|
Name |
Accession |
Description |
Interval |
E-value |
| ketoArg_3Met |
TIGR04543 |
2-ketoarginine methyltransferase; This SAM-dependent C-methyltransferase performs the middle ... |
35-360 |
1.93e-100 |
|
2-ketoarginine methyltransferase; This SAM-dependent C-methyltransferase performs the middle step of a three step conversion from arginine to beta-methylarginine. It performs a C-methylation at position 3 of 5-guanidino-2-oxopentanoic acid (keto-arginine). An aminotransferase converts arginine to 5-guanidino-2-oxopentanoic acid, and later converts 5-guanidino-3-methyl-2-oxopentanoic acid to beta-methylarginine.
Pssm-ID: 275336 [Multi-domain] Cd Length: 331 Bit Score: 300.43 E-value: 1.93e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490679508 35 LDYVKGFVGAKVIFQMLKLGVFDDLLAG--KTLEEIASGRSLDPYLLRTVFEYLSVEGLLVKEGrgggASFRLSDYGSRI 112
Cdd:TIGR04543 4 IQPIRGFVLAQAIYHLFESGLFDELAEAgpRSVGELAEELGLDSDRLTGFLRYLANEGIVVESD----GVFSLTEKGREL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490679508 113 KHYEGWFNILIGGYDNIFSNIGAMLEEGIGGYKRDGKWVGVGSCQISKYDTIPITKAFIESVKPDAKQIVDFGCGNALYL 192
Cdd:TIGR04543 80 AEFRPWYELLVGGYGETFLQLGEVLQQGAGWASRDGTKVGIGSCGISHYDAIPLVRSLLARLPGAPASLVDLGCGDGRFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490679508 193 CTLAKELGDIKAVGIEPDTSAYEAGLKKVAEMGLQDQVRLVNVDALDY---EIDEQPDFILFGFVLQEIIAQIGRPAFIE 269
Cdd:TIGR04543 160 ADFCEALPEISAIGVDPDAGSYRAARALIRERGLADRVSLVNAGAEDFlrsDLGSGPDFFVLGFVLQEILGQEGRGAVVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490679508 270 YLRKLGRKFADSYLMVMEVDYDIDNREVMHSPMGRGYYNPYFLLHPFTNQLLLPKREWDEIFAQAGYDVVRDEVTSPKAD 349
Cdd:TIGR04543 240 FLRTILARFPDAHLIVIEVDHRPDDPAVMRHGLGLAYYNPYYLLHYFTEQRLETDAFWEELFAEAGLSVVAKLTTDPEVD 319
|
330
....*....|.
gi 490679508 350 PSGFGICYVLK 360
Cdd:TIGR04543 320 STGLELGYLLR 330
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
174-276 |
1.00e-11 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 62.64 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490679508 174 VKPDAKqIVDFGCGNALYLCTLAKELGdIKAVGIEPDTSAYEAGLKKVAEMGLQDQVRLVNVDALDYEIDEQPDFIlfgf 253
Cdd:COG2230 49 LKPGMR-VLDIGCGWGGLALYLARRYG-VRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAI---- 122
|
90 100
....*....|....*....|...
gi 490679508 254 VLQEIIAQIGRPAFIEYLRKLGR 276
Cdd:COG2230 123 VSIGMFEHVGPENYPAYFAKVAR 145
|
|
| PKS_MT |
smart00828 |
Methyltransferase in polyketide synthase (PKS) enzymes; |
179-339 |
1.05e-08 |
|
Methyltransferase in polyketide synthase (PKS) enzymes;
Pssm-ID: 214839 [Multi-domain] Cd Length: 224 Bit Score: 55.11 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490679508 179 KQIVDFGCGNALYLCTLAKELGDIKAVGIEPDTSAYEAGLKKVAEMGLQDQVRLVNVDALDyeiDEQPDF--ILFGFvlq 256
Cdd:smart00828 1 KRVLDFGCGYGSDLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQGRIRIFYRDSAK---DPFPDTydLVFGF--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490679508 257 EIIAQIGRPAfiEYLRKLGRKFADSYLMVMEvdydidnrEVMHSPMGRgyynpyfLLHPFTNQLLLPKREWDEIFAQAGY 336
Cdd:smart00828 75 EVIHHIKDKM--DLFSNISRHLKDGGHLVLA--------DFIANLLSA-------IEHEETTSYLVTREEWAELLARNNL 137
|
...
gi 490679508 337 DVV 339
Cdd:smart00828 138 RVV 140
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
181-277 |
7.84e-07 |
|
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).
Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 47.04 E-value: 7.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490679508 181 IVDFGCGNALYLCTLAkELGDIKAVGIEPDTSAYEAgLKKVAEMGLQDQVRLVNVDALD--YEIDEQPDFILFGFVLQEI 258
Cdd:cd02440 2 VLDLGCGTGALALALA-SGPGARVTGVDISPVALEL-ARKAAAALLADNVEVLKGDAEElpPEADESFDVIISDPPLHHL 79
|
90
....*....|....*....
gi 490679508 259 IAqiGRPAFIEYLRKLGRK 277
Cdd:cd02440 80 VE--DLARFLEEARRLLKP 96
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
181-276 |
4.05e-06 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 44.86 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490679508 181 IVDFGCGNALYLCTLAKELGdIKAVGIEPDTSAYEAGLKKVAEMGLqdQVRLVNVDALDYEIDEQP-DFILFGFVLQEii 259
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRGG-ARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSfDLVVSSGVLHH-- 75
|
90
....*....|....*..
gi 490679508 260 aqIGRPAFIEYLRKLGR 276
Cdd:pfam13649 76 --LPDPDLEAALREIAR 90
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ketoArg_3Met |
TIGR04543 |
2-ketoarginine methyltransferase; This SAM-dependent C-methyltransferase performs the middle ... |
35-360 |
1.93e-100 |
|
2-ketoarginine methyltransferase; This SAM-dependent C-methyltransferase performs the middle step of a three step conversion from arginine to beta-methylarginine. It performs a C-methylation at position 3 of 5-guanidino-2-oxopentanoic acid (keto-arginine). An aminotransferase converts arginine to 5-guanidino-2-oxopentanoic acid, and later converts 5-guanidino-3-methyl-2-oxopentanoic acid to beta-methylarginine.
Pssm-ID: 275336 [Multi-domain] Cd Length: 331 Bit Score: 300.43 E-value: 1.93e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490679508 35 LDYVKGFVGAKVIFQMLKLGVFDDLLAG--KTLEEIASGRSLDPYLLRTVFEYLSVEGLLVKEGrgggASFRLSDYGSRI 112
Cdd:TIGR04543 4 IQPIRGFVLAQAIYHLFESGLFDELAEAgpRSVGELAEELGLDSDRLTGFLRYLANEGIVVESD----GVFSLTEKGREL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490679508 113 KHYEGWFNILIGGYDNIFSNIGAMLEEGIGGYKRDGKWVGVGSCQISKYDTIPITKAFIESVKPDAKQIVDFGCGNALYL 192
Cdd:TIGR04543 80 AEFRPWYELLVGGYGETFLQLGEVLQQGAGWASRDGTKVGIGSCGISHYDAIPLVRSLLARLPGAPASLVDLGCGDGRFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490679508 193 CTLAKELGDIKAVGIEPDTSAYEAGLKKVAEMGLQDQVRLVNVDALDY---EIDEQPDFILFGFVLQEIIAQIGRPAFIE 269
Cdd:TIGR04543 160 ADFCEALPEISAIGVDPDAGSYRAARALIRERGLADRVSLVNAGAEDFlrsDLGSGPDFFVLGFVLQEILGQEGRGAVVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490679508 270 YLRKLGRKFADSYLMVMEVDYDIDNREVMHSPMGRGYYNPYFLLHPFTNQLLLPKREWDEIFAQAGYDVVRDEVTSPKAD 349
Cdd:TIGR04543 240 FLRTILARFPDAHLIVIEVDHRPDDPAVMRHGLGLAYYNPYYLLHYFTEQRLETDAFWEELFAEAGLSVVAKLTTDPEVD 319
|
330
....*....|.
gi 490679508 350 PSGFGICYVLK 360
Cdd:TIGR04543 320 STGLELGYLLR 330
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
174-276 |
1.00e-11 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 62.64 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490679508 174 VKPDAKqIVDFGCGNALYLCTLAKELGdIKAVGIEPDTSAYEAGLKKVAEMGLQDQVRLVNVDALDYEIDEQPDFIlfgf 253
Cdd:COG2230 49 LKPGMR-VLDIGCGWGGLALYLARRYG-VRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAI---- 122
|
90 100
....*....|....*....|...
