|
Name |
Accession |
Description |
Interval |
E-value |
| Trm14_Arch |
NF040721 |
tRNA (guanine(6)-N2)-methyltransferase; |
1-380 |
0e+00 |
|
tRNA (guanine(6)-N2)-methyltransferase;
Pssm-ID: 468685 [Multi-domain] Cd Length: 370 Bit Score: 642.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 1 MDYYVTLSPGLEKISKNEIESFGGKIKEIRENKGRIFFSGDLKLIPKINYLSRTIERMNILLHREEIPNiALDDIYKRVY 80
Cdd:NF040721 1 MEFYATLSPGLEKISAEEIEELGGKIKEIREGKGRVFFEGDLELIPKLNYLSRTLERIVILLHREKFEG-SLEDIYKRVY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 81 NIDWTeWIKENQSFAIRPLRAGEHNFTSIDIGRVAGEAVIKSYQRDKNIRLKVNLDEPDVIVRVEVIFDELIVGIDTTGD 160
Cdd:NF040721 80 SIDFS-FIKPEQSFAIRPLRVGEHDFTSIDIGRVAGEAVIDSYLRDKGVRLKVNLDEPDVIVRVELIFDELLVGIDTTGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 161 IALDKRGYRVFNHPAHLNATIASSLVYLSDWKDDEMLLDPMCGSGTIPIEGALMKRNIPPGKFRENkygFKFIDIFGYEL 240
Cdd:NF040721 159 EGLHKRGYRVYQHPAHLNPTIASSLIYLSGWKDEESLLDPMCGSGTILIEAALIKRNIPPGKFRED---FAFKKIFGHEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 241 LDKIKKEIVenkniYKIIGLDKNQKYLDGAKDNAKNAEVLDTIEFICGDATKLHEKFNESDVIIANPPYGIRIGSKRSVK 320
Cdd:NF040721 236 LEKIKKDVE-----LKIYGIEKFRKHLEGAKKNAENAGVDDTIKFIQGDATKLDKYFDSVDVIVTNPPYGLRIGKKRIIK 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 321 KLYDEFLSSAKEIMHGSSRLIVITAEDKMFKDAIAKNNFEVKEEFNVMFGGLMTRVFYLT 380
Cdd:NF040721 311 KLYNNFLRSAKKILHKRSRIVVITAEKKIFEEAAAKNGFEIIEEFNVMYGGLLTKVFVLK 370
|
|
| RlmL |
COG0116 |
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ... |
1-351 |
1.21e-110 |
|
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: 328.21 E-value: 1.21e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 1 MDYYVTLSPGLEKISKNEIESFGGKikEIRENKGRIFFSGDLKLIPKINYLSRTIERMNILLHREEIPNiaLDDIYKRVY 80
Cdd:COG0116 1 FELFATCARGLEALLADELKELGAE--DVKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFKART--FDDLYEGAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 81 NIDWTEWIKENQSFAIRPLRAGEHNFTSIDIGRVAGEAVIKSYQRDKNIRLKVNLDEPDVIVRVEVIFDELIVGIDTTGD 160
Cdd:COG0116 77 AIPWEEYLPPDGTFAVDATSVKSKLFHSQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHVHLLKDRATLSLDTSGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 161 iALDKRGYRVFNHPAHLNATIASSLVYLSDWKDDEMLLDPMCGSGTIPIEGALMKRNIPPGKFREnkYGFKFIDIFGYEL 240
Cdd:COG0116 157 -SLHKRGYREAQGEAPLKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAALIAANIAPGLNRD--FAFEKWPDFDAEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 241 LDKIKKEIVEN---KNIYKIIGLDKNQKYLDGAKDNAKNAEVLDTIEFICGDATKLHEKfNESDVIIANPPYGIRIGSKR 317
Cdd:COG0116 234 WQELREEAEARikrDPPLPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLEPP-AEPGLIITNPPYGERLGEEE 312
|
330 340 350
....*....|....*....|....*....|....
