|
Name |
Accession |
Description |
Interval |
E-value |
| ubiE |
PRK00216 |
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ... |
1-228 |
4.07e-128 |
|
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;
Pssm-ID: 234689 [Multi-domain] Cd Length: 239 Bit Score: 361.39 E-value: 4.07e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 1 MAKADLDKDPFDVASMFDDVGKNYDLTNTVLSFGQDRVWRKRTRQRLDLKPGEKVLDLAAGTAVSTVELAKSG---AFCV 77
Cdd:PRK00216 1 FMTVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVgktGEVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 78 ACDFSQGMLAAGKDR--------DVSKVVGDGMQLPFADNSFDAVTISYGLRNIHDFRAGLKEMARVTKPGGRLTVAEFS 149
Cdd:PRK00216 81 GLDFSEGMLAVGREKlrdlglsgNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEFS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 509088952 150 TPVIPVFGTVYKEYLMRLLPQVARAVSSNPEAYIYLADSIRAWPSQAELAREINQNGWSDCGWQNLTFGIVALHSAIKP 228
Cdd:PRK00216 161 KPTNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELAAMLEEAGFERVRYRNLTGGIVALHVGYKP 239
|
|
| MenG_MenH_UbiE |
TIGR01934 |
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ... |
13-227 |
4.22e-91 |
|
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273884 [Multi-domain] Cd Length: 223 Bit Score: 267.21 E-value: 4.22e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 13 VASMFDDVGKNYDLTNTVLSFGQDRVWRKRTRQRLDLKPGEKVLDLAAGTAVSTVELAKSGAF---CVACDFSQGMLAAG 89
Cdd:TIGR01934 1 VQEMFDRIAPKYDLLNDLLSFGLHRLWRRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDrgkVTGVDFSSEMLEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 90 KDR-----DVSKVVGDGMQLPFADNSFDAVTISYGLRNIHDFRAGLKEMARVTKPGGRLTVAEFSTPVIPVFGTVYKEYL 164
Cdd:TIGR01934 81 KKKselplNIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILEFSKPANALLKKFYKFYL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 509088952 165 MRLLPQVARAVSSNPEAYIYLADSIRAWPSQAELAREINQNGWSDCGWQNLTFGIVALHSAIK 227
Cdd:TIGR01934 161 KNVLPSIGGLISKNAEAYTYLPESIRAFPSQEELAAMLKEAGFEEVRYRSLTFGVAAIHVGKK 223
|
|
| Ubie_methyltran |
pfam01209 |
ubiE/COQ5 methyltransferase family; |
13-227 |
7.14e-66 |
|
ubiE/COQ5 methyltransferase family;
Pssm-ID: 395966 [Multi-domain] Cd Length: 228 Bit Score: 203.44 E-value: 7.14e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 13 VASMFDDVGKNYDLTNTVLSFGQDRVWRKRTRQRLDLKPGEKVLDLAAGTAVSTVELAKS---GAFCVACDFSQGMLAAG 89
Cdd:pfam01209 4 VGDVFSSVASKYDLMNDVISFGIHRLWKDFTMKCMGVKRGNKFLDVAGGTGDWTFGLSDSagsSGKVVGLDINENMLKEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 90 KDR-------DVSKVVGDGMQLPFADNSFDAVTISYGLRNIHDFRAGLKEMARVTKPGGRLTVAEFSTPVIPVFGTVYKE 162
Cdd:pfam01209 84 EKKakeegkyNIEFLQGNAEELPFEDDSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLEFSKPENPLLSQAYEL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 509088952 163 YLMRLLPQVARAVSSNPEAYIYLADSIRAWPSQAELAREINQNGWSDCGWQNLTFGIVALHSAIK 227
Cdd:pfam01209 164 YFKYVMPFMGKMFAKSYKSYQYLQESIRDFPDQKTLASMFEKAGFKSVGYESLTGGIAAIHWGIK 228
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
17-151 |
2.19e-39 |
|
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: 132.81 E-value: 2.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 17 FDDVGKNYDLTNTVLsfgqdrvwrkrtrQRLDLKPGEKVLDLAAGTAVSTVELAKSGAFCVACDFSQGMLAAGKDR---- 92
Cdd:COG2226 1 FDRVAARYDGREALL-------------AALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERaaea 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 509088952 93 --DVSKVVGDGMQLPFADNSFDAVTISYGLRNIHDFRAGLKEMARVTKPGGRLTVAEFSTP 151
Cdd:COG2226 68 glNVEFVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPP 128
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
54-143 |
4.18e-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: 57.83 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 54 KVLDLAAGTAVSTVELAKSGAFCV-ACDFSQGML-------AAGKDRDVSKVVGDGMQLPF-ADNSFDAV----TISYGL 120
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARVtGVDISPVALelarkaaAALLADNVEVLKGDAEELPPeADESFDVIisdpPLHHLV 80
|
90 100
....*....|....*....|...
