|
Name |
Accession |
Description |
Interval |
E-value |
| UPF0020 |
pfam01170 |
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ... |
293-478 |
1.08e-68 |
|
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: 217.99 E-value: 1.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 293 RNITHF-GPTTLRSTLAYGMLRLCDPLPYDIIVDPMCGTGAIPIEGATEWSDCFHIAGDNNPLAVNRAANNIASLLTKSQ 371
Cdd:pfam01170 1 RGYRPFnGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPGKFDARVRAPLYGSDIDRRMVQGAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 372 IKEGKPSWGLPIDAVQWDICNLPLRTGSVDIIVTDLPFGKRMGSKKRNWNLYPACLREMSRVCTPtTGRAVLLTQDTKCF 451
Cdd:pfam01170 81 LNAENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRLGSKGALEALYPEFLREAKRVLRG-GGWLVLLTAENKDF 159
|
170 180
....*....|....*....|....*..
gi 530372214 452 TKALSGMRhvWRKVDTVWVNVGGLRAA 478
Cdd:pfam01170 160 EKAARERA--WRKKKEFNVHIGGTRVI 184
|
|
| RlmL super family |
cl43029 |
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ... |
42-459 |
2.61e-18 |
|
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
The actual alignment was detected with superfamily member COG0116:
Pssm-ID: 439886 [Multi-domain] Cd Length: 369 Bit Score: 86.31 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 42 ATVPTGFEQTAADEVREkLGSScKISRDRGKIYFVISVESLAQVH-CLRSVDNLFVVVQEFQDYQFKqtkeevlkDFEDL 120
Cdd:COG0116 5 ATCARGLEALLADELKE-LGAE-DVKVENGGVSFEGDLEDIYRANlWLRTASRVLLPLAEFKARTFD--------DLYEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 121 AGKLPWSNPLKVwkiNASFKkkkakrkkINQNSSKEKINNGQEVkidQRNVKKeftshaldshildyyenpAIKEdvstl 200
Cdd:COG0116 75 AKAIPWEEYLPP---DGTFA--------VDATSVKSKLFHSQFA---ALRVKD------------------AIVD----- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 201 igddlaSCKDETDESSK-EETEPqvlkfrvtcnragekhcftsneaardfggavqdyfkwkadmtnfDVEVLLNIHDNEV 279
Cdd:COG0116 118 ------RFREKYGARPSvDEDGP--------------------------------------------DVRIHVHLLKDRA 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 280 IVGIALTEESLHRRN---ITHFGPttLRSTLAYGMLRLCDPLPYDIIVDPMCGTGAIPIEGA----------------TE 340
Cdd:COG0116 148 TLSLDTSGESLHKRGyreAQGEAP--LKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAAliaaniapglnrdfafEK 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 341 WSDC---------------------FHIAG-DNNPLAVNRAANNIASLltksqikegkpswGLP--IDAVQWDICNLPlR 396
Cdd:COG0116 226 WPDFdaelwqelreeaearikrdppLPIFGsDIDPRAIEAARENAERA-------------GVAdlIEFEQADFRDLE-P 291
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530372214 397 TGSVDIIVTDLPFGKRMGSKKRNWNLYpaclREMSRVCTP--TTGRAVLLTQDTKcFTKALsGMR 459
Cdd:COG0116 292 PAEPGLIITNPPYGERLGEEEELEALY----RELGDVLKQrfKGWSAYILTSDPE-LEKAI-GLK 350
|
|
| THUMP |
smart00981 |
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ... |
226-283 |
6.32e-13 |
|
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: 64.22 E-value: 6.32e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 530372214 226 KFRVTCNRAGEKHCFTSNEAARDFGGAVQD-YFKWKADMTNFDVEVLLNIHDNEVIVGI 283
Cdd:smart00981 24 TFAVRAKRRGKNHEFTSLEVKRAIGDKLLEkTGGRKVDLKNPDVVIRVELRKDKAYLSI 82
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| UPF0020 |
pfam01170 |
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ... |
293-478 |
1.08e-68 |
|
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: 217.99 E-value: 1.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 293 RNITHF-GPTTLRSTLAYGMLRLCDPLPYDIIVDPMCGTGAIPIEGATEWSDCFHIAGDNNPLAVNRAANNIASLLTKSQ 371
Cdd:pfam01170 1 RGYRPFnGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPGKFDARVRAPLYGSDIDRRMVQGAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 372 IKEGKPSWGLPIDAVQWDICNLPLRTGSVDIIVTDLPFGKRMGSKKRNWNLYPACLREMSRVCTPtTGRAVLLTQDTKCF 451
Cdd:pfam01170 81 LNAENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRLGSKGALEALYPEFLREAKRVLRG-GGWLVLLTAENKDF 159
|
170 180
....*....|....*....|....*..
