|
Name |
Accession |
Description |
Interval |
E-value |
| HemK |
COG2890 |
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
1-280 |
4.17e-115 |
|
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 332.50 E-value: 4.17e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 1 MKIKDIINYGVSMIK--NTESPSLEIQMMIAKVIEKDRLYIMLNLEEDIDESKVEIIKTMIEKRKNSYPLQYILGEREFW 78
Cdd:COG2890 1 MTIRELLRWAAARLAaaGVDSARLEAELLLAHVLGLDRADLLLHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 79 GMDFNVSEGVLIPRQDTEILIEETLKKLKNHkhkSNLKGFEIGVGSGIISITLLKEIETLIMIGVDINDKAIELTKANAS 158
Cdd:COG2890 81 GLEFKVDPGVLIPRPETEELVELALALLPAG---APPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 159 KHQVSDRLCILNSNLFEKINKENQFDFIISNPPYIETKVIDSLQEDIKQHEPKLALDGGADGLDFYRDIIEQSKHYISPE 238
Cdd:COG2890 158 RLGLEDRVRFLQGDLFEPLPGDGRFDLIVSNPPYIPEDEIALLPPEVRDHEPRLALDGGEDGLDFYRRIIAQAPRLLKPG 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 503127684 239 GFIAFEIGYNQAEAVKKIFVENGYQNVTIAKDLAGFDRVVIG 280
Cdd:COG2890 238 GWLLLEIGEDQGEAVRALLEAAGFADVETHKDLAGRDRVVVA 279
|
|
| PRK09328 |
PRK09328 |
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional |
1-280 |
2.03e-110 |
|
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
Pssm-ID: 236467 [Multi-domain] Cd Length: 275 Bit Score: 320.19 E-value: 2.03e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 1 MKIKDIINYGVSMIKNtesPSLEIQMMIAKVIEKDRLYIMLNLEEDIDESKVEIIKTMIEKRKNSYPLQYILGEREFWGM 80
Cdd:PRK09328 2 MTIAEALREATARLAS---PRLDAELLLAHVLGLSRTDLLLNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFWGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 81 DFNVSEGVLIPRQDTEILIEETLKKLKNHkhkSNLKGFEIGVGSGIISITLLKEIETLIMIGVDINDKAIELTKANAsKH 160
Cdd:PRK09328 79 DFKVSPGVLIPRPETEELVEWALEALLLK---EPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNA-KH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 161 QVSDRLCILNSNLFEKINKEnQFDFIISNPPYIETKVIDSLQEDIKQHEPKLALDGGADGLDFYRDIIEQSKHYISPEGF 240
Cdd:PRK09328 155 GLGARVEFLQGDWFEPLPGG-RFDLIVSNPPYIPEADIHLLQPEVRDHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGW 233
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 503127684 241 IAFEIGYNQAEAVKKIFVENGYQNVTIAKDLAGFDRVVIG 280
Cdd:PRK09328 234 LLLEIGYDQGEAVRALLAAAGFADVETRKDLAGRDRVVLG 273
|
|
| RF_mod_PrmC |
TIGR03534 |
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ... |
23-279 |
4.10e-100 |
|
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: 293.22 E-value: 4.10e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 23 EIQMMIAKVIEKDRLYIMLNLEEDIDESKVEIIKTMIEKRKNSYPLQYILGEREFWGMDFNVSEGVLIPRQDTEILIEEt 102
Cdd:TIGR03534 1 DAELLLAHVLGKDRAQLLLHPEDELTPEELAAFDALLARRAAGEPVAYILGEREFYGLDFKVSPGVLIPRPETEELVEA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 103 lkklKNHKHKSNLKGFEIGVGSGIISITLLKEIETLIMIGVDINDKAIELTKANASKHQVsDRLCILNSNLFEKINKEnQ 182
Cdd:TIGR03534 80 ----ALERLKKGPRVLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKNARRLGL-ENVEFLQGDWFEPLPSG-K 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 183 FDFIISNPPYIETKVIDSLQEDIKQHEPKLALDGGADGLDFYRDIIEQSKHYISPEGFIAFEIGYNQAEAVKKIFVENGY 262
Cdd:TIGR03534 154 FDLIVSNPPYIPEADIHLLDPEVRDFEPRLALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFEAAGF 233
|
250
....*....|....*..