gi 509088952 121 RNIHDFragLKEMARVTKPGGRL 143
Cdd:cd02440 81 EDLARF---LEEARRLLKPGGVL 100
|
|
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
47-146 |
7.10e-04 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 39.03 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 47 LDLKPGEKVLDLAAGTAVSTVELAKSGAFCVACDFSQGMLAAGKDR-----DVSKVVGDGMQLPFADNSFDAV--TISYG 119
Cdd:smart00650 9 ANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKfaaadNLTVIHGDALKFDLPKLQPYKVvgNLPYN 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 509088952 120 ---------LRNIHDFRAGL----KEMAR--VTKPG----GRLTVA 146
Cdd:smart00650 89 istpilfklLEEPPAFRDAVlmvqKEVARrlAAKPGskdyGRLSVL 134
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ubiE |
PRK00216 |
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ... |
1-228 |
4.07e-128 |
|
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;
Pssm-ID: 234689 [Multi-domain] Cd Length: 239 Bit Score: 361.39 E-value: 4.07e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 1 MAKADLDKDPFDVASMFDDVGKNYDLTNTVLSFGQDRVWRKRTRQRLDLKPGEKVLDLAAGTAVSTVELAKSG---AFCV 77
Cdd:PRK00216 1 FMTVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVgktGEVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 78 ACDFSQGMLAAGKDR--------DVSKVVGDGMQLPFADNSFDAVTISYGLRNIHDFRAGLKEMARVTKPGGRLTVAEFS 149
Cdd:PRK00216 81 GLDFSEGMLAVGREKlrdlglsgNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEFS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 509088952 150 TPVIPVFGTVYKEYLMRLLPQVARAVSSNPEAYIYLADSIRAWPSQAELAREINQNGWSDCGWQNLTFGIVALHSAIKP 228
Cdd:PRK00216 161 KPTNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELAAMLEEAGFERVRYRNLTGGIVALHVGYKP 239
|
|
| MenG_MenH_UbiE |
TIGR01934 |
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ... |
13-227 |
4.22e-91 |
|
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273884 [Multi-domain] Cd Length: 223 Bit Score: 267.21 E-value: 4.22e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 13 VASMFDDVGKNYDLTNTVLSFGQDRVWRKRTRQRLDLKPGEKVLDLAAGTAVSTVELAKSGAF---CVACDFSQGMLAAG 89
Cdd:TIGR01934 1 VQEMFDRIAPKYDLLNDLLSFGLHRLWRRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDrgkVTGVDFSSEMLEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 90 KDR-----DVSKVVGDGMQLPFADNSFDAVTISYGLRNIHDFRAGLKEMARVTKPGGRLTVAEFSTPVIPVFGTVYKEYL 164
Cdd:TIGR01934 81 KKKselplNIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILEFSKPANALLKKFYKFYL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 509088952 165 MRLLPQVARAVSSNPEAYIYLADSIRAWPSQAELAREINQNGWSDCGWQNLTFGIVALHSAIK 227
Cdd:TIGR01934 161 KNVLPSIGGLISKNAEAYTYLPESIRAFPSQEELAAMLKEAGFEEVRYRSLTFGVAAIHVGKK 223
|
|
| Ubie_methyltran |
pfam01209 |
ubiE/COQ5 methyltransferase family; |
13-227 |
7.14e-66 |
|
ubiE/COQ5 methyltransferase family;
Pssm-ID: 395966 [Multi-domain] Cd Length: 228 Bit Score: 203.44 E-value: 7.14e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 13 VASMFDDVGKNYDLTNTVLSFGQDRVWRKRTRQRLDLKPGEKVLDLAAGTAVSTVELAKS---GAFCVACDFSQGMLAAG 89
