|
Name |
Accession |
Description |
Interval |
E-value |
| rlmL |
PRK11783 |
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ... |
1-702 |
0e+00 |
|
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2))-methyltransferase RlmL;
Pssm-ID: 236981 [Multi-domain] Cd Length: 702 Bit Score: 1393.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 1 MNSLFASTARGLEELLKTELENLGAVECQVVQGGVHFKGDTRLVYQSLMWSRLASRIMLPLGECKVYSDLDLYLGVQAIN 80
Cdd:PRK11783 1 MNSLFASCAKGLEELLKDELEALGASECKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSDLDLYLGVQAID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 81 WTEMFNPGATFAVHFSGLNDTIRNSQYGAMKVKDAIVDAFTRKNLPRPNVDRDAPDIRVNVWLHKETASIALDLSGDGLH 160
Cdd:PRK11783 81 WTEHFSPDKTFAVDFSGTNDEIRNTQFGALKVKDAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEATISLDLSGESLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 161 LRGYRDRAGIAPIKETLAAAIVMRSGW-QPGTPLLDPMCGSGTLLIEAAMLATDRAPGLHRGRWGFSGWAQHDEAIWQEV 239
Cdd:PRK11783 161 QRGYRQATGEAPLKENLAAAILLRSGWpQEGTPLLDPMCGSGTLLIEAAMMAADIAPGLHRERWGFSGWLGHDEALWQEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 240 KAEAQTRARKGLAEYSSHFYGSDSDARVIQRARTNARLAGIGELITFEVKDVAQLTNPLPKGPYGTVLSNPPYGERLDSE 319
Cdd:PRK11783 241 LEEAQERARAGLAELPSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKNPLPKGPTGLVISNPPYGERLGEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 320 PALIALHSLLGRIMKNQFGGWNLSLFSASPDLLSCLQLRADKQYKAKNGPLDCVQKNYHVAEStPDSKPAMVAEDYTNRL 399
Cdd:PRK11783 321 PALIALYSQLGRRLKQQFGGWNAALFSSSPELLSCLGLRADKQYKLKNGALECVLKNYTIAEE-STSSDAEGAQDFANRL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 400 RKNLKKFEKWARQEGIECYRLYDADLPEYNVAVDRYADWVVVQEYAPPKTIDAHKARQRLFDIIAATISVLGIAPNKLVL 479
Cdd:PRK11783 400 RKNLKKLKKWAKQEGIECYRLYDADLPEYNVAVDRYGDWVVVQEYAAPKTIDEEKARQRLFDALAATPEVLGIPPNKVVL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 480 KTRERQKGKNQYQKLGEKGEFLEVTEYNAHLWVNLTDYLDTGLFLDHRIARRMLGQMSKGKDFLNLFSYTGSATVHAGLG 559
Cdd:PRK11783 480 KTRERQKGKNQYQKLAEKGEFLEVTEYGAKLLVNLTDYLDTGLFLDHRPTRRMIGQMAKGKDFLNLFAYTGTASVHAALG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 560 GARSTTTVDMSRTYLEWAERNLRLNGLTGRAHRLIQADCLAWLREANEQFDLIFIDPPTFSNSKRMEDAFDVQRDHLALM 639
Cdd:PRK11783 560 GAKSTTTVDMSNTYLEWAERNFALNGLSGRQHRLIQADCLAWLKEAREQFDLIFIDPPTFSNSKRMEDSFDVQRDHVALI 639
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 238688381 640 KDLKRLLRAGGTIMFSNNKRGFRMDLDGLAKLGLKAQEITQKTLSQDFARNRQIHNCWLITAA 702
Cdd:PRK11783 640 KDAKRLLRPGGTLYFSNNKRGFKMDEEGLAKLGLKAEEITAKTLPPDFARNPKIHNCWLITHA 702
|
|
| RlmL |
COG0116 |
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ... |
2-372 |
8.36e-165 |
|
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA G2445 N2-methylase RlmL is part of the Pathway/BioSystem: 23S rRNA modification
Pssm-ID: 439886 [Multi-domain] Cd Length: 369 Bit Score: 478.06 E-value: 8.36e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 2 NSLFASTARGLEELLKTELENLGAVECQVVQGGVHFKGDTRLVYQSLMWSRLASRIMLPLGECKVYSDLDLYLGVQAINW 81
Cdd:COG0116 1 FELFATCARGLEALLADELKELGAEDVKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFKARTFDDLYEGAKAIPW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 82 TEMFNPGATFAVHFSGLNDTIRNSQYGAMKVKDAIVDAFTRKNLPRPNVDRDAPDIRVNVWLHKETASIALDLSGDGLHL 161
Cdd:COG0116 81 EEYLPPDGTFAVDATSVKSKLFHSQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHVHLLKDRATLSLDTSGESLHK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 162 RGYRDRAGIAPIKETLAAAIVMRSGWQPGTPLLDPMCGSGTLLIEAAMLATDRAPGLHRgRWGFSGWAQHDEAIWQEVKA 241
Cdd:COG0116 161 RGYREAQGEAPLKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAALIAANIAPGLNR-DFAFEKWPDFDAELWQELRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 242 EAQTRARKGLAeysSHFYGSDSDARVIQRARTNARLAGIGELITFEVKDVAQLTnplPKGPYGTVLSNPPYGERLDSEPA 321
Cdd:COG0116 240 EAEARIKRDPP---LPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLE---PPAEPGLIITNPPYGERLGEEEE 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 238688381 322 LIALHSLLGRIMKNQFGGWNLSLFSASPDLLSCLQLRADKQYKAKNGPLDC 372
Cdd:COG0116 314 LEALYRELGDVLKQRFKGWSAYILTSDPELEKAIGLKASKRRKLYNGGLEC 364
|
|
| UPF0020 |
pfam01170 |
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ... |
162-376 |
1.85e-69 |
|
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.