gi 503127684 263 QNVTIAKDLAGFDRVVI 279
Cdd:TIGR03534 234 ADVETRKDLAGKDRVVL 250
|
|
| PrmC_N |
pfam17827 |
PrmC N-terminal domain; This entry corresponds to the N-terminal alpha helical domain of the ... |
5-73 |
6.10e-13 |
|
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: 62.50 E-value: 6.10e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503127684 5 DIINYGVSMIK--NTESPSLEIQMMIAKVIEKDRLYIMLNLEEDIDESKVEIIKTMIEKRKNSYPLQYILG 73
Cdd:pfam17827 1 EALRWASSRLKeaGIESPRLDAELLLAHVLGLDRTDLLLHPEEELSEEELERFEELLERRAAGEPLQYILG 71
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
116-216 |
8.43e-06 |
|
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: 43.96 E-value: 8.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 116 KGFEIGVGSGIISITLLKEIETLImIGVDINDKAIELTKANAsKHQVSDRLCILNSNLFE-KINKENQFDFIISNPPYie 194
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARV-TGVDISPVALELARKAA-AALLADNVEVLKGDAEElPPEADESFDVIISDPPL-- 76
|
90 100
....*....|....*....|..
gi 503127684 195 TKVIDSLQEDIKQHEPKLALDG 216
Cdd:cd02440 77 HHLVEDLARFLEEARRLLKPGG 98
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HemK |
COG2890 |
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
1-280 |
4.17e-115 |
|
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 332.50 E-value: 4.17e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 1 MKIKDIINYGVSMIK--NTESPSLEIQMMIAKVIEKDRLYIMLNLEEDIDESKVEIIKTMIEKRKNSYPLQYILGEREFW 78
Cdd:COG2890 1 MTIRELLRWAAARLAaaGVDSARLEAELLLAHVLGLDRADLLLHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 79 GMDFNVSEGVLIPRQDTEILIEETLKKLKNHkhkSNLKGFEIGVGSGIISITLLKEIETLIMIGVDINDKAIELTKANAS 158
Cdd:COG2890 81 GLEFKVDPGVLIPRPETEELVELALALLPAG---APPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 159 KHQVSDRLCILNSNLFEKINKENQFDFIISNPPYIETKVIDSLQEDIKQHEPKLALDGGADGLDFYRDIIEQSKHYISPE 238
Cdd:COG2890 158 RLGLEDRVRFLQGDLFEPLPGDGRFDLIVSNPPYIPEDEIALLPPEVRDHEPRLALDGGEDGLDFYRRIIAQAPRLLKPG 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 503127684 239 GFIAFEIGYNQAEAVKKIFVENGYQNVTIAKDLAGFDRVVIG 280
Cdd:COG2890 238 GWLLLEIGEDQGEAVRALLEAAGFADVETHKDLAGRDRVVVA 279
|
|
| PRK09328 |
PRK09328 |
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional |
1-280 |
2.03e-110 |
|
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
Pssm-ID: 236467 [Multi-domain] Cd Length: 275 Bit Score: 320.19 E-value: 2.03e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 1 MKIKDIINYGVSMIKNtesPSLEIQMMIAKVIEKDRLYIMLNLEEDIDESKVEIIKTMIEKRKNSYPLQYILGEREFWGM 80
Cdd:PRK09328 2 MTIAEALREATARLAS---PRLDAELLLAHVLGLSRTDLLLNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFWGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 81 DFNVSEGVLIPRQDTEILIEETLKKLKNHkhkSNLKGFEIGVGSGIISITLLKEIETLIMIGVDINDKAIELTKANAsKH 160
