDATDNSQAALKIAEinAKQHEIkncNFYHGEWCQ-AL 175
Cdd:COG4976 32 ALLAEELLARLPPGPFGRVLDLGCGTGLLGEAL---RPRgYRLTGVDLSEEMLAKAR--EKGVYD---RLLVADLADlAE 103
|
90 100 110
....*....|....*....|....*....|....*...
gi 499261028 176 PRRDYHAIVGN--PPYIPDKDQHLQQLkhepREALAAG 211
Cdd:COG4976 104 PDGRFDLIVAAdvLTYLGDLAAVFAGV----ARALKPG 137
|
|
| prmA |
PRK00517 |
50S ribosomal protein L11 methyltransferase; |
95-157 |
4.91e-04 |
|
50S ribosomal protein L11 methyltransferase;
Pssm-ID: 234786 [Multi-domain] Cd Length: 250 Bit Score: 40.52 E-value: 4.91e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499261028 95 PETEMLVEWILKNLPKDEklRIADLGTGSGavALAIAVER-PHWTIDATDNSQAALKIAEINAK 157
Cdd:PRK00517 104 PTTRLCLEALEKLVLPGK--TVLDVGCGSG--ILAIAAAKlGAKKVLAVDIDPQAVEAARENAE 163
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
100-184 |
5.23e-04 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 39.53 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 100 LVEWILKNLPKDEKLRIADLGTGSGAVALAIAvERPHWTIDATDNSQAALKIAEINAKQHEIKN-CNFYHGEWCQALPRR 178
Cdd:COG2230 39 KLDLILRKLGLKPGMRVLDIGCGWGGLALYLA-RRYGVRVTGVTLSPEQLEYARERAAEAGLADrVEVRLADYRDLPADG 117
|
....*.
gi 499261028 179 DYHAIV 184
Cdd:COG2230 118 QFDAIV 123
|
|
| PRK15001 |
PRK15001 |
23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG; |
103-189 |
2.15e-03 |
|
23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;
Pssm-ID: 184963 [Multi-domain] Cd Length: 378 Bit Score: 39.24 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 103 WILKNLPKDEKLRIADLGTGSGAVALAIAVERPHWTIDATDNSQAALKIAEINAKQH---EIKNCNFYHGEWCQALPRRD 179
Cdd:PRK15001 219 FFMQHLPENLEGEIVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNmpeALDRCEFMINNALSGVEPFR 298
|
90
....*....|
gi 499261028 180 YHAIVGNPPY 189
Cdd:PRK15001 299 FNAVLCNPPF 308
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
118-211 |
3.31e-03 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 36.19 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261028 118 DLGTGSGAVALAIAVERPHWTIDATDNSQAALKIAEINAKQHEIKNCNFYHGEWCQA--LPRRDYHAIVGNP--PYIPDK 193
Cdd:pfam08242 2 EIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLgeLDPGSFDVVVASNvlHHLADP 81
|
90
....*....|....*...
gi 499261028 194 DQHLQQLkhepREALAAG 211
Cdd:pfam08242 82 RAVLRNI----RRLLKPG 95
|
|
|