Pssm-ID: 395932 [Multi-domain] Cd Length: 184 Bit Score: 224.93 E-value: 1.85e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 162 RGYRDRAGIAPIKETLAAAIVMRSGWQPGTPLLDPMCGSGTLLIEAAMLATDRAPGLHRgrwgfsgwaqhdeaiwqevka 241
Cdd:pfam01170 1 RGYRPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPGKFD--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 242 eaqtrarkglAEYSSHFYGSDSDARVIQRARTNARLAGIGELITFEVKDVAQLtnPLPKGPYGTVLSNPPYGERLDSEPA 321
Cdd:pfam01170 60 ----------ARVRAPLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADL--PLLEGSVDVIVTNPPYGIRLGSKGA 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 238688381 322 LIALHSLLGRIMKNQF--GGWNLSLFSASPDLLSCLQLRADKQYKAKNGPLDCVQKN 376
Cdd:pfam01170 128 LEALYPEFLREAKRVLrgGGWLVLLTAENKDFEKAARERAWRKKKEFNVHIGGTRVI 184
|
|
| THUMP_AdoMetMT |
cd11715 |
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ... |
24-156 |
2.10e-46 |
|
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of this family contain an N-terminal THUMP domain and a C-terminal S-adenosylmethionine-dependent methyltransferase domain. Members have been implicated in the modification of 23S RNA m2G2445, a highly conserved modification in bacteria and in the m2G6 modification of tRNA. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.
Pssm-ID: 212584 Cd Length: 152 Bit Score: 161.59 E-value: 2.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 24 GAVECQVVQGGVHFKGDTRLVYQSLMWSRLASRIMLPLGECKVYSDLDLYLGVQAINWTEMFNPGATFAVHFSGLNDTIR 103
Cdd:cd11715 21 GAEDVEVGPGGVSFEGDLEDAYRANLWLRTAHRVLLLLAEFEAEDFDDLYELAKAIDWEDYLDPDGTFAVRATRVGSKLF 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 238688381 104 NSQYGAMKVKDAIVDAFtRKNLPRPNVDRDAPDIRVNVWLHKETASIALDLSG 156
Cdd:cd11715 101 HSQFAALRVKDAIVDRF-REKGKRPSVDLDNPDVRIRVHLSKDRATLSLDLSG 152
|
|
| Trm14_Arch |
NF040721 |
tRNA (guanine(6)-N2)-methyltransferase; |
33-316 |
8.76e-36 |
|
tRNA (guanine(6)-N2)-methyltransferase;
Pssm-ID: 468685 [Multi-domain] Cd Length: 370 Bit Score: 139.04 E-value: 8.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 33 GGVHFKGDTRLVYQSLMWSRLASRIMLPLGECKVYSDL-DLYLGVQAINWTEMfNPGATFAVHFSGLNDTIRNSQYGAMK 111
Cdd:NF040721 34 GRVFFEGDLELIPKLNYLSRTLERIVILLHREKFEGSLeDIYKRVYSIDFSFI-KPEQSFAIRPLRVGEHDFTSIDIGRV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 112 VKDAIVDAFTRKNLPRPNVDRDAPDIRVNVWLHKETASIALDLSGD-GLHLRGYRDRAGIAPIKETLAAAIVMRSGWQPG 190
Cdd:NF040721 113 AGEAVIDSYLRDKGVRLKVNLDEPDVIVRVELIFDELLVGIDTTGDeGLHKRGYRVYQHPAHLNPTIASSLIYLSGWKDE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 191 TPLLDPMCGSGTLLIEAAMLATDRAPGLHRGRWGFSGWAQHDEAIWQEvkaeaqtrarkglAEYSSHFYGSDSDARVIQR 270
Cdd:NF040721 193 ESLLDPMCGSGTILIEAALIKRNIPPGKFREDFAFKKIFGHELLEKIK-------------KDVELKIYGIEKFRKHLEG 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 238688381 271 ARTNARLAGIGELITFEVKDVAQLTNPLPKGPYgtVLSNPPYGERL 316
Cdd:NF040721 260 AKKNAENAGVDDTIKFIQGDATKLDKYFDSVDV--IVTNPPYGLRI 303
|
|
| THUMP |
smart00981 |
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ... |
68-153 |
1.31e-14 |
|
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterised RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.
Pssm-ID: 214952 [Multi-domain] Cd Length: 83 Bit Score: 69.23 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 68 SDLDLYLGVQA-INWTEMFNPGATFAVHFSGLNdtiRNSQYGAMKVKDAIVDAFtRKNLPRPNVDRDAPDIRVNVWLHKE 146
Cdd:smart00981 1 DLEDLYETALElIRWEKIFKEGKTFAVRAKRRG---KNHEFTSLEVKRAIGDKL-LEKTGGRKVDLKNPDVVIRVELRKD 76
|
....*..