Cdd:PRK09328 79 DFKVSPGVLIPRPETEELVEWALEALLLK---EPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNA-KH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 161 QVSDRLCILNSNLFEKINKEnQFDFIISNPPYIETKVIDSLQEDIKQHEPKLALDGGADGLDFYRDIIEQSKHYISPEGF 240
Cdd:PRK09328 155 GLGARVEFLQGDWFEPLPGG-RFDLIVSNPPYIPEADIHLLQPEVRDHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGW 233
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 503127684 241 IAFEIGYNQAEAVKKIFVENGYQNVTIAKDLAGFDRVVIG 280
Cdd:PRK09328 234 LLLEIGYDQGEAVRALLAAAGFADVETRKDLAGRDRVVLG 273
|
|
| RF_mod_PrmC |
TIGR03534 |
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ... |
23-279 |
4.10e-100 |
|
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: 293.22 E-value: 4.10e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 23 EIQMMIAKVIEKDRLYIMLNLEEDIDESKVEIIKTMIEKRKNSYPLQYILGEREFWGMDFNVSEGVLIPRQDTEILIEEt 102
Cdd:TIGR03534 1 DAELLLAHVLGKDRAQLLLHPEDELTPEELAAFDALLARRAAGEPVAYILGEREFYGLDFKVSPGVLIPRPETEELVEA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 103 lkklKNHKHKSNLKGFEIGVGSGIISITLLKEIETLIMIGVDINDKAIELTKANASKHQVsDRLCILNSNLFEKINKEnQ 182
Cdd:TIGR03534 80 ----ALERLKKGPRVLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKNARRLGL-ENVEFLQGDWFEPLPSG-K 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 183 FDFIISNPPYIETKVIDSLQEDIKQHEPKLALDGGADGLDFYRDIIEQSKHYISPEGFIAFEIGYNQAEAVKKIFVENGY 262
Cdd:TIGR03534 154 FDLIVSNPPYIPEADIHLLDPEVRDFEPRLALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFEAAGF 233
|
250
....*....|....*..
gi 503127684 263 QNVTIAKDLAGFDRVVI 279
Cdd:TIGR03534 234 ADVETRKDLAGKDRVVL 250
|
|
| hemK_fam |
TIGR00536 |
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ... |
1-280 |
2.26e-66 |
|
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: 208.36 E-value: 2.26e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 1 MKIKDIINYGVSMIKNT---ESPSLEIQMMIAKVIEKDRLYIMLNLEEDIDESKVEIIKTMIEKRKNSYPLQYILGEREF 77
Cdd:TIGR00536 1 MTIQEFLRWASSALSRAiarENPWLEALLLLEHDLGRERDLLLAFLTEELTPDEKERIFRLVLRRVKGVPVAYLLGSKEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 78 WGMDFNVSEGVLIPRQDTEILIEETLKKLKNHKHKsnLKGFEIGVGSGIISITLLKEIETLIMIGVDINDKAIELTKANA 157
Cdd:TIGR00536 81 YGLEFFVNEHVLIPRPETEELVEKALASLISQPPI--LHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 158 SKHQVSDRLCILNSNLFEKINKEnQFDFIISNPPYIETKVIDSLQEDIKqHEPKLALDGGADGLDFYRDIIEQSKHYISP 237
Cdd:TIGR00536 159 EKNQLEHRVEFIQSNLFEPLAGQ-KIDIIVSNPPYIDEEDLADLPNVVR-FEPLLALVGGDDGLNILRQIIELAPDYLKP 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 503127684 238 EGFIAFEIGYNQAEAVKK-IFVENGYQNVTIAKDLAGFDRVVIG 280
Cdd:TIGR00536 237 NGFLVCEIGNWQQKSLKElLRIKFTWYDVENGRDLNGKERVVLG 280
|
|
| PRK01544 |
PRK01544 |
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ... |
19-278 |
5.01e-56 |
|
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) methyltransferase; Reviewed
