|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02336 |
PLN02336 |
phosphoethanolamine N-methyltransferase |
14-495 |
0e+00 |
|
phosphoethanolamine N-methyltransferase
Pssm-ID: 177970 [Multi-domain] Cd Length: 475 Bit Score: 659.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 14 KEHSRQATVEEMMLDSHAQELTQHELPEILSLLPSLSGQRVLELGAGIGRYTSHLLTLASHVTAVDFMESFVEKNRQDNS 93
Cdd:PLN02336 1 KEHSVDLTVEAMMLDSKASDLDKEERPEILSLLPPYEGKSVLELGAGIGRFTGELAKKAGQVIALDFIESVIKKNESING 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 94 HYSNASFLQADVTK--LDFPKNSFDIIFSNWLLMYLSDEELTSLTERMLGWLSPGGYLFFRESCNYQSGDFKRTFNPTHY 171
Cdd:PLN02336 81 HYKNVKFMCADVTSpdLNISDGSVDLIFSNWLLMYLSDKEVENLAERMVKWLKVGGYIFFRESCFHQSGDSKRKNNPTHY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 172 RSSAHYSHLMTTTLREESEGAEkqvFGFDIVLNKTVQTYIKMKKNQNQVCWLLEKVGrdtacQEGFRTFQQFLDNQQYTR 251
Cdd:PLN02336 161 REPRFYTKVFKECHTRDEDGNS---FELSLVGCKCIGAYVKNKKNQNQICWLWQKVS-----STNDKGFQRFLDNVQYKS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 252 KGILRYEKMFGAGYVSTGGPSTTKEFVDLLNLKPGMKVLDVGCGIGGGNFYMAKAFGVEVLGLDLSANMVDIAIERAMEE 331
Cdd:PLN02336 233 SGILRYERVFGEGFVSTGGLETTKEFVDKLDLKPGQKVLDVGCGIGGGDFYMAENFDVHVVGIDLSVNMISFALERAIGR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 332 KLpSVHFEVADATKREFPEASFDVVYSRDTILHIDEKLALFKRFHSWLKPGGQVLISDYCCGEKPWTPQFQEYVKQRGYI 411
Cdd:PLN02336 313 KC-SVEFEVADCTKKTYPDNSFDVIYSRDTILHIQDKPALFRSFFKWLKPGGKVLISDYCRSPGTPSPEFAEYIKQRGYD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 412 LYTPPQYGKFLQQAGFSNVRAEDRTAQFMQVIQTELERAAAMKDEFIKEFSEEDYLAIVNGWSDKLKRCKTGDQRWGLFH 491
Cdd:PLN02336 392 LHDVQAYGQMLKDAGFDDVIAEDRTDQFLQVLQRELDAVEKEKDEFISDFSEEDYNDIVGGWKAKLVRSSSGEQKWGLFI 471
|
....
gi 291190262 492 ATRN 495
Cdd:PLN02336 472 AKKK 475
|
|
| PTZ00098 |
PTZ00098 |
phosphoethanolamine N-methyltransferase; Provisional |
242-495 |
2.37e-73 |
|
phosphoethanolamine N-methyltransferase; Provisional
Pssm-ID: 173391 [Multi-domain] Cd Length: 263 Bit Score: 232.94 E-value: 2.37e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 242 QFLDNQQYTRKGILRYEKMFGAGYVSTGGPSTTKEFVDLLNLKPGMKVLDVGCGIGGGNFYMAKAFGVEVLGLDLSANMV 321
Cdd:PTZ00098 9 TYLENNQYSDEGIKAYEFIFGEDYISSGGIEATTKILSDIELNENSKVLDIGSGLGGGCKYINEKYGAHVHGVDICEKMV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 322 DIAIERAMEEKlpSVHFEVADATKREFPEASFDVVYSRDTILHI--DEKLALFKRFHSWLKPGGQVLISDYCCGEKP-WT 398
Cdd:PTZ00098 89 NIAKLRNSDKN--KIEFEANDILKKDFPENTFDMIYSRDAILHLsyADKKKLFEKCYKWLKPNGILLITDYCADKIEnWD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 399 PQFQEYVKQRGYILYTPPQYGKFLQQAGFSNVRAEDRTAQFMQVIQTELERAAAMKDEFIKEFSEEDYLAIVNGWSDKLK 478
Cdd:PTZ00098 167 EEFKAYIKKRKYTLIPIQEYGDLIKSCNFQNVVAKDISDYWLELLQVELKKLEEKKEEFLKLYSEKEYNSLKDGWTRKIK 246
|
250
....*....|....*..
gi 291190262 479 RCKTGDQRWGLFHATRN 495
Cdd:PTZ00098 247 DTKRKLQKWGYFKAQKM 263
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
275-410 |
1.41e-33 |
|
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: 123.95 E-value: 1.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 275 KEFVDLLNLKPGMKVLDVGCGIGGGNFYMAKAfGVEVLGLDLSANMVDIAIERAmEEKLPSVHFEVADATKREFPEASFD 354
Cdd:COG2226 12 EALLAALGLRPGARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERA-AEAGLNVEFVVGDAEDLPFPDGSFD 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 291190262 355 VVYSRDTILHIDEKLALFKRFHSWLKPGGQVLISDYCcgeKPWTPQFQEYVKQRGY 410
Cdd:COG2226 90 LVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFS---PPDLAELEELLAEAGF 142
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
276-389 |
5.39e-31 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 117.34 E-value: 5.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 276 EFVDLLNLKPGMKVLDVGCGIGGGNFYMAKAFGVEVLGLDLSANMVDIAIERAMEEKLP-SVHFEVADAtkREFP-EASF 353
Cdd:COG2230 42 LILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLAdRVEVRLADY--RDLPaDGQF 119
|
90 100 110
....*....|....*....|....*....|....*...
gi 291190262 354 DVVYSRDTILHIDEK--LALFKRFHSWLKPGGQVLISD 389
Cdd:COG2230 120 DAIVSIGMFEHVGPEnyPAYFAKVARLLKPGGRLLLHT 157
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
289-383 |
6.42e-29 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 109.58 E-value: 6.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 289 VLDVGCGIGGGNFYMAKAFGVEVLGLDLSANMVDIAIERAmEEKLPSVHFEVADATKREFPEASFDVVYSRDTILHI--D 366
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERA-AEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLpdP 79
|
90
....*....|....*..
gi 291190262 367 EKLALFKRFHSWLKPGG 383
Cdd:pfam13649 80 DLEAALREIARVLKPGG 96
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
283-390 |
9.04e-28 |
|
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: 107.41 E-value: 9.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 283 LKPGMKVLDVGCGIGGGNFYMAKAfGVEVLGLDLSANMVDIAIERAMEEKlpsVHFEVADATKREFPEASFDVVYSRDTI 362
Cdd:COG2227 22 LPAGGRVLDVGCGTGRLALALARR-GADVTGVDISPEALEIARERAAELN---VDFVQGDLEDLPLEDGSFDLVICSEVL 97
|
90 100
....*....|....*....|....*...
gi 291190262 363 LHIDEKLALFKRFHSWLKPGGQVLISDY 390
Cdd:COG2227 98 EHLPDPAALLRELARLLKPGGLLLLSTP 125
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
263-390 |
3.15e-26 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 105.38 E-value: 3.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 263 AGYVSTGGPSTTKEFVDLLNLKPGMKVLDVGCGIGGGNFYMAKAFGVEVLGLDLSANMVDIAIERAMEEKLPSVHFEVAD 342
Cdd:COG0500 4 SYYSDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVAD 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 291190262 343 ATKR-EFPEASFDVVYSRDTILHIDEKL--ALFKRFHSWLKPGGQVLISDY 390
Cdd:COG0500 84 LAELdPLPAESFDLVVAFGVLHHLPPEEreALLRELARALKPGGVLLLSAS 134
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
285-389 |
4.53e-26 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 101.82 E-value: 4.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 285 PGMKVLDVGCGIGGGNFYMAKAF-GVEVLGLDLSANMVDIAIERameekLPSVHFEVADAtkREF-PEASFDVVYSRDTI 362
Cdd:COG4106 1 PPRRVLDLGCGTGRLTALLAERFpGARVTGVDLSPEMLARARAR-----LPNVRFVVADL--RDLdPPEPFDLVVSNAAL 73
|
90 100
....*....|....*....|....*..
gi 291190262 363 LHIDEKLALFKRFHSWLKPGGQVLISD 389
Cdd:COG4106 74 HWLPDHAALLARLAAALAPGGVLAVQV 100
|
|
| PRK08317 |
PRK08317 |
hypothetical protein; Provisional |
280-389 |
3.48e-23 |
|
hypothetical protein; Provisional
Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 98.09 E-value: 3.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 280 LLNLKPGMKVLDVGCGIGGGNFYMAKAFGVE--VLGLDLSANMVDIAIERAmEEKLPSVHFEVADATKREFPEASFDVVY 357
Cdd:PRK08317 14 LLAVQPGDRVLDVGCGPGNDARELARRVGPEgrVVGIDRSEAMLALAKERA-AGLGPNVEFVRGDADGLPFPDGSFDAVR 92
|
90 100 110
....*....|....*....|....*....|..
gi 291190262 358 SRDTILHIDEKLALFKRFHSWLKPGGQVLISD 389
Cdd:PRK08317 93 SDRVLQHLEDPARALAEIARVLRPGGRVVVLD 124
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
28-153 |
7.42e-23 |
|
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: 94.29 E-value: 7.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 28 DSHAQELTQHElpEILSLLPSLSGQRVLELGAGIGRYTSHLLTLASHVTAVDFMESFVEKNRQDNSHYS-NASFLQADVT 106
Cdd:COG2226 2 DRVAARYDGRE--ALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGlNVEFVVGDAE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 291190262 107 KLDFPKNSFDIIFSNWLLMYLSDEELTsLTErMLGWLSPGGYLFFRE 153
Cdd:COG2226 80 DLPFPDGSFDLVISSFVLHHLPDPERA-LAE-IARVLKPGGRLVVVD 124
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
54-147 |
2.14e-22 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 91.47 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 54 VLELGAGIGRYTSHLLTLA-SHVTAVDFMESFVEKNRQDNSHYS-NASFLQADVTKLDFPKNSFDIIFSNWLLMYLSDEE 131
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRGgARVTGVDLSPEMLERARERAAEAGlNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80
|
90
....*....|....*.
gi 291190262 132 LTSLTERMLGWLSPGG 147
Cdd:pfam13649 81 LEAALREIARVLKPGG 96
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
290-387 |
3.30e-22 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 90.80 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 290 LDVGCGIGGGNFYMAKaFGVEVLGLDLSANMVDIAIERAmeeKLPSVHFEVADATKREFPEASFDVVYSRDTILHIDEKL 369
Cdd:pfam08241 1 LDVGCGTGLLTELLAR-LGARVTGVDISPEMLELAREKA---PREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPE 76
|
90
....*....|....*...