gi 238688381 147 TASIALD 153
Cdd:smart00981 77 KAYLSID 83
|
|
| TIGR01177 |
TIGR01177 |
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ... |
71-351 |
1.26e-07 |
|
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is found exclusively in the Archaea. [Hypothetical proteins, Conserved]
Pssm-ID: 273486 [Multi-domain] Cd Length: 329 Bit Score: 53.98 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 71 DLYLGVQAINWTEMFNpgATFAVHFSGLNDTIRNSQYGAMKVKDAIVDAFTRknlprpnVDRDAPDIRVNVWLHKETASI 150
Cdd:TIGR01177 68 DLYDFVAGLEASDLDR--KSFAVRVRDLRGYSVDKARLERKIGAILKKKGFK-------VSLRRPDIVVRVVITEDIFYL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 151 AL---DLSGDGLHLRGYRDRAGIAP--IKETLAAAIVMRSGWQPGTPLLDPMCGSGTLLIEAAMLatdrapGLHRgrwgf 225
Cdd:TIGR01177 139 GRvleERDKEQFIERKPDRRPFFKPgsMDPKLARAMVNLARVTEGDRVLDPFCGTGGFLIEAGLM------GAKV----- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 226 sgwaqhdeaiwqevkaeaqtrarkglaeysshfYGSDSDARVIQRARTNARLAGIgELITFEVKDVAQLtnPLPKGPYGT 305
Cdd:TIGR01177 208 ---------------------------------IGCDIDWKMVAGARINLEHYGI-EDFFVKRGDATKL--PLSSESVDA 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 238688381 306 VLSNPPYG-------ERLDS--EPALIALHSLLGRimknqfGGWNLSLFSASPDL 351
Cdd:TIGR01177 252 IATDPPYGrsttaagDGLESlyERSLEEFHEVLKS------EGWIVYAVPTRIDL 300
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| rlmL |
PRK11783 |
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ... |
1-702 |
0e+00 |
|
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2))-methyltransferase RlmL;
Pssm-ID: 236981 [Multi-domain] Cd Length: 702 Bit Score: 1393.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 1 MNSLFASTARGLEELLKTELENLGAVECQVVQGGVHFKGDTRLVYQSLMWSRLASRIMLPLGECKVYSDLDLYLGVQAIN 80
Cdd:PRK11783 1 MNSLFASCAKGLEELLKDELEALGASECKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSDLDLYLGVQAID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 81 WTEMFNPGATFAVHFSGLNDTIRNSQYGAMKVKDAIVDAFTRKNLPRPNVDRDAPDIRVNVWLHKETASIALDLSGDGLH 160
Cdd:PRK11783 81 WTEHFSPDKTFAVDFSGTNDEIRNTQFGALKVKDAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEATISLDLSGESLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 161 LRGYRDRAGIAPIKETLAAAIVMRSGW-QPGTPLLDPMCGSGTLLIEAAMLATDRAPGLHRGRWGFSGWAQHDEAIWQEV 239
Cdd:PRK11783 161 QRGYRQATGEAPLKENLAAAILLRSGWpQEGTPLLDPMCGSGTLLIEAAMMAADIAPGLHRERWGFSGWLGHDEALWQEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 240 KAEAQTRARKGLAEYSSHFYGSDSDARVIQRARTNARLAGIGELITFEVKDVAQLTNPLPKGPYGTVLSNPPYGERLDSE 319
Cdd:PRK11783 241 LEEAQERARAGLAELPSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKNPLPKGPTGLVISNPPYGERLGEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 320 PALIALHSLLGRIMKNQFGGWNLSLFSASPDLLSCLQLRADKQYKAKNGPLDCVQKNYHVAEStPDSKPAMVAEDYTNRL 399
Cdd:PRK11783 321 PALIALYSQLGRRLKQQFGGWNAALFSSSPELLSCLGLRADKQYKLKNGALECVLKNYTIAEE-STSSDAEGAQDFANRL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 400 RKNLKKFEKWARQEGIECYRLYDADLPEYNVAVDRYADWVVVQEYAPPKTIDAHKARQRLFDIIAATISVLGIAPNKLVL 479
Cdd:PRK11783 400 RKNLKKLKKWAKQEGIECYRLYDADLPEYNVAVDRYGDWVVVQEYAAPKTIDEEKARQRLFDALAATPEVLGIPPNKVVL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 480 KTRERQKGKNQYQKLGEKGEFLEVTEYNAHLWVNLTDYLDTGLFLDHRIARRMLGQMSKGKDFLNLFSYTGSATVHAGLG 559
Cdd:PRK11783 480 KTRERQKGKNQYQKLAEKGEFLEVTEYGAKLLVNLTDYLDTGLFLDHRPTRRMIGQMAKGKDFLNLFAYTGTASVHAALG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 560 GARSTTTVDMSRTYLEWAERNLRLNGLTGRAHRLIQADCLAWLREANEQFDLIFIDPPTFSNSKRMEDAFDVQRDHLALM 639
Cdd:PRK11783 560 GAKSTTTVDMSNTYLEWAERNFALNGLSGRQHRLIQADCLAWLKEAREQFDLIFIDPPTFSNSKRMEDSFDVQRDHVALI 639
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 238688381 640 KDLKRLLRAGGTIMFSNNKRGFRMDLDGLAKLGLKAQEITQKTLSQDFARNRQIHNCWLITAA 702
Cdd:PRK11783 640 KDAKRLLRPGGTLYFSNNKRGFKMDEEGLAKLGLKAEEITAKTLPPDFARNPKIHNCWLITHA 702
|
|
| RlmL |
COG0116 |
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ... |
2-372 |
8.36e-165 |
|
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA G2445 N2-methylase RlmL is part of the Pathway/BioSystem: 23S rRNA modification
Pssm-ID: 439886 [Multi-domain] Cd Length: 369 Bit Score: 478.06 E-value: 8.36e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 2 NSLFASTARGLEELLKTELENLGAVECQVVQGGVHFKGDTRLVYQSLMWSRLASRIMLPLGECKVYSDLDLYLGVQAINW 81
Cdd:COG0116 1 FELFATCARGLEALLADELKELGAEDVKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFKARTFDDLYEGAKAIPW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 82 TEMFNPGATFAVHFSGLNDTIRNSQYGAMKVKDAIVDAFTRKNLPRPNVDRDAPDIRVNVWLHKETASIALDLSGDGLHL 161