gi 530372214 452 TKALSGMRhvWRKVDTVWVNVGGLRAA 478
Cdd:pfam01170 160 EKAARERA--WRKKKEFNVHIGGTRVI 184
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
297-448 |
7.06e-20 |
|
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: 86.93 E-value: 7.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 297 HFGPTTLRSTLAYGMLRLCDPLPYDIIVDPMCGTGAIPIEGATEWSDCfhIAGDNNPLAVNRAANNIASLLTKSqikegk 376
Cdd:COG1041 4 FFYPGSLDPRLARALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGRRV--IGSDIDPKMVEGARENLEHYGYED------ 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530372214 377 pswglpIDAVQWDICNLPLRTGSVDIIVTDLPFGKRMGSKKRNW-NLYPACLREMSRVcTPTTGRAVLLTQDT 448
Cdd:COG1041 76 ------ADVIRGDARDLPLADESVDAIVTDPPYGRSSKISGEELlELYEKALEEAARV-LKPGGRVVIVTPRD 141
|
|
| RlmL |
COG0116 |
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ... |
42-459 |
2.61e-18 |
|
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: 86.31 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 42 ATVPTGFEQTAADEVREkLGSScKISRDRGKIYFVISVESLAQVH-CLRSVDNLFVVVQEFQDYQFKqtkeevlkDFEDL 120
Cdd:COG0116 5 ATCARGLEALLADELKE-LGAE-DVKVENGGVSFEGDLEDIYRANlWLRTASRVLLPLAEFKARTFD--------DLYEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 121 AGKLPWSNPLKVwkiNASFKkkkakrkkINQNSSKEKINNGQEVkidQRNVKKeftshaldshildyyenpAIKEdvstl 200
Cdd:COG0116 75 AKAIPWEEYLPP---DGTFA--------VDATSVKSKLFHSQFA---ALRVKD------------------AIVD----- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 201 igddlaSCKDETDESSK-EETEPqvlkfrvtcnragekhcftsneaardfggavqdyfkwkadmtnfDVEVLLNIHDNEV 279
Cdd:COG0116 118 ------RFREKYGARPSvDEDGP--------------------------------------------DVRIHVHLLKDRA 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 280 IVGIALTEESLHRRN---ITHFGPttLRSTLAYGMLRLCDPLPYDIIVDPMCGTGAIPIEGA----------------TE 340
Cdd:COG0116 148 TLSLDTSGESLHKRGyreAQGEAP--LKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAAliaaniapglnrdfafEK 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 341 WSDC---------------------FHIAG-DNNPLAVNRAANNIASLltksqikegkpswGLP--IDAVQWDICNLPlR 396
Cdd:COG0116 226 WPDFdaelwqelreeaearikrdppLPIFGsDIDPRAIEAARENAERA-------------GVAdlIEFEQADFRDLE-P 291
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530372214 397 TGSVDIIVTDLPFGKRMGSKKRNWNLYpaclREMSRVCTP--TTGRAVLLTQDTKcFTKALsGMR 459
Cdd:COG0116 292 PAEPGLIITNPPYGERLGEEEELEALY----RELGDVLKQrfKGWSAYILTSDPE-LEKAI-GLK 350
|
|
| THUMP_AdoMetMT |
cd11715 |
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ... |
40-286 |
3.60e-14 |
|
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: 69.92 E-value: 3.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 40 IGATVPTGFEQTAADEVREKLGSscKISRDRGKIYFVISVESLAQV-HCLRSVDNLFVVVQEFqdyqfkqtKEEVLKDFE 118
Cdd:cd11715 1 FFATCPPGLEELLAAELKALGAE--DVEVGPGGVSFEGDLEDAYRAnLWLRTAHRVLLLLAEF--------EAEDFDDLY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 119 DLAGKLPWSNPLKVwkinasfkkkkakrkkinqnsskekinngqevkidqrnvkkeftshaldshildyyenpaikedvs 198
Cdd:cd11715 71 ELAKAIDWEDYLDP------------------------------------------------------------------ 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 199 tligddlasckDETdesskeetepqvlkFRVTCNRAGEkHCFTSNEAARDFGGAVQDYFK-----WKADMTNFDVEVLLN 273
Cdd:cd11715 85 -----------DGT--------------FAVRATRVGS-KLFHSQFAALRVKDAIVDRFRekgkrPSVDLDNPDVRIRVH 138
|
250
....*....|...
