|
Name |
Accession |
Description |
Interval |
E-value |
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
60-168 |
2.37e-16 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 433377 [Multi-domain] Cd Length: 97 Bit Score: 72.61 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574 60 VLDVACGTGVDSIMLVEEG--FSVTSVDASDKMLKYAlkERWNRRKEPAFDkwvIEEANWLTLDkdvPAGDGFDAVICLG 137
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRGpnARVTGVDLSPEMLERA--RERAAEAGLNVE---FVQGDAEDLP---FPDGSFDLVVSSG 72
|
90 100 110
....*....|....*....|....*....|.
gi 6435574 138 nSFAHLPDskgdqSEHRLALKNIASMVRPGG 168
Cdd:pfam13649 73 -VLHHLPD-----PDLEAALREIARVLKPGG 97
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
29-172 |
1.25e-12 |
|
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism];
Pssm-ID: 225137 [Multi-domain] Cd Length: 243 Bit Score: 66.20 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574 29 VWQLYIgdtrSRTAEYKAWLLGLlrqhgchRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlKERWNRrkepafd 108
Cdd:COG2227 43 LRLDYI----REVARLRFDLPGL-------RVLDVGCGGGILSEPLARLGASVTGIDASEKPIEVA-KLHALE------- 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6435574 109 kwvieeaNWLTLD------KDVPAGDG-FDAVICLgNSFAHLPDSkgdqsehRLALKNIASMVRPGGLLVI 172
Cdd:COG2227 104 -------SGVNIDyrqatvEDLASAGGqFDVVTCM-EVLEHVPDP-------ESFLRACAKLVKPGGILFL 159
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
59-172 |
2.46e-12 |
|
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: 62.06 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574 59 RVLDVACGTGVDSIMLVE-EGFSVTSVDASDKMLKYAlKERWNRRKEpafDKWVIEEANWLTLDKDvpAGDGFDAVIClG 137
Cdd:cd02440 1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELA-RKAAAALLA---DNVEVLKGDAEELPPE--ADESFDVIIS-D 73
|
90 100 110
....*....|....*....|....*....|....*
gi 6435574 138 NSFAHLPDSkgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:cd02440 74 PPLHHLVED------LARFLEEARRLLKPGGVLVL 102
|
|
| PRK07580 |
PRK07580 |
Mg-protoporphyrin IX methyl transferase; Validated |
21-165 |
8.02e-09 |
|
Mg-protoporphyrin IX methyl transferase; Validated
Pssm-ID: 236059 [Multi-domain] Cd Length: 230 Bit Score: 54.84 E-value: 8.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574 21 YADGEAARVwQLYIGDTRSRT-AEYKAWLLGLLRQHGChRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlKERw 99
Cdd:PRK07580 29 YSDAPVSKV-RATVRAGHQRMrDTVLSWLPADGDLTGL-RILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEA-RER- 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6435574 100 nrrkepAFDKWVIEEANWLTLDKDvPAGDGFDAVICLgNSFAHLPDSKGDQsehrlALKNIASMVR 165
Cdd:PRK07580 105 ------APEAGLAGNITFEVGDLE-SLLGRFDTVVCL-DVLIHYPQEDAAR-----MLAHLASLTR 157
|
|
| MenG_MenH_UbiE |
TIGR01934 |
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ... |
58-172 |
5.33e-06 |
|
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: 46.49 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574 58 HRVLDVACGTGVDSIML---VEEGFSVTSVDASDKMLKYALKerwnRRKEPAFDKWVIEEAnwltldKDVPAGDG-FDAV 133
Cdd:TIGR01934 41 QKVLDVACGTGDLAIELaksAPDRGKVTGVDFSSEMLEVAKK----KSELPLNIEFIQADA------EALPFEDNsFDAV 110
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 6435574 134 IC---LGNsFAHLPdskgdqsehrLALKNIASMVRPGGLLVI 172
Cdd:TIGR01934 111 TIafgLRN-VTDIQ----------KALREMYRVLKPGGRLVI 141
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
60-168 |
2.37e-16 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 433377 [Multi-domain] Cd Length: 97 Bit Score: 72.61 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574 60 VLDVACGTGVDSIMLVEEG--FSVTSVDASDKMLKYAlkERWNRRKEPAFDkwvIEEANWLTLDkdvPAGDGFDAVICLG 137
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRGpnARVTGVDLSPEMLERA--RERAAEAGLNVE---FVQGDAEDLP---FPDGSFDLVVSSG 72
|
90 100 110
....*....|....*....|....*....|.