gi 291190262 370 ALFKRFHSWLKPGGQVLI 387
Cdd:pfam08241 77 RALREIARVLKPGGILII 94
|
|
| PLN02244 |
PLN02244 |
tocopherol O-methyltransferase |
288-434 |
1.68e-21 |
|
tocopherol O-methyltransferase
Pssm-ID: 215135 [Multi-domain] Cd Length: 340 Bit Score: 95.58 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 288 KVLDVGCGIGGGNFYMAKAFGVEVLGLDLS----ANMVDIAIERAMEEKlpsVHFEVADATKREFPEASFDVVYSRDTIL 363
Cdd:PLN02244 121 RIVDVGCGIGGSSRYLARKYGANVKGITLSpvqaARANALAAAQGLSDK---VSFQVADALNQPFEDGQFDLVWSMESGE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 364 HIDEKLALFKRFHSWLKPGGQVLISDYC-----CGEKPWTPQFQEYVKQ--RGYilYTPP-----QYGKFLQQAGFSNVR 431
Cdd:PLN02244 198 HMPDKRKFVQELARVAAPGGRIIIVTWChrdlePGETSLKPDEQKLLDKicAAY--YLPAwcstsDYVKLAESLGLQDIK 275
|
...
gi 291190262 432 AED 434
Cdd:PLN02244 276 TED 278
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
51-151 |
1.48e-20 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 86.42 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 51 GQRVLELGAGIGRYTSHLLTL--ASHVTAVDFMESFVEKNRQdnsHYSNASFLQADVTKLDFPKnSFDIIFSNWLLMYLS 128
Cdd:COG4106 2 PRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARA---RLPNVRFVVADLRDLDPPE-PFDLVVSNAALHWLP 77
|
90 100
....*....|....*....|...
gi 291190262 129 DeeLTSLTERMLGWLSPGGYLFF 151
Cdd:COG4106 78 D--HAALLARLAAALAPGGVLAV 98
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
26-151 |
6.08e-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: 85.45 E-value: 6.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 26 MLDSHAQELTQHELPEILSLLPsLSGQRVLELGAGIGRYTSHLLTLASHVTAVDFMESFVEKNRQDNSHySNASFLQADV 105
Cdd:COG2227 1 MSDPDARDFWDRRLAALLARLL-PAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAE-LNVDFVQGDL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 291190262 106 TKLDFPKNSFDIIFSNWLLMYLSDEEltSLTERMLGWLSPGGYLFF 151
Cdd:COG2227 79 EDLPLEDGSFDLVICSEVLEHLPDPA--ALLRELARLLKPGGLLLL 122
|
|
| ubiE |
PRK00216 |
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ... |
275-431 |
7.05e-20 |
|
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;
Pssm-ID: 234689 [Multi-domain] Cd Length: 239 Bit Score: 88.67 E-value: 7.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 275 KEFVDLLNLKPGMKVLDVGCGIGGGNFYMAKAFGV--EVLGLDLSANMVDIAIERAMEEKL-PSVHFEVADATKREFPEA 351
Cdd:PRK00216 41 RKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKtgEVVGLDFSEGMLAVGREKLRDLGLsGNVEFVQGDAEALPFPDN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 352 SFDVVysrdTI-------LHIDEklALfKRFHSWLKPGGQVLISDYccgEKPWTPQFqeyvkQRGYILYTP---PQYGKF 421
Cdd:PRK00216 121 SFDAV----TIafglrnvPDIDK--AL-REMYRVLKPGGRLVILEF---SKPTNPPL-----KKAYDFYLFkvlPLIGKL 185
|
170 180 190
....*....|....*....|....*....|....*..
gi 291190262 422 ---------------------------LQQAGFSNVR 431
Cdd:PRK00216 186 isknaeaysylaesirafpdqeelaamLEEAGFERVR 222
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
55-151 |
1.09e-19 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 83.87 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 55 LELGAGIGRYTSHLLTLASHVTAVDFMESFVEKNRQdNSHYSNASFLQADVTKLDFPKNSFDIIFSNWLLMYLSDEElTS 134
Cdd:pfam08241 1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELARE-KAPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPE-RA 78
|
90
....*....|....*..
gi 291190262 135 LTErMLGWLSPGGYLFF 151
Cdd:pfam08241 79 LRE-IARVLKPGGILII 94
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
275-428 |
4.74e-19 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 84.66 E-value: 4.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 275 KEFVDLLNLKPGMKVLDVGCGIGggnfYMAKAF---GVEVLGLDLSANMVDIAieramEEKLPSVHFEVADATKREFPEA 351
Cdd:COG4976 36 EELLARLPPGPFGRVLDLGCGTG----LLGEALrprGYRLTGVDLSEEMLAKA-----REKGVYDRLLVADLADLAEPDG 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291190262 352 SFDVVYSRDTILHIDEKLALFKRFHSWLKPGGqVLISDYccgekpwtpqfqEYVKQRGYILYTPPQYGKFLQQAGFS 428
Cdd:COG4976 107 RFDLIVAADVLTYLGDLAAVFAGVARALKPGG-LFIFSV------------EDADGSGRYAHSLDYVRDLLAAAGFE 170
|
|
| Methyltransf_23 |
pfam13489 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
280-430 |
6.80e-19 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 83.63 E-value: 6.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 280 LLNLKPGMKVLDVGCGIGggNFYM-AKAFGVEVLGLDLSANMVDIAIerameeklPSVHFEVADATKREFPEASFDVVYS 358
Cdd:pfam13489 17 LPKLPSPGRVLDFGCGTG--IFLRlLRAQGFSVTGVDPSPIAIERAL--------LNVRFDQFDEQEAAVPAGKFDVIVA 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291190262 359 RDTILHIDEKLALFKRFHSWLKPGGQVLISDYCCgEKPWTPQFQEY----VKQRGYILYTPPQYGKFLQQAGFSNV 430
Cdd:pfam13489 87 REVLEHVPDPPALLRQIAALLKPGGLLLLSTPLA-SDEADRLLLEWpylrPRNGHISLFSARSLKRLLEEAGFEVV 161
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
283-426 |
5.56e-18 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 80.54 E-value: 5.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 283 LKPGMKVLDVGCGIGGGNFYMAKAFG--VEVLGLDLSANMVDIAIERAMEEKLPSVHFEVADATKRE--FPEASFDVVYS 358
Cdd:pfam13847 1 IDKGMRVLDLGCGTGHLSFELAEELGpnAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEELPelLEDDKFDVVIS 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291190262 359 RDTILHIDEKLALFKRFHSWLKPGGQVLISDyCCGEKPWTPQFQE---YVKQRGYILYTPPQYGKFLQQAG 426
Cdd:pfam13847 81 NCVLNHIPDPDKVLQEILRVLKPGGRLIISD-PDSLAELPAHVKEdstYYAGCVGGAILKKKLYELLEEAG 150
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
23-176 |
1.15e-17 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 80.81 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 23 EEMMLDSHAQELTQHELPEILSLLPSLSGQRVLELGAGIGRYTSHLLTLASHVTAVDFMESFVEKNRQDNSHysnASFLQ 102
Cdd:COG4976 19 DAALVEDLGYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKGVY---DRLLV 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291190262 103 ADVTKLDFPKNSFDIIFSNWLLMYLSDeeLTSLTERMLGWLSPGGYLFFreSCNYQSGDFKRTFNPTHYRSSAH 176
Cdd:COG4976 96 ADLADLAEPDGRFDLIVAADVLTYLGD--LAAVFAGVARALKPGGLFIF--SVEDADGSGRYAHSLDYVRDLLA 165
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
288-390 |
2.08e-17 |
|
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: 77.86 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 288 KVLDVGCGIGGGNFYMAKAFGVEVLGLDLSANMVDIAIERAMEEKLPSVHFEVADATK-REFPEASFDVVYSRDTILHID 366
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEElPPEADESFDVIISDPPLHHLV 80
|
90 100
....*....|....*....|....*
gi 291190262 367 EKL-ALFKRFHSWLKPGGQVLISDY 390
Cdd:cd02440 81 EDLaRFLEEARRLLKPGGVLVLTLV 105
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
290-383 |
2.82e-17 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 77.02 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 290 LDVGCGIGGGNFYMAKAF-GVEVLGLDLSANMVDIAIERAMEEKLPS---VHFEVADATKREFPeaSFDVVYSRDTILHI 365
Cdd:pfam08242 1 LEIGCGTGTLLRALLEALpGLEYTGLDISPAALEAARERLAALGLLNavrVELFQLDLGELDPG--SFDVVVASNVLHHL 78
|
90
....*....|....*...
gi 291190262 366 DEKLALFKRFHSWLKPGG 383
Cdd:pfam08242 79 ADPRAVLRNIRRLLKPGG 96
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
28-151 |
4.92e-16 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 76.49 E-value: 4.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 28 DSHAQELTQHELPEILSLLPSLS-GQRVLELGAGIGRYTSHLL-TLASHVTAVDFMESFVEKNRQ--DNSHYSNASFLQA 103
Cdd:COG0500 3 DSYYSDELLPGLAALLALLERLPkGGRVLDLGCGTGRNLLALAaRFGGRVIGIDLSPEAIALARAraAKAGLGNVEFLVA 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 291190262 104 DVTKL-DFPKNSFDIIFSNWLLMYLSDEELTSLTERMLGWLSPGGYLFF 151
Cdd:COG0500 83 DLAELdPLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLL 131
|
|
| CMAS |
pfam02353 |
Mycolic acid cyclopropane synthetase; This family consist of ... |
279-466 |
1.75e-15 |
|
Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.