Pssm-ID: 234958 [Multi-domain] Cd Length: 506 Bit Score: 188.15 E-value: 5.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 19 SPSLEIQMMIAKVIEKDRLYIMLNLEEDIDESKVEIIKTMIEKRKNSYPLQYILGEREFWGMDFNVSEGVLIPRQDTEIL 98
Cdd:PRK01544 23 SPQLEARILLQHVINKPIEYLLINLDEQLNEAEIEAFEKLLERRLKHEPIAYITGVKEFYSREFIVNKHVLIPRSDTEVL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 99 IE---------------------ETLKKLKNHKHKSNLKGFEIGVGSGIISITLLKEIETLIMIGVDINDKAIELTKANA 157
Cdd:PRK01544 103 VDvvfqchsresgnpekkqlnpcFRGNDISSNCNDKFLNILELGTGSGCIAISLLCELPNANVIATDISLDAIEVAKSNA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 158 SKHQVSDRLCILNSNLFEKINKEnQFDFIISNPPYIETKVIDSLQEDIKQHEPKLALDGGADGLDFYRDIIEQSKHYISP 237
Cdd:PRK01544 183 IKYEVTDRIQIIHSNWFENIEKQ-KFDFIVSNPPYISHSEKSEMAIETINYEPSIALFAEEDGLQAYFIIAENAKQFLKP 261
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 503127684 238 EGFIAFEIGYNQAEAVKKIFVENGYQNVTIAKDLAGFDRVV 278
Cdd:PRK01544 262 NGKIILEIGFKQEEAVTQIFLDHGYNIESVYKDLQGHSRVI 302
|
|
| L3_gln_methyl |
TIGR03533 |
protein-(glutamine-N5) methyltransferase, ribosomal protein L3-specific; Members of this ... |
41-249 |
1.58e-36 |
|
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: 131.48 E-value: 1.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 41 LNLEEDIDE---------SKVEIIKTMIEKRKNSY-PLQYILGEREFWGMDFNVSEGVLIPRQDTEILIEEtlkklknhk 110
Cdd:TIGR03533 41 LHLPLDILEpfldarltpSEKERILELIERRIEERiPVAYLTNEAWFAGLEFYVDERVLIPRSPIAELIED--------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 111 hksnlkGF-------------EIGVGSGIISITLLKEIETLIMIGVDINDKAIELTKANASKHQVSDRLCILNSNLFEKI 177
Cdd:TIGR03533 112 ------GFapwlepepvkrilDLCTGSGCIAIACAYAFPEAEVDAVDISPDALAVAEINIERHGLEDRVTLIQSDLFAAL 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503127684 178 NKEnQFDFIISNPPYIETKVIDSLQEDIkQHEPKLALDGGADGLDFYRDIIEQSKHYISPEGFIAFEIGYNQ 249
Cdd:TIGR03533 186 PGR-KYDLIVSNPPYVDAEDMADLPAEY-HHEPELALASGEDGLDLVRRILAEAADHLNENGVLVVEVGNSM 255
|
|
| PRK14966 |
PRK14966 |
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; ... |
20-280 |
1.10e-35 |
|
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; Provisional
Pssm-ID: 184930 [Multi-domain] Cd Length: 423 Bit Score: 132.51 E-value: 1.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 20 PSLEIQMMIAKVIEKDRLYIMLNLEEDIDESKVEIIKTMIEKRKNSYPLQYILGEREFWGMDFNVSEGVLIPRQDTEILI 99
Cdd:PRK14966 163 PKNEARMLLQYASEYTRVQLLTRGGEEMPDEVRQRADRLAQRRLNGEPVAYILGVREFYGRRFAVNPNVLIPRPETEHLV 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 100 EETLKKLKnhkhkSNLKGFEIGVGSGIISITLLKEIETLIMIGVDINDKAIELTKANASkhQVSDRLCILNSNLFEK-IN 178
Cdd:PRK14966 243 EAVLARLP-----ENGRVWDLGTGSGAVAVTVALERPDAFVRASDISPPALETARKNAA--DLGARVEFAHGSWFDTdMP 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 179 KENQFDFIISNPPYIETKVIDSLQEDIKqHEPKLALDGGADGLDFYRDIIEQSKHYISPEGFIAFEIGYNQAEAVKKIFV 258
Cdd:PRK14966 316 SEGKWDIIVSNPPYIENGDKHLLQGDLR-FEPQIALTDFSDGLSCIRTLAQGAPDRLAEGGFLLLEHGFDQGAAVRGVLA 394
|
250 260
....*....|....*....|..