gi 2501584 318 SVKKLYDEFLSSAKEIMHGsSRLIVITAEDKMFK 351
Cdd:COG0116 313 ELEALYRELGDVLKQRFKG-WSAYILTSDPELEK 345
|
|
| UPF0020 |
pfam01170 |
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ... |
166-375 |
5.75e-87 |
|
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: 261.14 E-value: 5.75e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 166 RGYRVFNHPAHLNATIASSLVYLSDWKDDEMLLDPMCGSGTIPIEGALMKRNIPPGKFRENkygfkfidifgyelldkik 245
Cdd:pfam01170 1 RGYRPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPGKFDAR------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 246 keivenkNIYKIIGLDKNQKYLDGAKDNAKNAEVLDTIEFICGDATKLHEKFNESDVIIANPPYGIRIGSKRSVKKLYDE 325
Cdd:pfam01170 62 -------VRAPLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRLGSKGALEALYPE 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2501584 326 FLSSAKEIMHGSSRLIVITAEDKMFKDAIAKNNFEVKEEFNVMFGGLMTR 375
Cdd:pfam01170 135 FLREAKRVLRGGGWLVLLTAENKDFEKAARERAWRKKKEFNVHIGGTRVI 184
|
|
| rlmL |
PRK11783 |
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ... |
1-326 |
2.97e-60 |
|
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: 206.58 E-value: 2.97e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 1 MDYYVTLSPGLEKISKNEIESFGgkIKEIRENKGRIFFSGDLKLIPKINYLSRTIERMNILLHREEIPNIalDDIYKRVY 80
Cdd:PRK11783 2 NSLFASCAKGLEELLKDELEALG--ASECKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSD--LDLYLGVQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 81 NIDWTEWIKENQSFAIRplragehnF--TSIDIG-------RVAgEAVIKSYQRDKNIRLKVNLDEPDVIVRVEVIFDEL 151
Cdd:PRK11783 78 AIDWTEHFSPDKTFAVD--------FsgTNDEIRntqfgalKVK-DAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 152 IVGIDTTGDiALDKRGYRVFNHPAHLNATIASSLVYLSDW-KDDEMLLDPMCGSGTIPIEGALMKRNIPPGKFREnKYGF 230
Cdd:PRK11783 149 TISLDLSGE-SLHQRGYRQATGEAPLKENLAAAILLRSGWpQEGTPLLDPMCGSGTLLIEAAMMAADIAPGLHRE-RWGF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 231 KFIDIFGYELLDKIKKEIVENKNI------YKIIGLDKNQKYLDGAKDNAKNAEVLDTIEFICGDATKLHEKFNESD--V 302
Cdd:PRK11783 227 SGWLGHDEALWQELLEEAQERARAglaelpSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKNPLPKGPtgL 306
|
330 340
....*....|....*....|....
gi 2501584 303 IIANPPYGIRIGSKRSVKKLYDEF 326
Cdd:PRK11783 307 VISNPPYGERLGEEPALIALYSQL 330
|
|
| THUMP_AdoMetMT |
cd11715 |
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ... |
3-159 |
9.51e-44 |
|
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: 148.88 E-value: 9.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 3 YYVTLSPGLEKISKNEIESFGGKikEIRENKGRIFFSGDLKLIPKINYLSRTIERMNILLHREEIPNiaLDDIYKRVYNI 82
Cdd:cd11715 1 FFATCPPGLEELLAAELKALGAE--DVEVGPGGVSFEGDLEDAYRANLWLRTAHRVLLLLAEFEAED--FDDLYELAKAI 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2501584 83 DWTEWIKENQSFAIRPLRAGEHNFTSIDIGRVAGEAVIKSYqRDKNIRLKVNLDEPDVIVRVEVIFDELIVGIDTTG 159