gi 530372214 274 IHDNEVIVGIALT 286
Cdd:cd11715 139 LSKDRATLSLDLS 151
|
|
| THUMP |
smart00981 |
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ... |
226-283 |
6.32e-13 |
|
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: 64.22 E-value: 6.32e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 530372214 226 KFRVTCNRAGEKHCFTSNEAARDFGGAVQD-YFKWKADMTNFDVEVLLNIHDNEVIVGI 283
Cdd:smart00981 24 TFAVRAKRRGKNHEFTSLEVKRAIGDKLLEkTGGRKVDLKNPDVVIRVELRKDKAYLSI 82
|
|
| THUMP |
pfam02926 |
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ... |
226-283 |
2.66e-10 |
|
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: 58.60 E-value: 2.66e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 530372214 226 KFRVTCNRAGEKHCFTSNEAARDFGGAVQDYFKWKADMTNFDVEVLLNIHDNEVIVGI 283
Cdd:pfam02926 84 TFAVRVKRRGKNHEFTSLEINREVGKAIVEKTGLKVDLENPDIVVHVEIIKDKAYISI 141
|
|
| TIGR01177 |
TIGR01177 |
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ... |
260-443 |
1.52e-09 |
|
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: 59.37 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 260 KADMTNFDVEVLLNIHDNEVIVGIALT--------EESLHRRniTHFGPTTLRSTLAYGMLRLCDPLPYDIIVDPMCGTG 331
Cdd:TIGR01177 117 KVSLRRPDIVVRVVITEDIFYLGRVLEerdkeqfiERKPDRR--PFFKPGSMDPKLARAMVNLARVTEGDRVLDPFCGTG 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 332 AIPIEGATewsdcfhiagdnnpLAVNRAANNIAslltkSQIKEGKPS----WGLP-IDAVQWDICNLPLRTGSVDIIVTD 406
Cdd:TIGR01177 195 GFLIEAGL--------------MGAKVIGCDID-----WKMVAGARInlehYGIEdFFVKRGDATKLPLSSESVDAIATD 255
|
170 180 190
....*....|....*....|....*....|....*....
gi 530372214 407 LPFGkRMGSKKRNWN--LYPACLREMSRVCTPTTGRAVL 443
Cdd:TIGR01177 256 PPYG-RSTTAAGDGLesLYERSLEEFHEVLKSEGWIVYA 293
|
|
| rlmL |
PRK11783 |
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ... |
238-338 |
2.72e-08 |
|
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: 56.35 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 238 HCFTSNEAARD--FGG-----AVQDYFKWKA------DMTNFDVEVLLNIHDNEVIVGIALTEESLHRRNI-THFGPTTL 303
Cdd:PRK11783 94 DFSGTNDEIRNtqFGAlkvkdAIVDRFRRKGgprpsvDKEQPDIRINARLNKGEATISLDLSGESLHQRGYrQATGEAPL 173
|
90 100 110
....*....|....*....|....*....|....*.