gi 6435574 138 nSFAHLPDskgdqSEHRLALKNIASMVRPGG 168
Cdd:pfam13649 73 -VLHHLPD-----PDLEAALREIARVLKPGG 97
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
61-172 |
7.83e-13 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 429883 [Multi-domain] Cd Length: 94 Bit Score: 63.07 E-value: 7.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574 61 LDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkerwNRRKEPAFDKWVIEEANwltldkDVPAGDG-FDAVICLgNS 139
Cdd:pfam08241 1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELA-----REKAPREGLTFVVGDAE------DLPFPDNsFDLVLSS-EV 68
|
90 100 110
....*....|....*....|....*....|...
gi 6435574 140 FAHLPDskgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:pfam08241 69 LHHVED-------PERALREIARVLKPGGILII 94
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
29-172 |
1.25e-12 |
|
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism];
Pssm-ID: 225137 [Multi-domain] Cd Length: 243 Bit Score: 66.20 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574 29 VWQLYIgdtrSRTAEYKAWLLGLlrqhgchRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlKERWNRrkepafd 108
Cdd:COG2227 43 LRLDYI----REVARLRFDLPGL-------RVLDVGCGGGILSEPLARLGASVTGIDASEKPIEVA-KLHALE------- 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6435574 109 kwvieeaNWLTLD------KDVPAGDG-FDAVICLgNSFAHLPDSkgdqsehRLALKNIASMVRPGGLLVI 172
Cdd:COG2227 104 -------SGVNIDyrqatvEDLASAGGqFDVVTCM-EVLEHVPDP-------ESFLRACAKLVKPGGILFL 159
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
59-172 |
2.46e-12 |
|
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: 62.06 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574 59 RVLDVACGTGVDSIMLVE-EGFSVTSVDASDKMLKYAlKERWNRRKEpafDKWVIEEANWLTLDKDvpAGDGFDAVIClG 137
Cdd:cd02440 1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELA-RKAAAALLA---DNVEVLKGDAEELPPE--ADESFDVIIS-D 73
|
90 100 110
....*....|....*....|....*....|....*
gi 6435574 138 NSFAHLPDSkgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:cd02440 74 PPLHHLVED------LARFLEEARRLLKPGGVLVL 102
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
61-170 |
1.53e-10 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 56.99 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574 61 LDVACGTGVDSIMLVEE--GFSVTSVDASDKMLKYAlkerwnRRKEPAFDKWVIEEANWLTLDKDVPAGDGFDAVICLgN 138
Cdd:pfam08242 1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAA------RERLAALGLLNAVRVELFQLDLGELDPGSFDVVVAS-N 73
|
90 100 110
....*....|....*....|....*....|..
gi 6435574 139 SFAHLPDSKGdqsehrlALKNIASMVRPGGLL 170
Cdd:pfam08242 74 VLHHLADPRA-------VLRNIRRLLKPGGVL 98
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
59-174 |
2.54e-10 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 433524 [Multi-domain] Cd Length: 150 Bit Score: 57.81 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574 59 RVLDVACGTGVDSIMLVEEGFS---VTSVDASDKMLKYALKerwnRRKEPAFDKWVIEEANWLTLDKDVpAGDGFDAVIC 135
Cdd:pfam13847 6 RVLDLGCGTGHLSFELAEEVGPnaeVVGIDISEEAIEKARE----NAQKLGFDNVEFEQGDIEELPELL-EDDKFDVVIS 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 6435574 136 LGnSFAHLPDSkgdqsehRLALKNIASMVRPGGLLVIDH 174
Cdd:pfam13847 81 NC-VLNLIPDP-------DKVLQEILRVLKPGGRLIISD 111
|
|
| Methyltransf_23 |
pfam13489 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