gi 490679508 254 VLQEIIAQIGRPAFIEYLRKLGR 276
Cdd:COG2230 123 VSIGMFEHVGPENYPAYFAKVAR 145
|
|
| PKS_MT |
smart00828 |
Methyltransferase in polyketide synthase (PKS) enzymes; |
179-339 |
1.05e-08 |
|
Methyltransferase in polyketide synthase (PKS) enzymes;
Pssm-ID: 214839 [Multi-domain] Cd Length: 224 Bit Score: 55.11 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490679508 179 KQIVDFGCGNALYLCTLAKELGDIKAVGIEPDTSAYEAGLKKVAEMGLQDQVRLVNVDALDyeiDEQPDF--ILFGFvlq 256
Cdd:smart00828 1 KRVLDFGCGYGSDLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQGRIRIFYRDSAK---DPFPDTydLVFGF--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490679508 257 EIIAQIGRPAfiEYLRKLGRKFADSYLMVMEvdydidnrEVMHSPMGRgyynpyfLLHPFTNQLLLPKREWDEIFAQAGY 336
Cdd:smart00828 75 EVIHHIKDKM--DLFSNISRHLKDGGHLVLA--------DFIANLLSA-------IEHEETTSYLVTREEWAELLARNNL 137
|
...
gi 490679508 337 DVV 339
Cdd:smart00828 138 RVV 140
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
178-256 |
6.59e-07 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 47.13 E-value: 6.59e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490679508 178 AKQIVDFGCGNALYLCTLAKELGDIKAVGIEPDTSAYEAGLKKVAemglqdQVRLVNVDALDYEIDEQPDFILFGFVLQ 256
Cdd:COG4106 2 PRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLP------NVRFVVADLRDLDPPEPFDLVVSNAALH 74
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
181-277 |
7.84e-07 |
|
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).
Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 47.04 E-value: 7.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490679508 181 IVDFGCGNALYLCTLAkELGDIKAVGIEPDTSAYEAgLKKVAEMGLQDQVRLVNVDALD--YEIDEQPDFILFGFVLQEI 258
Cdd:cd02440 2 VLDLGCGTGALALALA-SGPGARVTGVDISPVALEL-ARKAAAALLADNVEVLKGDAEElpPEADESFDVIISDPPLHHL 79
|
90
....*....|....*....
gi 490679508 259 IAqiGRPAFIEYLRKLGRK 277
Cdd:cd02440 80 VE--DLARFLEEARRLLKP 96
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
169-276 |
1.13e-06 |
|
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: 47.32 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490679508 169 AFIESVKPDAKQIVDFGCGNALYLCTLAkELGdIKAVGIEPDTSAYEAGLKKVAEMGlqdqVRLVNVDALDYEI-DEQPD 247
Cdd:COG2227 16 ALLARLLPAGGRVLDVGCGTGRLALALA-RRG-ADVTGVDISPEALEIARERAAELN----VDFVQGDLEDLPLeDGSFD 89
|
90 100
....*....|....*....|....*....
gi 490679508 248 FILFGFVLQEIiaqigrPAFIEYLRKLGR 276
Cdd:COG2227 90 LVICSEVLEHL------PDPAALLRELAR 112
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
181-276 |
4.05e-06 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 44.86 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490679508 181 IVDFGCGNALYLCTLAKELGdIKAVGIEPDTSAYEAGLKKVAEMGLqdQVRLVNVDALDYEIDEQP-DFILFGFVLQEii 259
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRGG-ARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSfDLVVSSGVLHH-- 75
|
90
....*....|....*..
gi 490679508 260 aqIGRPAFIEYLRKLGR 276
Cdd:pfam13649 76 --LPDPDLEAALREIAR 90
|
|
| dimerization2 |
pfam16864 |
dimerization domain; This domain, found in methyltransferases, functions as a dimerization ... |
35-107 |
5.70e-06 |
|
dimerization domain; This domain, found in methyltransferases, functions as a dimerization domain.
