|
Name |
Accession |
Description |
Interval |
E-value |
| Pox_MCEL |
pfam03291 |
mRNA capping enzyme; This family of enzymes are related to pfam03919. |
136-468 |
3.81e-141 |
|
mRNA capping enzyme; This family of enzymes are related to pfam03919.
Pssm-ID: 281307 [Multi-domain] Cd Length: 332 Bit Score: 409.51 E-value: 3.81e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997907 136 EKQKNLEEGHSSTVAAHYNELQEVG--LEKRSQSRIFYLRNFNNWMKSVLIGEFLEKVRQKKkRDITVLDLGCGKGGDLL 213
Cdd:pfam03291 1 EGPFETNSNITDIVATHYNERPETGelLKPRQASPIIYLRNFNNWIKSLLISLYASKTFQNS-NKRKVLDLGCGKGGDLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997907 214 KWKKGRINKLVCTDIADVSVKQCQQRYEDMKNRRDS-EYIFSAEFITADSSKELLIDKFRDPQMCFDICSCQFVCHYSFE 292
Cdd:pfam03291 80 KWFKGGISQLIGTDIAEVSIEQCRERYNKLRSGNKSkYYKFDAEFITGDCFVSSLREVFEDPFGKFDIVSCQFAIHYSFE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997907 293 SYEQADMMLRNACERLSPGGYFIGTTPNSFEL----IRRLEASE--TESFGNEIYTVKFQ-KKGDYPLFGCKYDFNLEGV 365
Cdd:pfam03291 160 SEEKARTMLRNVAELLASGGVFIGTTPDSDFIsaltIKRLFAIEkdLPSFGNSIYSVKFEeEPPQVPLFGIKYDYNLEDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997907 366 V-DVPEFLVYFPLLNEMAKKYNMKLVYKKTFLEFYEEKIKnNENKMLLKRMQALEPYPanessklvsekvddyehAAKYM 444
Cdd:pfam03291 240 VdDVPEYIVPFETLVSLAEEYGLELVDKKTFADIFEEEIK-KEFKKLIKRMSAMESRP-----------------STRNF 301
|
330 340
....*....|....*....|....
gi 767997907 445 KNSQVRLPLGTLSKSEWEATRSFL 468
Cdd:pfam03291 302 FGLQRSAGKGTLGGDEWEAASFYL 325
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
184-320 |
2.37e-12 |
|
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: 63.88 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997907 184 IGEFLEKVRQKKKRditVLDLGCGkGGDLLKWKKGRINKLVCTDIADVSVKQCQQRYEDMKnrrdseyifsAEFITADss 263
Cdd:COG2227 14 LAALLARLLPAGGR---VLDVGCG-TGRLALALARRGADVTGVDISPEALEIARERAAELN----------VDFVQGD-- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 767997907 264 kellIDKFRDPQMCFDIcscqFVCHYSFESYEQADMMLRNACERLSPGGYFIGTTPN 320
Cdd:COG2227 78 ----LEDLPLEDGSFDL----VICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
200-315 |
3.52e-10 |
|
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: 57.05 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997907 200 TVLDLGCGKGGDLLKWKKGRINKLVCTDIADVSVKQCQQRyedmKNRRDSEYIfsaEFITADSSKellIDKFRDPQmcFD 279
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKA----AAALLADNV---EVLKGDAEE---LPPEADES--FD 68
|
90 100 110
....*....|....*....|....*....|....*.
gi 767997907 280 ICSCQFVCHYSFESYEQadmMLRNACERLSPGGYFI 315
Cdd:cd02440 69 VIISDPPLHHLVEDLAR---FLEEARRLLKPGGVLV 101
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Pox_MCEL |
pfam03291 |
mRNA capping enzyme; This family of enzymes are related to pfam03919. |
136-468 |
3.81e-141 |
|
mRNA capping enzyme; This family of enzymes are related to pfam03919.