Cdd:COG0116 81 EEYLPPDGTFAVDATSVKSKLFHSQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHVHLLKDRATLSLDTSGESLHK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 162 RGYRDRAGIAPIKETLAAAIVMRSGWQPGTPLLDPMCGSGTLLIEAAMLATDRAPGLHRgRWGFSGWAQHDEAIWQEVKA 241
Cdd:COG0116 161 RGYREAQGEAPLKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAALIAANIAPGLNR-DFAFEKWPDFDAELWQELRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 242 EAQTRARKGLAeysSHFYGSDSDARVIQRARTNARLAGIGELITFEVKDVAQLTnplPKGPYGTVLSNPPYGERLDSEPA 321
Cdd:COG0116 240 EAEARIKRDPP---LPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLE---PPAEPGLIITNPPYGERLGEEEE 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 238688381 322 LIALHSLLGRIMKNQFGGWNLSLFSASPDLLSCLQLRADKQYKAKNGPLDC 372
Cdd:COG0116 314 LEALYRELGDVLKQRFKGWSAYILTSDPELEKAIGLKASKRRKLYNGGLEC 364
|
|
| RlmK |
COG1092 |
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ... |
383-700 |
7.64e-126 |
|
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification
Pssm-ID: 440709 [Multi-domain] Cd Length: 392 Bit Score: 379.14 E-value: 7.64e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 383 TPDSKPAMVAEDYTNRLRKNLKKFEKWARQEGIECYRLYDAD---LPeyNVAVDRYADWVVVQEYAPPKTIdahkarqRL 459
Cdd:COG1092 64 SRDPDEPIDAAFFANRLRKALALRRKLAKREGTNAYRLVHGEadgLP--GLIVDRYGDVLVVQEYSAGMER-------RR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 460 FDIIAATISVLGiaPNKLVLKTRER---QKGKNQYQKL--GEKGEFLEVTEYNAHLWVNLTDYLDTGLFLDHRIARRMLG 534
Cdd:COG1092 135 DEILEALVEVLG--PEGIYLRSDVRvrqLEGLPQYEGVlyGEAPEEVEVEENGLKFLVDLTDGQKTGLFLDQRENRARVA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 535 QMSKGKDFLNLFSYTGSATVHAGLGGARSTTTVDMSRTYLEWAERNLRLNGLTGRaHRLIQADCLAWLREA---NEQFDL 611
Cdd:COG1092 213 ELAKGKRVLNLFSYTGGFSVHAAAGGAKSVTSVDLSATALEWAKENAALNGLDDR-HEFVQADAFDWLRELareGERFDL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 612 IFIDPPTFSNSKRmeDAFDVQRDHLALMKDLKRLLRAGGTIMFSNNKRGFRMDL------DGLAKLGLKAQEITQKTLSQ 685
Cdd:COG1092 292 IILDPPAFAKSKK--DLFDAQRDYKDLNRLALKLLAPGGILVTSSCSRHFSLDLfleilaRAARDAGRRVRIIERLTQPP 369
|
330 340
....*....|....*....|
gi 238688381 686 DFARNRQIHN-----CWLIT 700
Cdd:COG1092 370 DHPVLPAFPEgeylkGLLLR 389
|
|
| UPF0020 |
pfam01170 |
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ... |
162-376 |
1.85e-69 |
|
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.
Pssm-ID: 395932 [Multi-domain] Cd Length: 184 Bit Score: 224.93 E-value: 1.85e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 162 RGYRDRAGIAPIKETLAAAIVMRSGWQPGTPLLDPMCGSGTLLIEAAMLATDRAPGLHRgrwgfsgwaqhdeaiwqevka 241
Cdd:pfam01170 1 RGYRPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPGKFD--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 242 eaqtrarkglAEYSSHFYGSDSDARVIQRARTNARLAGIGELITFEVKDVAQLtnPLPKGPYGTVLSNPPYGERLDSEPA 321
Cdd:pfam01170 60 ----------ARVRAPLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADL--PLLEGSVDVIVTNPPYGIRLGSKGA 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 238688381 322 LIALHSLLGRIMKNQF--GGWNLSLFSASPDLLSCLQLRADKQYKAKNGPLDCVQKN 376
Cdd:pfam01170 128 LEALYPEFLREAKRVLrgGGWLVLLTAENKDFEKAARERAWRKKKEFNVHIGGTRVI 184
|
|
| THUMP_AdoMetMT |
cd11715 |
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ... |
24-156 |
2.10e-46 |
|
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of this family contain an N-terminal THUMP domain and a C-terminal S-adenosylmethionine-dependent methyltransferase domain. Members have been implicated in the modification of 23S RNA m2G2445, a highly conserved modification in bacteria and in the m2G6 modification of tRNA. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.
Pssm-ID: 212584 Cd Length: 152 Bit Score: 161.59 E-value: 2.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 24 GAVECQVVQGGVHFKGDTRLVYQSLMWSRLASRIMLPLGECKVYSDLDLYLGVQAINWTEMFNPGATFAVHFSGLNDTIR 103
Cdd:cd11715 21 GAEDVEVGPGGVSFEGDLEDAYRANLWLRTAHRVLLLLAEFEAEDFDDLYELAKAIDWEDYLDPDGTFAVRATRVGSKLF 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 238688381 104 NSQYGAMKVKDAIVDAFtRKNLPRPNVDRDAPDIRVNVWLHKETASIALDLSG 156
Cdd:cd11715 101 HSQFAALRVKDAIVDRF-REKGKRPSVDLDNPDVRIRVHLSKDRATLSLDLSG 152
|
|
| THUMP |
cd11688 |
THUMP domain, predicted to bind RNA; The THUMP domain is named after THioUridine synthases, ... |
4-151 |
4.75e-43 |
|
THUMP domain, predicted to bind RNA; The THUMP domain is named after THioUridine synthases, RNA Methyltransferases and Pseudo-uridine synthases. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.