gi 503127684 259 ENGYQNVTIAKDLAGFDRVVIG 280
Cdd:PRK14966 395 ENGFSGVETLPDLAGLDRVTLG 416
|
|
| PrmC_rel_meth |
TIGR03704 |
putative protein-(glutamine-N5) methyltransferase, unknown substrate-specific; This protein ... |
55-280 |
2.20e-24 |
|
putative protein-(glutamine-N5) methyltransferase, unknown substrate-specific; This protein family is closely related to two different families of protein-(glutamine-N5) methyltransferase. The first is PrmB, which modifies ribosomal protein L3 in some bacteria. The second is PrmC (HemK), which modifies peptide chain release factors 1 and 2 in most bacteria and also in eukaryotes. The glutamine side chain-binding motif NPPY shared by PrmB and PrmC is N[VAT]PY in this family. The protein substrate is unknown. [Protein synthesis, Ribosomal proteins: synthesis and modification]
Pssm-ID: 274733 [Multi-domain] Cd Length: 251 Bit Score: 98.32 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 55 IKTMIEKRKNSYPLQYILGEREFWGMDFNVSEGVLIPRQDTEILIEETLKKLKNHKHKSNLkgFEIGVGSGIISITLLKE 134
Cdd:TIGR03704 30 LAAMVDRRVAGLPLEHVLGWAEFCGLRIAVDPGVFVPRRRTEFLVDEAAALARPRSGTLVV--VDLCCGSGAVGAALAAA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 135 IETLIMIGVDINDKAIELTKANASKHQVSdrlcILNSNLFEKINKE--NQFDFIISNPPYIETKVIDSLQEDIKQHEPKL 212
Cdd:TIGR03704 108 LDGIELHAADIDPAAVRCARRNLADAGGT----VHEGDLYDALPTAlrGRVDILAANAPYVPTDAIALMPPEARDHEPRV 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503127684 213 ALDGGADGLDFYRDIIEQSKHYISPEGFIAFEIGYNQAEAVKKIFVENGYQnVTIAKDLAGFDRVVIG 280
Cdd:TIGR03704 184 ALDGGADGLDVLRRVAAGAPDWLAPGGHLLVETSERQAPLAVEAFARAGLI-ARVASSEELYATVVIG 250
|
|
| PRK14968 |
PRK14968 |
putative methyltransferase; Provisional |
84-279 |
6.54e-22 |
|
putative methyltransferase; Provisional
Pssm-ID: 237872 [Multi-domain] Cd Length: 188 Bit Score: 90.34 E-value: 6.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 84 VSEGVLIPRQDTEILIEetlkklkNHKHKSNLKGFEIGVGSGIISITLLKEieTLIMIGVDINDKAIELTKANASKHQVS 163
Cdd:PRK14968 1 LNDEVYEPAEDSFLLAE-------NAVDKKGDRVLEVGTGSGIVAIVAAKN--GKKVVGVDINPYAVECAKCNAKLNNIR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 164 DR-LCILNSNLFEKInKENQFDFIISNPPYIETKVIDSLQEDIkqhepKLALDGGADGLDFYRDIIEQSKHYISPEGFIA 242
Cdd:PRK14968 72 NNgVEVIRSDLFEPF-RGDKFDVILFNPPYLPTEEEEEWDDWL-----NYALSGGKDGREVIDRFLDEVGRYLKPGGRIL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 503127684 243 FEI----GYnqaEAVKKIFVENGYQNVTIAKDLAGFDRVVI 279
Cdd:PRK14968 146 LLQssltGE---DEVLEYLEKLGFEAEVVAEEKFPFEELIV 183
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
119-243 |
9.36e-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: 69.02 E-value: 9.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 119 EIGVGSGIISITLLKEIETLIMIGVDINDKAIELTKANASKHQVSDRLCILNSNL--FEKINKENQFDFIISNPPYIET- 195