gi 530372214 304 RSTLAYGMLRLCD-PLPYDIIVDPMCGTGAIPIEGA 338
Cdd:PRK11783 174 KENLAAAILLRSGwPQEGTPLLDPMCGSGTLLIEAA 209
|
|
| THUMP_ThiI |
cd11716 |
THUMP domain of thiamine biosynthesis protein ThiI; ThiI is an enzyme responsible for the ... |
227-281 |
3.29e-08 |
|
THUMP domain of thiamine biosynthesis protein ThiI; ThiI is an enzyme responsible for the formation of the modified base S(4)U (4-thiouridine) found at position 8 in some prokaryotic tRNAs. This modification acts as a signal for UV exposure, triggering a response that provides protection against its damaging effects. ThiI consists of an N-terminal THUMP domain, followed by an NFLD domain, and a C-terminal PP-loop pyrophosphatase domain. The N-terminal THUMP domain has been implicated in the recognition of the acceptor-stem region. 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: 212585 Cd Length: 166 Bit Score: 53.22 E-value: 3.29e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 530372214 227 FRVTCNRAGEKHCFTSNEAARDFGGAVQDYFK-WKADMTNFDVEVLLNIHDNEVIV 281
Cdd:cd11716 102 FKVRAKRADKSFPFTSMEINREVGAALLENTPdLKVDLKNPDVTIRVEIREDGAYV 157
|
|
| ThiI |
COG0301 |
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ... |
227-281 |
6.12e-07 |
|
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis]; Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440070 [Multi-domain] Cd Length: 382 Bit Score: 51.63 E-value: 6.12e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 530372214 227 FRVTCNRAGEKHCFTSNEAARDFGGAVQDYFK-WKADMTNFDVEVLLNIHDNEVIV 281
Cdd:COG0301 103 FKVRAKRAGKHFPFTSPELEREVGGALLENTPgLKVDLKNPDVTIRVEVRDDKAYV 158
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| UPF0020 |
pfam01170 |
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ... |
293-478 |
1.08e-68 |
|
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: 217.99 E-value: 1.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 293 RNITHF-GPTTLRSTLAYGMLRLCDPLPYDIIVDPMCGTGAIPIEGATEWSDCFHIAGDNNPLAVNRAANNIASLLTKSQ 371
Cdd:pfam01170 1 RGYRPFnGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPGKFDARVRAPLYGSDIDRRMVQGAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 372 IKEGKPSWGLPIDAVQWDICNLPLRTGSVDIIVTDLPFGKRMGSKKRNWNLYPACLREMSRVCTPtTGRAVLLTQDTKCF 451
Cdd:pfam01170 81 LNAENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRLGSKGALEALYPEFLREAKRVLRG-GGWLVLLTAENKDF 159
|
170 180
....*....|....*....|....*..
gi 530372214 452 TKALSGMRhvWRKVDTVWVNVGGLRAA 478
Cdd:pfam01170 160 EKAARERA--WRKKKEFNVHIGGTRVI 184
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
297-448 |
7.06e-20 |
|
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: 86.93 E-value: 7.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 297 HFGPTTLRSTLAYGMLRLCDPLPYDIIVDPMCGTGAIPIEGATEWSDCfhIAGDNNPLAVNRAANNIASLLTKSqikegk 376
Cdd:COG1041 4 FFYPGSLDPRLARALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGRRV--IGSDIDPKMVEGARENLEHYGYED------ 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530372214 377 pswglpIDAVQWDICNLPLRTGSVDIIVTDLPFGKRMGSKKRNW-NLYPACLREMSRVcTPTTGRAVLLTQDT 448
Cdd:COG1041 76 ------ADVIRGDARDLPLADESVDAIVTDPPYGRSSKISGEELlELYEKALEEAARV-LKPGGRVVIVTPRD 141
|
|
| RlmL |
COG0116 |
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ... |
42-459 |
2.61e-18 |
|
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: 86.31 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 42 ATVPTGFEQTAADEVREkLGSScKISRDRGKIYFVISVESLAQVH-CLRSVDNLFVVVQEFQDYQFKqtkeevlkDFEDL 120
Cdd:COG0116 5 ATCARGLEALLADELKE-LGAE-DVKVENGGVSFEGDLEDIYRANlWLRTASRVLLPLAEFKARTFD--------DLYEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 121 AGKLPWSNPLKVwkiNASFKkkkakrkkINQNSSKEKINNGQEVkidQRNVKKeftshaldshildyyenpAIKEdvstl 200
Cdd:COG0116 75 AKAIPWEEYLPP---DGTFA--------VDATSVKSKLFHSQFA---ALRVKD------------------AIVD----- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 201 igddlaSCKDETDESSK-EETEPqvlkfrvtcnragekhcftsneaardfggavqdyfkwkadmtnfDVEVLLNIHDNEV 279