Cdd:pfam01209 4 VGDVFSSVASKYDLMNDVISFGIHRLWKDFTMKCMGVKRGNKFLDVAGGTGDWTFGLSDSagsSGKVVGLDINENMLKEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 90 KDR-------DVSKVVGDGMQLPFADNSFDAVTISYGLRNIHDFRAGLKEMARVTKPGGRLTVAEFSTPVIPVFGTVYKE 162
Cdd:pfam01209 84 EKKakeegkyNIEFLQGNAEELPFEDDSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLEFSKPENPLLSQAYEL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 509088952 163 YLMRLLPQVARAVSSNPEAYIYLADSIRAWPSQAELAREINQNGWSDCGWQNLTFGIVALHSAIK 227
Cdd:pfam01209 164 YFKYVMPFMGKMFAKSYKSYQYLQESIRDFPDQKTLASMFEKAGFKSVGYESLTGGIAAIHWGIK 228
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
17-151 |
2.19e-39 |
|
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: 132.81 E-value: 2.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 17 FDDVGKNYDLTNTVLsfgqdrvwrkrtrQRLDLKPGEKVLDLAAGTAVSTVELAKSGAFCVACDFSQGMLAAGKDR---- 92
Cdd:COG2226 1 FDRVAARYDGREALL-------------AALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERaaea 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 509088952 93 --DVSKVVGDGMQLPFADNSFDAVTISYGLRNIHDFRAGLKEMARVTKPGGRLTVAEFSTP 151
Cdd:COG2226 68 glNVEFVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPP 128
|
|
| PLN02233 |
PLN02233 |
ubiquinone biosynthesis methyltransferase |
16-208 |
3.39e-25 |
|
ubiquinone biosynthesis methyltransferase
Pssm-ID: 177877 [Multi-domain] Cd Length: 261 Bit Score: 99.58 E-value: 3.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 16 MFDDVGKNYDLTNTVLSFGQDRVWRKRTRQRLDLKPGEKVLDLAAGT---AVSTVELAKSGAFCVACDFSQGMLAAGKDR 92
Cdd:PLN02233 38 LFNRIAPVYDNLNDLLSLGQHRIWKRMAVSWSGAKMGDRVLDLCCGSgdlAFLLSEKVGSDGKVMGLDFSSEQLAVAASR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 93 DVSK----------VVGDGMQLPFADNSFDAVTISYGLRNIHDFRAGLKEMARVTKPGGRLTVAEFSTPVIPVFGTVYKE 162
Cdd:PLN02233 118 QELKakscykniewIEGDATDLPFDDCYFDAITMGYGLRNVVDRLKAMQEMYRVLKPGSRVSILDFNKSTQPFTTSMQEW 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 509088952 163 YLMRLLPQVARAVSSNPEaYIYLADSIRAWPSQAELAREINQNGWS 208
Cdd:PLN02233 198 MIDNVVVPVATGYGLAKE-YEYLKSSINEYLTGEELEKLALEAGFS 242
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
55-141 |
1.32e-24 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 93.01 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 55 VLDLAAGTAVSTVELAKS-GAFCVACDFSQGMLAAGKDR------DVSKVVGDGMQLPFADNSFDAVTISYGL--RNIHD 125
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERaaeaglNVEFVQGDAEDLPFPDGSFDLVVSSGVLhhLPDPD 80
|
90
....*....|....*.
gi 509088952 126 FRAGLKEMARVTKPGG 141
Cdd:pfam13649 81 LEAALREIARVLKPGG 96
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
56-143 |
2.09e-24 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 92.73 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 56 LDLAAGTAVSTVELAKSGAFCVACDFSQGMLAAGKDR----DVSKVVGDGMQLPFADNSFDAVTISYGLRNIHDFRAGLK 131
Cdd:pfam08241 1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKapreGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERALR 80
|
90
....*....|..