33-172 |
2.04e-09 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 55.51 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574 33 YIGDTRSRTAEYKAWLLGLLRQHGchRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMlkyalkerwnrrKEPAFDKWVI 112
Cdd:pfam13489 1 YAHQRERLLADLLLRLLPKLPSPG--RVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIA------------IERALLNVRF 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574 113 EEANwltLDKDVPAGDGFDAVICLgNSFAHLPDskgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:pfam13489 67 DQFD---EQEAAVPAGKFDVIVAR-EVLEHVPD-------PPALLRQIAALLKPGGLLLL 115
|
|
| PRK07580 |
PRK07580 |
Mg-protoporphyrin IX methyl transferase; Validated |
21-165 |
8.02e-09 |
|
Mg-protoporphyrin IX methyl transferase; Validated
Pssm-ID: 236059 [Multi-domain] Cd Length: 230 Bit Score: 54.84 E-value: 8.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574 21 YADGEAARVwQLYIGDTRSRT-AEYKAWLLGLLRQHGChRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlKERw 99
Cdd:PRK07580 29 YSDAPVSKV-RATVRAGHQRMrDTVLSWLPADGDLTGL-RILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEA-RER- 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6435574 100 nrrkepAFDKWVIEEANWLTLDKDvPAGDGFDAVICLgNSFAHLPDSKGDQsehrlALKNIASMVR 165
Cdd:PRK07580 105 ------APEAGLAGNITFEVGDLE-SLLGRFDTVVCL-DVLIHYPQEDAAR-----MLAHLASLTR 157
|
|
| PRK08317 |
PRK08317 |
hypothetical protein; Provisional |
42-178 |
8.08e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 54.94 E-value: 8.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574 42 AEYKAWLLGLLRQHGCHRVLDVACGTGVDSIML---VEEGFSVTSVDASDKMLKYAlKERwnRRKEPAFDKWVIEEANWL 118
Cdd:PRK08317 5 RRYRARTFELLAVQPGDRVLDVGCGPGNDARELarrVGPEGRVVGIDRSEAMLALA-KER--AAGLGPNVEFVRGDADGL 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6435574 119 tldkdvPAGDG-FDAVICLgNSFAHLPDSKGdqsehrlALKNIASMVRPGGLLVIDHKNYD 178
Cdd:PRK08317 82 ------PFPDGsFDAVRSD-RVLQHLEDPAR-------ALAEIARVLRPGGRVVVLDTDWD 128
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
33-194 |
4.92e-08 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 223574 [Multi-domain] Cd Length: 257 Bit Score: 52.98 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574 33 YIGDTRSRTAEYKAWLLGLLRQHGCHRVLDVACGTGVDSIM--LVEEGFSVTSVDASDKMLKYALKerwnRRKEPAFDKW 110
Cdd:COG0500 25 AFLLLAEELLDLLLVLRLLRLLPGGLGVLDIGCGTGRLALLarLGGRGAYVVGVDLSPEMLALARA----RAEGAGLGLV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574 111 VIEEANWLTLDKDVPAGDGFDAVICLGNSFAHLPDSkgdqsehrlALKNIASMVRPGGLLVIDHKNYDYILSTGCAPPGK 190
Cdd:COG0500 101 DFVVADALGGVLPFEDSASFDLVISLLVLHLLPPAK---------ALRELLRVLKPGGRLVLSDLLRDGLLEGRLAALLG 171
|
....
gi 6435574 191 NIYY 194
Cdd:COG0500 172 FGDP 175
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE [Coenzyme transport and metabolism]; |
59-172 |
5.49e-08 |
|
Ubiquinone/menaquinone biosynthesis C-methylase UbiE [Coenzyme transport and metabolism];
Pssm-ID: 225136 [Multi-domain] Cd Length: 238 Bit Score: 52.27 E-value: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574 59 RVLDVACGTGVDSIMLVEEG--FSVTSVDASDKMLKYALKerwnRRKEPAFDKWVIEEANWLTLD-KDvpagDGFDAVIC 135
Cdd:COG2226 54 KVLDVACGTGDMALLLAKSVgtGEVVGLDISESMLEVARE----KLKKKGVQNVEFVVGDAENLPfPD----NSFDAVTI 125
|
90 100 110
....*....|....*....|....*....|....*..