Pssm-ID: 396777 [Multi-domain] Cd Length: 272 Bit Score: 76.60 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 279 DLLNLKPGMKVLDVGCGIGGGNFYMAKAFGVEVLGLDLSANMVDIAIERAMEEKLPSVHfEVADATKREFPEaSFDVVYS 358
Cdd:pfam02353 55 DKLGLKPGMTLLDIGCGWGGLMRRAAERYDVNVVGLTLSKNQYKLARKRVAAEGLARKV-EVLLQDYRDFDE-PFDRIVS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 359 RDTILHIDEK--LALFKRFHSWLKPGGQVLISDYCCGEKPWTPQ-------FQEYVKQRGYiLYTPPQYGKFLQQAGFSN 429
Cdd:pfam02353 133 VGMFEHVGHEnyDTFFKKLYNLLPPGGLMLLHTITGLHPDETSErglplkfIDKYIFPGGE-LPSISMIVESSSEAGFTV 211
|
170 180 190
....*....|....*....|....*....|....*..
gi 291190262 430 VRAEDRTAQFMQVIQTELERAAAMKDEFIKEFSEEDY 466
Cdd:pfam02353 212 EDVESLRPHYAKTLDLWAENLQANKDEAIALQSEEFY 248
|
|
| BioC |
TIGR02072 |
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ... |
29-151 |
3.57e-15 |
|
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: 75.02 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 29 SHAQELTQHELPEILSLLPSLSGQRVLELGAGIGRYTSHLLTL--ASHVTAVDFMESFVEKNRQDNShySNASFLQADVT 106
Cdd:TIGR02072 13 AKIQREMAKRLLALLKEKGIFIPASVLDIGCGTGYLTRALLKRfpQAEFIALDISAGMLAQAKTKLS--ENVQFICGDAE 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 291190262 107 KLDFPKNSFDIIFSNWLLMYLSDeeLTSLTERMLGWLSPGGYLFF 151
Cdd:TIGR02072 91 KLPLEDSSFDLIVSNLALQWCDD--LSQALSELARVLKPGGLLAF 133
|
|
| Ubie_methyltran |
pfam01209 |
ubiE/COQ5 methyltransferase family; |
275-422 |
5.13e-14 |
|
ubiE/COQ5 methyltransferase family;
Pssm-ID: 395966 [Multi-domain] Cd Length: 228 Bit Score: 71.32 E-value: 5.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 275 KEFV-DLLNLKPGMKVLDVGCGIGGGNFYMAKAFGV--EVLGLDLSANMVDIAIERAMEEKLPSVHFEVADATKREFPEA 351
Cdd:pfam01209 31 KDFTmKCMGVKRGNKFLDVAGGTGDWTFGLSDSAGSsgKVVGLDINENMLKEGEKKAKEEGKYNIEFLQGNAEELPFEDD 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291190262 352 SFDVVYSRDTILHIDEKLALFKRFHSWLKPGGQVLISDYccgEKPWTPQFQEYVKQrgYILYTPPQYGKFL 422
Cdd:pfam01209 111 SFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLEF---SKPENPLLSQAYEL--YFKYVMPFMGKMF 176
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
53-151 |
1.31e-13 |
|
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: 67.07 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 53 RVLELGAGIGRYTSHLL-TLASHVTAVDFMESFVEKNRQDNSHY--SNASFLQADVTKLDF-PKNSFDIIFSNWLLMYLs 128
Cdd:cd02440 1 RVLDLGCGTGALALALAsGPGARVTGVDISPVALELARKAAAALlaDNVEVLKGDAEELPPeADESFDVIISDPPLHHL- 79
|
90 100
....*....|....*....|...
gi 291190262 129 DEELTSLTERMLGWLSPGGYLFF 151
Cdd:cd02440 80 VEDLARFLEEARRLLKPGGVLVL 102
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
33-151 |
5.57e-13 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 66.49 E-value: 5.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 33 ELTQHELPEILSLLPSLSGQRVLELGAGIGRytsHLLTLASH----VTAVDFMESFVEKNRQDNSHY---SNASFLQADV 105
Cdd:COG2230 34 EAQEAKLDLILRKLGLKPGMRVLDIGCGWGG---LALYLARRygvrVTGVTLSPEQLEYARERAAEAglaDRVEVRLADY 110
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 291190262 106 TKLDFPkNSFDIIFSNWLLMYLSDEELTSLTERMLGWLSPGGYLFF 151
Cdd:COG2230 111 RDLPAD-GQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
280-418 |
3.07e-12 |
|
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: 64.97 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 280 LLNL---KPGMKVLDVGCGIGGgnfyM---AKAFGVEVLGLDLSANMVDIAIERAMEEKLPSVHFEVADATKREFPEASF 353
Cdd:COG1041 18 LVNLagaKEGDTVLDPFCGTGT----IlieAGLLGRRVIGSDIDPKMVEGARENLEHYGYEDADVIRGDARDLPLADESV 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291190262 354 DVV-----YSRDTILHIDEKLALFKRF----HSWLKPGGQVLISdyccgekpWTPQFQEYVKQRGY-ILYTPPQY 418
Cdd:COG1041 94 DAIvtdppYGRSSKISGEELLELYEKAleeaARVLKPGGRVVIV--------TPRDIDELLEEAGFkVLERHEQR 160
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
55-149 |
4.94e-11 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 59.30 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 55 LELGAGIGRYTSHLLTLA--SHVTAVDFMESFVEKNRQDNSHYSNASFLQADVTKLDFPK---NSFDIIFSNWLLMYLSD 129
Cdd:pfam08242 1 LEIGCGTGTLLRALLEALpgLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGEldpGSFDVVVASNVLHHLAD 80
|
90 100
....*....|....*....|
gi 291190262 130 eeLTSLTERMLGWLSPGGYL 149
Cdd:pfam08242 81 --PRAVLRNIRRLLKPGGVL 98
|
|
| BioC |
TIGR02072 |
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ... |
288-391 |
5.38e-11 |
|
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: 62.69 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 288 KVLDVGCGIGGGNFYMAKAF-GVEVLGLDLSANMVDIAieramEEKLPS-VHFEVADATKREFPEASFDVVYSRDTILHI 365
Cdd:TIGR02072 37 SVLDIGCGTGYLTRALLKRFpQAEFIALDISAGMLAQA-----KTKLSEnVQFICGDAEKLPLEDSSFDLIVSNLALQWC 111
|
90 100
....*....|....*....|....*.
gi 291190262 366 DEKLALFKRFHSWLKPGGQVLISDYC 391
Cdd:TIGR02072 112 DDLSQALSELARVLKPGGLLAFSTFG 137
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
50-156 |
6.23e-11 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 60.51 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 50 SGQRVLELGAGIGRYTSHLLTLA---SHVTAVDFMESFVEKNRQ--DNSHYSNASFLQADVTKLD--FPKNSFDIIFSNW 122
Cdd:pfam13847 3 KGMRVLDLGCGTGHLSFELAEELgpnAEVVGIDISEEAIEKAREnaQKLGFDNVEFEQGDIEELPelLEDDKFDVVISNC 82
|
90 100 110
....*....|....*....|....*....|....
gi 291190262 123 LLMYLSDEELTslTERMLGWLSPGGYLFFRESCN 156
Cdd:pfam13847 83 VLNHIPDPDKV--LQEILRVLKPGGRLIISDPDS 114
|
|
| PTZ00098 |
PTZ00098 |
phosphoethanolamine N-methyltransferase; Provisional |
41-155 |
1.01e-10 |
|
phosphoethanolamine N-methyltransferase; Provisional
Pssm-ID: 173391 [Multi-domain] Cd Length: 263 Bit Score: 62.29 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 41 EILSLLPSLSGQRVLELGAGIG---RYTSHllTLASHVTAVDFMESFVEKNRQDNSHYSNASFLQADVTKLDFPKNSFDI 117
Cdd:PTZ00098 43 KILSDIELNENSKVLDIGSGLGggcKYINE--KYGAHVHGVDICEKMVNIAKLRNSDKNKIEFEANDILKKDFPENTFDM 120
|
90 100 110
....*....|....*....|....*....|....*...
gi 291190262 118 IFSNWLLMYLSDEELTSLTERMLGWLSPGGYLFFRESC 155
Cdd:PTZ00098 121 IYSRDAILHLSYADKKKLFEKCYKWLKPNGILLITDYC 158
|
|
| PRK11705 |
PRK11705 |
cyclopropane fatty acyl phospholipid synthase; |
281-358 |
2.63e-10 |
|
cyclopropane fatty acyl phospholipid synthase;
Pssm-ID: 183282 Cd Length: 383 Bit Score: 62.17 E-value: 2.63e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291190262 281 LNLKPGMKVLDVGCGIGGGNFYMAKAFGVEVLGLDLSANMVDIAIERAmeEKLPsVHFEVADAtkREFPEaSFDVVYS 358
Cdd:PRK11705 163 LQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVGVTISAEQQKLAQERC--AGLP-VEIRLQDY--RDLNG-QFDRIVS 234
|
|
| PCMT |
pfam01135 |
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT); |
264-387 |
3.37e-10 |
|
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
Pssm-ID: 395902 [Multi-domain] Cd Length: 205 Bit Score: 59.69 E-value: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 264 GYVST-GGPSTTKEFVDLLNLKPGMKVLDVGCGIGGGNFYMAKAFGVE--VLGLDLSANMVDIAIERAMEEKLPSVHFEV 340
Cdd:pfam01135 51 GYGQTiSAPHMHAMMLELLELKPGMRVLEIGSGSGYLTACFARMVGEVgrVVSIEHIPELVEIARRNLEKLGLENVIVVV 130
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 291190262 341 ADATKREFPEASFDVVYSRDTILHIDEklALFKRfhswLKPGGQVLI 387
Cdd:pfam01135 131 GDGRQGWPEFAPYDAIHVGAAAPEIPE--ALIDQ----LKEGGRLVI 171
|
|
| Methyltransf_PK |
pfam05891 |
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ... |
53-153 |
4.68e-10 |
|
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron PVT and in uterine cells in C. elegans [worm-base]. In Saccharomyces cerevisiae this is AdoMet dependent proline di-methyltransferase. This enzyme catalyzes the di-methylation of ribosomal proteins Rpl12 and Rps25 at N-terminal proline residues. The methyltransferases described here specifically recognize the N-terminal X-Pro-Lys sequence motif, and they may account for nearly all previously described eukaryotic protein N-terminal methylation reactions. A number of other yeast and human proteins also share the recognition motif and may be similarly modified. As with other methyltransferases, this family carries the characteriztic GxGxG motif.