gi 509088952 132 EMARVTKPGGRL 143
Cdd:pfam08241 81 EIARVLKPGGIL 92
|
|
| PRK08317 |
PRK08317 |
hypothetical protein; Provisional |
40-148 |
4.88e-22 |
|
hypothetical protein; Provisional
Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 90.38 E-value: 4.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 40 RKRTRQRLDLKPGEKVLDLAAGTAVSTVELAK---SGAFCVACDFSQGMLAAGKDRD------VSKVVGDGMQLPFADNS 110
Cdd:PRK08317 8 RARTFELLAVQPGDRVLDVGCGPGNDARELARrvgPEGRVVGIDRSEAMLALAKERAaglgpnVEFVRGDADGLPFPDGS 87
|
90 100 110
....*....|....*....|....*....|....*...
gi 509088952 111 FDAVTISYGLRNIHDFRAGLKEMARVTKPGGRLTVAEF 148
Cdd:PRK08317 88 FDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLDT 125
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
36-151 |
6.64e-20 |
|
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: 81.99 E-value: 6.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 36 DRVWRKRTRQRLD--LKPGEKVLDLAAGTAVSTVELAKSGAFCVACDFSQGMLAAGKDR----DVSKVVGDGMQLPFADN 109
Cdd:COG2227 7 RDFWDRRLAALLArlLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERaaelNVDFVQGDLEDLPLEDG 86
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 509088952 110 SFDAVTISYGLRNIHDFRAGLKEMARVTKPGGRLTvaeFSTP 151
Cdd:COG2227 87 SFDLVICSEVLEHLPDPAALLRELARLLKPGGLLL---LSTP 125
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
12-143 |
1.07e-17 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 77.73 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 12 DVASMFDDVGKNYD--LTNTVLSFGQDRVwRKRTRQRLDLKPGEKVLDLAAGTAVSTVELAKSGAFCVACDFSQGMLAAG 89
Cdd:COG4976 6 YVEALFDQYADSYDaaLVEDLGYEAPALL-AEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKA 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 509088952 90 KDRDVSK--VVGDGMQLPFADNSFDAVTISYGLRNIHDFRAGLKEMARVTKPGGRL 143
Cdd:COG4976 85 REKGVYDrlLVADLADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLF 140
|
|
| PRK05785 |
PRK05785 |
hypothetical protein; Provisional |
17-138 |
2.14e-15 |
|
hypothetical protein; Provisional
Pssm-ID: 235607 [Multi-domain] Cd Length: 226 Bit Score: 72.41 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 17 FDDVGKNYDLTNTVLSFGQDRVWRK---RTRQRLDLKPGeKVLDLAAGTAVSTVELAK-SGAFCVACDFSQGMLAAGKDR 92
Cdd:PRK05785 15 YNKIPKAYDRANRFISFNQDVRWRAelvKTILKYCGRPK-KVLDVAAGKGELSYHFKKvFKYYVVALDYAENMLKMNLVA 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 509088952 93 DvSKVVGDGMQLPFADNSFDAVTISYGLRNIHDFRAGLKEMARVTK 138
Cdd:PRK05785 94 D-DKVVGSFEALPFRDKSFDVVMSSFALHASDNIEKVIAEFTRVSR 138
|
|
| BioC |
TIGR02072 |
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ... |
41-152 |
1.32e-13 |
|
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
Pssm-ID: 273953 [Multi-domain] Cd Length: 240 Bit Score: 67.70 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 41 KRTRQRLDLKPgEKVLDLAAGTAVSTVELAKSGAF--CVACDFSQGMLAAGKDRD---VSKVVGDGMQLPFADNSFDAVT 115
Cdd:TIGR02072 25 ALLKEKGIFIP-ASVLDIGCGTGYLTRALLKRFPQaeFIALDISAGMLAQAKTKLsenVQFICGDAEKLPLEDSSFDLIV 103
|
90 100 110
....*....|....*....|....*....|....*..