Cdd:cd11715 77 DWEDYLDPDGTFAVRATRVGSKLFHSQFAALRVKDAIVDRF-REKGKRPSVDLDNPDVRIRVHLSKDRATLSLDLSG 152
|
|
| TIGR01177 |
TIGR01177 |
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ... |
3-379 |
3.83e-24 |
|
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: 101.36 E-value: 3.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 3 YYVTLSPGLEKISKNEIESfggkIKEIRENKGRIFFSGDLKLI---PKINYLSRTIERMNIllhREEIPNIALDDIYKRV 79
Cdd:TIGR01177 1 FYVELSGEHPELPLAELKA----LAEVYGRVGDVEGVDRGLAIisaPIIDILERLAFTHEV---GRSYDTCAAKDLYDFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 80 YNIDWTEWIkeNQSFAIRPLRAGEHNFTSIDIGRVAGeAVIKSYQrdknirLKVNLDEPDVIVRVEVIFDELIVGI---D 156
Cdd:TIGR01177 74 AGLEASDLD--RKSFAVRVRDLRGYSVDKARLERKIG-AILKKKG------FKVSLRRPDIVVRVVITEDIFYLGRvleE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 157 TTGDIALDKR-GYRVFNHPAHLNATIASSLVYLSDWKDDEMLLDPMCGSGTIPIEGALMKrnippgkfrenkygfkfidi 235
Cdd:TIGR01177 145 RDKEQFIERKpDRRPFFKPGSMDPKLARAMVNLARVTEGDRVLDPFCGTGGFLIEAGLMG-------------------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 236 fgyelldkikkeivenkniYKIIGLDKNQKYLDGAKDNAKNAEVLDtIEFICGDATKLHEKFNESDVIIANPPYGIRIGS 315
Cdd:TIGR01177 205 -------------------AKVIGCDIDWKMVAGARINLEHYGIED-FFVKRGDATKLPLSSESVDAIATDPPYGRSTTA 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2501584 316 KR-SVKKLYDEFLSSAKEIMHGSSRlIVITAEDKMFKDAIAKNNFEVKEEFNVMFGGLMTRVFYL 379
Cdd:TIGR01177 265 AGdGLESLYERSLEEFHEVLKSEGW-IVYAVPTRIDLESLAEDAFRVVKRFEVRVHRSLTRHIYV 328
|
|
| THUMP |
smart00981 |
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ... |
72-156 |
1.34e-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: 68.46 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 72 LDDIYKRVYN-IDWTEWIKENQSFAIRPLRAG-EHNFTSIDIGRVAGEAVIKSYQRdknirLKVNLDEPDVIVRVEVIFD 149
Cdd:smart00981 2 LEDLYETALElIRWEKIFKEGKTFAVRAKRRGkNHEFTSLEVKRAIGDKLLEKTGG-----RKVDLKNPDVVIRVELRKD 76
|
....*..
gi 2501584 150 ELIVGID 156
Cdd:smart00981 77 KAYLSID 83
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Trm14_Arch |
NF040721 |
tRNA (guanine(6)-N2)-methyltransferase; |
1-380 |
0e+00 |
|
tRNA (guanine(6)-N2)-methyltransferase;
Pssm-ID: 468685 [Multi-domain] Cd Length: 370 Bit Score: 642.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 1 MDYYVTLSPGLEKISKNEIESFGGKIKEIRENKGRIFFSGDLKLIPKINYLSRTIERMNILLHREEIPNiALDDIYKRVY 80
Cdd:NF040721 1 MEFYATLSPGLEKISAEEIEELGGKIKEIREGKGRVFFEGDLELIPKLNYLSRTLERIVILLHREKFEG-SLEDIYKRVY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 81 NIDWTeWIKENQSFAIRPLRAGEHNFTSIDIGRVAGEAVIKSYQRDKNIRLKVNLDEPDVIVRVEVIFDELIVGIDTTGD 160
Cdd:NF040721 80 SIDFS-FIKPEQSFAIRPLRVGEHDFTSIDIGRVAGEAVIDSYLRDKGVRLKVNLDEPDVIVRVELIFDELLVGIDTTGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 161 IALDKRGYRVFNHPAHLNATIASSLVYLSDWKDDEMLLDPMCGSGTIPIEGALMKRNIPPGKFRENkygFKFIDIFGYEL 240