Cdd:COG0116 118 ------RFREKYGARPSvDEDGP--------------------------------------------DVRIHVHLLKDRA 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 280 IVGIALTEESLHRRN---ITHFGPttLRSTLAYGMLRLCDPLPYDIIVDPMCGTGAIPIEGA----------------TE 340
Cdd:COG0116 148 TLSLDTSGESLHKRGyreAQGEAP--LKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAAliaaniapglnrdfafEK 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 341 WSDC---------------------FHIAG-DNNPLAVNRAANNIASLltksqikegkpswGLP--IDAVQWDICNLPlR 396
Cdd:COG0116 226 WPDFdaelwqelreeaearikrdppLPIFGsDIDPRAIEAARENAERA-------------GVAdlIEFEQADFRDLE-P 291
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530372214 397 TGSVDIIVTDLPFGKRMGSKKRNWNLYpaclREMSRVCTP--TTGRAVLLTQDTKcFTKALsGMR 459
Cdd:COG0116 292 PAEPGLIITNPPYGERLGEEEELEALY----RELGDVLKQrfKGWSAYILTSDPE-LEKAI-GLK 350
|
|
| THUMP_AdoMetMT |
cd11715 |
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ... |
40-286 |
3.60e-14 |
|
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: 69.92 E-value: 3.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 40 IGATVPTGFEQTAADEVREKLGSscKISRDRGKIYFVISVESLAQV-HCLRSVDNLFVVVQEFqdyqfkqtKEEVLKDFE 118
Cdd:cd11715 1 FFATCPPGLEELLAAELKALGAE--DVEVGPGGVSFEGDLEDAYRAnLWLRTAHRVLLLLAEF--------EAEDFDDLY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 119 DLAGKLPWSNPLKVwkinasfkkkkakrkkinqnsskekinngqevkidqrnvkkeftshaldshildyyenpaikedvs 198
Cdd:cd11715 71 ELAKAIDWEDYLDP------------------------------------------------------------------ 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 199 tligddlasckDETdesskeetepqvlkFRVTCNRAGEkHCFTSNEAARDFGGAVQDYFK-----WKADMTNFDVEVLLN 273
Cdd:cd11715 85 -----------DGT--------------FAVRATRVGS-KLFHSQFAALRVKDAIVDRFRekgkrPSVDLDNPDVRIRVH 138
|
250
....*....|...
gi 530372214 274 IHDNEVIVGIALT 286
Cdd:cd11715 139 LSKDRATLSLDLS 151
|
|
| THUMP |
smart00981 |
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ... |
226-283 |
6.32e-13 |
|
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: 64.22 E-value: 6.32e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 530372214 226 KFRVTCNRAGEKHCFTSNEAARDFGGAVQD-YFKWKADMTNFDVEVLLNIHDNEVIVGI 283
Cdd:smart00981 24 TFAVRAKRRGKNHEFTSLEVKRAIGDKLLEkTGGRKVDLKNPDVVIRVELRKDKAYLSI 82
|
|
| THUMP |
pfam02926 |
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ... |
226-283 |
2.66e-10 |
|
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: 58.60 E-value: 2.66e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 530372214 226 KFRVTCNRAGEKHCFTSNEAARDFGGAVQDYFKWKADMTNFDVEVLLNIHDNEVIVGI 283
Cdd:pfam02926 84 TFAVRVKRRGKNHEFTSLEINREVGKAIVEKTGLKVDLENPDIVVHVEIIKDKAYISI 141
|
|
| TIGR01177 |
TIGR01177 |
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ... |
260-443 |
1.52e-09 |
|
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: 59.37 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 260 KADMTNFDVEVLLNIHDNEVIVGIALT--------EESLHRRniTHFGPTTLRSTLAYGMLRLCDPLPYDIIVDPMCGTG 331
Cdd:TIGR01177 117 KVSLRRPDIVVRVVITEDIFYLGRVLEerdkeqfiERKPDRR--PFFKPGSMDPKLARAMVNLARVTEGDRVLDPFCGTG 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 332 AIPIEGATewsdcfhiagdnnpLAVNRAANNIAslltkSQIKEGKPS----WGLP-IDAVQWDICNLPLRTGSVDIIVTD 406
Cdd:TIGR01177 195 GFLIEAGL--------------MGAKVIGCDID-----WKMVAGARInlehYGIEdFFVKRGDATKLPLSSESVDAIATD 255
|
170 180 190
....*....|....*....|....*....|....*....
gi 530372214 407 LPFGkRMGSKKRNWN--LYPACLREMSRVCTPTTGRAVL 443
Cdd:TIGR01177 256 PPYG-RSTTAAGDGLesLYERSLEEFHEVLKSEGWIVYA 293
|
|
| rlmL |
PRK11783 |
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ... |
238-338 |
2.72e-08 |
|
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: 56.35 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 238 HCFTSNEAARD--FGG-----AVQDYFKWKA------DMTNFDVEVLLNIHDNEVIVGIALTEESLHRRNI-THFGPTTL 303
Cdd:PRK11783 94 DFSGTNDEIRNtqFGAlkvkdAIVDRFRRKGgprpsvDKEQPDIRINARLNKGEATISLDLSGESLHQRGYrQATGEAPL 173
|
90 100 110
....*....|....*....|....*....|....*.