gi 509088952 116 ISYGLRNIHDFRAGLKEMARVTKPGGrltVAEFSTPV 152
Cdd:TIGR02072 104 SNLALQWCDDLSQALSELARVLKPGG---LLAFSTFG 137
|
|
| PLN02232 |
PLN02232 |
ubiquinone biosynthesis methyltransferase |
80-208 |
5.71e-13 |
|
ubiquinone biosynthesis methyltransferase
Pssm-ID: 165876 Cd Length: 160 Bit Score: 64.32 E-value: 5.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 80 DFSQGMLAAGKDRDVSK----------VVGDGMQLPFADNSFDAVTISYGLRNIHDFRAGLKEMARVTKPGGRLTVAEFS 149
Cdd:PLN02232 4 DFSSEQLAVAATRQSLKarscykciewIEGDAIDLPFDDCEFDAVTMGYGLRNVVDRLRAMKEMYRVLKPGSRVSILDFN 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 509088952 150 TPVIPVfGTVYKEYLMRLLPQVARAVSSNPEAYIYLADSIRAWPSQAELAREINQNGWS 208
Cdd:PLN02232 84 KSNQSV-TTFMQGWMIDNVVVPVATVYDLAKEYEYLKYSINGYLTGEELETLALEAGFS 141
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
51-143 |
1.34e-12 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 61.76 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 51 PGEKVLDLAAGTAVSTVELAK--SGAFCVACDFSQGMLAAGKDR--DVSKVVGDGMQLPFaDNSFDAVTISYGLRNIHDF 126
Cdd:COG4106 1 PPRRVLDLGCGTGRLTALLAErfPGARVTGVDLSPEMLARARARlpNVRFVVADLRDLDP-PEPFDLVVSNAALHWLPDH 79
|
90
....*....|....*..
gi 509088952 127 RAGLKEMARVTKPGGRL 143
Cdd:COG4106 80 AALLARLAAALAPGGVL 96
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
54-143 |
4.18e-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: 57.83 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 54 KVLDLAAGTAVSTVELAKSGAFCV-ACDFSQGML-------AAGKDRDVSKVVGDGMQLPF-ADNSFDAV----TISYGL 120
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARVtGVDISPVALelarkaaAALLADNVEVLKGDAEELPPeADESFDVIisdpPLHHLV 80
|
90 100
....*....|....*....|...
gi 509088952 121 RNIHDFragLKEMARVTKPGGRL 143
Cdd:cd02440 81 EDLARF---LEEARRLLKPGGVL 100
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
45-143 |
2.67e-10 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 56.86 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 45 QRLDLKPGEKVLDLAAGTAVSTVELAKS-GAFCVACDFSQGMLAAGKDR--------DVSKVVGDGMQLPfADNSFDAVt 115
Cdd:COG2230 45 RKLGLKPGMRVLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYARERaaeagladRVEVRLADYRDLP-ADGQFDAI- 122
|
90 100 110
....*....|....*....|....*....|....
gi 509088952 116 IS------YGLRNIHDFragLKEMARVTKPGGRL 143
Cdd:COG2230 123 VSigmfehVGPENYPAY---FAKVARLLKPGGRL 153
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
49-143 |
4.71e-10 |
|
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: 56.50 E-value: 4.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 49 LKPGEKVLDLAAGTAVSTVELAKSGAFCVACDFSQGMLAAGK-------DRDVSKVVGDGMQLPFADNSFDAV------- 114
Cdd:COG1041 24 AKEGDTVLDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGARenlehygYEDADVIRGDARDLPLADESVDAIvtdppyg 103
|
90 100 110
....*....|....*....|....*....|.