Cdd:NF040721 159 EGLHKRGYRVYQHPAHLNPTIASSLIYLSGWKDEESLLDPMCGSGTILIEAALIKRNIPPGKFRED---FAFKKIFGHEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 241 LDKIKKEIVenkniYKIIGLDKNQKYLDGAKDNAKNAEVLDTIEFICGDATKLHEKFNESDVIIANPPYGIRIGSKRSVK 320
Cdd:NF040721 236 LEKIKKDVE-----LKIYGIEKFRKHLEGAKKNAENAGVDDTIKFIQGDATKLDKYFDSVDVIVTNPPYGLRIGKKRIIK 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 321 KLYDEFLSSAKEIMHGSSRLIVITAEDKMFKDAIAKNNFEVKEEFNVMFGGLMTRVFYLT 380
Cdd:NF040721 311 KLYNNFLRSAKKILHKRSRIVVITAEKKIFEEAAAKNGFEIIEEFNVMYGGLLTKVFVLK 370
|
|
| RlmL |
COG0116 |
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ... |
1-351 |
1.21e-110 |
|
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: 328.21 E-value: 1.21e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 1 MDYYVTLSPGLEKISKNEIESFGGKikEIRENKGRIFFSGDLKLIPKINYLSRTIERMNILLHREEIPNiaLDDIYKRVY 80
Cdd:COG0116 1 FELFATCARGLEALLADELKELGAE--DVKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFKART--FDDLYEGAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 81 NIDWTEWIKENQSFAIRPLRAGEHNFTSIDIGRVAGEAVIKSYQRDKNIRLKVNLDEPDVIVRVEVIFDELIVGIDTTGD 160
Cdd:COG0116 77 AIPWEEYLPPDGTFAVDATSVKSKLFHSQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHVHLLKDRATLSLDTSGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 161 iALDKRGYRVFNHPAHLNATIASSLVYLSDWKDDEMLLDPMCGSGTIPIEGALMKRNIPPGKFREnkYGFKFIDIFGYEL 240
Cdd:COG0116 157 -SLHKRGYREAQGEAPLKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAALIAANIAPGLNRD--FAFEKWPDFDAEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 241 LDKIKKEIVEN---KNIYKIIGLDKNQKYLDGAKDNAKNAEVLDTIEFICGDATKLHEKfNESDVIIANPPYGIRIGSKR 317
Cdd:COG0116 234 WQELREEAEARikrDPPLPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLEPP-AEPGLIITNPPYGERLGEEE 312
|
330 340 350
....*....|....*....|....*....|....
gi 2501584 318 SVKKLYDEFLSSAKEIMHGsSRLIVITAEDKMFK 351
Cdd:COG0116 313 ELEALYRELGDVLKQRFKG-WSAYILTSDPELEK 345
|
|
| UPF0020 |
pfam01170 |
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ... |
166-375 |
5.75e-87 |
|
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: 261.14 E-value: 5.75e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 166 RGYRVFNHPAHLNATIASSLVYLSDWKDDEMLLDPMCGSGTIPIEGALMKRNIPPGKFRENkygfkfidifgyelldkik 245
Cdd:pfam01170 1 RGYRPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPGKFDAR------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 246 keivenkNIYKIIGLDKNQKYLDGAKDNAKNAEVLDTIEFICGDATKLHEKFNESDVIIANPPYGIRIGSKRSVKKLYDE 325
Cdd:pfam01170 62 -------VRAPLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRLGSKGALEALYPE 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2501584 326 FLSSAKEIMHGSSRLIVITAEDKMFKDAIAKNNFEVKEEFNVMFGGLMTR 375
Cdd:pfam01170 135 FLREAKRVLRGGGWLVLLTAENKDFEKAARERAWRKKKEFNVHIGGTRVI 184
|
|
| rlmL |
PRK11783 |