Pssm-ID: 212583 Cd Length: 148 Bit Score: 152.26 E-value: 4.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 4 LFASTARGLEELLKTELENLGAV-----ECQVV-QGGVHFKGDT-RLVYQSLMWSRLASRIMLPLGECKVySDLDLYLGV 76
Cdd:cd11688 1 VFATTGKGLEEILAAELYELLEVrgfdaEIQVVpHGRVHFKTDTdEAVYQLVMWSRLISRIMPPLGECKA-DLEDLYETA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 238688381 77 QAINWTEMFNPGATFAVHFSGLNDTIRNSQYGAMKVKDAIVDAFTrknlprPNVDRDAPDIRVNVWLHKETASIA 151
Cdd:cd11688 80 LEINEPEMGNEGAKFAVRARRRNKTILNSQEIAMKVGDAIVDAFN------PEVDLDNPDIVVNVEVHKEIASIA 148
|
|
| Trm14_Arch |
NF040721 |
tRNA (guanine(6)-N2)-methyltransferase; |
33-316 |
8.76e-36 |
|
tRNA (guanine(6)-N2)-methyltransferase;
Pssm-ID: 468685 [Multi-domain] Cd Length: 370 Bit Score: 139.04 E-value: 8.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 33 GGVHFKGDTRLVYQSLMWSRLASRIMLPLGECKVYSDL-DLYLGVQAINWTEMfNPGATFAVHFSGLNDTIRNSQYGAMK 111
Cdd:NF040721 34 GRVFFEGDLELIPKLNYLSRTLERIVILLHREKFEGSLeDIYKRVYSIDFSFI-KPEQSFAIRPLRVGEHDFTSIDIGRV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 112 VKDAIVDAFTRKNLPRPNVDRDAPDIRVNVWLHKETASIALDLSGD-GLHLRGYRDRAGIAPIKETLAAAIVMRSGWQPG 190
Cdd:NF040721 113 AGEAVIDSYLRDKGVRLKVNLDEPDVIVRVELIFDELLVGIDTTGDeGLHKRGYRVYQHPAHLNPTIASSLIYLSGWKDE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 191 TPLLDPMCGSGTLLIEAAMLATDRAPGLHRGRWGFSGWAQHDEAIWQEvkaeaqtrarkglAEYSSHFYGSDSDARVIQR 270
Cdd:NF040721 193 ESLLDPMCGSGTILIEAALIKRNIPPGKFREDFAFKKIFGHELLEKIK-------------KDVELKIYGIEKFRKHLEG 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 238688381 271 ARTNARLAGIGELITFEVKDVAQLTNPLPKGPYgtVLSNPPYGERL 316
Cdd:NF040721 260 AKKNAENAGVDDTIKFIQGDATKLDKYFDSVDV--IVTNPPYGLRI 303
|
|
| THUMP |
pfam02926 |
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ... |
24-154 |
4.08e-21 |
|
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and PSUSs. The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterized RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.
Pssm-ID: 460749 Cd Length: 143 Bit Score: 90.19 E-value: 4.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 24 GAVECQVVQGGVHFKGDTRLVYQSLMWSRLASRImlPLGECKVYSDLDLYLGVQAINWTEMFNPGATFAVHFSGLNDtir 103
Cdd:pfam02926 20 GRGRILVVLKGENPEEDRELLKEALEKAPGIERF--PVAETCEADLEDILELAKEIIKDKFKKEGETFAVRVKRRGK--- 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 238688381 104 NSQYGAMKVKDAIVDAFTRKNLPRpnVDRDAPDIRVNVWLHKETASIALDL 154
Cdd:pfam02926 95 NHEFTSLEINREVGKAIVEKTGLK--VDLENPDIVVHVEIIKDKAYISIDR 143
|
|
| PRK15128 |
PRK15128 |
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI; |
395-623 |
7.54e-19 |
|
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI;
Pssm-ID: 185082 [Multi-domain] Cd Length: 396 Bit Score: 89.13 E-value: 7.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 395 YTNRLRKnLKKFEKW-ARQEGIECYRLYDAD---LPeyNVAVDRYADWVVVQeyappkTIDAHKARQRlfdiiAATISVL 470
Cdd:PRK15128 79 FTRRLQQ-AQKWRDWlAQKDGLDSYRLIAGEsdgLP--GITIDRFGNFLVLQ------LLSAGAEYQR-----AALISAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 471 GIAPNKLVLKTRE----RQKGK---NQYQKLGE-KGEFLEVTEYNAHLWVNLTDYLDTGLFLDHRIARRMLGQMSKGKDF 542
Cdd:PRK15128 145 QTLYPECAIYDRSdvavRKKEGmelTQGPVTGElPPALLPIEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRRYVENKRV 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 543 LNLFSYTGSATVHAGLGGARSTTTVDMSRTYLEWAERNLRLNGLTGRAHRLIQADCLAWL---REANEQFDLIFIDPPTF 619
Cdd:PRK15128 225 LNCFSYTGGFAVSALMGGCSQVVSVDTSQEALDIARQNVELNKLDLSKAEFVRDDVFKLLrtyRDRGEKFDVIVMDPPKF 304
|
....
gi 238688381 620 SNSK 623
Cdd:PRK15128 305 VENK 308
|
|
| Methyltrans_SAM |
pfam10672 |
S-adenosylmethionine-dependent methyltransferase; Members of this family are ... |
477-653 |
3.36e-18 |
|
S-adenosylmethionine-dependent methyltransferase; Members of this family are S-adenosylmethionine-dependent methyltransferases from gamma-proteobacterial species. The diversity in the roles of methylation is matched by the almost bewildering number of methyltransferase enzymes that catalyze the methylation reaction. Although several classes of methyltransferase enzymes are known, the great majority of methylation reactions are catalyzed by the S-adenosylmethionine-dependent methyltransferases.
Pssm-ID: 287624 [Multi-domain] Cd Length: 286 Bit Score: 85.70 E-value: 3.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 477 LVLKTRERQKGKNQYQkLGEKGEFLEVTEYNAHLWVNLTDYLDTGLFLDHRIARRMLGQMSKGKDFLNLFSYTGSATVHA 556
Cdd:pfam10672 63 LVLQHRYADGAPSEVL-SGELLETPVVVENGLKYQLDIGRNQNFGLFLDMRLGRRWVQENAKGKNVLNLFAYTCGFSVAA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 557 GLGGARSTTTVDMSRTYLEWAERNLRLNGLTGRAHRLIQADCL-AW--LREANeQFDLIFIDPPTFSNSkrmedAFDVQR 633
Cdd:pfam10672 142 IAGGASQVVNVDMARGSLNKGRDNHRLNGHDLGRVSFLGHDIFkSWgkIKKLG-PYDLVIIDPPSFQKG-----SFALTK 215
|
170 180
....*....|....*....|
gi 238688381 634 DHLALMKDLKRLLRAGGTIM 653
Cdd:pfam10672 216 DYKKILRRLPELLVEGGTVL 235
|
|
| THUMP |
smart00981 |
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ... |
68-153 |
1.31e-14 |
|
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterised RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.