Pssm-ID: 465287 Cd Length: 87 Bit Score: 44.09 E-value: 5.70e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490679508 35 LDYVKGFVGAKVIFQMLKLGVFDDLLAG-KTLEEIASGRSLDPYLLRTVFEYLSVEGLLVKEGRGGGASFRLSD 107
Cdd:pfam16864 2 LDLIDGFRASKVLFTACELGVFDLLAEGpLSAEEVAARLGASVDGTERLLDACVALGLLEREKTDGKGLYSNTE 75
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
159-258 |
7.08e-06 |
|
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: 45.37 E-value: 7.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490679508 159 SKYDTipiTKAFIESVKPDA-KQIVDFGCGNALYLCTLAKELGDIkaVGIEPDTSAYEAGLKKVAEMGLQDQVRLVNVDA 237
Cdd:COG2226 6 ARYDG---REALLAALGLRPgARVLDLGCGTGRLALALAERGARV--TGVDISPEMLELARERAAEAGLNVEFVVGDAED 80
|
90 100
....*....|....*....|.
gi 490679508 238 LDYEiDEQPDFILFGFVLQEI 258
Cdd:COG2226 81 LPFP-DGSFDLVISSFVLHHL 100
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
176-256 |
1.36e-04 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 42.60 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490679508 176 PDAKQIVDFGCGNALYLCTLAKELGDiKAVGIEPDTSAYEAGLKKVAEMGLqDQVRLVNVDALDYEIDEQP--DFILFGF 253
Cdd:COG0500 25 PKGGRVLDLGCGTGRNLLALAARFGG-RVIGIDLSPEAIALARARAAKAGL-GNVEFLVADLAELDPLPAEsfDLVVAFG 102
|
...
gi 490679508 254 VLQ 256
Cdd:COG0500 103 VLH 105
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
176-247 |
1.90e-04 |
|
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: 42.44 E-value: 1.90e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490679508 176 PDAKQIVDFGCGN-ALYLCtLAKELGDIKAVGIEPDTSAYEAGLKKVAEMGLQDQVRLVNVDALDYEIDEQPD 247
Cdd:COG4123 36 KKGGRVLDLGTGTgVIALM-LAQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAAELPPG 107
|
|
| Methyltransf_23 |
pfam13489 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
175-339 |
2.15e-04 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 41.26 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490679508 175 KPDAKQIVDFGCGNAlYLCTLAKELGdIKAVGIEPDTSAYEAGLKKVAEMGLQDQVRLVNvdaldyeiDEQPDFILFGFV 254
Cdd:pfam13489 20 LPSPGRVLDFGCGTG-IFLRLLRAQG-FSVTGVDPSPIAIERALLNVRFDQFDEQEAAVP--------AGKFDVIVAREV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490679508 255 LQEIiaqigrPAFIEYLRKLGRKFA-DSYLMVMEVDYDIDNREVMHspmgrgyYNPYfLLHPFTNQLLLPKREWDEIFAQ 333
Cdd:pfam13489 90 LEHV------PDPPALLRQIAALLKpGGLLLLSTPLASDEADRLLL-------EWPY-LRPRNGHISLFSARSLKRLLEE 155
|
....*.
gi 490679508 334 AGYDVV 339
Cdd:pfam13489 156 AGFEVV 161
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
182-256 |
3.17e-04 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 39.66 E-value: 3.17e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490679508 182 VDFGCGNALYLCTLAKELGDIKAVGIEPDTSAYEAGLKKVAEMGLQD--QVRLVNVDALDYEiDEQPDFILFGFVLQ 256
Cdd:pfam08242 1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNavRVELFQLDLGELD-PGSFDVVVASNVLH 76
|
|
| Methyltransf_4 |
pfam02390 |
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ... |
177-240 |
7.13e-03 |
|
Putative methyltransferase; This is a family of putative methyltransferases. The aligned region contains the GXGXG S-AdoMet binding site suggesting a putative methyltransferase activity.
Pssm-ID: 367068 Cd Length: 173 Bit Score: 36.88 E-value: 7.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490679508 177 DAKQIVDFGCGNALYLCTLAKELGDIKAVGIEPDTSAYEAGLKKVAEMGLQDqVRLVNVDALDY 240
Cdd:pfam02390 1 DAPVFLEIGCGMGGFLVAMAKANPDKNFIGIEIRVPGVAKALKKIDALGLQN-LRILCGNALDV 63
|
|
| |