gi 509088952 115 -TISYGLRNIHDFRAG-LKEMARVTKPGGRL 143
Cdd:COG1041 104 rSSKISGEELLELYEKaLEEAARVLKPGGRV 134
|
|
| PRK10258 |
PRK10258 |
biotin biosynthesis protein BioC; Provisional |
55-198 |
8.37e-10 |
|
biotin biosynthesis protein BioC; Provisional
Pssm-ID: 182340 [Multi-domain] Cd Length: 251 Bit Score: 57.08 E-value: 8.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 55 VLDLAAGTAVSTVELAKSGAFCVACDFSQGMLAAGKDRDVSK--VVGDGMQLPFADNSFDAVTISYGLRNIHDFRAGLKE 132
Cdd:PRK10258 46 VLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQKDAADhyLAGDIESLPLATATFDLAWSNLAVQWCGNLSTALRE 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 509088952 133 MARVTKPGGRL---TVAEFSTPVipvfgtvykeylmrlLPQVARAVSSNPEAYIYLA-----DSIRAWPSQAEL 198
Cdd:PRK10258 126 LYRVVRPGGVVaftTLVQGSLPE---------------LHQAWQAVDERPHANRFLPpdaieQALNGWRYQHHI 184
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
48-143 |
8.55e-10 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 56.46 E-value: 8.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 48 DLKPGEKVLDLAAGTAVSTVELAKSGAFCV-ACDFSQGMLAAGKDR-------DVSKVVGDGMQL-PFADNSFDAVTISY 118
Cdd:COG0500 23 RLPKGGRVLDLGCGTGRNLLALAARFGGRViGIDLSPEAIALARARaakaglgNVEFLVADLAELdPLPAESFDLVVAFG 102
|
90 100 110
....*....|....*....|....*....|
gi 509088952 119 glrNIHDF-----RAGLKEMARVTKPGGRL 143
Cdd:COG0500 103 ---VLHHLppeerEALLRELARALKPGGVL 129
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
49-149 |
3.21e-09 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 53.96 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 49 LKPGEKVLDLAAGTAVSTVELAK---SGAFCVACDFSQGMLAAGKDR-------DVSKVVGDGMQLP--FADNSFDAVTI 116
Cdd:pfam13847 1 IDKGMRVLDLGCGTGHLSFELAEelgPNAEVVGIDISEEAIEKARENaqklgfdNVEFEQGDIEELPelLEDDKFDVVIS 80
|
90 100 110
....*....|....*....|....*....|...
gi 509088952 117 SYGLRNIHDFRAGLKEMARVTKPGGRLTVAEFS 149
Cdd:pfam13847 81 NCVLNHIPDPDKVLQEILRVLKPGGRLIISDPD 113
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
56-143 |
2.28e-08 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 50.44 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 56 LDLAAGTAVSTVELAKSGAFC--VACDFSQGMLAAGKDR-------DVSKVVGDGMQLPFAD-NSFDAVTISYGLRNIHD 125
Cdd:pfam08242 1 LEIGCGTGTLLRALLEALPGLeyTGLDISPAALEAARERlaalgllNAVRVELFQLDLGELDpGSFDVVVASNVLHHLAD 80
|
90
....*....|....*...
gi 509088952 126 FRAGLKEMARVTKPGGRL 143
Cdd:pfam08242 81 PRAVLRNIRRLLKPGGVL 98
|
|
| Methyltransf_23 |
pfam13489 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
40-151 |
4.03e-07 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 48.19 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 40 RKRTRQRLDLKPGEKVLDLAAGTAVSTVELAKSGAFCVACDFSQGMLAAGKDRDVSKVVgDGMQLPFADNSFDAVTISYG 119
Cdd:pfam13489 11 DLLLRLLPKLPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQF-DEQEAAVPAGKFDVIVAREV 89
|
90 100 110
....*....|....*....|....*....|..
gi 509088952 120 LRNIHDFRAGLKEMARVTKPGGRLtvaEFSTP 151
Cdd:pfam13489 90 LEHVPDPPALLRQIAALLKPGGLL---LLSTP 118
|
|
| arsM |
PRK11873 |
arsenite methyltransferase; |
49-146 |
5.50e-07 |
|
arsenite methyltransferase;
Pssm-ID: 237007 [Multi-domain] Cd Length: 272 Bit Score: 49.18 E-value: 5.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 49 LKPGEKVLDLAAGTA----VSTVELAKSG-AFCVacDFSQGMLAAGKD----RDVSKV---VGDGMQLPFADNSFDaVTI 116
Cdd:PRK11873 75 LKPGETVLDLGSGGGfdcfLAARRVGPTGkVIGV--DMTPEMLAKARAnarkAGYTNVefrLGEIEALPVADNSVD-VII 151
|
90 100 110
....*....|....*....|....*....|.