gi 530372214 304 RSTLAYGMLRLCD-PLPYDIIVDPMCGTGAIPIEGA 338
Cdd:PRK11783 174 KENLAAAILLRSGwPQEGTPLLDPMCGSGTLLIEAA 209
|
|
| THUMP_ThiI |
cd11716 |
THUMP domain of thiamine biosynthesis protein ThiI; ThiI is an enzyme responsible for the ... |
227-281 |
3.29e-08 |
|
THUMP domain of thiamine biosynthesis protein ThiI; ThiI is an enzyme responsible for the formation of the modified base S(4)U (4-thiouridine) found at position 8 in some prokaryotic tRNAs. This modification acts as a signal for UV exposure, triggering a response that provides protection against its damaging effects. ThiI consists of an N-terminal THUMP domain, followed by an NFLD domain, and a C-terminal PP-loop pyrophosphatase domain. The N-terminal THUMP domain has been implicated in the recognition of the acceptor-stem region. 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: 212585 Cd Length: 166 Bit Score: 53.22 E-value: 3.29e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 530372214 227 FRVTCNRAGEKHCFTSNEAARDFGGAVQDYFK-WKADMTNFDVEVLLNIHDNEVIV 281
Cdd:cd11716 102 FKVRAKRADKSFPFTSMEINREVGAALLENTPdLKVDLKNPDVTIRVEIREDGAYV 157
|
|
| ThiI |
COG0301 |
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ... |
227-281 |
6.12e-07 |
|
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis]; Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440070 [Multi-domain] Cd Length: 382 Bit Score: 51.63 E-value: 6.12e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 530372214 227 FRVTCNRAGEKHCFTSNEAARDFGGAVQDYFK-WKADMTNFDVEVLLNIHDNEVIV 281
Cdd:COG0301 103 FKVRAKRAGKHFPFTSPELEREVGGALLENTPgLKVDLKNPDVTIRVEVRDDKAYV 158
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
311-445 |
1.59e-06 |
|
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 441828 [Multi-domain] Cd Length: 143 Bit Score: 47.68 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 311 MLRLCDPLPYDIIVDPMCGTGAIPIEGAtewSDCFHIAG-DNNPLAVNRAANNIASLltksqikegkpswGLPIDAVQWD 389
Cdd:COG2226 14 LLAALGLRPGARVLDLGCGTGRLALALA---ERGARVTGvDISPEMLELARERAAEA-------------GLNVEFVVGD 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 530372214 390 ICNLPLRTGSVDIIVTDLPFgkrmgskkRNWNLYPACLREMSRVCTPtTGRAVLLT 445
Cdd:COG2226 78 AEDLPFPDGSFDLVISSFVL--------HHLPDPERALAEIARVLKP-GGRLVVVD 124
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
323-436 |
6.05e-05 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 41.78 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 323 IVDPMCGTGAIPIEGATEWSdcFHIAG-DNNPLAVNRAANNIASLltksqikegkpswGLPIDAVQWDICNLPLRTGSVD 401
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRGG--ARVTGvDLSPEMLERARERAAEA-------------GLNVEFVQGDAEDLPFPDGSFD 65
|
90 100 110
....*....|....*....|....*....|....*
gi 530372214 402 IIVTDLPFGkrmgskKRNWNLYPACLREMSRVCTP 436
Cdd:pfam13649 66 LVVSSGVLH------HLPDPDLEAALREIARVLKP 94
|
|
| YtxK |
COG0827 |
Adenine-specific DNA N6-methylase [Replication, recombination and repair]; |
323-411 |
4.09e-03 |
|
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
Pssm-ID: 440589 [Multi-domain] Cd Length: 327 Bit Score: 39.55 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372214 323 IVDPMCGTGAIPIEGATEWSDCFHIAG-DNNPLAVNRAANNIASLltksqikegkpswGLPIDAVQWDICNlPLRTGSVD 401
Cdd:COG0827 119 ILDPAVGTGNLLTTVLNQLKKKVNAYGvEVDDLLIRLAAVLANLQ-------------GHPVELFHQDALQ-PLLIDPVD 184
|
90
....*....|
gi 530372214 402 IIVTDLPFGK 411
Cdd:COG0827 185 VVISDLPVGY 194
|
|
| |