Pssm-ID: 214952 [Multi-domain] Cd Length: 83 Bit Score: 69.23 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 68 SDLDLYLGVQA-INWTEMFNPGATFAVHFSGLNdtiRNSQYGAMKVKDAIVDAFtRKNLPRPNVDRDAPDIRVNVWLHKE 146
Cdd:smart00981 1 DLEDLYETALElIRWEKIFKEGKTFAVRAKRRG---KNHEFTSLEVKRAIGDKL-LEKTGGRKVDLKNPDVVIRVELRKD 76
|
....*..
gi 238688381 147 TASIALD 153
Cdd:smart00981 77 KAYLSID 83
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
177-313 |
1.03e-13 |
|
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: 69.59 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 177 LAAAIVMRSGWQPGTPLLDPMCGSGTLLIEAAMLatdrapglhrGRwgfsgwaqhdeaiwqevkaeaqtrarkglaeyss 256
Cdd:COG1041 14 LARALVNLAGAKEGDTVLDPFCGTGTILIEAGLL----------GR---------------------------------- 49
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 238688381 257 HFYGSDSDARVIQRARTNARLAGIgELITFEVKDVAQLtnPLPKGPYGTVLSNPPYG 313
Cdd:COG1041 50 RVIGSDIDPKMVEGARENLEHYGY-EDADVIRGDARDL--PLADESVDAIVTDPPYG 103
|
|
| RsmD |
COG0742 |
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
532-617 |
1.03e-09 |
|
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: 58.17 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 532 MLGQMSKGKDFLNLFSYTGSatvhagLG------GARSTTTVDMSRTYLEWAERNLRLNGLTGRAhRLIQADCLAWL-RE 604
Cdd:COG0742 35 ILGPDIEGARVLDLFAGSGA------LGlealsrGAASVVFVEKDRKAAAVIRKNLEKLGLEDRA-RVIRGDALRFLkRL 107
|
90
....*....|...
gi 238688381 605 ANEQFDLIFIDPP 617
Cdd:COG0742 108 AGEPFDLVFLDPP 120
|
|
| TrmR |
COG4122 |
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ... |
519-656 |
5.98e-09 |
|
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: 55.96 E-value: 5.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 519 DTGLFLdhriarRMLGQMSKGKDFLNLFSYTGSATVH--AGLGGARSTTTVDMSRTYLEWAERNLRLNGLTGRAhRLIQA 596
Cdd:COG4122 3 EQGRLL------YLLARLLGAKRILEIGTGTGYSTLWlaRALPDDGRLTTIEIDPERAAIARENFARAGLADRI-RLILG 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 238688381 597 DCLAWLRE-ANEQFDLIFIDpptfSNSKRMEDAFDvqrdhlalmkDLKRLLRAGGTIMFSN 656
Cdd:COG4122 76 DALEVLPRlADGPFDLVFID----ADKSNYPDYLE----------LALPLLRPGGLIVADN 122
|
|
| Cons_hypoth95 |
pfam03602 |
Conserved hypothetical protein 95; |
532-617 |
8.78e-08 |
|
Conserved hypothetical protein 95;
Pssm-ID: 427391 [Multi-domain] Cd Length: 179 Bit Score: 52.63 E-value: 8.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 532 MLGQMSKGKDFLNLFSYTGSATVHAGLGGARSTTTVDMSRTYLEWAERNLRLNGLtgRAHRLIQADCLAWLR--EANEQF 609
Cdd:pfam03602 35 WLAPYIEGARVLDLFAGSGALGLEALSRGAKRVTLVEKDKRAVQILKENLQLLGL--PGAVLVMDALLALLRlaGKGPVF 112
|
....*...
gi 238688381 610 DLIFIDPP 617
Cdd:pfam03602 113 DIVFLDPP 120
|
|
| TIGR01177 |
TIGR01177 |
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ... |
71-351 |
1.26e-07 |
|
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is found exclusively in the Archaea. [Hypothetical proteins, Conserved]
Pssm-ID: 273486 [Multi-domain] Cd Length: 329 Bit Score: 53.98 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 71 DLYLGVQAINWTEMFNpgATFAVHFSGLNDTIRNSQYGAMKVKDAIVDAFTRknlprpnVDRDAPDIRVNVWLHKETASI 150
Cdd:TIGR01177 68 DLYDFVAGLEASDLDR--KSFAVRVRDLRGYSVDKARLERKIGAILKKKGFK-------VSLRRPDIVVRVVITEDIFYL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 151 AL---DLSGDGLHLRGYRDRAGIAP--IKETLAAAIVMRSGWQPGTPLLDPMCGSGTLLIEAAMLatdrapGLHRgrwgf 225
Cdd:TIGR01177 139 GRvleERDKEQFIERKPDRRPFFKPgsMDPKLARAMVNLARVTEGDRVLDPFCGTGGFLIEAGLM------GAKV----- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 226 sgwaqhdeaiwqevkaeaqtrarkglaeysshfYGSDSDARVIQRARTNARLAGIgELITFEVKDVAQLtnPLPKGPYGT 305
Cdd:TIGR01177 208 ---------------------------------IGCDIDWKMVAGARINLEHYGI-EDFFVKRGDATKL--PLSSESVDA 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 238688381 306 VLSNPPYG-------ERLDS--EPALIALHSLLGRimknqfGGWNLSLFSASPDL 351
Cdd:TIGR01177 252 IATDPPYGrsttaagDGLESlyERSLEEFHEVLKS------EGWIVYAVPTRIDL 300
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
541-655 |
1.19e-06 |
|
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).
Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 47.42 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 541 DFLNLFSYTGSATVHAGLGGARSTTTVDMSRTYLEWAERNlRLNGLTGRAhRLIQADCLAWLREANEQFDLIFIDPPTFS 620
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKA-AAALLADNV-EVLKGDAEELPPEADESFDVIISDPPLHH 78
|
90 100 110
....*....|....*....|....*....|....*
gi 238688381 621 NSKRMEDAFDVqrdhlalmkdLKRLLRAGGTIMFS 655
Cdd:cd02440 79 LVEDLARFLEE----------ARRLLKPGGVLVLT 103
|
|
| YhdJ |
COG0863 |
DNA modification methylase [Replication, recombination and repair]; |
592-652 |
1.06e-05 |
|
DNA modification methylase [Replication, recombination and repair];
Pssm-ID: 440623 Cd Length: 236 Bit Score: 47.22 E-value: 1.06e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 238688381 592 RLIQADCLAWLRE-ANEQFDLIFIDPP-----TFSNSKRMEDAFDVQRDHLALMKD----LKRLLRAGGTI 652
Cdd:COG0863 1 RLICGDCLEVLKElPDESVDLIVTDPPynlgkKYGLGRREIGNELSFEEYLEFLREwlaeCYRVLKPGGSL 71
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
525-655 |
2.68e-05 |
|
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: 44.24 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 525 DHRIARRMLGQMSKGKDFLNLFSYTGSATVHAGLGGARsTTTVDMSRTYLEWAERNLRLNGLtgrahRLIQADCLAwLRE 604
Cdd:COG2227 11 DRRLAALLARLLPAGGRVLDVGCGTGRLALALARRGAD-VTGVDISPEALEIARERAAELNV-----DFVQGDLED-LPL 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 238688381 605 ANEQFDLIFidpptfsnskrmedAFDVQ---RDHLALMKDLKRLLRAGGTIMFS 655
Cdd:COG2227 84 EDGSFDLVI--------------CSEVLehlPDPAALLRELARLLKPGGLLLLS 123
|
|
| COG2521 |
COG2521 |
Predicted archaeal methyltransferase [General function prediction only]; |
557-654 |
4.88e-05 |
|
Predicted archaeal methyltransferase [General function prediction only];
Pssm-ID: 442011 [Multi-domain] Cd Length: 285 Bit Score: 45.67 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 557 GLG---------GARSTTTVDMSRTYLEWAERNLRLNGLTGRAHRLIQADCLAWLRE-ANEQFDLIFIDPPTFSNSKRME 626
Cdd:COG2521 142 GLGytaiealkrGAREVITVEKDPNVLELAELNPWSRELANERIKIILGDASEVIKTfPDESFDAIIHDPPRFSLAGELY 221
|
90 100
....*....|....*....|....*...
gi 238688381 627 DafdvqrdhLALMKDLKRLLRAGGtIMF 654
Cdd:COG2521 222 S--------LEFYRELYRVLKPGG-RLF 240
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
549-650 |
4.88e-05 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 42.55 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 549 TGSATVH-AGLGGARsTTTVDMSRTYLEWAERNLRLNGLTgraHRLIQADCLAwLREANEQFDLIFidpptfsnskrmed 627
Cdd:pfam13649 8 TGRLTLAlARRGGAR-VTGVDLSPEMLERARERAAEAGLN---VEFVQGDAED-LPFPDGSFDLVV-------------- 68
|
90 100
....*....|....*....|....*...
gi 238688381 628 AFDV-----QRDHLALMKDLKRLLRAGG 650
Cdd:pfam13649 69 SSGVlhhlpDPDLEAALREIARVLKPGG 96
|
|
| PRK14967 |
PRK14967 |
putative methyltransferase; Provisional |
519-683 |
9.20e-05 |
|
putative methyltransferase; Provisional
Pssm-ID: 184931 [Multi-domain] Cd Length: 223 Bit Score: 44.27 E-value: 9.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 519 DTGLFLDhRIARRMLGQmskGKDFLNLFSYTGSATVHAGLGGARSTTTVDMSRTYLEWAERNLRLNGLTGRAHRLIQADC 598
Cdd:PRK14967 21 DTQLLAD-ALAAEGLGP---GRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNALLAGVDVDVRRGDWARA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 599 LAWLReaneqFDLIFIDPP------TFSNSKRMEDAFDVQRDHLALM----KDLKRLLRAGGTIMFSNNK-RGFRMDLDG 667
Cdd:PRK14967 97 VEFRP-----FDVVVSNPPyvpappDAPPSRGPARAWDAGPDGRAVLdrlcDAAPALLAPGGSLLLVQSElSGVERTLTR 171
|
170
....*....|....*.
gi 238688381 668 LAKLGLKAQEITQKTL 683
Cdd:PRK14967 172 LSEAGLDAEVVASQWI 187
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
549-654 |
1.16e-04 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 42.99 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 549 TGSATVH-AGLGGARsTTTVDMSRTYLEWAERNLRLNGLTGRAhRLIQADCLAWlrEANEQFDLIFidpptfsnskrMED 627
Cdd:COG2230 62 WGGLALYlARRYGVR-VTGVTLSPEQLEYARERAAEAGLADRV-EVRLADYRDL--PADGQFDAIV-----------SIG 126
|
90 100
....*....|....*....|....*....
gi 238688381 628 AFD-VQRDHL-ALMKDLKRLLRAGGTIMF 654
Cdd:COG2230 127 MFEhVGPENYpAYFAKVARLLKPGGRLLL 155
|
|
| COG4262 |
COG4262 |
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ... |
562-654 |
3.28e-04 |
|
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction only];
Pssm-ID: 443404 [Multi-domain] Cd Length: 426 Bit Score: 43.70 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 562 RSTTTVDMSRTYLEWAERNLRLNGLTGRAH-----RLIQADCLAWLREANEQFDLIFIDPP---TFSNSKRMEDAFdvqr 633
Cdd:COG4262 311 ESVTLVDLDPEVTDLAKTNPFLRELNGGALndprvTVVNADAFQFLRETDEKYDVIIVDLPdpsNFSLGKLYSVEF---- 386
|
90 100
....*....|....*....|.
gi 238688381 634 dhlalMKDLKRLLRAGGTIMF 654
Cdd:COG4262 387 -----YRLVRRHLAPGGVLVV 402
|
|
| Methyltransf_24 |
pfam13578 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
547-654 |
4.28e-04 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 433324 [Multi-domain] Cd Length: 106 Bit Score: 40.37 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 547 SYTGSATVHAGL----GGARSTTTVDMSRTYLEwAERNLRLNGLTGRAhRLIQADCLAWLRE-ANEQFDLIFID-PPTFS 620
Cdd:pfam13578 5 TYSGVSTLWLAAalrdNGLGRLTAVDPDPGAEE-AGALLRKAGLDDRV-RLIVGDSREALPSlADGPIDLLFIDgDHTYE 82
|
90 100 110
....*....|....*....|....*....|....