gi 6435574 136 lGNSFAHLPDskgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:COG2226 126 -SFGLRNVTD-------IDKALKEMYRVLKPGGRLLV 154
|
|
| ubiE |
PRK00216 |
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ... |
58-172 |
3.43e-07 |
|
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;
Pssm-ID: 234689 [Multi-domain] Cd Length: 239 Bit Score: 50.15 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574 58 HRVLDVACGTGVDSIMLVEEG---FSVTSVDASDKMLKYAlKERWNRRKEPAFDKWVIEEANWLTLDKDVpagdgFDAV- 133
Cdd:PRK00216 53 DKVLDLACGTGDLAIALAKAVgktGEVVGLDFSEGMLAVG-REKLRDLGLSGNVEFVQGDAEALPFPDNS-----FDAVt 126
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 6435574 134 ICLG--NsfahLPDskgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:PRK00216 127 IAFGlrN----VPD-------IDKALREMYRVLKPGGRLVI 156
|
|
| MenG_MenH_UbiE |
TIGR01934 |
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ... |
58-172 |
5.33e-06 |
|
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: 46.49 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574 58 HRVLDVACGTGVDSIML---VEEGFSVTSVDASDKMLKYALKerwnRRKEPAFDKWVIEEAnwltldKDVPAGDG-FDAV 133
Cdd:TIGR01934 41 QKVLDVACGTGDLAIELaksAPDRGKVTGVDFSSEMLEVAKK----KSELPLNIEFIQADA------EALPFEDNsFDAV 110
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 6435574 134 IC---LGNsFAHLPdskgdqsehrLALKNIASMVRPGGLLVI 172
Cdd:TIGR01934 111 TIafgLRN-VTDIQ----------KALREMYRVLKPGGRLVI 141
|
|
| PLN02396 |
PLN02396 |
hexaprenyldihydroxybenzoate methyltransferase |
59-176 |
7.90e-04 |
|
hexaprenyldihydroxybenzoate methyltransferase
Pssm-ID: 178018 [Multi-domain] Cd Length: 322 Bit Score: 40.49 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574 59 RVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkeRWNRRKEPafdkwVIEEANWL--TLDKDVPAGDGFDAVICL 136
Cdd:PLN02396 134 KFIDIGCGGGLLSEPLARMGATVTGVDAVDKNVKIA---RLHADMDP-----VTSTIEYLctTAEKLADEGRKFDAVLSL 205
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 6435574 137 gnsfahlpdskgDQSEHRLA----LKNIASMVRPGGLLVIDHKN 176
Cdd:PLN02396 206 ------------EVIEHVANpaefCKSLSALTIPNGATVLSTIN 237
|
|
| PRK10258 |
PRK10258 |
biotin biosynthesis protein BioC; Provisional |
48-106 |
1.05e-03 |
|
biotin biosynthesis protein BioC; Provisional
Pssm-ID: 182340 [Multi-domain] Cd Length: 251 Bit Score: 39.74 E-value: 1.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 6435574 48 LLGLLRQHGCHRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkerwnRRKEPA 106
Cdd:PRK10258 34 LLAMLPQRKFTHVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQA------RQKDAA 86
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
35-172 |
1.60e-03 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 225139 [Multi-domain] Cd Length: 283 Bit Score: 39.15 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574 35 GDTRSRTAEYKAW--LLGLLRQHGCHRVLDVACGTGVDSIMLVEE-GFSVTSVDASDKMLKYALKErwnRRKEPAFDKWV 111
Cdd:COG2230 49 PDMTLEEAQRAKLdlILEKLGLKPGMTLLDIGCGWGGLAIYAAEEyGVTVVGVTLSEEQLAYAEKR---IAARGLEDNVE 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6435574 112 IEEANWLTLDKDvpagdgFDAVICLGnSFAHLpdskGDQSEHRLaLKNIASMVRPGGLLVI 172
Cdd:COG2230 126 VRLQDYRDFEEP------FDRIVSVG-MFEHV----GKENYDDF-FKKVYALLKPGGRMLL 174
|
|
| PRK09328 |
PRK09328 |
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional |
47-174 |
5.72e-03 |
|
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
Pssm-ID: 236467 [Multi-domain] Cd Length: 275 Bit Score: 37.45 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574 47 WLLGLLRQHGCHRVLDVACGTGVDSIMLVEE--GFSVTSVDASDKMLKYALKerwNRRKEPAfDKWVIEEANWLTldkDV 124
Cdd:PRK09328 99 WALEALLLKEPLRVLDLGTGSGAIALALAKErpDAEVTAVDISPEALAVARR---NAKHGLG-ARVEFLQGDWFE---PL 171
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574 125 PAGDgFDAVIClgN----SFAHLPDSKGDQSEH--RLAL--------------KNIASMVRPGGLLVIDH 174
Cdd:PRK09328 172 PGGR-FDLIVS--NppyiPEADIHLLQPEVRDHepHLALfggedgldfyrriiEQAPRYLKPGGWLLLEI 238
|
|
| HemK |
COG2890 |
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
47-174 |
6.68e-03 |
|
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];
Pssm-ID: 225443 [Multi-domain] Cd Length: 280 Bit Score: 37.32 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574 47 WLLGLLRQHGCHrVLDVACGTGVDSIMLVEEG--FSVTSVDASDKMLKYAlkeRWNRRKEpAFDKWVIEEANWLTldkdv 124
Cdd:COG2890 102 AALALLLQLDKR-ILDLGTGSGAIAIALAKEGpdAEVIAVDISPDALALA---RENAERN-GLVRVLVVQSDLFE----- 171
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6435574 125 PAGDGFDAVIC----LGNSFAHLPDSKGDqSEHRLAL--------------KNIASMVRPGGLLVIDH 174
Cdd:COG2890 172 PLRGKFDLIVSnppyIPAEDPELLPEVVR-YEPLLALvgggdglevyrrilGEAPDILKPGGVLILEI 238
|
|
|