Pssm-ID: 461771 Cd Length: 218 Bit Score: 59.31 E-value: 4.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 53 RVLELGAGIGRYTSHLLT-LASHVTAVDFMESFVEKNRQD--NSHYSNASFLQADVTKLDFPKNSFDIIFSNWLLMYLSD 129
Cdd:pfam05891 58 VALDCGAGIGRVTKNLLLpLFSKVDLVEPVEDFIEKAKEYlaEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTD 137
|
90 100
....*....|....*....|....
gi 291190262 130 EELTSLTERMLGWLSPGGYLFFRE 153
Cdd:pfam05891 138 EDLVAFLKRCKGGLKPNGFIVVKE 161
|
|
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
41-121 |
6.07e-10 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 58.29 E-value: 6.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 41 EILSLLPSLSGQRVLELGAGIGRYTSHLLTLASHVTAVDFMESFVEKNRQDNSHYSNASFLQADVTKLDFPKNSFDIIFS 120
Cdd:smart00650 4 KIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAAADNLTVIHGDALKFDLPKLQPYKVVG 83
|
.
gi 291190262 121 N 121
Cdd:smart00650 84 N 84
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
260-387 |
1.87e-09 |
|
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: 57.12 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 260 MFGAGYVSTGgpstTKEFVDLLNLKPGMKVLDVGCGIG--GGnfYMAKAFGV-EVLGLDLSANMVDIAIERAMEEKLPSV 336
Cdd:COG2813 28 VFSRDRLDIG----TRLLLEHLPEPLGGRVLDLGCGYGviGL--ALAKRNPEaRVTLVDVNARAVELARANAAANGLENV 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291190262 337 HFEVADATkREFPEASFDVVYS----------RDTILHideklALFKRFHSWLKPGGQVLI 387
Cdd:COG2813 102 EVLWSDGL-SGVPDGSFDLILSnppfhagravDKEVAH-----ALIADAARHLRPGGELWL 156
|
|
| TrmA |
COG2265 |
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ... |
278-356 |
6.02e-09 |
|
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 441866 [Multi-domain] Cd Length: 377 Bit Score: 57.88 E-value: 6.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 278 VDLLNLKPGMKVLDVGCGIGggNF--YMAKAFGvEVLGLDLSANMVDIAIERAMEEKLPSVHFEVADATK---REFPEAS 352
Cdd:COG2265 226 LEWLDLTGGERVLDLYCGVG--TFalPLARRAK-KVIGVEIVPEAVEDARENARLNGLKNVEFVAGDLEEvlpELLWGGR 302
|
....
gi 291190262 353 FDVV 356
Cdd:COG2265 303 PDVV 306
|
|
| UbiG |
TIGR01983 |
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ... |
286-388 |
2.23e-08 |
|
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase believed to act at two points in the ubiquinone biosynthetic pathway in bacteria (UbiG) and fungi (COQ3). A separate methylase (MenG/UbiE) catalyzes the single C-methylation step. The most commonly used names for genes in this family do not indicate whether this gene is an O-methyl, or C-methyl transferase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273910 Cd Length: 224 Bit Score: 54.61 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 286 GMKVLDVGCGIGGGNFYMAKaFGVEVLGLDLSANMVDIAIERAMEEKLpSVHFEVADAtkREFPEA---SFDVVYSRDTI 362
Cdd:TIGR01983 47 GLRVLDVGCGGGLLSEPLAR-LGANVTGIDASEENIEVAKLHAKKDPL-QIDYRCTTV--EDLAEKkagSFDVVTCMEVL 122
|
90 100
....*....|....*....|....*.
gi 291190262 363 LHIDEKLALFKRFHSWLKPGGQVLIS 388
Cdd:TIGR01983 123 EHVPDPQAFIRACAQLLKPGGILFFS 148
|
|
| arsM |
PRK11873 |
arsenite methyltransferase; |
279-433 |
2.37e-08 |
|
arsenite methyltransferase;
Pssm-ID: 237007 [Multi-domain] Cd Length: 272 Bit Score: 55.34 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 279 DLLNLKPGMKVLDVGCGIGGGNFYMAKAFGVE--VLGLDLSANMVDIAIERAMEEKLPSVHFEVADATKREFPEASFDVV 356
Cdd:PRK11873 71 ALAELKPGETVLDLGSGGGFDCFLAARRVGPTgkVIGVDMTPEMLAKARANARKAGYTNVEFRLGEIEALPVADNSVDVI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 357 YSRDTILHIDEKLALFKRFHSWLKPGGQVLISDYCC-GEKPwtpqfqEYVKQR---------GYILYTppQYGKFLQQAG 426
Cdd:PRK11873 151 ISNCVINLSPDKERVFKEAFRVLKPGGRFAISDVVLrGELP------EEIRNDaelyagcvaGALQEE--EYLAMLAEAG 222
|
....*..
gi 291190262 427 FSNVRAE 433
Cdd:PRK11873 223 FVDITIQ 229
|
|
| Methyltransf_23 |
pfam13489 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
32-153 |
3.75e-08 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 52.82 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 32 QELTQHELPEILSLL--PSLSGQRVLELGAGIGRYTSHLLTLASHVTAVDFMESFVEKNRqdnshySNASFLQADVTKLD 109
Cdd:pfam13489 2 AHQRERLLADLLLRLlpKLPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERAL------LNVRFDQFDEQEAA 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 291190262 110 FPKNSFDIIFSNWLLMYLSDeeLTSLTERMLGWLSPGGYLFFRE 153
Cdd:pfam13489 76 VPAGKFDVIVAREVLEHVPD--PPALLRQIAALLKPGGLLLLST 117
|
|
| PLN02233 |
PLN02233 |
ubiquinone biosynthesis methyltransferase |
284-440 |
8.15e-08 |
|
ubiquinone biosynthesis methyltransferase
Pssm-ID: 177877 [Multi-domain] Cd Length: 261 Bit Score: 53.36 E-value: 8.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 284 KPGMKVLDVGCGIGGGNFYMAKAFGV--EVLGLDLSANMVDIAIERaMEEKLPSVHFEV----ADATKREFPEASFDVVY 357
Cdd:PLN02233 72 KMGDRVLDLCCGSGDLAFLLSEKVGSdgKVMGLDFSSEQLAVAASR-QELKAKSCYKNIewieGDATDLPFDDCYFDAIT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 358 SRDTILHIDEKLALFKRFHSWLKPGGQVLISDYCCGEKPWTPQFQEYV---------------KQRGYILYTPPQY--GK 420
Cdd:PLN02233 151 MGYGLRNVVDRLKAMQEMYRVLKPGSRVSILDFNKSTQPFTTSMQEWMidnvvvpvatgyglaKEYEYLKSSINEYltGE 230
|
170 180
....*....|....*....|....
gi 291190262 421 FLQ----QAGFSNVRAEDRTAQFM 440
Cdd:PLN02233 231 ELEklalEAGFSSAKHYEISGGLM 254
|
|
| PRK08317 |
PRK08317 |
hypothetical protein; Provisional |
51-149 |
1.11e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 52.63 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 51 GQRVLELGAGIG---RYTSHLLTLASHVTAVDFMESFVE--KNRQDNSHySNASFLQADVTKLDFPKNSFDIIFSNWLLM 125
Cdd:PRK08317 20 GDRVLDVGCGPGndaRELARRVGPEGRVVGIDRSEAMLAlaKERAAGLG-PNVEFVRGDADGLPFPDGSFDAVRSDRVLQ 98
|
90 100
....*....|....*....|....
gi 291190262 126 YLSDEElTSLTErMLGWLSPGGYL 149
Cdd:PRK08317 99 HLEDPA-RALAE-IARVLRPGGRV 120
|
|
| PRK01683 |
PRK01683 |
trans-aconitate 2-methyltransferase; Provisional |
288-386 |
1.50e-07 |
|
trans-aconitate 2-methyltransferase; Provisional
Pssm-ID: 234970 Cd Length: 258 Bit Score: 52.64 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 288 KVLDVGCGIGGGNFYMAKAFGV-EVLGLDLSANMVDIAIERameekLPSVHFEVADATKREfPEASFDVVYSRDTILHID 366
Cdd:PRK01683 34 YVVDLGCGPGNSTELLVERWPAaRITGIDSSPAMLAEARSR-----LPDCQFVEADIASWQ-PPQALDLIFANASLQWLP 107
|
90 100
....*....|....*....|
gi 291190262 367 EKLALFKRFHSWLKPGGqVL 386
Cdd:PRK01683 108 DHLELFPRLVSLLAPGG-VL 126
|
|
| PRK07580 |
PRK07580 |
Mg-protoporphyrin IX methyl transferase; Validated |
279-364 |
2.70e-07 |
|
Mg-protoporphyrin IX methyl transferase; Validated
Pssm-ID: 236059 [Multi-domain] Cd Length: 230 Bit Score: 51.38 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 279 DLLNLKpGMKVLDVGCGIGGGNFYMAKAfGVEVLGLDLSANMVDIAIERAMEEKLP-SVHFEVADAtkrEFPEASFDVVY 357
Cdd:PRK07580 58 ADGDLT-GLRILDAGCGVGSLSIPLARR-GAKVVASDISPQMVEEARERAPEAGLAgNITFEVGDL---ESLLGRFDTVV 132
|
....*..
gi 291190262 358 SRDTILH 364
Cdd:PRK07580 133 CLDVLIH 139
|
|
| Nnt1 |
COG3897 |
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ... |
285-410 |
7.08e-07 |
|
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443104 [Multi-domain] Cd Length: 216 Bit Score: 49.88 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 285 PGMKVLDVGCGIGGGNFYMAKAFGVEVLGLDLSANMVDIAIERAMEEKLPsVHFEVADATKREfPEASFDVV------YS 358
Cdd:COG3897 70 AGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALAALRLNAALNGVA-ITTRLGDWRDPP-AAGGFDLIlggdvlYE 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 291190262 359 RDTILHIdekLALFKRFhswLKPGGQVLISDYccgEKPWTPQFQEY-VKQRGY 410
Cdd:COG3897 148 RDLAEPL---LPFLDRL---AAPGGEVLIGDP---GRGYLPAFRERlEALAGY 191
|
|
| PRK10258 |
PRK10258 |
biotin biosynthesis protein BioC; Provisional |
28-151 |
8.32e-07 |
|
biotin biosynthesis protein BioC; Provisional
Pssm-ID: 182340 [Multi-domain] Cd Length: 251 Bit Score: 50.14 E-value: 8.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 28 DSHAqELTQHELPEILSLLPSLSGQRVLELGAGIGRYTSHLLTLASHVTAVDFMESFVEKNR-QDNSHYsnasFLQADVT 106
Cdd:PRK10258 21 EQHA-ELQRQSADALLAMLPQRKFTHVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARqKDAADH----YLAGDIE 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 291190262 107 KLDFPKNSFDIIFSNWLLMYLSDeeLTSLTERMLGWLSPGGYLFF 151
Cdd:PRK10258 96 SLPLATATFDLAWSNLAVQWCGN--LSTALRELYRVVRPGGVVAF 138
|
|
| PRK10258 |
PRK10258 |
biotin biosynthesis protein BioC; Provisional |
289-438 |
9.20e-07 |
|
biotin biosynthesis protein BioC; Provisional
Pssm-ID: 182340 [Multi-domain] Cd Length: 251 Bit Score: 50.14 E-value: 9.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 289 VLDVGCGIGGGNFYMaKAFGVEVLGLDLSANMVDIAIERAMEEklpsvHFEVADATKREFPEASFDVVYSRDTILHIDEK 368
Cdd:PRK10258 46 VLDAGCGPGWMSRYW-RERGSQVTALDLSPPMLAQARQKDAAD-----HYLAGDIESLPLATATFDLAWSNLAVQWCGNL 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291190262 369 LALFKRFHSWLKPGGQVLISDYCCGEKPWTPQFQEYVKQRgyilytpPQYGKFLQQ----AGFSNVRAEDRTAQ 438
Cdd:PRK10258 120 STALRELYRVVRPGGVVAFTTLVQGSLPELHQAWQAVDER-------PHANRFLPPdaieQALNGWRYQHHIQP 186
|
|
| ksgA |
PRK14896 |
16S ribosomal RNA methyltransferase A; |
42-121 |
9.59e-07 |
|
16S ribosomal RNA methyltransferase A;
Pssm-ID: 237852 [Multi-domain] Cd Length: 258 Bit Score: 50.28 E-value: 9.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 42 ILSLLPSLSGQRVLELGAGIGRYTSHLLTLASHVTAVDFMESFVEKNRQDNSHYSNASFLQADVTKLDFPKnsFDIIFSN 121
Cdd:PRK14896 21 IVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDDEIAAGNVEIIEGDALKVDLPE--FNKVVSN 98
|
|
| RsmA |
COG0030 |
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ... |
42-121 |
9.94e-07 |
|
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) [Translation, ribosomal structure and biogenesis]; 16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) is part of the Pathway/BioSystem: 16S rRNA modification
Pssm-ID: 439801 [Multi-domain] Cd Length: 270 Bit Score: 50.12 E-value: 9.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 42 ILSLLPSLSGQRVLELGAGIGRYTSHLLTLASHVTAVDFMESFVEKNRQDNSHYSNASFLQADVTKLDFPK---NSFDII 118
Cdd:COG0030 29 IVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAAYPNLTVIEGDALKVDLPAlaaGEPLKV 108
|
...