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ... |
1-326 |
2.97e-60 |
|
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: 206.58 E-value: 2.97e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 1 MDYYVTLSPGLEKISKNEIESFGgkIKEIRENKGRIFFSGDLKLIPKINYLSRTIERMNILLHREEIPNIalDDIYKRVY 80
Cdd:PRK11783 2 NSLFASCAKGLEELLKDELEALG--ASECKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSD--LDLYLGVQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 81 NIDWTEWIKENQSFAIRplragehnF--TSIDIG-------RVAgEAVIKSYQRDKNIRLKVNLDEPDVIVRVEVIFDEL 151
Cdd:PRK11783 78 AIDWTEHFSPDKTFAVD--------FsgTNDEIRntqfgalKVK-DAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 152 IVGIDTTGDiALDKRGYRVFNHPAHLNATIASSLVYLSDW-KDDEMLLDPMCGSGTIPIEGALMKRNIPPGKFREnKYGF 230
Cdd:PRK11783 149 TISLDLSGE-SLHQRGYRQATGEAPLKENLAAAILLRSGWpQEGTPLLDPMCGSGTLLIEAAMMAADIAPGLHRE-RWGF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 231 KFIDIFGYELLDKIKKEIVENKNI------YKIIGLDKNQKYLDGAKDNAKNAEVLDTIEFICGDATKLHEKFNESD--V 302
Cdd:PRK11783 227 SGWLGHDEALWQELLEEAQERARAglaelpSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKNPLPKGPtgL 306
|
330 340
....*....|....*....|....
gi 2501584 303 IIANPPYGIRIGSKRSVKKLYDEF 326
Cdd:PRK11783 307 VISNPPYGERLGEEPALIALYSQL 330
|
|
| THUMP_AdoMetMT |
cd11715 |
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ... |
3-159 |
9.51e-44 |
|
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: 148.88 E-value: 9.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 3 YYVTLSPGLEKISKNEIESFGGKikEIRENKGRIFFSGDLKLIPKINYLSRTIERMNILLHREEIPNiaLDDIYKRVYNI 82
Cdd:cd11715 1 FFATCPPGLEELLAAELKALGAE--DVEVGPGGVSFEGDLEDAYRANLWLRTAHRVLLLLAEFEAED--FDDLYELAKAI 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2501584 83 DWTEWIKENQSFAIRPLRAGEHNFTSIDIGRVAGEAVIKSYqRDKNIRLKVNLDEPDVIVRVEVIFDELIVGIDTTG 159
Cdd:cd11715 77 DWEDYLDPDGTFAVRATRVGSKLFHSQFAALRVKDAIVDRF-REKGKRPSVDLDNPDVRIRVHLSKDRATLSLDLSG 152
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
171-378 |
1.86e-26 |
|
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: 103.88 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 171 FNHPAHLNATIASSLVYLSDWKDDEMLLDPMCGSGTIPIEGALMKRNIppgkfrenkygfkfidifgyelldkikkeive 250
Cdd:COG1041 4 FFYPGSLDPRLARALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGRRV-------------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 251 nkniykiIGLDKNQKYLDGAKDNAKNAEVLDtIEFICGDATKLHEKFNESDVIIANPPYGIRIGSK-RSVKKLYDEFLSS 329
Cdd:COG1041 52 -------IGSDIDPKMVEGARENLEHYGYED-ADVIRGDARDLPLADESVDAIVTDPPYGRSSKISgEELLELYEKALEE 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2501584 330 AKEIMHGSSRLIVITaeDKMFKDAIAKNNFEVKEEFNVMFGGLMTRVFY 378
Cdd:COG1041 124 AARVLKPGGRVVIVT--PRDIDELLEEAGFKVLERHEQRVHKSLTRYIL 170
|
|
| TIGR01177 |
TIGR01177 |
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ... |
3-379 |
3.83e-24 |
|