gi 509088952 117 SYGLRNIH-DFRAGLKEMARVTKPGGRLTVA 146
Cdd:PRK11873 152 SNCVINLSpDKERVFKEAFRVLKPGGRFAIS 182
|
|
| PLN02336 |
PLN02336 |
phosphoethanolamine N-methyltransferase |
46-148 |
5.92e-06 |
|
phosphoethanolamine N-methyltransferase
Pssm-ID: 177970 [Multi-domain] Cd Length: 475 Bit Score: 46.28 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 46 RLDLKPGEKVLDLAAGTAVSTVELAKS-GAFCVACDFSQGML------AAGKDRDVSKVVGDGMQLPFADNSFDAVTISY 118
Cdd:PLN02336 261 KLDLKPGQKVLDVGCGIGGGDFYMAENfDVHVVGIDLSVNMIsfalerAIGRKCSVEFEVADCTKKTYPDNSFDVIYSRD 340
|
90 100 110
....*....|....*....|....*....|
gi 509088952 119 GLRNIHDFRAGLKEMARVTKPGGRLTVAEF 148
Cdd:PLN02336 341 TILHIQDKPALFRSFFKWLKPGGKVLISDY 370
|
|
| PLN02244 |
PLN02244 |
tocopherol O-methyltransferase |
87-143 |
7.46e-06 |
|
tocopherol O-methyltransferase
Pssm-ID: 215135 [Multi-domain] Cd Length: 340 Bit Score: 45.89 E-value: 7.46e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 509088952 87 AAGKDRDVSKVVGDGMQLPFADNSFDAVTISYGLRNIHDFRAGLKEMARVTKPGGRL 143
Cdd:PLN02244 163 AQGLSDKVSFQVADALNQPFEDGQFDLVWSMESGEHMPDKRKFVQELARVAAPGGRI 219
|
|
| COG4627 |
COG4627 |
Predicted SAM-depedendent methyltransferase [General function prediction only]; |
104-146 |
6.24e-05 |
|
Predicted SAM-depedendent methyltransferase [General function prediction only];
Pssm-ID: 443666 [Multi-domain] Cd Length: 161 Bit Score: 42.16 E-value: 6.24e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 509088952 104 LPFADNSFDAVtisYGLRNI-----HDFRAGLKEMARVTKPGGRLTVA 146
Cdd:COG4627 40 LPFPDNSVDAI---YSSHVLehldyEEAPLALKECYRVLKPGGILRIV 84
|
|
| COG2521 |
COG2521 |
Predicted archaeal methyltransferase [General function prediction only]; |
45-143 |
1.74e-04 |
|
Predicted archaeal methyltransferase [General function prediction only];
Pssm-ID: 442011 [Multi-domain] Cd Length: 285 Bit Score: 41.82 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 45 QRLDLKPGEKVLDLAAGTAVSTVELAKSGAFCVacdfsqgmLAAGKDRDV---------SK---------VVGDGMQL-- 104
Cdd:COG2521 126 KLVGVRRGDRVLDTCTGLGYTAIEALKRGAREV--------ITVEKDPNVlelaelnpwSRelanerikiILGDASEVik 197
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 509088952 105 PFADNSFDAVtisyglrnIHD---F-RAGL-------KEMARVTKPGGRL 143
Cdd:COG2521 198 TFPDESFDAI--------IHDpprFsLAGElyslefyRELYRVLKPGGRL 239
|
|
| RsmB |
COG0144 |
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ... |
47-143 |
3.13e-04 |
|
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and biogenesis]; 16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family is part of the Pathway/BioSystem: 16S rRNA modification
Pssm-ID: 439914 [Multi-domain] Cd Length: 441 Bit Score: 41.15 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 47 LDLKPGEKVLDLAAG-----TAVStvELAKSGAFCVACDFSQGMLAAGKDR-------DVSKVVGDGMQLP-FADNSFDA 113
Cdd:COG0144 245 LDPKPGERVLDLCAApggktLHLA--ELMGNKGRVVAVDISEHRLKRLRENlarlglsNVEVVVADARELLeWLPGKFDR 322
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 509088952 114 V----------TIS------YgLRNIHDF-------RAGLKEMARVTKPGGRL 143
Cdd:COG0144 323 VlldapcsgtgTLRrhpdikW-RRTPEDIaelaalqRELLDAAARLLKPGGRL 374
|
|
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
47-146 |
7.10e-04 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 39.03 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 47 LDLKPGEKVLDLAAGTAVSTVELAKSGAFCVACDFSQGMLAAGKDR-----DVSKVVGDGMQLPFADNSFDAV--TISYG 119
Cdd:smart00650 9 ANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKfaaadNLTVIHGDALKFDLPKLQPYKVvgNLPYN 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 509088952 120 ---------LRNIHDFRAGL----KEMAR--VTKPG----GRLTVA 146
Cdd:smart00650 89 istpilfklLEEPPAFRDAVlmvqKEVARrlAAKPGskdyGRLSVL 134
|
|
| PLN02490 |
PLN02490 |
MPBQ/MSBQ methyltransferase |
51-156 |
2.66e-03 |
|
MPBQ/MSBQ methyltransferase
Pssm-ID: 215270 [Multi-domain] Cd Length: 340 Bit Score: 38.33 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 51 PGEKVLDLAAGTAVSTVELAKS--GAFCVACDFSQGMLAAGKDR----DVSKVVGDGMQLPFADNSFD----AVTISYGl 120
Cdd:PLN02490 113 RNLKVVDVGGGTGFTTLGIVKHvdAKNVTILDQSPHQLAKAKQKeplkECKIIEGDAEDLPFPTDYADryvsAGSIEYW- 191
|
90 100 110
....*....|....*....|....*....|....*.