Cdd:COG4123 43 DLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLkeFAAELPPGSFDLVVSNPPYFKAg 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 503127684 196 --KVIDSLQEDIKQHEPKLALDggadgldfyrDIIEQSKHYISPEGFIAF 243
Cdd:COG4123 123 sgRKSPDEARAIARHEDALTLE----------DLIRAAARLLKPGGRFAL 162
|
|
| PrmC_N |
pfam17827 |
PrmC N-terminal domain; This entry corresponds to the N-terminal alpha helical domain of the ... |
5-73 |
6.10e-13 |
|
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: 62.50 E-value: 6.10e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503127684 5 DIINYGVSMIK--NTESPSLEIQMMIAKVIEKDRLYIMLNLEEDIDESKVEIIKTMIEKRKNSYPLQYILG 73
Cdd:pfam17827 1 EALRWASSRLKeaGIESPRLDAELLLAHVLGLDRTDLLLHPEEELSEEELERFEELLERRAAGEPLQYILG 71
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
120-192 |
1.38e-12 |
|
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification
Pssm-ID: 442062 [Multi-domain] Cd Length: 191 Bit Score: 64.83 E-value: 1.38e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503127684 120 IGVGSGIISITLLKEIETLIMIGVDINDKAIELTKANASKHQVsDRLCILNSNLFEKInKENQFDFIISNPPY 192
Cdd:COG2813 56 LGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAANGL-ENVEVLWSDGLSGV-PDGSFDLILSNPPF 126
|
|
| hemK_rel_arch |
TIGR00537 |
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ... |
119-239 |
3.38e-11 |
|
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 129628 [Multi-domain] Cd Length: 179 Bit Score: 60.64 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 119 EIGVGSGIISITLLKEIETLimIGVDINDKAIELTKANASKHQVSdrLCILNSNLFEKINKenQFDFIISNPPYIETKvi 198
Cdd:TIGR00537 25 EIGAGTGLVAIRLKGKGKCI--LTTDINPFAVKELRENAKLNNVG--LDVVMTDLFKGVRG--KFDVILFNPPYLPLE-- 96
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 503127684 199 dslQEDIKQHEPKLALDGGADGLDFYRDIIEQSKHYISPEG 239
Cdd:TIGR00537 97 ---DDLRRGDWLDVAIDGGKDGRKVIDRFLDELPEILKEGG 134
|
|
| MTS |
pfam05175 |
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ... |
116-239 |
8.39e-11 |
|
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: 59.53 E-value: 8.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 116 KGFEIGVGSGIISITLLKEIETLIMIGVDINDKAIELTKANASKHQVsDRLCILNSNLFEKInKENQFDFIISNPPYiet 195
Cdd:pfam05175 34 KVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGL-ENGEVVASDVYSGV-EDGKFDLIISNPPF--- 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 503127684 196 kvidslqedikqHEpklaldGGADGLDFYRDIIEQSKHYISPEG 239
Cdd:pfam05175 109 ------------HA------GLATTYNVAQRFIADAKRHLRPGG 134
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
116-216 |
8.43e-06 |
|
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: 43.96 E-value: 8.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 116 KGFEIGVGSGIISITLLKEIETLImIGVDINDKAIELTKANAsKHQVSDRLCILNSNLFE-KINKENQFDFIISNPPYie 194
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARV-TGVDISPVALELARKAA-AALLADNVEVLKGDAEElPPEADESFDVIISDPPL-- 76
|
90 100
....*....|....*....|..