Pssm-ID: 281307 [Multi-domain] Cd Length: 332 Bit Score: 409.51 E-value: 3.81e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997907 136 EKQKNLEEGHSSTVAAHYNELQEVG--LEKRSQSRIFYLRNFNNWMKSVLIGEFLEKVRQKKkRDITVLDLGCGKGGDLL 213
Cdd:pfam03291 1 EGPFETNSNITDIVATHYNERPETGelLKPRQASPIIYLRNFNNWIKSLLISLYASKTFQNS-NKRKVLDLGCGKGGDLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997907 214 KWKKGRINKLVCTDIADVSVKQCQQRYEDMKNRRDS-EYIFSAEFITADSSKELLIDKFRDPQMCFDICSCQFVCHYSFE 292
Cdd:pfam03291 80 KWFKGGISQLIGTDIAEVSIEQCRERYNKLRSGNKSkYYKFDAEFITGDCFVSSLREVFEDPFGKFDIVSCQFAIHYSFE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997907 293 SYEQADMMLRNACERLSPGGYFIGTTPNSFEL----IRRLEASE--TESFGNEIYTVKFQ-KKGDYPLFGCKYDFNLEGV 365
Cdd:pfam03291 160 SEEKARTMLRNVAELLASGGVFIGTTPDSDFIsaltIKRLFAIEkdLPSFGNSIYSVKFEeEPPQVPLFGIKYDYNLEDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997907 366 V-DVPEFLVYFPLLNEMAKKYNMKLVYKKTFLEFYEEKIKnNENKMLLKRMQALEPYPanessklvsekvddyehAAKYM 444
Cdd:pfam03291 240 VdDVPEYIVPFETLVSLAEEYGLELVDKKTFADIFEEEIK-KEFKKLIKRMSAMESRP-----------------STRNF 301
|
330 340
....*....|....*....|....
gi 767997907 445 KNSQVRLPLGTLSKSEWEATRSFL 468
Cdd:pfam03291 302 FGLQRSAGKGTLGGDEWEAASFYL 325
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
184-320 |
2.37e-12 |
|
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: 63.88 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997907 184 IGEFLEKVRQKKKRditVLDLGCGkGGDLLKWKKGRINKLVCTDIADVSVKQCQQRYEDMKnrrdseyifsAEFITADss 263
Cdd:COG2227 14 LAALLARLLPAGGR---VLDVGCG-TGRLALALARRGADVTGVDISPEALEIARERAAELN----------VDFVQGD-- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 767997907 264 kellIDKFRDPQMCFDIcscqFVCHYSFESYEQADMMLRNACERLSPGGYFIGTTPN 320
Cdd:COG2227 78 ----LEDLPLEDGSFDL----VICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
200-315 |
3.52e-10 |
|
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: 57.05 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997907 200 TVLDLGCGKGGDLLKWKKGRINKLVCTDIADVSVKQCQQRyedmKNRRDSEYIfsaEFITADSSKellIDKFRDPQmcFD 279
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKA----AAALLADNV---EVLKGDAEE---LPPEADES--FD 68
|
90 100 110
....*....|....*....|....*....|....*.
gi 767997907 280 ICSCQFVCHYSFESYEQadmMLRNACERLSPGGYFI 315
Cdd:cd02440 69 VIISDPPLHHLVEDLAR---FLEEARRLLKPGGVLV 101
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
201-312 |
5.02e-10 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 56.42 E-value: 5.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997907 201 VLDLGCGKGGDLLKWKKGRINKLVCTDIADVSVKQCQQRYEDMKNRrdseyifsAEFITADsskellIDKFRDPQMCFDI 280
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLN--------VEFVQGD------AEDLPFPDGSFDL 66
|
90 100 110
....*....|....*....|....*....|..
gi 767997907 281 CSCQFVCHYSfeSYEQADMMLRNACERLSPGG 312
Cdd:pfam13649 67 VVSSGVLHHL--PDPDLEAALREIARVLKPGG 96
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
196-331 |
1.37e-09 |
|
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: 56.54 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997907 196 KRDITVLDLGCGKGGDLLKWKKgRINKLVCTDIADVSVKQCQQRYEDMKNRrdseyifsAEFITADSskELLidKFRDPQ 275
Cdd:COG2226 21 RPGARVLDLGCGTGRLALALAE-RGARVTGVDISPEMLELARERAAEAGLN--------VEFVVGDA--EDL--PFPDGS 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 767997907 276 mcFDICSCQFVCHYsFESYEQAdmmLRNACERLSPGGYFI---GTTPNSFELIRRLEAS 331
Cdd:COG2226 88 --FDLVISSFVLHH-LPDPERA---LAEIARVLKPGGRLVvvdFSPPDLAELEELLAEA 140
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
193-315 |
1.03e-05 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 46.45 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997907 193 QKKKRDITVLDLGCGKGGDLLKWKKGRINKLVCTDIADVSVKQCQQRYEDMKnrrdseyIFSAEFITADSSKELLIdkfr 272
Cdd:COG0500 22 ERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAG-------LGNVEFLVADLAELDPL---- 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 767997907 273 dPQMCFD-ICSCQFVCHYSFESYEQAdmmLRNACERLSPGGYFI 315
Cdd:COG0500 91 -PAESFDlVVAFGVLHHLPPEEREAL---LRELARALKPGGVLL 130
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
202-315 |
2.40e-05 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 43.04 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997907 202 LDLGCGKGGdLLKWKKGRINKLVCTDIADVSVKQCQQRYEDMKNrrdseyifsaEFITADSSKELLIDKfrdpqmCFDIC 281
Cdd:pfam08241 1 LDVGCGTGL-LTELLARLGARVTGVDISPEMLELAREKAPREGL----------TFVVGDAEDLPFPDN------SFDLV 63
|
90 100 110
....*....|....*....|....*....|....