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: 101.36 E-value: 3.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 3 YYVTLSPGLEKISKNEIESfggkIKEIRENKGRIFFSGDLKLI---PKINYLSRTIERMNIllhREEIPNIALDDIYKRV 79
Cdd:TIGR01177 1 FYVELSGEHPELPLAELKA----LAEVYGRVGDVEGVDRGLAIisaPIIDILERLAFTHEV---GRSYDTCAAKDLYDFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 80 YNIDWTEWIkeNQSFAIRPLRAGEHNFTSIDIGRVAGeAVIKSYQrdknirLKVNLDEPDVIVRVEVIFDELIVGI---D 156
Cdd:TIGR01177 74 AGLEASDLD--RKSFAVRVRDLRGYSVDKARLERKIG-AILKKKG------FKVSLRRPDIVVRVVITEDIFYLGRvleE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 157 TTGDIALDKR-GYRVFNHPAHLNATIASSLVYLSDWKDDEMLLDPMCGSGTIPIEGALMKrnippgkfrenkygfkfidi 235
Cdd:TIGR01177 145 RDKEQFIERKpDRRPFFKPGSMDPKLARAMVNLARVTEGDRVLDPFCGTGGFLIEAGLMG-------------------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 236 fgyelldkikkeivenkniYKIIGLDKNQKYLDGAKDNAKNAEVLDtIEFICGDATKLHEKFNESDVIIANPPYGIRIGS 315
Cdd:TIGR01177 205 -------------------AKVIGCDIDWKMVAGARINLEHYGIED-FFVKRGDATKLPLSSESVDAIATDPPYGRSTTA 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2501584 316 KR-SVKKLYDEFLSSAKEIMHGSSRlIVITAEDKMFKDAIAKNNFEVKEEFNVMFGGLMTRVFYL 379
Cdd:TIGR01177 265 AGdGLESLYERSLEEFHEVLKSEGW-IVYAVPTRIDLESLAEDAFRVVKRFEVRVHRSLTRHIYV 328
|
|
| THUMP |
pfam02926 |
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ... |
16-157 |
1.08e-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: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 16 KNEIESFGGKIKEIRENKGRIFFS-------GDLKLIPKINYLSRTIERMNIllhrEEIPNIALDDIYKRVYNIDWTEWI 88
Cdd:pfam02926 4 EELLKKGGINVEVVRSGRGRILVVlkgenpeEDRELLKEALEKAPGIERFPV----AETCEADLEDILELAKEIIKDKFK 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 89 KENQSFAIRPLRAG-EHNFTSIDIGRVAGEAVIKSYQRdknirlKVNLDEPDVIVRVEVIFDELIVGIDT 157
Cdd:pfam02926 80 KEGETFAVRVKRRGkNHEFTSLEINREVGKAIVEKTGL------KVDLENPDIVVHVEIIKDKAYISIDR 143
|
|
| THUMP |
smart00981 |
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ... |
72-156 |
1.34e-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: 68.46 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 72 LDDIYKRVYN-IDWTEWIKENQSFAIRPLRAG-EHNFTSIDIGRVAGEAVIKSYQRdknirLKVNLDEPDVIVRVEVIFD 149
Cdd:smart00981 2 LEDLYETALElIRWEKIFKEGKTFAVRAKRRGkNHEFTSLEVKRAIGDKLLEKTGG-----RKVDLKNPDVVIRVELRKD 76
|
....*..
gi 2501584 150 ELIVGID 156
Cdd:smart00981 77 KAYLSID 83
|
|
| THUMP_ThiI |
cd11716 |
THUMP domain of thiamine biosynthesis protein ThiI; ThiI is an enzyme responsible for the ... |
72-153 |
1.66e-10 |
|
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: 59.38 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 72 LDDIYKRVYNIdWTEWIKENQSFAIRPLRAG-EHNFTSIDIGRVAGEAVIKSYQRdknirLKVNLDEPDVIVRVEVIFDE 150
Cdd:cd11716 81 LEDIKEAALEL-LKEELKKGKTFKVRAKRADkSFPFTSMEINREVGAALLENTPD-----LKVDLKNPDVTIRVEIREDG 154
|
...