gi 291190262 119 FSN 121
Cdd:COG0030 109 VGN 111
|
|
| PTZ00338 |
PTZ00338 |
dimethyladenosine transferase-like protein; Provisional |
54-121 |
1.10e-06 |
|
dimethyladenosine transferase-like protein; Provisional
Pssm-ID: 240367 [Multi-domain] Cd Length: 294 Bit Score: 50.39 E-value: 1.10e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291190262 54 VLELGAGIGRYTSHLLTLASHVTAVDF---MESFVEKNRQDNSHYSNASFLQADVTKLDFPKnsFDIIFSN 121
Cdd:PTZ00338 40 VLEIGPGTGNLTEKLLQLAKKVIAIEIdprMVAELKKRFQNSPLASKLEVIEGDALKTEFPY--FDVCVAN 108
|
|
| Pcm |
COG2518 |
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ... |
279-357 |
1.36e-06 |
|
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442008 [Multi-domain] Cd Length: 197 Bit Score: 48.93 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 279 DLLNLKPGMKVLDVGCGIGggnfYMAkA----FGVEVLGLDLSANMVDIAIERAMEEKLPSVHFEVADATKREFPEASFD 354
Cdd:COG2518 60 EALDLKPGDRVLEIGTGSG----YQA-AvlarLAGRVYSVERDPELAERARERLAALGYDNVTVRVGDGALGWPEHAPFD 134
|
...
gi 291190262 355 VVY 357
Cdd:COG2518 135 RII 137
|
|
| ksgA |
TIGR00755 |
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ... |
26-121 |
1.66e-06 |
|
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, this protein is responsible for the dimethylation of two adjacent adenosine residues in a conserved hairpin of 16S rRNA in bacteria, 18S rRNA in eukaryotes. This adjacent dimethylation is the only rRNA modification shared by bacteria and eukaryotes. A single member of this family is present in each of the first 20 completed microbial genomes. This protein is essential in yeast, but not in E. coli, where its deletion leads to resistance to the antibiotic kasugamycin. Alternate name: S-adenosylmethionine--6-N',N'-adenosyl (rRNA) dimethyltransferase [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 273252 [Multi-domain] Cd Length: 254 Bit Score: 49.54 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 26 MLDSHAQELTQHE--LPEILSLLPSLSGQRVLELGAGIGRYTSHLLTLASHVTAVDFMESFVEKNRQDNSHYSNASFLQA 103
Cdd:TIGR00755 3 PRKSLGQNFLVDEnvIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLLSLYNNLEIIEG 82
|
90 100
....*....|....*....|
gi 291190262 104 DVTKLDFPKNSFDI--IFSN 121
Cdd:TIGR00755 83 DALKFDLNELAKDLtkVVGN 102
|
|
| PKS_MT |
smart00828 |
Methyltransferase in polyketide synthase (PKS) enzymes; |
288-389 |
2.93e-06 |
|
Methyltransferase in polyketide synthase (PKS) enzymes;
Pssm-ID: 214839 [Multi-domain] Cd Length: 224 Bit Score: 48.18 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 288 KVLDVGCGIGGGNFYMAKAFG-VEVLGLDLSANMVDIAIERAMEEKLP---SVHFEvaDATKREFPeASFDVVYSRDTIL 363
Cdd:smart00828 2 RVLDFGCGYGSDLIDLAERHPhLQLHGYTISPEQAEVGRERIRALGLQgriRIFYR--DSAKDPFP-DTYDLVFGFEVIH 78
|
90 100
....*....|....*....|....*.
gi 291190262 364 HIDEKLALFKRFHSWLKPGGQVLISD 389
Cdd:smart00828 79 HIKDKMDLFSNISRHLKDGGHLVLAD 104
|
|
| MTS |
pfam05175 |
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ... |
260-387 |
2.97e-06 |
|
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: 47.59 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 260 MFGAGYVSTGgpstTKEFVDLLNLKPGMKVLDVGCGIGGGNFYMAKAFG-VEVLGLDLSANMVDIAIERAMEEKLPSVHF 338
Cdd:pfam05175 10 VFSHGRLDIG----SRLLLEHLPKDLSGKVLDLGCGAGVLGAALAKESPdAELTMVDINARALESARENLAANGLENGEV 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 291190262 339 EVADATKrEFPEASFDVVYS-------RDTILHIDEklALFKRFHSWLKPGGQVLI 387
Cdd:pfam05175 86 VASDVYS-GVEDGKFDLIISnppfhagLATTYNVAQ--RFIADAKRHLRPGGELWI 138
|
|
| TehB |
pfam03848 |
Tellurite resistance protein TehB; |
41-148 |
8.53e-06 |
|
Tellurite resistance protein TehB;
Pssm-ID: 397776 Cd Length: 193 Bit Score: 46.38 E-value: 8.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 41 EILSLLPSLSGQRVLELGAGIGRYTSHLLTLASHVTAVDFMESFVeKNRQDNSHYSNASFLQA---DVTKLDFPKNsFDI 117
Cdd:pfam03848 21 EVLEAVKIVKPGKVLDLGCGQGRNSLYLSLLGYDVTAWDKNENSI-ANLQRIKEKENLDNIHTalyDINNATIDEN-YDF 98
|
90 100 110
....*....|....*....|....*....|.
gi 291190262 118 IFSNWLLMYLSDEELTSLTERMLGWLSPGGY 148
Cdd:pfam03848 99 ILSTVVLMFLEPERIPGIIANMQECTNPGGY 129
|
|
| mycolic_MTase |
NF040660 |
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ... |
278-387 |
1.21e-05 |
|
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include tailoring enzymes that make site-specific modifications to mycolic acid precursor molecules. These include Mycobacterium tuberculosis enzymes MmaA1-MmaA4, CmaA1-CmaA2, and PcaA. The family also includes UmaA, reported to be the lone member of this family not involved in mycolic acid biosynthesis. No members of this family are found in species that lack mycolic acids. This model excludes two more distantly related paralogs, Rv0447c (UfaA1 ) and Rv3720, that are also encoded in the Mycobacterium tuberculosis H37Rv genome.
Pssm-ID: 468626 Cd Length: 283 Bit Score: 47.07 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 278 VDLLNLKPGMKVLDVGCGIGGGNFYMAKAFGVEVLGLDLSANMVDIAIERAMEEKLPSVHfEVADATKREFPEaSFDVVY 357
Cdd:NF040660 53 LGKLNLEPGMTLLDIGCGWGATMRRAVEKYDVNVVGLTLSKNQAAHVQQVLDEIDTPRSR-RVLLQGWEEFDE-PVDRIV 130
|
90 100 110
....*....|....*....|....*....|..
gi 291190262 358 SRDTILHI--DEKLALFKRFHSWLKPGGQVLI 387
Cdd:NF040660 131 SIGAFEHFghERYDDFFKRAYNILPADGRMLL 162
|
|
| COG2263 |
COG2263 |
Predicted RNA methylase [General function prediction only]; |
45-121 |
1.55e-05 |
|
Predicted RNA methylase [General function prediction only];
Pssm-ID: 441864 [Multi-domain] Cd Length: 199 Bit Score: 45.67 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 45 LLPSLSGQRVLELGAGIGR--YTSHLLTlASHVTAVDFMESFVEKNRQD-NSHYSNASFLQADVTKLDFPKnSFDIIFSN 121
Cdd:COG2263 40 LRGDIEGKTVLDLGCGTGMlaIGAALLG-AKKVVGVDIDPEALEIARENaERLGVRVDFIRADVTRIPLGG-SVDTVVMN 117
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
43-121 |
1.76e-05 |
|
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: 45.57 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 43 LSLLPSLSGQRVLELGAGIGRYTSHLLTLA--SHVTAVDfmESFV-----EKNRQDNsHYSNASFLQADVTKlDFPKNSF 115
Cdd:COG2813 42 LEHLPEPLGGRVLDLGCGYGVIGLALAKRNpeARVTLVD--VNARavelaRANAAAN-GLENVEVLWSDGLS-GVPDGSF 117
|
....*.
gi 291190262 116 DIIFSN 121
Cdd:COG2813 118 DLILSN 123
|
|
| COG4627 |
COG4627 |
Predicted SAM-depedendent methyltransferase [General function prediction only]; |
284-388 |
1.88e-05 |
|
Predicted SAM-depedendent methyltransferase [General function prediction only];
Pssm-ID: 443666 [Multi-domain] Cd Length: 161 Bit Score: 44.86 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 284 KPGMKVLDVGCGigggNFYMAkafgvEVLGLDLSAN-MVDIaierameeklpsvhfeVADATKRE-FPEASFDVVYSRDT 361
Cdd:COG4627 1 SLSPLKLNIGCG----PKRLP-----GWLNVDIVPApGVDI----------------VGDLTDPLpFPDNSVDAIYSSHV 55
|
90 100
....*....|....*....|....*....