gi 509088952 121 rniHDFRAGLKEMARVTKPGGRltvAEFSTPVIPVF 156
Cdd:PLN02490 192 ---PDPQRGIKEAYRVLKIGGK---ACLIGPVHPTF 221
|
|
| NNMT_PNMT_TEMT |
pfam01234 |
NNMT/PNMT/TEMT family; |
93-143 |
2.84e-03 |
|
NNMT/PNMT/TEMT family;
Pssm-ID: 395988 Cd Length: 261 Bit Score: 37.79 E-value: 2.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 509088952 93 DV--SKVVGDGMQLPFADNSFDAVTISYGLRNIHDFRAGLKEMARVTKPGGRL 143
Cdd:pfam01234 143 DVhqSPPLGAGVQLPPADCVVTIFCLEYACPDLEEYCRALRNLASLLKPGGHL 195
|
|
| MetW |
pfam07021 |
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ... |
49-157 |
3.01e-03 |
|
Methionine biosynthesis protein MetW; This family consists of several bacterial and one archaeal methionine biosynthesis MetW proteins. Biosynthesis of methionine from homoserine in Pseudomonas putida takes place in three steps. The first step is the acylation of homoserine to yield an acyl-L-homoserine. This reaction is catalyzed by the products of the metXW genes and is equivalent to the first step in enterobacteria, gram-positive bacteria and fungi, except that in these microorganizms the reaction is catalyzed by a single polypeptide (the product of the metA gene in Escherichia coli and the met5 gene product in Neurospora crassa). In Pseudomonas putida, as in gram-positive bacteria and certain fungi, the second and third steps are a direct sulfhydrylation that converts the O-acyl-L-homoserine into homocysteine and further methylation to yield methionine. The latter reaction can be mediated by either of the two methionine synthetases present in the cells.
Pssm-ID: 399779 Cd Length: 193 Bit Score: 37.43 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 49 LKPGEKVLDLAAGTAVSTVELAKS-GAFCVACDFSQGMLAAGKDRDVSKVVGD---GMQLpFADNSFDAVTISYGLRNIH 124
Cdd:pfam07021 11 IPPGSRVLDLGCGDGTLLYLLKEEkGVDGYGIELDAAGVAECVAKGLYVIQGDldeGLEH-FPDKSFDYVILSQTLQATR 89
|
90 100 110
....*....|....*....|....*....|...
gi 509088952 125 DFRAGLKEMARVtkpgGRLTVAEFstpviPVFG 157
Cdd:pfam07021 90 NPREVLDEMLRI----GRRCIVSF-----PNFG 113
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
47-145 |
5.42e-03 |
|
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: 36.71 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509088952 47 LDLKPGEKVLDLAAGTAVSTVELAKS--GAFCVACD-------FSQGMLAAGKDRDVSKVVGDGMQlPFADNSFDAVtIS 117
Cdd:COG2813 45 LPEPLGGRVLDLGCGYGVIGLALAKRnpEARVTLVDvnaraveLARANAAANGLENVEVLWSDGLS-GVPDGSFDLI-LS 122
|
90 100 110
....*....|....*....|....*....|....*...
gi 509088952 118 yglrN--IHDFRAGLKEMA--------RVTKPGGRLTV 145
Cdd:COG2813 123 ----NppFHAGRAVDKEVAhaliadaaRHLRPGGELWL 156
|
|
| |