gi 2501584 151 LIV 153
Cdd:cd11716 155 AYV 157
|
|
| THUMP_SPOUT |
cd11718 |
THUMP domain associated with SPOUT RNA Methylases; Members of this archaeal protein family are ... |
72-155 |
2.77e-10 |
|
THUMP domain associated with SPOUT RNA Methylases; Members of this archaeal protein family are characterized by containing an N-terminal THUMP domain and a C-terminal SPOUT RNA methyltransferase domain. No functional information is available 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: 212587 Cd Length: 145 Bit Score: 58.06 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 72 LDDIYKRVYNIdwTEWIKENQSFAIRPLRAGEHNFTSIDIGRVAGEAVIKSYQRDknirlkVNLDEPDVIVRVEVIFDEL 151
Cdd:cd11718 70 LDEIVRVAEEI--AKHISEGETFAVRTTRRGKHDFTSIDVNVVLGAAVKELTGAE------VDLNNPDKVVYVEIIGDRA 141
|
....
gi 2501584 152 IVGI 155
Cdd:cd11718 142 YISI 145
|
|
| ThiI |
COG0301 |
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ... |
72-153 |
3.68e-10 |
|
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: 60.87 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 72 LDDIYKRVYNIdWTEWIKeNQSFAIRPLRAGEH-NFTSIDIGRVAGEAVIKSYQRdknirLKVNLDEPDVIVRVEVIFDE 150
Cdd:COG0301 83 LEDIKEAALEL-AKEELK-GKTFKVRAKRAGKHfPFTSPELEREVGGALLENTPG-----LKVDLKNPDVTIRVEVRDDK 155
|
...
gi 2501584 151 LIV 153
Cdd:COG0301 156 AYV 158
|
|
| THUMP |
cd11688 |
THUMP domain, predicted to bind RNA; The THUMP domain is named after THioUridine synthases, ... |
4-147 |
5.52e-10 |
|
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: 57.50 E-value: 5.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 4 YVTLSPGLEKISKNEIESFG---GKIKEIR-ENKGRIFFSGDLKLIP-KINYLSRTIERmnILLHREEIPnIALDDIYKR 78
Cdd:cd11688 2 FATTGKGLEEILAAELYELLevrGFDAEIQvVPHGRVHFKTDTDEAVyQLVMWSRLISR--IMPPLGECK-ADLEDLYET 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2501584 79 VYNIDWTEWIKENQSFAIRPLRAGEHNFTSIDIGRVAGEAVIKSYQRdknirlKVNLDEPDVIVRVEVI 147
Cdd:cd11688 79 ALEINEPEMGNEGAKFAVRARRRNKTILNSQEIAMKVGDAIVDAFNP------EVDLDNPDIVVNVEVH 141
|
|
| Tan1 |
COG1818 |
tRNA(Ser,Leu) C12 N-acetylase TAN1, contains THUMP domain [Translation, ribosomal structure ... |
1-161 |
1.34e-07 |
|
tRNA(Ser,Leu) C12 N-acetylase TAN1, contains THUMP domain [Translation, ribosomal structure and biogenesis]; tRNA(Ser,Leu) C12 N-acetylase TAN1, contains THUMP domain is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 441423 Cd Length: 162 Bit Score: 50.66 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 1 MDYYVTLSPGLEKISKNEIESFG----GKIKEIREN-KGRIFFSGDL------KLIPKINYLSRTIERMNILlhrEEIPN 69
Cdd:COG1818 1 MNLIVTTPRGRERDAIEELRDILeegdPNAEVVPTGfSGVLLVKTSLdpyeavEKLKEEPWEPRYILRVIPV---DRVVK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 70 IALDDIYKRVYNIdWTEWIKENQSFAIRPLRAGEHNFTSIDIGRVAGEAViksyqrdKNIrLKVNLDEPDVIVRVEVIFD 149
Cdd:COG1818 78 TDLEEIVEAAKEL-AKKKIPEGETFAVRCEKRGKSKLSSREVIRAIGEAI-------KRG-AKVDLENPDWVVLVEILGD 148
|
170
....*....|..