gi 767997907 282 SCQFVCHYsFESYEQAdmmLRNACERLSPGGYFI 315
Cdd:pfam08241 64 LSSEVLHH-VEDPERA---LREIARVLKPGGILI 93
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
202-314 |
9.23e-05 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 41.58 E-value: 9.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997907 202 LDLGCGKGGDLLKWKKGRIN-KLVCTDIADVSVKQCQQRYEDMKNRRDSEYifsaEFITADSSKELLIDkfrdpqmcFDI 280
Cdd:pfam08242 1 LEIGCGTGTLLRALLEALPGlEYTGLDISPAALEAARERLAALGLLNAVRV----ELFQLDLGELDPGS--------FDV 68
|
90 100 110
....*....|....*....|....*....|....
gi 767997907 281 CSCQFVCHYSfesyEQADMMLRNACERLSPGGYF 314
Cdd:pfam08242 69 VVASNVLHHL----ADPRAVLRNIRRLLKPGGVL 98
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
183-321 |
1.19e-04 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 43.06 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997907 183 LIGEFLEKVRQKKKRdiTVLDLGCGKG--GDLLKWKKGRInklVCTDIADVSVKQCQQRyedmknrrdSEYIfsaEFITA 260
Cdd:COG4976 34 LAEELLARLPPGPFG--RVLDLGCGTGllGEALRPRGYRL---TGVDLSEEMLAKAREK---------GVYD---RLLVA 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767997907 261 DsskellIDKFRDPQMCFDIcscqFVCHYSFESYEQADMMLRNACERLSPGGYFIGTTPNS 321
Cdd:COG4976 97 D------LADLAEPDGRFDL----IVAADVLTYLGDLAAVFAGVARALKPGGLFIFSVEDA 147
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
195-353 |
1.30e-04 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 42.40 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997907 195 KKRDITVLDLGCGKGGDLLKW--KKGRINKLVCTDIADVSVKQCQQryedmkNRRDSEYIFsAEFITADSSKELLIDKFR 272
Cdd:pfam13847 1 IDKGMRVLDLGCGTGHLSFELaeELGPNAEVVGIDISEEAIEKARE------NAQKLGFDN-VEFEQGDIEELPELLEDD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997907 273 dpqmCFDICSCQFVCHYSFESyeqaDMMLRNACERLSPGGYFIGTTPNSFELIRRLEASETESFGNEIYTVKFQKKGDYP 352
Cdd:pfam13847 74 ----KFDVVISNCVLNHIPDP----DKVLQEILRVLKPGGRLIISDPDSLAELPAHVKEDSTYYAGCVGGAILKKKLYEL 145
|
.
gi 767997907 353 L 353
Cdd:pfam13847 146 L 146
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
200-319 |
4.39e-04 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 41.07 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997907 200 TVLDLGCGKGGDLLKW-KKGRInKLVCTDIADVSVKQCQQRYEDMKNRRdseyifSAEFITADsskellidkFRD--PQM 276
Cdd:COG2230 54 RVLDIGCGWGGLALYLaRRYGV-RVTGVTLSPEQLEYARERAAEAGLAD------RVEVRLAD---------YRDlpADG 117
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 767997907 277 CFD-ICSCQFVCHYSFESYEQadmMLRNACERLSPGGYFIGTTP 319
Cdd:COG2230 118 QFDaIVSIGMFEHVGPENYPA---YFAKVARLLKPGGRLLLHTP 158
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
200-315 |
8.54e-04 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 38.65 E-value: 8.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997907 200 TVLDLGCGKGGDLLK----WKKGRInklVCTDIADVSVKQCQQRYEDmknrrdseyifsAEFITADsskellidkFRD-- 273
Cdd:COG4106 4 RVLDLGCGTGRLTALlaerFPGARV---TGVDLSPEMLARARARLPN------------VRFVVAD---------LRDld 59
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 767997907 274 PQMCFDICSCQFVCHYSfesyEQADMMLRNACERLSPGGYFI 315
Cdd:COG4106 60 PPEPFDLVVSNAALHWL----PDHAALLARLAAALAPGGVLA 97
|
|
|