gi 291190262 362 ILHID--EKLALFKRFHSWLKPGGQVLIS 388
Cdd:COG4627 56 LEHLDyeEAPLALKECYRVLKPGGILRIV 84
|
|
| Gcd14 |
COG2519 |
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ... |
280-406 |
2.00e-05 |
|
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 442009 [Multi-domain] Cd Length: 249 Bit Score: 45.92 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 280 LLNLKPGMKVLDVGCGIGGGNFYMAKAFGVE--VLGLDLSANMVDIA---IERAMEekLPSVHFEVADATKrEFPEASFD 354
Cdd:COG2519 86 RLDIFPGARVLEAGTGSGALTLALARAVGPEgkVYSYERREDFAEIArknLERFGL--PDNVELKLGDIRE-GIDEGDVD 162
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 291190262 355 VVysrdtILHIDEKLALFKRFHSWLKPGGQVLIsdYCcgekPWTPQFQEYVK 406
Cdd:COG2519 163 AV-----FLDMPDPWEALEAVAKALKPGGVLVA--YV----PTVNQVSKLVE 203
|
|
| TrmR |
COG4122 |
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ... |
280-389 |
2.01e-05 |
|
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 443298 Cd Length: 173 Bit Score: 45.18 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 280 LLNLKPGMKVLDVGCGIGGGNFYMAKAF--GVEVLGLDLSANMVDIA---IERA-MEEKlpsVHFEVADATK--REFPEA 351
Cdd:COG4122 11 LARLLGAKRILEIGTGTGYSTLWLARALpdDGRLTTIEIDPERAAIArenFARAgLADR---IRLILGDALEvlPRLADG 87
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 291190262 352 SFDVVYsrdtilhID----EKLALFKRFHSWLKPGGqVLISD 389
Cdd:COG4122 88 PFDLVF-------IDadksNYPDYLELALPLLRPGG-LIVAD 121
|
|
| HemK |
COG2890 |
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
41-151 |
2.07e-05 |
|
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 46.30 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 41 EILSLLPSLSGQRVLELGAG---IGrytshlLTLAS-----HVTAVDFMESFVE---KNRQDNSHYSNASFLQADVTKLD 109
Cdd:COG2890 103 LALALLPAGAPPRVLDLGTGsgaIA------LALAKerpdaRVTAVDISPDALAvarRNAERLGLEDRVRFLQGDLFEPL 176
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291190262 110 FPKNSFDIIFSNwlLMYLSDEELTSL----------------------TERML----GWLSPGGYLFF 151
Cdd:COG2890 177 PGDGRFDLIVSN--PPYIPEDEIALLppevrdheprlaldggedgldfYRRIIaqapRLLKPGGWLLL 242
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
279-358 |
2.17e-05 |
|
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: 45.91 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 279 DLLNLKPGMKVLDVGCGIGGGNFYMAKAF-GVEVLGLDLSANMVDIAIERAMEEKLPS-VHFEVAD--ATKREFPEASFD 354
Cdd:COG4123 31 AFAPVKKGGRVLDLGTGTGVIALMLAQRSpGARITGVEIQPEAAELARRNVALNGLEDrITVIHGDlkEFAAELPPGSFD 110
|
....
gi 291190262 355 VVYS 358
Cdd:COG4123 111 LVVS 114
|
|
| ubiE |
PRK00216 |
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ... |
44-118 |
2.61e-05 |
|
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;
Pssm-ID: 234689 [Multi-domain] Cd Length: 239 Bit Score: 45.53 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 44 SLLPSLSGQRVLELGAGIGRYTSHLLTLA---SHVTAVDFMESFVE--KNRQDNSHYS-NASFLQADVTKLDFPKNSFDI 117
Cdd:PRK00216 45 KWLGVRPGDKVLDLACGTGDLAIALAKAVgktGEVVGLDFSEGMLAvgREKLRDLGLSgNVEFVQGDAEALPFPDNSFDA 124
|
.
gi 291190262 118 I 118
Cdd:PRK00216 125 V 125
|
|
| COG2263 |
COG2263 |
Predicted RNA methylase [General function prediction only]; |
277-356 |
3.04e-05 |
|
Predicted RNA methylase [General function prediction only];
Pssm-ID: 441864 [Multi-domain] Cd Length: 199 Bit Score: 44.89 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 277 FVDLLNLKPGMKVLDVGCGIGggnfyM----AKAFGVE-VLGLDLSANMVDIAIERAMEEKLPsVHFEVADATKREFPEa 351
Cdd:COG2263 37 LAYLRGDIEGKTVLDLGCGTG-----MlaigAALLGAKkVVGVDIDPEALEIARENAERLGVR-VDFIRADVTRIPLGG- 109
|
....*
gi 291190262 352 SFDVV 356
Cdd:COG2263 110 SVDTV 114
|
|
| PrmA |
COG2264 |
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis]; |
282-388 |
5.72e-05 |
|
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441865 [Multi-domain] Cd Length: 284 Bit Score: 44.78 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 282 NLKPGMKVLDVGCG-----IGggnfymAKAFGV-EVLGLDLSANMVDIAIERA----MEEKlpsVHFEVADAtkreFPEA 351
Cdd:COG2264 145 LLKPGKTVLDVGCGsgilaIA------AAKLGAkRVLAVDIDPVAVEAARENAelngVEDR---IEVVLGDL----LEDG 211
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 291190262 352 SFDVVYS---RDTIlhidekLALFKRFHSWLKPGGQVLIS 388
Cdd:COG2264 212 PYDLVVAnilANPL------IELAPDLAALLKPGGYLILS 245
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
50-121 |
9.27e-05 |
|
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: 43.98 E-value: 9.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 50 SGQRVLELGAGIGrytshLLTL-------ASHVTAVDFMESFVE---KNRQDNSHYSNASFLQADVTKL--DFPKNSFDI 117
Cdd:COG4123 37 KGGRVLDLGTGTG-----VIALmlaqrspGARITGVEIQPEAAElarRNVALNGLEDRITVIHGDLKEFaaELPPGSFDL 111
|
....
gi 291190262 118 IFSN 121
Cdd:COG4123 112 VVSN 115
|
|
| MetW |
pfam07021 |
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ... |
276-362 |
1.07e-04 |
|
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: 43.21 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 276 EFVDLLNL-KPGMKVLDVGCGIGGGNFYMAKAFGVEVLGLDLSANMVDIAIERAMeeklpSVHFEVADATKREFPEASFD 354
Cdd:pfam07021 3 DFRYILEWiPPGSRVLDLGCGDGTLLYLLKEEKGVDGYGIELDAAGVAECVAKGL-----YVIQGDLDEGLEHFPDKSFD 77
|
....*...
gi 291190262 355 VVYSRDTI 362
Cdd:pfam07021 78 YVILSQTL 85
|
|
| PRK14103 |
PRK14103 |
trans-aconitate 2-methyltransferase; Provisional |
277-383 |
1.23e-04 |
|
trans-aconitate 2-methyltransferase; Provisional
Pssm-ID: 184509 Cd Length: 255 Bit Score: 43.52 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 277 FVDLL---NLKPGMKVLDVGCGIGGGNFYMAKAF-GVEVLGLDLSANMVDIAIERAmeeklpsVHFEVADAtkREF-PEA 351
Cdd:PRK14103 18 FYDLLarvGAERARRVVDLGCGPGNLTRYLARRWpGAVIEALDSSPEMVAAARERG-------VDARTGDV--RDWkPKP 88
|
90 100 110
....*....|....*....|....*....|..
gi 291190262 352 SFDVVYSRDTILHIDEKLALFKRFHSWLKPGG 383
Cdd:PRK14103 89 DTDVVVSNAALQWVPEHADLLVRWVDELAPGS 120
|
|
| TPMT |
pfam05724 |
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ... |
269-386 |
1.45e-04 |
|
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase proteins from both eukaryotes and prokaryotes. Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyzes S-methylation of aromatic and heterocyclic sulfhydryl compounds, including anticancer and immunosuppressive thiopurines.
Pssm-ID: 399030 Cd Length: 218 Bit Score: 43.18 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 269 GGPSTTKEFVDLLNLKPGMKVLDVGCGIGGGNFYMAkAFGVEVLGLDLSanmvDIAIERAMEEKLPSVHFEVADATKRE- 347
Cdd:pfam05724 21 GVNPLLVRHWDALKLPPGLRVLVPLCGKALDMVWLA-EQGHFVVGVEIS----ELAVEKFFAEAGLSPPITELSGFKEYs 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 291190262 348 -------------FPEAS---FDVVYSRDTILHIDEKL--ALFKRFHSWLKPGGQVL 386
Cdd:pfam05724 96 sgnislycgdfftLPREElgkFDLIYDRAALCALPPEMrpRYAKQMYELLPPGGRGL 152
|
|
| Ubie_methyltran |
pfam01209 |
ubiE/COQ5 methyltransferase family; |
49-153 |
1.61e-04 |
|
ubiE/COQ5 methyltransferase family;
Pssm-ID: 395966 [Multi-domain] Cd Length: 228 Bit Score: 43.20 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 49 LSGQRVLELGAGIGRYTSHLLTLAS---HVTAVDFMESFVE--KNRQDNSHYSNASFLQADVTKLDFPKNSFDIIFSNWL 123
Cdd:pfam01209 41 KRGNKFLDVAGGTGDWTFGLSDSAGssgKVVGLDINENMLKegEKKAKEEGKYNIEFLQGNAEELPFEDDSFDIVTISFG 120
|
90 100 110
....*....|....*....|....*....|
gi 291190262 124 LMYLSDeELTSLTErMLGWLSPGGYLFFRE 153
Cdd:pfam01209 121 LRNFPD-YLKVLKE-AFRVLKPGGRVVCLE 148
|
|
| PRK14968 |
PRK14968 |
putative methyltransferase; Provisional |
279-411 |
1.77e-04 |
|
putative methyltransferase; Provisional
Pssm-ID: 237872 [Multi-domain] Cd Length: 188 Bit Score: 42.58 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 279 DLLNLKPGMKVLDVGCGIGGGNFYMAKAfGVEVLGLDLSANMVDIAIERAM--EEKLPSVHFEVADATKrEFPEASFDVV 356
Cdd:PRK14968 17 ENAVDKKGDRVLEVGTGSGIVAIVAAKN-GKKVVGVDINPYAVECAKCNAKlnNIRNNGVEVIRSDLFE-PFRGDKFDVI 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291190262 357 -----Y---SRDTILHIDEKLAL---------FKRFHS----WLKPGG--QVLISDYCCGEKpwtpqFQEYVKQRGYI 411
Cdd:PRK14968 95 lfnppYlptEEEEEWDDWLNYALsggkdgrevIDRFLDevgrYLKPGGriLLLQSSLTGEDE-----VLEYLEKLGFE 167
|
|
| RrnaAD |
pfam00398 |
Ribosomal RNA adenine dimethylase; |
41-121 |
1.82e-04 |
|
Ribosomal RNA adenine dimethylase;
Pssm-ID: 395321 [Multi-domain] Cd Length: 263 Bit Score: 43.12 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 41 EILSLLPSLSGQRVLELGAGIGRYTSHLLTLASHVTAVDFMESFVEKNRQDNSHYSNASFLQADVTKLDFPKNSF----- 115
Cdd:pfam00398 21 EIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLSLDENLTVIHQDFLKFEFPSLVThihqe 100
|
....*.