gi 503127684 195 TKVIDSLQEDIKQHEPKLALDG 216
Cdd:cd02440 77 HHLVEDLARFLEEARRLLKPGG 98
|
|
| rsmC |
PRK09489 |
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC; |
114-207 |
1.15e-05 |
|
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
Pssm-ID: 181902 [Multi-domain] Cd Length: 342 Bit Score: 46.08 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 114 NLKG--FEIGVGSGIISITLLKEIETLIMIGVDINDKAIELTKANASKHQVSDRlcILNSNLFEKInkENQFDFIISNPP 191
Cdd:PRK09489 195 HTKGkvLDVGCGAGVLSAVLARHSPKIRLTLSDVSAAALESSRATLAANGLEGE--VFASNVFSDI--KGRFDMIISNPP 270
|
90
....*....|....*....
gi 503127684 192 Y---IETKvIDSLQEDIKQ 207
Cdd:PRK09489 271 FhdgIQTS-LDAAQTLIRG 288
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
119-189 |
2.71e-05 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 42.17 E-value: 2.71e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503127684 119 EIGVGSGIISITLLKEIETLImIGVDINDKAIELTKANASKHQVSDRLCILNsnlFEKIN-KENQFDFIISN 189
Cdd:pfam13649 3 DLGCGTGRLTLALARRGGARV-TGVDLSPEMLERARERAAEAGLNVEFVQGD---AEDLPfPDGSFDLVVSS 70
|
|
| HsdM |
COG0286 |
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms]; |
133-262 |
3.37e-05 |
|
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
Pssm-ID: 440055 [Multi-domain] Cd Length: 243 Bit Score: 44.02 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 133 KEIETLIMIGVDINDKAIELTKANASKHQVSDRLCILNSNLFEKINKENQFDFIISNPPYIETKVIDSLQEDIKQ-HEPK 211
Cdd:COG0286 71 DERKKLSLYGQEINPTTYRLAKMNLLLHGIGDPNIELGDTLSNDGDELEKFDVVLANPPFGGKWKKEELKDDLLGrFGYG 150
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 503127684 212 LALDGGADGLdFyrdiIEQSKHYISPEGFIAF----EIGYNQAE-AVKKIFVENGY 262
Cdd:COG0286 151 LPPKSNADLL-F----LQHILSLLKPGGRAAVvlpdGVLFRGAEkEIRKKLLENDL 201
|
|
| prmA |
PRK00517 |
50S ribosomal protein L11 methyltransferase; |
120-270 |
5.68e-05 |
|
50S ribosomal protein L11 methyltransferase;
Pssm-ID: 234786 [Multi-domain] Cd Length: 250 Bit Score: 43.60 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 120 IGVGSGIISITLLK----EIetlimIGVDINDKAIELTKANASKHQVSDRLCILNSNLfekinkenQFDFIISNppyIET 195
Cdd:PRK00517 126 VGCGSGILAIAAAKlgakKV-----LAVDIDPQAVEAARENAELNGVELNVYLPQGDL--------KADVIVAN---ILA 189
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503127684 196 KVIDSLQEDIKQHepkLALDGgadgldfyrDIIeqskhyISpeGFIAfeigyNQAEAVKKIFVENGYQNVTIAKD 270
Cdd:PRK00517 190 NPLLELAPDLARL---LKPGG---------RLI------LS--GILE-----EQADEVLEAYEEAGFTLDEVLER 239
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
122-192 |
1.08e-04 |
|
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440663 [Multi-domain] Cd Length: 172 Bit Score: 41.86 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 122 VGSGiisiTLLkeIETLIM----IGVDINDKAIELTKANAskhqvsDRLCILNSNLF----EKIN-KENQFDFIISNPPY 192
Cdd:COG1041 35 CGTG----TIL--IEAGLLgrrvIGSDIDPKMVEGARENL------EHYGYEDADVIrgdaRDLPlADESVDAIVTDPPY 102
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
119-189 |
1.76e-04 |
|
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: 40.39 E-value: 1.76e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503127684 119 EIGVGSGIISITLLKEIETliMIGVDINDKAIELTKANASKHQVSdrlcILNSNLFEKINKENQFDFIISN 189
Cdd:COG2227 30 DVGCGTGRLALALARRGAD--VTGVDISPEALEIARERAAELNVD----FVQGDLEDLPLEDGSFDLVICS 94