gi 238688381 621 nskrmedafDVQRDhlalMKDLKRLLRAGGTIMF 654
Cdd:pfam13578 83 ---------AVLND----LELWLPRLAPGGVILF 103
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
577-654 |
4.34e-04 |
|
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 443299 [Multi-domain] Cd Length: 238 Bit Score: 42.44 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 577 AERNLRLNGLTGRAHrLIQADCLAWLRE-ANEQFDLIFIDPPTFSNSK------------RMEDAFdvqrDHLALMKDLK 643
Cdd:COG4123 77 ARRNVALNGLEDRIT-VIHGDLKEFAAElPPGSFDLVVSNPPYFKAGSgrkspdearaiaRHEDAL----TLEDLIRAAA 151
|
90
....*....|.
gi 238688381 644 RLLRAGGTIMF 654
Cdd:COG4123 152 RLLKPGGRFAL 162
|
|
| TrmA |
COG2265 |
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ... |
526-617 |
5.39e-04 |
|
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: 42.86 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 526 HRIARRMLGQMskgKDFLNLfsyTGSATV---HAGLGG--------ARSTTTVDMSRTYLEWAERNLRLNGLTGraHRLI 594
Cdd:COG2265 215 PEQAEALYAAA---LEWLDL---TGGERVldlYCGVGTfalplarrAKKVIGVEIVPEAVEDARENARLNGLKN--VEFV 286
|
90 100
....*....|....*....|....*
gi 238688381 595 QADCLAWLRE--ANEQFDLIFIDPP 617
Cdd:COG2265 287 AGDLEEVLPEllWGGRPDVVVLDPP 311
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
524-694 |
5.56e-04 |
|
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: 41.47 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 524 LDHRIARRM--LGQMSKGKDFLNLFSYTGSATVHAGLGGARSTTtVDMSRTYLEWAERNLRLNGLTGraHRLIQADCLAw 601
Cdd:COG1041 10 LDPRLARALvnLAGAKEGDTVLDPFCGTGTILIEAGLLGRRVIG-SDIDPKMVEGARENLEHYGYED--ADVIRGDARD- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 602 LREANEQFDLIFIDPP--TFSNSKRmedafdvqRDHLALMKD----LKRLLRAGGTIMFSNNKRGFRMdldgLAKLGLKA 675
Cdd:COG1041 86 LPLADESVDAIVTDPPygRSSKISG--------EELLELYEKaleeAARVLKPGGRVVIVTPRDIDEL----LEEAGFKV 153
|
170
....*....|....*....
gi 238688381 676 QEITQKTLSQDFArnRQIH 694
Cdd:COG1041 154 LERHEQRVHKSLT--RYIL 170
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
257-312 |
7.69e-04 |
|
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 443299 [Multi-domain] Cd Length: 238 Bit Score: 41.67 E-value: 7.69e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 238688381 257 HFYGSDSDARVIQRARTNARLAGIGELITFEVKDVAQLTNPLPKGPYGTVLSNPPY 312
Cdd:COG4123 63 RITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAAELPPGSFDLVVSNPPY 118
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
529-674 |
9.26e-04 |
|
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: 39.98 E-value: 9.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 529 ARRMLGQMS--KGKDFLNLFSYTGSATVHAGLGGARsTTTVDMSRTYLEWAERNLRLNGLTGRahrLIQADCLAwLREAN 606
Cdd:COG2226 11 REALLAALGlrPGARVLDLGCGTGRLALALAERGAR-VTGVDISPEMLELARERAAEAGLNVE---FVVGDAED-LPFPD 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238688381 607 EQFDLIFidpptfsnskrMEDAFDVQRDHLALMKDLKRLLRAGGTIMFSNNKRGFRMDLDG-LAKLGLK 674
Cdd:COG2226 86 GSFDLVI-----------SSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEElLAEAGFE 143
|
|
| COG2263 |
COG2263 |
Predicted RNA methylase [General function prediction only]; |
256-313 |
1.09e-03 |
|
Predicted RNA methylase [General function prediction only];
Pssm-ID: 441864 [Multi-domain] Cd Length: 199 Bit Score: 40.66 E-value: 1.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 238688381 256 SHFYGSDSDARVIQRARTNARlaGIGELITFEVKDVAQLTnplPKGPYGTVLSNPPYG 313
Cdd:COG2263 69 KKVVGVDIDPEALEIARENAE--RLGVRVDFIRADVTRIP---LGGSVDTVVMNPPFG 121
|
|
| rsmD |
PRK10909 |
16S rRNA m(2)G966-methyltransferase; Provisional |
543-617 |
1.36e-03 |
|
16S rRNA m(2)G966-methyltransferase; Provisional
Pssm-ID: 236793 Cd Length: 199 Bit Score: 40.47 E-value: 1.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 238688381 543 LNLFSYTGSATVHAGLGGARSTTTVDMSRTYLEWAERNLRLngLTGRAHRLIQADCLAWLREANEQFDLIFIDPP 617
Cdd:PRK10909 58 LDCFAGSGALGLEALSRYAAGATLLEMDRAVAQQLIKNLAT--LKAGNARVVNTNALSFLAQPGTPHNVVFVDPP 130
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
549-654 |
2.01e-03 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 38.03 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238688381 549 TGSATVHAGLGGARsTTTVDMSRTYLEWAERNLRLNGLTgrahrLIQADCLAwLREANEQFDLIFidpptfsnskrMEDA 628
Cdd:pfam08241 7 TGLLTELLARLGAR-VTGVDISPEMLELAREKAPREGLT-----FVVGDAED-LPFPDNSFDLVL-----------SSEV 68
|
90 100
....*....|....*....|....*.
gi 238688381 629 FDVQRDHLALMKDLKRLLRAGGTIMF 654
Cdd:pfam08241 69 LHHVEDPERALREIARVLKPGGILII 94
|
|
| |