gi 291190262 116 DIIFSN 121
Cdd:pfam00398 101 FLVVGN 106
|
|
| RsmD |
COG0742 |
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
45-149 |
1.83e-04 |
|
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA G966 N2-methylase RsmD is part of the Pathway/BioSystem: 16S rRNA modification
Pssm-ID: 440505 [Multi-domain] Cd Length: 183 Bit Score: 42.38 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 45 LLPSLSGQRVLELGAGIG--------RYtshlltlASHVTavdfmesFVEKNR------QDNSH----YSNASFLQADVT 106
Cdd:COG0742 36 LGPDIEGARVLDLFAGSGalglealsRG-------AASVV-------FVEKDRkaaaviRKNLEklglEDRARVIRGDAL 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 291190262 107 KL--DFPKNSFDIIF------SNWLlmylsDEELTSLTERmlGWLSPGGYL 149
Cdd:COG0742 102 RFlkRLAGEPFDLVFldppyaKGLL-----EKALELLAEN--GLLAPGGLI 145
|
|
| Nnt1 |
COG3897 |
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ... |
47-147 |
2.27e-04 |
|
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443104 [Multi-domain] Cd Length: 216 Bit Score: 42.56 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 47 PSLSGQRVLELGAGIGrytshLLTL------ASHVTAVD---FMESFVEKNRQDNShySNASFLQADVTKLDfPKNSFDI 117
Cdd:COG3897 67 PEVAGKRVLELGCGLG-----LVGIaaakagAADVTATDydpEALAALRLNAALNG--VAITTRLGDWRDPP-AAGGFDL 138
|
90 100 110
....*....|....*....|....*....|....*..
gi 291190262 118 IFsnwllmyLSD---EEltSLTERMLGWL----SPGG 147
Cdd:COG3897 139 IL-------GGDvlyER--DLAEPLLPFLdrlaAPGG 166
|
|
| COG4076 |
COG4076 |
Predicted RNA methylase [General function prediction only]; |
51-132 |
3.10e-04 |
|
Predicted RNA methylase [General function prediction only];
Pssm-ID: 443253 [Multi-domain] Cd Length: 230 Bit Score: 42.33 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 51 GQRVLELGAGIGrytshLLTL------ASHVTAVD---FMESFVEKNRQDNSHYSNASFLQADVTKLDFPkNSFDIIFSN 121
Cdd:COG4076 36 GDVVLDIGTGSG-----LLSMlaaragAKKVYAVEvnpDIAAVARRIIAANGLSDRITVINADATDLDLP-EKADVIISE 109
|
90
....*....|.
gi 291190262 122 WLLMYLSDEEL 132
Cdd:COG4076 110 MLDTALLDEGQ 120
|
|
| rumA |
PRK13168 |
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD; |
278-342 |
3.12e-04 |
|
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;
Pssm-ID: 237291 [Multi-domain] Cd Length: 443 Bit Score: 43.22 E-value: 3.12e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291190262 278 VDLLNLKPGMKVLDVGCGIggGNFY--MAKaFGVEVLGLDLSANMVDIAIERAMEEKLPSVHFEVAD 342
Cdd:PRK13168 290 LEWLDPQPGDRVLDLFCGL--GNFTlpLAR-QAAEVVGVEGVEAMVERARENARRNGLDNVTFYHAN 353
|
|
| PRK12335 |
PRK12335 |
tellurite resistance protein TehB; Provisional |
41-148 |
3.53e-04 |
|
tellurite resistance protein TehB; Provisional
Pssm-ID: 183450 [Multi-domain] Cd Length: 287 Bit Score: 42.62 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 41 EILSLLPSLSGQRVLELGAGIGRYTSHLLTLASHVTAVD-------FMESFVEK---NRQDNSHYSNASFLQadvtkldf 110
Cdd:PRK12335 111 EVLEAVQTVKPGKALDLGCGQGRNSLYLALLGFDVTAVDinqqsleNLQEIAEKenlNIRTGLYDINSASIQ-------- 182
|
90 100 110
....*....|....*....|....*....|....*...
gi 291190262 111 pkNSFDIIFSNWLLMYLSDEELTSLTERMLGWLSPGGY 148
Cdd:PRK12335 183 --EEYDFILSTVVLMFLNRERIPAIIKNMQEHTNPGGY 218
|
|
| RsmB |
COG0144 |
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ... |
278-356 |
5.39e-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: 42.30 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 278 VDLLNLKPGMKVLDVGCGIGGGNFYMAKAF--GVEVLGLDLSANMVDIAIERAMEEKLPSVHFEVADATKR-EFPEASFD 354
Cdd:COG0144 242 ALLLDPKPGERVLDLCAAPGGKTLHLAELMgnKGRVVAVDISEHRLKRLRENLARLGLSNVEVVVADARELlEWLPGKFD 321
|
..
gi 291190262 355 VV 356
Cdd:COG0144 322 RV 323
|
|
| Pcm |
COG2518 |
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ... |
41-104 |
5.80e-04 |
|
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442008 [Multi-domain] Cd Length: 197 Bit Score: 41.23 E-value: 5.80e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291190262 41 EILSLLPslsGQRVLELGAGIGrYTSHLL-TLASHVTAVDFMESFVEKNRQ--DNSHYSNASFLQAD 104
Cdd:COG2518 60 EALDLKP---GDRVLEIGTGSG-YQAAVLaRLAGRVYSVERDPELAERARErlAALGYDNVTVRVGD 122
|
|
| arsM |
PRK11873 |
arsenite methyltransferase; |
51-121 |
7.65e-04 |
|
arsenite methyltransferase;
Pssm-ID: 237007 [Multi-domain] Cd Length: 272 Bit Score: 41.47 E-value: 7.65e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291190262 51 GQRVLELGAGIGR---YTSHLLTLASHVTAVDFMESFVEKNR--QDNSHYSNASFLQADVTKLDFPKNSFDIIFSN 121
Cdd:PRK11873 78 GETVLDLGSGGGFdcfLAARRVGPTGKVIGVDMTPEMLAKARanARKAGYTNVEFRLGEIEALPVADNSVDVIISN 153
|
|
| MeTrc |
smart00138 |
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ... |
336-387 |
8.04e-04 |
|
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to form gamma-glutamyl methyl ester residues.
Pssm-ID: 214534 [Multi-domain] Cd Length: 264 Bit Score: 41.12 E-value: 8.04e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 291190262 336 VHFEVADATKREFPEASFDVVYSRDTILHIDE--KLALFKRFHSWLKPGGQVLI 387
Cdd:smart00138 187 VRFAKHNLLAESPPLGDFDLIFCRNVLIYFDEptQRKLLNRFAEALKPGGYLFL 240
|
|
| PRK06202 |
PRK06202 |
hypothetical protein; Provisional |
287-389 |
1.37e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 180466 [Multi-domain] Cd Length: 232 Bit Score: 40.37 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 287 MKVLDVGCgiGGGNF-----YMAKAFG--VEVLGLDLSANMVDIAIERAmeeKLPSVHFE--VADATKREfpEASFDVVY 357
Cdd:PRK06202 62 LTLLDIGC--GGGDLaidlaRWARRDGlrLEVTAIDPDPRAVAFARANP---RRPGVTFRqaVSDELVAE--GERFDVVT 134
|
90 100 110
....*....|....*....|....*....|....
gi 291190262 358 SRDTILHIDEklALFKRF--HSWLKPGGQVLISD 389
Cdd:PRK06202 135 SNHFLHHLDD--AEVVRLlaDSAALARRLVLHND 166
|
|
| Methyltransf_9 |
pfam08003 |
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ... |
286-440 |
1.45e-03 |
|
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It also includes two putative methyltransferase proteins, Swiss:Q8EEE6 and Swiss:Q88MX8.
Pssm-ID: 429781 [Multi-domain] Cd Length: 315 Bit Score: 40.85 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 286 GMKVLDVGCGIGggnFYM--------AKAFGVE--------------VLGLDLSANMVDIAIerameEKLPsvhfevada 343
Cdd:pfam08003 116 GRTILDVGCGNG---YHMwrmlgegaAMVVGIDpselflcqfeavrkLLGNDQRAHLLPLGI-----EQLP--------- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 344 tkrefPEASFDVVYSRDTILH----IDEKLALFKRfhswLKPGGQ-VLISDYCCGEKPW--TPQfQEYVKQRG-YILYTP 415
Cdd:pfam08003 179 -----ALAAFDTVFSMGVLYHrrspLDHLLQLKDQ----LVKGGElVLETLVIDGDENTvlVPG-DRYAQMRNvYFIPSA 248
|
170 180 190
....*....|....*....|....*....|....
gi 291190262 416 PQYGKFLQQAGFSNVR---------AEDRTAQFM 440
Cdd:pfam08003 249 AALINWLEKCGFVDVRivdvsvttlEEQRRTEWM 282
|
|
| COG3963 |
COG3963 |
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism]; |
42-149 |
1.52e-03 |
|
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
Pssm-ID: 443163 Cd Length: 193 Bit Score: 39.81 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 42 ILSLLPSLSGQRVLELGAGIGRYTSHLLTL---ASHVTAVDFMESFVEKNRQdnsHYSNASFLQADVTKLD-----FPKN 113
Cdd:COG3963 37 MASEVDWSGAGPVVELGPGTGVFTRAILARgvpDARLLAVEINPEFAEHLRR---RFPRVTVVNGDAEDLAellaeHGIG 113
|
90 100 110
....*....|....*....|....*....|....*...
gi 291190262 114 SFDIIFSN--WLLMylSDEELTSLTERMLGWLSPGGYL 149
Cdd:COG3963 114 KVDAVVSGlpLLSF--PPELRRAILDAAFRVLAPGGVF 149
|
|
| PRK11207 |
PRK11207 |
tellurite resistance methyltransferase TehB; |
40-148 |
1.65e-03 |
|
tellurite resistance methyltransferase TehB;
Pssm-ID: 183040 Cd Length: 197 Bit Score: 39.72 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 40 PEILSLLPSLSGQRVLELGAGIGRYTSHLLTLASHVTAVD-------FMESFVEKNRQDNSHYSnasflQADVTKLDFpK 112
Cdd:PRK11207 20 SEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGFDVTAWDknpmsiaNLERIKAAENLDNLHTA-----VVDLNNLTF-D 93
|
90 100 110
....*....|....*....|....*....|....*.
gi 291190262 113 NSFDIIFSNWLLMYLSDEELTSLTERMLGWLSPGGY 148
Cdd:PRK11207 94 GEYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGY 129
|
|
| COG4076 |
COG4076 |
Predicted RNA methylase [General function prediction only]; |
284-386 |
1.66e-03 |
|
Predicted RNA methylase [General function prediction only];
Pssm-ID: 443253 [Multi-domain] Cd Length: 230 Bit Score: 40.02 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 284 KPGMKVLDVGCGIGGGNFYMAKAFGVEVLGLDLSANMVDIAIERAMEEKLPS-VHFEVADATKREFPEAsFDVVYSR--D 360
Cdd:COG4076 34 KPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDrITVINADATDLDLPEK-ADVIISEmlD 112
|
90 100 110
....*....|....*....|....*....|.
gi 291190262 361 TILhIDEKL-----ALFKRFhswLKPGGQVL 386
Cdd:COG4076 113 TAL-LDEGQvpilnHARKRL---LKPGGRII 139
|
|
| PrmA |
pfam06325 |
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ... |
261-388 |
1.84e-03 |
|
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.