|
|
| RlmL |
COG0116 |
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ... |
132-192 |
3.20e-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: 41.62 E-value: 3.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503127684 132 LKEIETLImIGVDINDKAIELTKANASKHQVSDRLCILNSNLFEkINKENQFDFIISNPPY 192
Cdd:COG0116 246 KRDPPLPI-FGSDIDPRAIEAARENAERAGVADLIEFEQADFRD-LEPPAEPGLIITNPPY 304
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
113-189 |
3.46e-04 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 40.09 E-value: 3.46e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503127684 113 SNLKGFEIGVGSGIISITLLKEIETLI-MIGVDINDKAIELTKANASKHQVSD-RLCILNSNLFEKINKENQFDFIISN 189
Cdd:pfam13847 3 KGMRVLDLGCGTGHLSFELAEELGPNAeVVGIDISEEAIEKARENAQKLGFDNvEFEQGDIEELPELLEDDKFDVVISN 81
|
|
| YtxK |
COG0827 |
Adenine-specific DNA N6-methylase [Replication, recombination and repair]; |
113-243 |
1.26e-03 |
|
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
Pssm-ID: 440589 [Multi-domain] Cd Length: 327 Bit Score: 39.55 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 113 SNLKGFEIGVGSGIISITLLKEIETLIMI-GVDINDKAIELTKANASKHQVSDRLCILNsnlFEKINKENQFDFIISNPP 191
Cdd:COG0827 115 EGLRILDPAVGTGNLLTTVLNQLKKKVNAyGVEVDDLLIRLAAVLANLQGHPVELFHQD---ALQPLLIDPVDVVISDLP 191
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 503127684 192 YIEtkvidsLQEDIKQHEPKLALDGGADGLDFYrdIIEQSKHYISPEGFIAF 243
Cdd:COG0827 192 VGY------YPNDERAKRFKLKADEGHSYAHHL--FIEQSLNYLKPGGYLFF 235
|
|
| COG2263 |
COG2263 |
Predicted RNA methylase [General function prediction only]; |
118-191 |
1.28e-03 |
|
Predicted RNA methylase [General function prediction only];
Pssm-ID: 441864 [Multi-domain] Cd Length: 199 Bit Score: 39.12 E-value: 1.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503127684 118 FEIGVGSGIISI-TLLKEIETLImiGVDINDKAIELTKANASKhqVSDRLCILNSNlFEKINKENQFDFIISNPP 191
Cdd:COG2263 50 LDLGCGTGMLAIgAALLGAKKVV--GVDIDPEALEIARENAER--LGVRVDFIRAD-VTRIPLGGSVDTVVMNPP 119
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
119-189 |
1.64e-03 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 36.87 E-value: 1.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503127684 119 EIGVGSGIISITLLKEIETLImiGVDINDKAIELTKANASKHQVSDRLCilnsnLFEKIN-KENQFDFIISN 189
Cdd:pfam08241 2 DVGCGTGLLTELLARLGARVT--GVDISPEMLELAREKAPREGLTFVVG-----DAEDLPfPDNSFDLVLSS 66
|
|
| UPF0020 |
pfam01170 |
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ... |
123-192 |
3.89e-03 |
|
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: 37.33 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503127684 123 GSGIISI-----------TLLKEIETLIMIGVDINDKAIELTKANASKHQVSDRL---CILNSNLFEKinkENQFDFIIS 188
Cdd:pfam01170 38 GSGTILIeaalmganiapGKFDARVRAPLYGSDIDRRMVQGARLNAENAGVGDLIefvQADAADLPLL---EGSVDVIVT 114
|
....
gi 503127684 189 NPPY 192
Cdd:pfam01170 115 NPPY 118
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
118-189 |
6.99e-03 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 35.42 E-value: 6.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503127684 118 FEIGVGSGIISITLLKEIETLIMIGVDINDKAIELTKANASKHQVSDRLCILNSNLFEKINKENQFDFIISN 189
Cdd:pfam08242 1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGSFDVVVAS 72
|
|
| |