gi 2501584 150 ELIVGIDTTGDI 161
Cdd:COG1818 149 KAGISVLKPEDI 160
|
|
| COG2263 |
COG2263 |
Predicted RNA methylase [General function prediction only]; |
256-369 |
2.76e-06 |
|
Predicted RNA methylase [General function prediction only];
Pssm-ID: 441864 [Multi-domain] Cd Length: 199 Bit Score: 47.59 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 256 KIIGLDKNQKYLDGAKDNAKNAEVldTIEFICGDATKLhEKFNESDVIIANPPYGirigskrSVKKLYD-EFLSSAKEI- 333
Cdd:COG2263 70 KVVGVDIDPEALEIARENAERLGV--RVDFIRADVTRI-PLGGSVDTVVMNPPFG-------AQRRHADrPFLEKALEIa 139
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2501584 334 -------MHGSSRLIvitaedkmfKDAIAKNNFEVKEEFNVMF 369
Cdd:COG2263 140 aviysihNAGSLDFV---------ERFAADRGGEITHVFRAEF 173
|
|
| HemK |
COG2890 |
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
256-309 |
2.62e-05 |
|
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 45.53 E-value: 2.62e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2501584 256 KIIGLDKNQKYLDGAKDNAKNAEVLDTIEFICGD---ATKLHEKFnesDVIIANPPY 309
Cdd:COG2890 138 RVTAVDISPDALAVARRNAERLGLEDRVRFLQGDlfePLPGDGRF---DLIVSNPPY 191
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
256-309 |
8.97e-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: 43.59 E-value: 8.97e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2501584 256 KIIGLDKNQKYLDGAKDNAKNAEVLDTIEFICGDATKLHEKFNES--DVIIANPPY 309
Cdd:COG4123 63 RITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAAELPPGsfDLVVSNPPY 118
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
256-343 |
3.28e-04 |
|
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: 39.72 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501584 256 KIIGLDKNQKYLDGAKDNAKNAEvLDTIEFICGDATKLHEKFNES-DVIIANPPYGirigskrSVKKLYDEFLSSAKEIM 334
Cdd:cd02440 23 RVTGVDISPVALELARKAAAALL-ADNVEVLKGDAEELPPEADESfDVIISDPPLH-------HLVEDLARFLEEARRLL 94
|
....*....
gi 2501584 335 HGSSRLIVI 343
Cdd:cd02440 95 KPGGVLVLT 103
|
|
| PRK09328 |
PRK09328 |
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional |
250-309 |
5.68e-04 |
|
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
Pssm-ID: 236467 [Multi-domain] Cd Length: 275 Bit Score: 41.30 E-value: 5.68e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2501584 250 ENKNIyKIIGLDKNQKYLDGAKDNAKNAeVLDTIEFICGDATK--LHEKFnesDVIIANPPY 309
Cdd:PRK09328 129 ERPDA-EVTAVDISPEALAVARRNAKHG-LGARVEFLQGDWFEplPGGRF---DLIVSNPPY 185
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
255-306 |
5.90e-04 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 38.70 E-value: 5.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2501584 255 YKIIGLDKNQKYLDGAKDNAKNAEVldTIEFICGDATKLHEKFNESDVIIAN 306
Cdd:pfam13649 21 ARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSFDLVVSS 70
|
|
| Methyltransf_15 |
pfam09445 |
RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as ... |
256-310 |
8.48e-03 |
|
RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as Schizosaccharomyces pombe Tgs1 and Giardia lamblia Tgs2 catalyze methylation of the exocyclic N2 amine of 7-methylguanosine.
Pssm-ID: 370496 Cd Length: 165 Bit Score: 36.93 E-value: 8.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2501584 256 KIIGLDKNQKYLDGAKDNAKNAEVLDTIEFICGDATKL--HEKFNE--SDVIIANPPYG 310
Cdd:pfam09445 24 SVISIDINLEHLACAQHNAEVYGVSDRIWLIHGDWFELlaKLKFEKikYDCVFASPPWG 82
|
|
| |