Pssm-ID: 428888 [Multi-domain] Cd Length: 294 Bit Score: 40.33 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 261 FGagyvsTGGPSTTK---EFVDLLnLKPGMKVLDVGCG-----IGggnfymAKAFGV-EVLGLDLSANMVDIAIERAmee 331
Cdd:pfam06325 140 FG-----TGTHPTTKlclEALERL-VKPGESVLDVGCGsgilaIA------ALKLGAkKVVGVDIDPVAVRAAKENA--- 204
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 291190262 332 KLPSVHFEVADATKREFPEASFDVVYSrdTILH--IDEKLALFKRFhswLKPGGQVLIS 388
Cdd:pfam06325 205 ELNGVEARLEVYLPGDLPKEKADVVVA--NILAdpLIELAPDIYAL---VKPGGYLILS 258
|
|
| PLN02585 |
PLN02585 |
magnesium protoporphyrin IX methyltransferase |
286-364 |
1.99e-03 |
|
magnesium protoporphyrin IX methyltransferase
Pssm-ID: 215319 [Multi-domain] Cd Length: 315 Bit Score: 40.23 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 286 GMKVLDVGCGIGGGNFYMAKAfGVEVLGLDLSANMVDIAIERAMEE---KLPSV--HFEVADAtkrEFPEASFDVVYSRD 360
Cdd:PLN02585 145 GVTVCDAGCGTGSLAIPLALE-GAIVSASDISAAMVAEAERRAKEAlaaLPPEVlpKFEANDL---ESLSGKYDTVTCLD 220
|
....
gi 291190262 361 TILH 364
Cdd:PLN02585 221 VLIH 224
|
|
| PRK13942 |
PRK13942 |
protein-L-isoaspartate O-methyltransferase; Provisional |
279-387 |
2.00e-03 |
|
protein-L-isoaspartate O-methyltransferase; Provisional
Pssm-ID: 184409 Cd Length: 212 Bit Score: 39.61 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 279 DLLNLKPGMKVLDVGCGIGggnfYMAkAFGVEVLGLDlsaNMVdIAIERAME------EKLPSVHFE-----VADATKRE 347
Cdd:PRK13942 70 ELLDLKEGMKVLEIGTGSG----YHA-AVVAEIVGKS---GKV-VTIERIPElaekakKTLKKLGYDnveviVGDGTLGY 140
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 291190262 348 FPEASFDVVYSRDTILHIDEklALFKRfhswLKPGGQVLI 387
Cdd:PRK13942 141 EENAPYDRIYVTAAGPDIPK--PLIEQ----LKDGGIMVI 174
|
|
| MeTrc |
smart00138 |
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ... |
104-150 |
2.01e-03 |
|
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to form gamma-glutamyl methyl ester residues.
Pssm-ID: 214534 [Multi-domain] Cd Length: 264 Bit Score: 39.96 E-value: 2.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 291190262 104 DVTKLDFPKNSFDIIFSNWLLMYLSDEELTSLTERMLGWLSPGGYLF 150
Cdd:smart00138 193 NLLAESPPLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLF 239
|
|
| CheR |
pfam01739 |
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ... |
336-387 |
3.00e-03 |
|
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase - the C-terminal domain (this one) binds SAM.
Pssm-ID: 426403 Cd Length: 190 Bit Score: 38.80 E-value: 3.00e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 291190262 336 VHFEVADATKREFPEASFDVVYSRDTILHIDE--KLALFKRFHSWLKPGGQVLI 387
Cdd:pfam01739 119 VLFEYLNLLDEYPPLGDFDVIFCRNVLIYFDEetQRKILNRFAEKLKPGGYLFL 172
|
|
| PRK09328 |
PRK09328 |
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional |
278-387 |
3.91e-03 |
|
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
Pssm-ID: 236467 [Multi-domain] Cd Length: 275 Bit Score: 38.99 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 278 VDLLNLKPGMKVLDVGCG---IGggnFYMAKAF-GVEVLGLDLSANMVDIAIERAMEEKLPSVHFEVADATKrEFPEASF 353
Cdd:PRK09328 101 LEALLLKEPLRVLDLGTGsgaIA---LALAKERpDAEVTAVDISPEALAVARRNAKHGLGARVEFLQGDWFE-PLPGGRF 176
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 354 DVV-----Y-SRDTILHIDE-------KLALF---------KRF----HSWLKPGGQVLI 387
Cdd:PRK09328 177 DLIvsnppYiPEADIHLLQPevrdhepHLALFggedgldfyRRIieqaPRYLKPGGWLLL 236
|
|
| RlmE |
COG0293 |
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ... |
283-387 |
4.68e-03 |
|
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and biogenesis]; 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ is part of the Pathway/BioSystem: 23S rRNA modification
Pssm-ID: 440062 [Multi-domain] Cd Length: 208 Bit Score: 38.51 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 283 LKPGMKVLDVGCGIGGGNFYMAKAFGVE--VLGLDLsanmvdiaieRAMEEkLPSVHF--------EVADATKREFPEAS 352
Cdd:COG0293 48 IKPGMRVVDLGAAPGGWSQVAAKRVGGKgrVIALDL----------LPMEP-IPGVEFiqgdfredEVLDQLLEALGGRK 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 291190262 353 FDVVYS---------RDT----ILHIDEkLALFkrF-HSWLKPGGQVLI 387
Cdd:COG0293 117 VDLVLSdmapntsghKSVdharSMYLVE-LALD--FaRKVLKPGGAFVV 162
|
|
| CheR |
COG1352 |
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms]; |
99-150 |
4.74e-03 |
|
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
Pssm-ID: 440963 [Multi-domain] Cd Length: 272 Bit Score: 38.99 E-value: 4.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 291190262 99 SFLQADVTKLDFPKNSFDIIF-SNwLLMYLSDEELTSLTERMLGWLSPGGYLF 150
Cdd:COG1352 191 TFAQHNLLDDPPPFGRFDLIFcRN-VLIYFDPELQRRVLRRFHDSLAPGGYLF 242
|
|
| metW |
TIGR02081 |
methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that ... |
285-362 |
4.74e-03 |
|
methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that acylates homoserine as a first step toward methionine biosynthesis, in many species. It appears to act in methionine biosynthesis but is not fully characterized. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273958 Cd Length: 194 Bit Score: 38.12 E-value: 4.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291190262 285 PGMKVLDVGCGIGGGNFYMAKAFGVEVLGLDLSANMVDIAIERAMeeklpSVHFEVADATKREFPEASFDVVYSRDTI 362
Cdd:TIGR02081 13 PGSRVLDLGCGDGELLALLRDEKQVRGYGIEIDQDGVLACVARGV-----NVIQGDLDEGLEAFPDKSFDYVILSQTL 85
|
|
| Zn_ADH7 |
cd08261 |
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ... |
282-356 |
5.06e-03 |
|
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.
Pssm-ID: 176222 [Multi-domain] Cd Length: 337 Bit Score: 39.09 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 282 NLKPGMKVLDVGCG-IGGGNFYMAKAFGVEVLGLDLSANMVDIAIERAMEEKLPS----VHFEVADATKREFPEASFDVV 356
Cdd:cd08261 156 GVTAGDTVLVVGAGpIGLGVIQVAKARGARVIVVDIDDERLEFARELGADDTINVgdedVAARLRELTDGEGADVVIDAT 235
|
|
| PRK11207 |
PRK11207 |
tellurite resistance methyltransferase TehB; |
270-392 |
5.07e-03 |
|
tellurite resistance methyltransferase TehB;
Pssm-ID: 183040 Cd Length: 197 Bit Score: 38.18 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 270 GPSTT-KEFVDLLNLKPGMKVLDVGCGIGGGNFYMAkAFGVEVLGLDlsANMVDIA-IER-AMEEKLPSVHFEVADATKR 346
Cdd:PRK11207 14 GLTRThSEVLEAVKVVKPGKTLDLGCGNGRNSLYLA-ANGFDVTAWD--KNPMSIAnLERiKAAENLDNLHTAVVDLNNL 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 291190262 347 EFpEASFDVVYSRDTILHIDEKL--ALFKRFHSWLKPGGQVLI------SDYCC 392
Cdd:PRK11207 91 TF-DGEYDFILSTVVLMFLEAKTipGLIANMQRCTKPGGYNLIvaamdtADYPC 143
|
|
| YtxK |
COG0827 |
Adenine-specific DNA N6-methylase [Replication, recombination and repair]; |
277-412 |
6.10e-03 |
|
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
Pssm-ID: 440589 [Multi-domain] Cd Length: 327 Bit Score: 38.78 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 277 FVDLLNLKPGMKVLDVGCGIggGNFYMA---------KAFGVEVLGLdlsanMVDIAIERAMEEKLPsVHFEVADATkRE 347
Cdd:COG0827 107 LVEKFTKKEGLRILDPAVGT--GNLLTTvlnqlkkkvNAYGVEVDDL-----LIRLAAVLANLQGHP-VELFHQDAL-QP 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 348 FPEASFDVV--------YSRDTILHIDEKLALFKRFHSW----------LKPGGQV--LISDYCCgEKPWTPQFQEYVKQ 407
Cdd:COG0827 178 LLIDPVDVVisdlpvgyYPNDERAKRFKLKADEGHSYAHhlfieqslnyLKPGGYLffLVPSNLF-ESDQAAQLREFLKE 256
|
....*
gi 291190262 408 RGYIL 412
Cdd:COG0827 257 KAHIQ 261
|
|
| rrmA |
PRK11088 |
23S rRNA methyltransferase A; Provisional |
289-357 |
6.68e-03 |
|
23S rRNA methyltransferase A; Provisional
Pssm-ID: 236841 [Multi-domain] Cd Length: 272 Bit Score: 38.35 E-value: 6.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291190262 289 VLDVGCGIGggnFY-------MAKAFGVEVLGLDLSAnmvdIAIERAmEEKLPSVHFEVADATKREFPEASFDVVY 357
Cdd:PRK11088 89 LLDIGCGEG---YYthaladaLPEITTMQLFGLDISK----VAIKYA-AKRYPQVTFCVASSHRLPFADQSLDAII 156
|
|
| TrmR |
COG4122 |
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ... |
41-151 |
7.72e-03 |
|
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 443298 Cd Length: 173 Bit Score: 37.47 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291190262 41 EILSLLPSLSG-QRVLELGAGIGrYTSHLLTLA----SHVTAVDFMESFVEKNRQ--DNSHYSN-ASFLQADVTKL--DF 110
Cdd:COG4122 6 RLLYLLARLLGaKRILEIGTGTG-YSTLWLARAlpddGRLTTIEIDPERAAIAREnfARAGLADrIRLILGDALEVlpRL 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 291190262 111 PKNSFDIIF-----SNWLLMYlsdeeltsltERMLGWLSPGGYLFF 151
Cdd:COG4122 85 ADGPFDLVFidadkSNYPDYL----------ELALPLLRPGGLIVA 120
|
|
| |
